THERAPEUTIC METHODS USING ILT-BINDING AGENTS CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims priority to United States Provisional Application No. 63/347,451 filed May 31, 2022 and United States Provisional Application No.63/429,491 filed December 1, 2022, the content of each of which is incorporated by reference in its entirety herein. SEQUENCE LISTING [0002] This application contains a computer readable Sequence Listing which has been submitted in XML file format with this application, the entire content of which is incorporated by reference herein in its entirety. The Sequence Listing XML file submitted with this application is entitled “13370-179-228_SEQLISTING.xml”, was created on May 25, 2023, and is 205,024 bytes in size. 1. FIELD [0003] The present disclosure provides methods of treating a subject having cancer using a binding agent (e.g., antibodies and antigen-binding fragments thereof) that specifically binds ILT2 and/or ILT4. The present disclosure also provides methods of using a biomarker to predict a subject’s responsiveness to the therapy disclosed herein and the efficacy of the therapy. 2. BACKGROUND [0004] The basis for immunotherapy is the manipulation and/or modulation of the immune system, including both innate immune responses and adaptive immune responses. The general aim of immunotherapy is to treat diseases by controlling the immune response to a “foreign agent”, for example a pathogen or a tumor cell. However, in some instances immunotherapy is used to treat autoimmune diseases which may arise from an abnormal immune response against proteins, molecules, and/or tissues normally present in the body. Immunotherapy may include methods to induce or enhance specific immune responses or to inhibit or reduce specific immune responses. [0005] The immune system is a highly complex system made up of a great number of cell types, including but not limited to, T-cells, T-cell subsets, B-cells, natural killer cells, antigen- presenting cells, dendritic cells, monocytes, and macrophages. These cells possess complex and subtle systems for controlling their interactions and responses. The cells utilize both activating and inhibitory mechanisms and feedback loops to keep responses in check and not allow negative consequences of an uncontrolled immune response (e.g., autoimmune diseases or a cytokine storm). [0006] Some of the inhibitory mechanisms of the immune system use proteins from the leukocyte Ig-like receptor (LILR) family. The leukocyte Ig-like receptor subfamily B (LILRB) is a group of type I transmembrane glycoproteins with extracellular Ig-like domains and cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs). This group of ITIM- containing receptors includes 5 members: LILRB1 (also known as CD85J, LIR1, ILT2), LILRB2 (also known as CD85D, LIR2, ILT4), LILRB3 (also known as CD85A, LIR3, ILT5), LILRB4 (also known as CD85K, LIR5, ILT3), and LILRB5 (also known as CD85C, LIR8). The biological functions and clinical significance of many of these LILRBs (ILTs) are still being investigated. There is also a LILR subfamily A (LILRA) that is a group of type I transmembrane glycoproteins with extracellular Ig-like domains and cytoplasmic immunoreceptor tyrosine-based activating motifs (ITAMs). This group of ITAM-containing receptors includes 6 members: LILRA1 (also known as CD85I, LIR6), LILRA2 (also known as CD85H, LIR7, ILT1), LILRA3 (also known as CD85E, LIR4, ILT6, monocyte inhibitory receptor HM43/31), LILRA4 (also known as CD85G, ILT7), LILRA5 (also known as CD85F, LIR9, ILT11), and LILRA6 (also known as ILT8). The inhibitory and activating proteins of the LILR family appear to work in concert to modulate immune homeostasis. [0007] The concept of cancer immunosurveillance is based on the theory that the immune system can recognize tumor cells, mount an immune response, and suppress the development and/or growth of a tumor. However, it is clear that many cancerous/tumor cells have developed mechanisms and/or hijacked normal inhibitory mechanisms to evade the immune system which can allow for uninhibited growth of tumor cells. Cancer/tumor immunotherapy (immuno- oncology) focuses on the development of new and novel agents that can activate and/or boost the immune system to achieve a more effective attack against cancer/tumor cells resulting in increased killing of cancer/tumor cells and/or inhibition of cancer/tumor growth. 3. SUMMARY [0008] The present disclosure provides methods of treating cancer in a subject in need thereof, comprising administering to a subject an agent that binds immunoglobulin-like transcript 2 (ILT2) and immunoglobulin-like transcript 4 (ILT4). [0009] In one aspect, the present disclosure provides a method of treating cancer in a subject, the method comprising administering to the subject a therapeutically effective amount of (a) a binding agent comprising (i) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145; or (ii) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:143; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:142; wherein the binding agent is administered at a dose of between about 200 mg and about 1800 mg. [0010] In certain embodiments, the cancer is hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple-negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, or prostate cancer. In certain embodiment, the cancer is a microsatellite instability – high (MSI-H) tumor or a deficient mismatch repair (dMMR) positive tumor. [0011] In certain embodiment, wherein the binding agent is a dose of between about 200 mg and about 1800 mg, including for examples, about 200 mg, about 300 mg, about 400 mg, about 500 mg, about 600 mg, about 700 mg, about 800 mg, about 900 mg, about 1000 mg, about 1100 mg, about 1200 mg, about 1300 mg, about 1400 mg, about 1500 mg, about 1600 mg, about 1700 mg, and about 1800 mg. In certain embodiment, the binding agent is administered at a dose of about 600 mg. In certain embodiment, the binding agent is administered at a dose of about 1200 mg. In certain embodiment, the binding agent is administered at a dose of about 1800 mg. [0012] In certain embodiment, the binding agent is administered at a dose that achieves at least about 95% (e.g., at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) of receptor occupancy in immune cells within 24 hours of administration. In certain embodiment, the binding agent is administered at a dose that achieves at least about 75% (e.g., at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or more) receptor occupancy in immune cells twenty-one (21) days or three weeks after administration. [0013] In certain embodiment, the immune cells are selected from the group consisting of granulocytes, myeloid antigen presenting cells, natural killer cells, monocytes, CD33+ myeloid cells, T cells, and B cells. [0014] In certain embodiment, the binding agent is administered once every week, 2 weeks, 3 weeks, or 4 weeks. In certain embodiment, the binding agent is administered once every 3 weeks. [0015] In certain embodiment, the binding agent is administered over about 30 minutes, about 60 minutes or about 90 minutes. In certain embodiment, the binding agent is administered over about 30 minutes at a dose of ≤ 600 mg (e.g., about 200 mg, about 300 mg, about 400 mg, about 500 mg, about 600 mg). In certain embodiment, the binding agent is administered over about 60 minutes at a dose of ≥ 600 mg (e.g., about 600 mg, about 800 mg, about 1000 mg, about 1200 mg, about 1400 mg, about 1600 mg, and about 1800 mg). [0016] In certain embodiment, the binding agent is administered intravenously. [0017] In certain embodiment, the binding agent is administered intravenously at a dose of about 600 mg once every 3 weeks. In certain embodiment, the binding agent is administered intravenously at a dose of about 1200 mg once every 3 weeks. In certain embodiment, the binding agent is administered intravenously at a dose of about 1800 mg once every 3 weeks. [0018] In certain embodiment, (1) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:115, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (2) the heavy chain variable region of the binding agent comprises the VH- CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (3) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:76, the VH-CDR2 having the amino acid sequence of SEQ ID NO:113, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (4) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:114, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; or (5) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:116, the VH-CDR2 having the amino acid sequence of SEQ ID NO:124, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:110; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:99, the VL-CDR2 having the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:101. [0019] In certain embodiment, (1) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8A; or (2) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8B. [0020] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:145; or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:144 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:145. [0021] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145. [0022] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142. [0023] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142. [0024] In one aspect, the present disclosure provides a method for: (a) inhibiting tumor growth in a subject; (b) increasing or enhancing an immune response to a tumor or tumor cells in a subject; (c) activating or enhancing a persistent or long-term immune response to a tumor or tumor cells in a subject; (d) inhibiting tumor relapse or tumor regrowth in a subject; or (e) inducing a persistent or long-term immunity that inhibits tumor relapse or tumor regrowth in a subject; the method comprising administering to the subject a therapeutically effective amount of a binding agent comprising (i) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region comprising a light chain variable region CDR1 (VL- CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145; or (ii) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:143; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:142; wherein the binding agent is administered at a dose of between about 200 mg and about 1800 mg. [0025] In certain embodiment, (1) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:115, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (2) the heavy chain variable region of the binding agent comprises the VH- CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (3) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:76, the VH-CDR2 having the amino acid sequence of SEQ ID NO:113, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (4) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:114, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; or (5) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:116, the VH-CDR2 having the amino acid sequence of SEQ ID NO:124, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:110; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:99, the VL-CDR2 having the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:101. [0026] In certain embodiment, (1) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8A; or (2) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8B. [0027] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:145; or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:144 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:145. [0028] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145. [0029] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142. [0030] In certain embodiment, (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142. [0031] In certain embodiment, the tumor comprises a microsatellite instability – high (MSI-H) tumor or a deficient mismatch repair (dMMR) positive tumor. [0032] In certain embodiment, the tumor is a hepatocellular carcinoma, a small cell lung tumor, a thyroid tumor, a mesothelioma, a glioblastoma, a renal cell carcinoma, a non-small cell lung tumor, a melanoma (skin cutaneous and uveal), a pancreatic ductal adenocarcinoma, a gastric tumor, a squamous cell carcinoma of the head and neck, a biliary duct tumor, a breast tumor, a triple-negative breast tumor, an ovarian tumor, a cervical tumor, an endocervical tumor, a colorectal tumor, an esophageal tumor, a gastroesophageal junction adenocarcinoma, a squamous cell carcinoma of head and neck, a bladder tumor, an uterine tumor, a cholangiocarcinoma, or a prostate tumor. [0033] In certain embodiment, the binding agent is (a) an antibody; (b) a recombinant antibody; (c) an antibody fragment comprising at least one antigen-binding site; (d) a chimeric antibody; (e) a humanized antibody; (f) a bispecific or multispecific antibody; or (g) attached to a half-life extending moiety. [0034] In certain embodiment, the binding agent is an IgG1 antibody, an IgG2 antibody, or an IgG4 antibody; optionally wherein the binding agent is a human IgG1 antibody, a human IgG2 antibody, or a human IgG4 antibody; further optionally the human IgG1 antibody has reduced or no effector function. [0035] In certain embodiment, the binding agent comprises a kappa light chain or a lambda light chain, optionally wherein the antibody comprises a human kappa light chain or a human lambda light chain. [0036] In certain embodiment, the antibody fragment is a Fab, a Fab’, a F(ab’)2, a Fv, a scFv, a (scFv)2, a single chain antibody, a dual variable region antibody, a diabody, or a nanobody. [0037] In certain embodiment, the binding agent comprises a heavy chain comprising an amino acid sequence with 80% identity to the sequence of SEQ ID NO:156 and a light chain comprising an amino acid sequence with 80% identity to the sequence of SEQ ID NO:157. [0038] In certain embodiment, the binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:156 and a light chain comprising the amino acid sequence of SEQ ID NO:157. [0039] In certain embodiment, the binding agent has one or more of the following properties: (1) binds rhesus ILT2; (2) binds cyno ILT2; (3) does not bind ILT3, ILT5, and LILRB5; (4) does not bind LILRA2, LILRA4, LILRA5, and LILRA6; (5) is an ILT2 antagonist; (6) is an ILT4 antagonist, (7) inhibits ILT2 activity; (8) inhibits ILT4 activity; (9) inhibits ILT2 signaling in cells that express ILT2; (10) inhibits ILT4 signaling in cells that express ILT4; (11) inhibits binding of ILT2 to MHC I molecules; (12) inhibits binding of ILT4 to MHC I molecules; (13) inhibits ILT2-induced suppression of myeloid cells; (14) inhibits ILT4-induced suppression of myeloid cells; (15) inhibits ILT2-induced suppression of myeloid cell activity; (16) inhibits ILT4-induced suppression of myeloid cell activity; (17) restores FcR activation in myeloid cells; (18) enhances NK cell activity; (19) enhances CTL activity; (20) enhances macrophage phagocytosis; and (21) inhibits MDSC mediated suppression of immune cells. [0040] In certain embodiment, the subject is a human. [0041] In one aspect, the present disclosure provides a method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, the method comprising comparing the expression level of CD163 in a sample of the subject before receiving the therapy to a CD163 reference level, wherein the subject is identified as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. [0042] In one aspect, the present disclosure provides a method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, the method comprising: (a) measuring the expression level of CD163 in a sample of the subject before receiving the therapy; (b) comparing the expression level of CD163 in (a) to a CD163 reference level; and (c) identifying the subject as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. [0043] In one aspect, the present disclosure provides a method for selectively treating a cancer or a tumor in a subject identified to have a higher expression level of CD163 than a CD163 reference level, the method comprising administering a therapeutically effective amount of a binding agent specifically binding to human ILT2 and/or human ILT4 to the subject. [0044] In one aspect, the present disclosure provides a method for treating a subject having a cancer or a tumor, comprising: (a) comparing the expression level of CD163 in a sample of the subject before receiving a therapy to a CD163 reference level, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; and (b) administering a therapeutically effective amount of the binding agent to the subject if the expression level of CD163 is higher than the CD163 reference level. [0045] In one aspect, the present disclosure provides a method for treating a subject having a cancer or a tumor, comprising: (a) measuring the expression level of CD163 in a sample obtained from the subject before receiving a therapy, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; (b) comparing the expression level of CD163 to a CD163 reference level; and (c) administering the therapy to the subject if the expression level of CD163 is higher than the CD163 reference level. [0046] In certain embodiment, the CD163 reference level is the expression level of CD163 in a sample from a healthy or non-diseased subject, or the expression level of CD163 in samples from a population of healthy or non-diseased subjects, wherein the sample from the healthy or non-diseased subject or the samples from a population of healthy or non-diseased subjects are from the same source as the sample from the subject having the cancer or tumor. [0047] In one aspect, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, the method comprising comparing (a) the expression level of CD163 in a sample of the subject before receiving the therapy and (b) the expression level of CD163 in a sample of the subject after receiving the therapy, wherein the therapy is determined to be effective if the expression level of CD163 in (b) is reduced as compared to the expression level of CD163 in (a). [0048] In one aspect, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, the method comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving the therapy, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) determining the therapy is effective if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). [0049] In one aspect, the present disclosure provides a method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) comparing (i) the expression level of CD163 in a sample of the subject before receiving the therapy and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; and (b) continuing administering the therapy to the subject if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). [0050] In one aspect, the present disclosure provides a method of treating a subject having a cancer or a tumor, comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) continuing administering the therapy to the subject if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). [0051] In one aspect, the present disclosure provides a method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) comparing (i) the expression level of CD163 in a sample of the subject before receiving the therapy and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; and (b) increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (a-ii) is not reduced as compared to the expression level of CD163 in (a-i). [0052] In one aspect, the present disclosure provides a method of treating a subject having a cancer or a tumor, comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (a-ii) is not reduced as compared to the expression level of CD163 in (a-i). [0053] In certain embodiment, the sample is a peripheral blood sample or a tumor biopsy. [0054] In certain embodiment, the sample comprises cells isolated from peripheral blood or a tumor biopsy of the subject. [0055] In certain embodiment, the isolated cells are selected from the group consisting of monocytes, MDSCs, pan-myeloid cells, pan-dendritic cells, and combinations thereof. [0056] In certain embodiment, the expression level of CD163 is a protein expression level of CD163. [0057] In certain embodiment, the protein expression level is measured by flow cytometry, immunohistochemistry, Western Blot, or enzyme-linked immunosorbent assay (ELISA). [0058] In certain embodiment, the expression level of CD163 is an mRNA expression level of CD163. [0059] In certain embodiment, the mRNA expression level is measured by quantitative reverse- transcriptase PCR (RT-qPCR), microarray, Northern blot, or RNA sequencing. [0060] In certain embodiment, the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received one dose or multiple doses of the binding agent. [0061] In certain embodiment, the sample obtained from the subject after receiving the therapy is a sample obtained from the subject between 15 days after the subject received a first dose of the binding agent and 15 days after the subject received a second dose of the binding agent. [0062] In certain embodiment, the antigen-binding domain binds specifically to both human ILT2 and human ILT4 and comprises a heavy chain variable region (VH) comprising a heavy chain complementarity-determining region 1 (VH-CDR1), a heavy chain complementarity- determining region 2 (VH-CDR2), and a heavy chain complementarity-determining region 3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region (VL) comprising a light chain complementarity-determining region 1 (VL-CDR1), a light chain complementarity-determining region 2 (VL-CDR2), and a light chain complementarity- determining region 3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145. [0063] In certain embodiment, (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:115, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH- CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL- CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:113, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:114, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:116, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:124, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101. [0064] In certain embodiment, (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:144, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:145; or (b) the VH comprises the amino acid sequence of SEQ ID NO:144, and/or the VL comprises the amino acid sequence of SEQ ID NO:145. [0065] In certain embodiment, the antigen-binding domain comprises (a) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:156, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:157; or (b) a heavy chain comprising the amino acid sequence of SEQ ID NO:156, and/or a light chain comprising the amino acid sequence of SEQ ID NO:157. [0066] In certain embodiment, the antigen-binding domain binds specifically to both human ILT2 and human ILT4 and comprises: (i) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:139; and a VL comprising a VL- CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:140; (ii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:133; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:134; (iii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:143; and a VL comprising a VL- CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:142; (iv) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:131; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:132; (v) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:137; and a VL comprising a VL- CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:138; (vi) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:135; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:136; or (vii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:141; and a VL comprising a VL- CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:142. [0067] In certain embodiment, (i) the VH comprises the VH-CDR1, the VH-CDR2, and the VH- CDR3 from the amino acid sequence of SEQ ID NO:139; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:140, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL- CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL- CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:123, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:105, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (ii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:133; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:134, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:118, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:118, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:119, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:120, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:121, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:82, the VL- CDR1 comprises the amino acid sequence of SEQ ID NO:83, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:122, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:85; or (iii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:143; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:142, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:115, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:113, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:114, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:116, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:117, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (iv) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:131; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:132, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:71, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:71, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:77, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:78, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:81, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:82, the VL- CDR1 comprises the amino acid sequence of SEQ ID NO:83, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:84, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:85; or (v) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:137; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:138, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL- CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL- CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:104, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:105, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (vi) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:135; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:136, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:98, the VL- CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (vii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH- CDR3 from the amino acid sequence of SEQ ID NO:141; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:142, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:106, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:106, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:77, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:108, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:109, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101. [0068] In certain embodiment, (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:139, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:140; or the VH comprises the amino acid sequence of SEQ ID NO:139, and/or the VL comprises the amino acid sequence of SEQ ID NO:140, (b) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:133, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:134; or the VH comprises the amino acid sequence of SEQ ID NO:133, and/or the VL comprises the amino acid sequence of SEQ ID NO:134, (c) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:143, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142; or the VH comprises the amino acid sequence of SEQ ID NO:143, and/or the VL comprises the amino acid sequence of SEQ ID NO:142, (d) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:131, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:132; or the VH comprises the amino acid sequence of SEQ ID NO:131, and/or the VL comprises the amino acid sequence of SEQ ID NO:132, (e) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:137, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:138; or the VH comprises the amino acid sequence of SEQ ID NO:137, and/or the VL comprises the amino acid sequence of SEQ ID NO:138, (f) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:135, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:136; or the VH comprises the amino acid sequence of SEQ ID NO:135, and/or the VL comprises the amino acid sequence of SEQ ID NO:136, or (g) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:141, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142; or the VH comprises the amino acid sequence of SEQ ID NO:141, and/or the VL comprises the amino acid sequence of SEQ ID NO:142. [0069] In certain embodiment, the antigen-binding domain comprises: (a) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:148, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:149; (b) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:152, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:153; (c) a heavy chain comprising the amino acid sequence of SEQ ID NO:148, and/or a light chain comprising the amino acid sequence of SEQ ID NO:149; or (d) a heavy chain comprising the amino acid sequence of SEQ ID NO:152, and/or a light chain comprising the amino acid sequence of SEQ ID NO:153. [0070] In certain embodiment, the antigen-binding domain binds specifically to human ILT2 and comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:125; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL- CDR3 from the amino acid sequence of SEQ ID NO:126. [0071] In certain embodiment, (i) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:31, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:23, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (ii) the VH- CDR1 comprises the amino acid sequence of SEQ ID NO:22, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:23, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL- CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (iii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:28, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:29, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:22, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:30, the VH-CDR3 the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:32, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:33, the VH- CDR3 comprises the amino acid sequence of SEQ ID NO:34, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:35, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:36, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:37. [0072] In certain embodiment, (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:125, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:126; or (b) the VH comprises the amino acid sequence of SEQ ID NO:125, and/or the VL comprises the amino acid sequence of SEQ ID NO:126. [0073] In certain embodiment, the antigen-binding domain binds specifically to human ILT4 and comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:129; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:130; or (b) a VH comprising a VH- CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:127; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:128. [0074] In certain embodiment, (a) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:129; and the VL comprises the VL- CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:130, and wherein (i) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:63, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:55, and the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56,the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (ii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:54, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:55, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (iii) the VH comprises the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:60, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:61, the VH- CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:54, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:62, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:64, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:65, and the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:66, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:67, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:68, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:69; or (b) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:127; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:128, and wherein (i) the VH- CDR1 comprises the amino acid sequence of SEQ ID NO:47, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:39, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL- CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (ii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:38, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:39, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (iii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:44, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:45, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:38, the VH-CDR2 comprising the amino acid sequence of SEQ ID NO:46, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:48, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:49, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:50, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:51, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:52, and the VL-CDR3 comprises an amino acid sequence of SEQ ID NO:53. [0075] In certain embodiment, (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:129, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:130; (b) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:127, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:128; (c) the VH comprises the amino acid sequence of SEQ ID NO:129, and/or the VL comprises the amino acid sequence of SEQ ID NO:130; or (d) the VH comprises the amino acid sequence of SEQ ID NO:127, and/or the VL comprises the amino acid sequence of SEQ ID NO:128. [0076] Where aspects or embodiments of the disclosure are described in terms of a Markush group or other grouping of alternatives, the present disclosure encompasses not only the entire group listed as a whole, but also each member of the group individually and all possible subgroups of the main group, and also the main group absent one or more of the group members. The present disclosure also envisages the explicit exclusion of one or more of any of the group members in the claimed disclosure. 4. BRIEF DESCRIPTION OF THE FIGURES [0077] Figure 1 depicts the expression of ILT2 and ILT4 in various immune cells assayed by flow cytometry. [0078] Figure 2 depicts the inhibition of the interaction between ILT2 or ILT4 and MHC I molecules by anti-ILT antibodies. [0079] Figure 3 depicts the binding of anti-ILT2/ILT4 antibodies to monocytes. [0080] Figures 4A and 4B depict the inhibition of the interaction between human ILT2 or ILT4 and MHC I molecules by anti-ILT antibodies. Figure 4A depicts the measurement by Raji reporter assay. Figure 4B depicts the measurement by 721.221-HLA-G cell reporter assay. [0081] Figure 5 depicts the inhibition of the interaction between cyno ILT2 and MHC I molecules by anti-ILT antibodies. [0082] Figure 6 depicts the effect of anti-ILT antibodies on cytolytic activity of NKL cells. [0083] Figure 7 depicts the effect of anti-ILT antibodies on activity of human primary NK cells. [0084] Figure 8 depicts the effect of anti-ILT antibodies on cytolytic activity of primary NK cells. [0085] Figure 9 depicts the effect of anti-ILT antibodies on cytolytic activity of primary NK cells in ADCC assay with classic MHC-I-expressing target cells. [0086] Figure 10 depicts the effect of anti-ILT antibodies on MDSC activity in MLR assay. [0087] Figures 11A-11C depict the effect of anti-ILT antibodies on MDSC activity in MLR assay. Figure 11A depicts T cell proliferation. Figure 11B depicts TNF-α secretion. Figure 11C depicts GM-CSF secretion. [0088] Figure 12 depicts the effect of anti-ILT antibodies on LPS-mediated stimulation of human PBMCs as assessed by cytokine production. [0089] Figure 13 depicts the effect of anti-ILT antibodies on LPS-mediated stimulation of cyno PBMCs as assessed by cytokine production. [0090] Figure 14 depicts the effect of anti-ILT antibodies on LPS-mediated stimulation of tolerized dendritic cells as assessed by cytokine production. [0091] Figure 15 depicts the effect of anti-ILT antibodies on cytokine production from HMGB1-treated cells. [0092] Figure 16 depicts the effect of anti-ILT antibodies on cytokine production from STING agonist-treated cells. [0093] Figure 17 depicts the effect of anti-ILT antibodies suppression of T-cell mediated stimulation of myeloid cells. [0094] Figure 18 depicts effect of anti-ILT antibodies on macrophage phagocytosis. [0095] Figure 19 depicts the effect of anti-ILT antibodies on cytokine production by dendritic cells. [0096] Figure 20 depicts the effect of anti-ILT antibodies on cytokine production from human blood cells. [0097] Figure 21 depicts the effect of anti-ILT antibodies on cytokine production from cyno blood cells. [0098] Figure 22 depicts the effect of anti-ILT antibodies on cytolytic activity of T cells. [0099] Figure 23 depicts the effects of anti-ILT2/ILT4 antibodies on polarization of monocyte-derived macrophages by assaying expression markers via flow cytometry. [00100] Figure 24 depicts the effect of Hz73D1.v1 (NGM707) on tumor growth in a CD34 humanized mouse melanoma model. [00101] Figure 25 depicts the experimental design of a mouse melanoma xenograft model. [00102] Figure 26 depicts the effect of ILT2 and ILT4 blockade individually on tumor growth. [00103] Figure 27 depicts the additive effect of ILT2 and ILT4 blockade on monocyte LPS activation. [00104] Figure 28 depicts the effect of Hz73D1.v1 (NGM707) in synergistically activating the immune system in vivo by blocking both ILT2 and ILT4 as shown by CX3CR1 MFI on Temra cells. [00105] Figure 29 depicts the effect of Hz73D1.v1 (NGM707) in synergistically activating the immune system in vivo by blocking both ILT2 and ILT4 as shown by the interferon gamma secretion. [00106] Figure 30 depicts the effect of Hz73D1.v1 (NGM707) in reversing a suppressive myeloid phenotype induced by cancer-associated fibroblasts. [00107] Figure 31 depicts the objective responses and tumor lesion assessment of subjects treated with NGM707 with different doses. Each column represents one subject. EOT; end of therapy; PD: progressive disease; SD: stable disease; NCR/NPD: non-complete response/non- progressive disease; PR: partial response; AE: adverse events. Columns from top to bottom: 1-8, 1800 mg; 9-12, 1200 mg; 13-23, 600 mg; 24-27, 200 mg; 28-30, 60 mg, 31-32, 20 mg; 33-34, 6 mg. [00108] Figures 32A and 32B depict the pharmacokinetic analysis. Figure 32A depicts the NGM707 serum concentration in each subject after administration of a specific dose of NGM707 in three consecutive cycles of treatment. Figure 32B depicts the mean NGM707 serum concentration from subjects administered with the same dose during the first cycle of treatment. [00109] Figure 33 depicts the receptor occupancy measured in monocytes isolated from subjects treated with different doses of NGM707. Each line represents a subject. [00110] Figures 34A and 34B depict the decreased CD163 expression on non-classical monocytes was associated with benefit from NGM707 monotherapy. C1D1: cycle 1, day 1; C1D15: cycle 1, day 15; SD: stable disease; PD: progressive disease. Figure 34A depicts the raw expression level of CD163. Figure 34B depicts the relative expression level of CD163 C1D15 to C1D1. SD or Better (circles ●); PD (diamonds, ♦). [00111] Figures 35A and 35B depict the immunohistochemical measurement of CD163 expression on patient biopsies. Figure 35A depicts the immunohistochemical staining of CD163 on two colorectal cancer (CRC) patient biopsies collected before treatment (baseline) and after treatment with 600mg of NGM707 (collected on C1D20-C1D21). Pt 11002 and Pt 11004 are two CRC patients. Figure 35B depicts the quantification of CD163+ staining from Figure 35A. On-Txt: on-treatment.11002 (circles ●), 11004 (triangles, ▲). [00112] Figure 36 depicts immunohistochemical measurement of CD163 in nonclassical monocytes from cultured PBMCs treated with NGM707 or anti-KLH control antibody. [00113] Figures 37A and 37B depicts chemokine profile of partial responder on NGM707 monotherapy, 1800 mg. Figure 37A shows the plasma concentration (pg/ml) of CCL3, CXCL9, CXCL10, and CXCL11 over the course of therapy. Figure 37B presents the same data relative to the pretreatment (baseline) level of each individual chemokine. [00114] Figure 38 depicts inflammatory immune status and tumor cell proliferation signature in patients treated with NGM707 monotherapy. Figure 38 shows that T Cell Inflammation Signature (“TIS”) was significantly increased, and the proliferation signature significantly decreased, in patients showing stable disease (“SD”) or a better clinical outcome relative to those that showed progressive disease (“PD”) over the course of NGM707 monotherapy, as described in Example 24. 5. DETAILED DESCRIPTION [00115] The present disclosure provides novel methods for using agents, including but not limited to polypeptides such as antibodies, that bind immunoglobulin-like transcript 2 (ILT2), immunoglobulin-like transcript 4 (ILT4), or both ILT2 and ILT4. [00116] “ILT-binding agents” as used herein encompass ILT2-binding agents, ILT4-binding agents, and agents binding to both ILT2 and ILT4 (referred to as ILT2/ILT4-binding agents or ILT2/ILT4 dual binders). Although LILRB family members are referred to by many names in art, the terms “ILT2” (also known as LILRB1) and “ILT4” (also known as LILRB2) are used in the present disclosure. The ILT-binding agents include, but are not limited to, polypeptides, antibodies (including antigen-binding fragments thereof), scaffold proteins, and heterodimeric molecules. ILT-binding agents include, but are not limited to, antagonists of ILT2 and/or ILT4 activity, inhibitors of ILT2 and/or ILT4 activity, and/or agents that inhibit ILT2 and/or ILT4 suppressive activity. Related polypeptides, polynucleotides, vectors, compositions comprising the agents, cells comprising the related polynucleotides or vectors, and methods of making the agents are also provided. In some embodiments, the ILT-binding agent disclosed herein inhibits ILT2 and/or ILT4 activity. In some embodiments, the ILT-binding agent disclosed herein enhances an immune response. In some embodiments, the ILT-binding agent disclosed herein reverses suppression of an immune cell activity. 5.1. Definitions [00117] Unless otherwise defined herein, technical and scientific terms used in the present description have the meanings that are commonly understood by those of ordinary skill in the art. Whenever appropriate, terms used in the singular will also include the plural and vice versa. In the event that any description of a term set forth conflicts with any document incorporated herein by reference, the description of the term set forth below shall control. [00118] The term “binding agent” as used herein refers to a molecule that binds a specific antigen or target (e.g., ILT2 and/or ILT4). A binding agent may comprise a protein, peptide, nucleic acid, carbohydrate, lipid, or small molecular weight compound. In some embodiments, a binding agent comprises a full-length antibody. In some embodiments, a binding agent is an antigen-binding fragment of an antibody. In some embodiments, a binding agent comprises an alternative protein scaffold or artificial scaffold (e.g., a non-immunoglobulin backbone). In some embodiments, a binding agent is a fusion protein comprising an antigen-binding site. In some embodiments, a binding agent is a bispecific or multispecific molecule comprising at least one antigen-binding site. [00119] The term “antibody” is used herein in the broadest sense and encompasses various antibody structures, including but not limited to, an immunoglobulin molecule that recognizes and binds a target through at least one antigen-binding site, polyclonal antibodies, recombinant antibodies, monoclonal antibodies (including full length monoclonal antibodies), chimeric antibodies, humanized antibodies, human antibodies, bispecific antibodies, multispecific antibodies, diabodies, tribodies, tetrabodies, single chain Fv (scFv) antibodies, and antibody fragments as long as they exhibit the desired antigen-binding activity. In general, the basic antibody structural unit comprises a tetramer. Each tetramer includes two identical pairs of polypeptide chains, each pair having one “light” (about 25 kDa) and one “heavy” chain (about 50-70 kDa). The amino-terminal portion of each chain includes a variable region of about 100 to 110 or more amino acids primarily responsible for antigen recognition. The carboxy-terminal portion of the heavy chain may define a constant region primarily responsible for effector function. Typically, human light chains are classified as kappa and lambda light chains. Furthermore, human heavy chains are typically classified as mu, delta, gamma, alpha, or epsilon, and define the antibody's isotype as IgM, IgD, IgG, IgA, and IgE, respectively. Within light and heavy chains, the variable and constant regions are joined by a “J” region of about 12 or more amino acids, with the heavy chain also including a “D” region of about 10 more amino acids. See generally, Fundamental Immunology Ch.7 (Paul, W., ed., 2nd ed. Raven Press, N.Y. (1989)). [00120] The variable regions of each light/heavy chain pair form the antibody binding site. Thus, in general, an intact antibody has two binding sites. Except in bifunctional or bispecific antibodies, the two binding sites are, in general, the same. [00121] Typically, the variable domains of both the heavy and light chains comprise three hypervariable regions, also called complementarity determining regions (CDRs), which are located within relatively conserved framework regions (FR). The CDRs are usually aligned by the framework regions, enabling binding to a specific epitope. In general, from N-terminal to C- terminal, both light and heavy chains variable domains comprise FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4. The assignment of amino acids to each domain is, generally, in accordance with the definitions of Sequences of Proteins of Immunological Interest, Kabat, et al.; National Institutes of Health, Bethesda, Md. ; 5th ed.; NIH Publ. No.91-3242 (1991); Kabat (1978) Adv. Prot. Chem.32:1-75; Kabat, et al., (1977) J. Biol. Chem.252:6609-6616; Chothia, et al., (1987) J Mol. Biol.196:901-917 or Chothia, et al., (1989) Nature 342:878-883. [00122] “CDR” or “CDRs” as used herein means complementarity determining region(s) in a immunoglobulin variable region, defined using the Kabat numbering system, unless otherwise indicated [00123] “Framework region” or “FR” as used herein means the immunoglobulin variable regions excluding the CDR regions. [00124] The term “intact antibody” or “full-length antibody” refers to an antibody having a structure substantially similar to a native antibody structure. This includes, for example, an antibody comprising two light chains each comprising a variable region and a light chain constant region (CL) and two heavy chains each comprising a variable region and at least heavy chain constant regions CH1, CH2, and CH3. Generally, an intact antibody includes a hinge region (or a portion thereof) between the CH1 and CH2 regions. [00125] The term “antibody fragment” or “antibody fragments” or “antigen binding fragment” as used herein refers to a molecule other than an intact antibody that comprises a portion of an antibody and generally an antigen-binding site. The antibody fragment retains the ability to bind specifically to the antigen bound by the full-length antibody, e.g. fragments that retain one or more CDR regions, e.g. all six CDRs. Examples of antibody fragments include, but are not limited to, Fab, Fab′, F(ab′)2, Fv, single chain antibody molecules (e.g., scFv), sc(Fv)2, disulfide-linked scFv (dsscFv), diabodies, tribodies, tetrabodies, minibodies, dual variable domain antibodies (DVD), single variable domain antibodies (e.g., camelid antibodies), and multispecific antibodies formed from antibody fragments. [00126] The term “monoclonal antibody” as used herein refers to a substantially homogenous antibody population involved in the highly specific recognition and binding of a single antigenic determinant or epitope. The term “monoclonal antibody” encompasses intact and full-length monoclonal antibodies as well as antibody fragments (e.g., Fab, Fab′, F(ab′) ₂ , Fv), single chain antibodies (e.g., scFv), fusion proteins comprising an antibody fragment, and any other modified immunoglobulin molecule comprising at least one antigen-binding site. Furthermore, “monoclonal antibody” refers to such antibodies made by any number of techniques, including but not limited to, hybridoma production, phage library display, recombinant expression, and transgenic animals. [00127] The term “chimeric antibody” refers to an antibody in which a portion of the heavy and/or light chain is derived from a first source or species, while the remainder of the heavy and/or light chain is derived from a different source or species. [00128] The term “humanized antibody” as used herein refers to an antibody that comprises a human heavy chain variable region and a light chain variable region wherein the native CDR amino acid residues are replaced by residues from corresponding CDRs from a nonhuman antibody (e.g., mouse, rat, rabbit, or nonhuman primate), wherein the nonhuman antibody has the desired specificity, affinity, and/or activity. In some embodiments, one or more framework region amino acid residues of the human heavy chain or light chain variable regions are replaced by corresponding residues from the nonhuman antibody. Furthermore, humanized antibodies can comprise amino acid residues that are not found in the human antibody or in the nonhuman antibody. In some embodiments, these modifications are made to further refine and/or optimize antibody characteristics. In some embodiments, the humanized antibody comprises at least a portion of a human immunoglobulin constant region (e.g., CH1, CH2, CH3, Fc, and/or hinge region). [00129] The term “human antibody” as used herein refers to an antibody that possesses an amino acid sequence that corresponds to an antibody produced by a human and/or an antibody that has been made using any of the techniques that are known to those of skill in the art for making human antibodies. These techniques include, but not limited to, phage display libraries, yeast display libraries, transgenic animals, recombinant protein production, and B-cell hybridoma technology. [00130] The terms “epitope” and “antigenic determinant” are used interchangeably herein and refer to that portion of an antigen or target capable of being recognized and bound by a particular antibody. When the antigen or target is a polypeptide, epitopes can be formed both from contiguous amino acids and noncontiguous amino acids juxtaposed by tertiary folding of the protein. Epitopes formed from contiguous amino acids (also referred to as linear epitopes) are typically retained upon protein denaturing, whereas epitopes formed by tertiary folding (also referred to as conformational epitopes) are typically lost upon protein denaturing. An epitope typically includes at least 3, and more usually, at least 5, 6, 7, or 8-10 amino acids in a unique spatial conformation. Epitopes can be predicted using any one of a large number of software bioinformatic tools available on the internet. X-ray crystallography may be used to characterize an epitope on a target protein by analyzing the amino acid residue interactions of an antigen/antibody complex. [00131] The term “specifically binds” as used herein refers to an agent that interacts more frequently, more rapidly, with greater duration, with greater affinity, or with some combination of the above to a particular antigen, epitope, protein, or target molecule than with alternative substances. A binding agent that specifically binds an antigen can be identified, for example, by immunoassays, ELISAs, surface plasmon resonance (SPR), or other techniques known to those of skill in the art. In some embodiments, an agent that specifically binds an antigen (e.g., human ILT2) can bind related antigens (e.g., rhesus ILT2 and/or cyno ILT2). In some embodiments, an agent that specifically binds an antigen (e.g., human ILT2) can bind a second antigen (e.g., human ILT4) and is referred to herein as a “dual binder”. In some embodiments, a binding agent that specifically binds an antigen can bind the target antigen at a higher affinity than its affinity for a different antigen. The different antigen can be a related antigen. In some embodiments, a binding agent that specifically binds an antigen can bind the target antigen with an affinity that is at least 20 times greater, at least 30 times greater, at least 40 times greater, at least 50 times greater, at least 60 times greater, at least 70 times greater, at least 80 times greater, at least 90 times greater, or at least 100 times greater, than its affinity for a different antigen. In some embodiments, a binding agent that specifically binds a particular antigen binds a different antigen at such a low affinity that binding cannot be detected using an assay described herein or otherwise known in the art. In some embodiments, affinity is measured using SPR technology in a Biacore system as described herein or as known to those of skill in the art. [00132] The terms “polypeptide” and “peptide” and “protein” are used interchangeably herein and refer to polymers of amino acids of any length. The polymer may be linear or branched, it may comprise modified amino acids, and it may be interrupted by non-amino acids. The terms also encompass an amino acid polymer that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid, including but not limited to, unnatural amino acids, as well as other modifications known in the art. It is understood that, because the polypeptides of this disclosure may be based upon antibodies, the term “polypeptide” encompasses polypeptides as a single chain and polypeptides of two or more associated chains. [00133] The terms “polynucleotide” and “nucleic acid” and “nucleic acid molecule” are used interchangeably herein and refer to polymers of nucleotides of any length, and include DNA and RNA. The nucleotides can be deoxyribonucleotides, ribonucleotides, modified nucleotides or bases, and/or their analogs, or any substrate that can be incorporated into a polymer by DNA or RNA polymerase. [00134] The terms “identical” or percent “identity” or “sequence identity” in the context of two or more nucleic acids or polypeptides, refer to two or more sequences or subsequences that are the same or have a specified percentage of nucleotides or amino acid residues that are the same, when compared and aligned (introducing gaps, if necessary) for maximum correspondence, not considering any conservative amino acid substitutions as part of the sequence identity. The percent identity may be measured using sequence comparison software or algorithms or by visual inspection. Various algorithms and software that may be used to obtain alignments of amino acid or nucleotide sequences are well-known in the art. These include, but are not limited to, BLAST, ALIGN, Megalign, BestFit, GCG Wisconsin Package, and variants thereof. In some embodiments, two nucleic acids or polypeptides of the disclosure are substantially identical, meaning they have at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, and in some embodiments at least 95%, 96%, 97%, 98%, 99% nucleotide or amino acid residue identity, when compared and aligned for maximum correspondence, as measured using a sequence comparison algorithm or by visual inspection. In some embodiments, identity exists over a region of the sequences that is at least about 10, at least about 20, at least about 20-40, at least about 40-60, at least about 60-80 nucleotides or amino acid residues in length, or any integral value there between. In some embodiments, identity exists over a longer region than 60-80 nucleotides or amino acid residues, such as at least about 80-100 nucleotides or amino acid residues, and in some embodiments the sequences are substantially identical over the full length of the sequences being compared, for example, (i) the coding region of a nucleotide sequence or (ii) an amino acid sequence. [00135] The phrase “conservative amino acid substitution” as used herein refers to a substitution in which one amino acid residue is replaced with another amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been generally defined in the art, including basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). For example, substitution of an alanine for a valine is considered to be a conservative substitution. Generally, conservative substitutions in the sequences of polypeptides and/or antibodies do not abrogate the binding of the polypeptide or antibody to the target binding site. Methods of identifying nucleotide and amino acid conservative substitutions that do not eliminate binding are well-known in the art. [00136] The term “vector” as used herein means a construct that is capable of delivering, and usually expressing, one or more gene(s) or sequence(s) of interest in a host cell. Examples of vectors include, but are not limited to, viral vectors, naked DNA or RNA expression vectors, plasmid, cosmid, or phage vectors, DNA or RNA expression vectors associated with cationic condensing agents, and DNA or RNA expression vectors encapsulated in liposomes. [00137] The term “isolated” as used herein refers to a polypeptide, soluble protein, antibody, polynucleotide, vector, cell, or composition that is in a form not found in nature. An “isolated” antibody is substantially free of material from the cellular source from which it is derived. In some embodiments, isolated polypeptides, soluble proteins, antibodies, polynucleotides, vectors, cells, or compositions are those that have been purified to a degree that they are no longer in a form in which they are found in nature. In some embodiments, a polypeptide, soluble protein, antibody, polynucleotide, vector, cell, or composition that is isolated is substantially pure. A polypeptide, soluble protein, antibody, polynucleotide, vector, cell, or composition can be isolated from a natural source (e.g., tissue) or from a source such as an engineered cell line. [00138] The term “substantially pure” as used herein refers to material that is at least 50% pure (i.e., free from contaminants), at least 90% pure, at least 95% pure, at least 98% pure, or at least 99% pure. [00139] The term “subject” refers to any animal (e.g., a mammal), including, but not limited to, humans, non-human primates, canines, felines, rabbits, rodents, and the like. [00140] The term “pharmaceutically acceptable” as used herein refers to a substance approved or approvable by a regulatory agency or listed in the U.S. Pharmacopeia, European Pharmacopeia, or other generally recognized pharmacopeia for use in animals, including humans. [00141] The terms “pharmaceutically acceptable excipient, carrier, or adjuvant” or “acceptable pharmaceutical carrier” as used herein refer to an excipient, carrier, or adjuvant that can be administered to a subject, together with at least one therapeutic agent, and that is generally safe, non-toxic, and has no effect on the pharmacological activity of the therapeutic agent. In general, those of skill in the art and government agencies consider a pharmaceutically acceptable excipient, carrier, or adjuvant to be an inactive ingredient of any formulation. [00142] The term “pharmaceutical formulation” or “pharmaceutical composition” as used herein refers to a preparation that is in such form as to permit the biological activity of the agent to be effective. A pharmaceutical formulation or composition generally comprises additional components, such as a pharmaceutically acceptable excipient, carrier, adjuvant, buffers, etc. [00143] The term “effective amount” or “therapeutically effective amount” as used herein refers to the amount of an agent that is sufficient to reduce and/or ameliorate the severity and/or duration of (i) a disease, disorder or condition in a subject, and/or (ii) a symptom in a subject. The term also encompasses an amount of an agent necessary for the (i) reduction or amelioration of the advancement or progression of a given disease, disorder, or condition, (ii) reduction or amelioration of the recurrence, development, or onset of a given disease, disorder, or condition, and/or (iii) the improvement or enhancement of the prophylactic or therapeutic effect(s) of another agent or therapy (e.g., an agent other than the binding agents provided herein). [00144] The term “therapeutic effect” as used herein refers to the effect and/or ability of an agent to reduce and/or ameliorate the severity and/or duration of (i) a disease, disorder, or condition in a subject, and/or (ii) a symptom in a subject. The term also encompasses the ability of an agent to (i) reduce or ameliorate the advancement or progression of a given disease, disorder, or condition, (ii) reduce or ameliorate the recurrence, development, or onset of a given disease, disorder, or condition, and/or (iii) to improve or enhance the prophylactic or therapeutic effect(s) of another agent or therapy (e.g., an agent other than the binding agents provided herein). [00145] The term “treat” or “treatment” or “treating” or “to treat” or “alleviate” or alleviation” or “alleviating” or “to alleviate” as used herein refers to therapeutic measures that aim to slow down, lessen symptoms of, and/or halt progression of a pathologic condition or disorder. Thus, those in need of treatment include those already with the disorder. [00146] The term “prevent” or “prevention” or “preventing” as used herein refers to the partial or total inhibition of the development, recurrence, onset, or spread of a disease, disorder, or condition, or a symptom thereof in a subject. [00147] The term “immune response” as used herein includes responses from both the innate immune system and the adaptive immune system. It includes both cell-mediated and/or humoral immune responses. It includes both T-cell and B-cell responses, as well as responses from other cells of the immune system such as natural killer (NK) cells, monocytes, macrophages, dendritic cells, etc. [00148] As used herein, the term “receptor occupancy” or “RO” is a measure of the binding of a molecule to its target. Receptor occupancy assays measure the binding of a molecule to its receptor protein (or target) and provide quantitative data for the same. [00149] As used herein, the term “refractory”, refers to a disease that does not respond to treatment, e.g., cancer. In embodiments, a refractory cancer may be resistant to treatment prior to or at the beginning of treatment. In other embodiments, refractory cancer may become refractory during treatment. [00150] As used herein, the term “relapsed” includes subjects who have received at least one prior treatment for the disease, e.g., cancer. Relapsed subjects generally have developed progressive disease following a response to the prior treatment. [00151] As used herein, reference to “about” or “approximately” a value or parameter includes (and describes) embodiments that are directed to that value or parameter. For example, a description referring to “about X” includes description of “X”. [00152] As used in the present disclosure and claims, the singular forms “a”, “an” and “the” include plural forms unless the context clearly dictates otherwise. [00153] It is understood that wherever embodiments are described herein with the term “comprising” otherwise analogous embodiments described in terms of “consisting of” and/or “consisting essentially of” are also provided. It is also understood that wherever embodiments are described herein with the phrase “consisting essentially of” otherwise analogous embodiments described in terms of “consisting of” are also provided. [00154] The term “and/or” as used in a phrase such as “A and/or B” herein is intended to include both A and B; A or B; A (alone); and B (alone). Likewise, the term “and/or” as used in a phrase such as “A, B, and/or C” is intended to encompass each of the following embodiments: A, B, and C; A, B, or C; A or C; A or B; B or C; A and C; A and B; B and C; A (alone); B (alone); and C (alone). [00155] “Kabat” as used herein means an immunoglobulin alignment and numbering system pioneered by Elvin A. Kabat ((1991) Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md.). 5.2. ILT-Binding Agents [00156] Amino acid (aa) sequences for human ILT2 (UniProtKB No. Q8NHL6), human ILT4 (UniProtKB No. Q8N423), rhesus macaque (“rhesus”) ILT2 (NCBI Ref No. XP_028694980.1), and cynomolgus monkey (“cyno”) ILT2 (in house sequence has 98% identity to UniProtKB No. A0A2K5VN04) are provided herein as SEQ ID NO:1, SEQ ID NO:8, SEQ ID NO:15, and SEQ ID NO:166, respectively. As used herein, reference to amino acid positions of ILT2 or ILT4 refer to the numbering of amino acid sequences including the signal sequence. [00157] A genomic orthologue for human ILT2 is found in the monkey genome, however, no genomic orthologue for human ILT4 appears to exist. Expression patterns of the monkey ILT2 orthologue are comparable to the combined expression patterns of human ILT2 and human ILT4. Without being bound by theory, it is believed that the ILT2 orthologue in monkeys may have biological/functional capabilities that are equivalent to a combination of the biological functions of human ILT2 and human ILT4. [00158] ILT2 is a single pass type I transmembrane protein with a predicted molecular weight of approximately 71 kDa. ILT2 (human, rhesus, and cyno) is characterized by an extracellular domain comprising four Ig-like C2 type domains, a transmembrane domain, and a long cytoplasmic domain containing 4 ITIM domains (see, e.g., Borges et al., 1997, J. Immunol., 159:5192-5196). The four Ig-like C2-type domains may be referred to herein as Domain 1 (D1), Domain 2 (D2), Domain 3 (D3), and Domain 4 (D4). D1 is situated at the N-terminal portion of the protein, then D2, D3, with D4 situated closest to the transmembrane region. As characterized within UniProtKB, human ILT2 is a protein of 650 amino acids (aa) - the signal sequence is aa 1-23, the extracellular domain is aa 24-461, the transmembrane region is aa 462- 482, and the cytoplasmic domain is aa 483-650. Within the extracellular domain, D1 is aa 27- 115, D2 is aa 116-221, D3 is aa 222-312, D4 is aa 313-409, and the “stem region” is aa 410-461. Within the cytoplasmic domain, ITIMs are aa 531-536, 560-565, 612-617, and 642-647. Rhesus ILT2 is a protein of 639 amino acids (aa) - as compared to structural characterization of human ILT2 the signal sequence is aa 1-23, the extracellular domain is aa 24-460, the transmembrane region is aa 461-481, and the cytoplasmic domain is aa 482-639. Within the extracellular domain, D1 is aa 27-114, D2 is aa 115-220, D3 is aa 221-311, D4 is aa 312-408, and the “stem region” is aa 409-460. Within the cytoplasmic domain, ITIMs are aa 530-535, 559-564, 601- 606, and 631-636. Cyno ILT2 is a protein of 651 amino acids (aa) - as compared to structural characterization of human ILT2 the signal sequence is aa 1-23, the extracellular domain is aa 24- 461, the transmembrane region is aa 462-482, and the cytoplasmic domain is aa 483-651. Within the extracellular domain, D1 is aa 27-114, D2 is aa 115-220, D3 is aa 221-311, D4 is aa 312-408, and the “stem region” is aa 409-461. Within the cytoplasmic domain, ITIMs are aa 531-536, 561-566, 613-618, and 643-648. ILT2 is expressed (to varying degrees) on natural killer (NK) cells, monocytes, macrophages, eosinophils, basophils, dendritic cells (DCs), subset of T-cells, and B-cells. Ligand known to interact with ILT2 include HLA class I molecules (e.g., HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, and HLA-G). ILT2 appears to bind more strongly with the “non-classical” MHC I molecule HLA-G than to classical HLA class I molecules. [00159] ILT4 has a similar structure to ILT2. It is a single pass type I transmembrane protein with a predicted molecular weight of approximately 65 kDa. ILT4 is characterized by an extracellular domain comprising four Ig-like C2 type domains, a transmembrane domain, and a long cytoplasmic domain containing 3 ITIM domains (see, e.g., Borges et al., 1997, J. Immunol., 159:5192-5196). As ILT2, the four Ig-like C2-type domains may be referred to herein as D1, D2, D3, and D4. D1 is situated at the N-terminal portion of the protein, then D2, D3, with D4 situated closest to the transmembrane region. As characterized within UniProtKB, human ILT4 is a protein of 598 amino acids (aa) - the signal sequence is aa 1-21, the extracellular domain is aa 22-461, the transmembrane region is aa 462-482, and the cytoplasmic domain is aa 483-598. Within the extracellular domain, D1 is aa 27-110, D2 is aa 111-229, D3 is aa 230-318, D4 is aa 330-419, and the “stem region” is aa 420-461. Within the cytoplasmic domain, ITIMs are aa 531-536, 560-565, and 590-595. ILT4 is expressed on myeloid cells such as monocytes, macrophages, dendritic cells, but not on lymphoid cells. Ligands of ILT4 include HLA class I molecules, ANGPTL proteins, myelin inhibitors, and β-amyloid. [00160] Domains of ILT2 or ILT4 (e.g., human ILT2, rhesus ILT2, cyno ILT2, or human ILT4) may be defined differently by those skilled in the art, therefore the N-terminal amino acids and the C-terminal amino acids of any ILT2 or ILT4 domain or region may vary by 1, 2, 3, 4, 5, or more amino acid residues. [00161] The present disclosure provides agents that bind ILT2, ILT4, or ILT2 and ILT4, i.e., ILT-binding agents. Agents that bind both ILT2 and ILT4 (ILT2/ILT4-binding agents) may be referred to herein as “dual binders”. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds ILT2 or a fragment of ILT2. In some embodiments, a fragment of ILT2 comprises the extracellular domain of ILT2. In some embodiments, a fragment of ILT2 comprises one or more of the Ig-like C2 type domains (e.g., D1, D2, D3, and/or D4). In some embodiments, a fragment of ILT2 comprises D1 and D2. In some embodiments, a fragment of ILT2 comprises D2 and D3. In some embodiments, a fragment of ILT2 comprises D3 and D4. In some embodiments, a fragment of ILT2 comprises D1, D2, and D3. In some embodiments, a fragment of ILT2 comprises D2, D3, and D4. In some embodiments, a fragment of ILT2 comprises one or more of the Ig-like C2 type domains and the stem region. In some embodiments, a fragment of ILT2 comprises D4-stem, D3-D4-stem, or D2-D3-D4-stem. [00162] In some embodiments, the extracellular domain of human ILT2 comprises amino acids 24-461 of SEQ ID NO:1. In some embodiments, D1 of human ILT2 comprises amino acids 27- 115 of SEQ ID NO:1. In some embodiments, D2 of human ILT2 comprises amino acids 116- 221 of SEQ ID NO:1. In some embodiments, D3 of human ILT2 comprises amino acids 222- 312 of SEQ ID NO:1. In some embodiments, D4 of human ILT2 comprises amino acids 313- 409 of SEQ ID NO:1. In some embodiments, D1-D2 of human ILT2 comprises amino acids 27- 221 of SEQ ID NO:1. In some embodiments, D2-D3 of human ILT2 comprises amino acids 116-312 of SEQ ID NO:1. In some embodiments, D3-D4 of human ILT2 comprises amino acids 222-409 of SEQ ID NO:1. In some embodiments, D1-D2-D3 of human ILT2 comprises amino acids 27-312 of SEQ ID NO:1. In some embodiments, D2-D3-D4 of human ILT2 comprises amino acids 116-409 of SEQ ID NO:1. In some embodiments, D4-stem of human ILT2 comprises amino acids 313-461 of SEQ ID NO:1. In some embodiments, D3-D4-stem of human ILT2 comprises amino acids 222-461 of SEQ ID NO:1. In some embodiments, D2-D3- D4-stem of human ILT2 comprises amino acids 116-461 of SEQ ID NO:1. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:3. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:4. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:5. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:6. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:7. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:4 and SEQ ID NO:5. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:5 and SEQ ID NO:6. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:6 and SEQ ID NO:7. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:4, SEQ ID NO:5, and SEQ ID NO:6. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:5, SEQ ID NO:6, and SEQ ID NO:7. [00163] In some embodiments, the extracellular domain of rhesus ILT2 comprises amino acids 24-460 of SEQ ID NO:15. In some embodiments, D1 of rhesus ILT2 comprises amino acids 27- 114 of SEQ ID NO:15. In some embodiments, D2 of rhesus ILT2 comprises amino acids 115- 220 of SEQ ID NO:15. In some embodiments, D3 of rhesus ILT2 comprises amino acids 221- 311 of SEQ ID NO:15. In some embodiments, D4 of rhesus ILT2 comprises amino acids 312- 408 of SEQ ID NO:15. In some embodiments, D1-D2 of rhesus ILT2 comprises amino acids 27-220 of SEQ ID NO:15. In some embodiments, D2-D3 of rhesus ILT2 comprises amino acids 115-311 of SEQ ID NO:15. In some embodiments, D3-D4 of rhesus ILT2 comprises amino acids 221-408 of SEQ ID NO:15. In some embodiments, D1-D2-D3 of rhesus ILT2 comprises amino acids 27-311 of SEQ ID NO:15. In some embodiments, D2-D3-D4 of rhesus ILT2 comprises amino acids 115-408 of SEQ ID NO:15. In some embodiments, D4-stem of rhesus ILT2 comprises amino acids 312-460 of SEQ ID NO:15. In some embodiments, D3-D4-stem of rhesus ILT2 comprises amino acids 221-460 of SEQ ID NO:15. In some embodiments, D2-D3- D4-stem of rhesus ILT2 comprises amino acids 115-460 of SEQ ID NO:15. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequence of SEQ ID NO:17. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequence of SEQ ID NO:18. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequence of SEQ ID NO:19. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequence of SEQ ID NO:20. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequence of SEQ ID NO:21. In some embodiments, a fragment of rhesus ILT2 comprises the amino acid sequences of SEQ ID NO:18 and SEQ ID NO:19. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:19 and SEQ ID NO:20. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:20 and SEQ ID NO:21. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:18, SEQ ID NO:19, and SEQ ID NO:20. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:19, SEQ ID NO:20, and SEQ ID NO:21. [00164] In some embodiments, the extracellular domain of cyno ILT2 comprises amino acids 24-461 of SEQ ID NO:166. In some embodiments, D1 of cyno ILT2 comprises amino acids 27- 114 of SEQ ID NO:166. In some embodiments, D2 of cyno ILT2 comprises amino acids 115- 220 of SEQ ID NO:166. In some embodiments, D3 of cyno ILT2 comprises amino acids 221- 311 of SEQ ID NO:166. In some embodiments, D4 of cyno ILT2 comprises amino acids 312- 408 of SEQ ID NO:166. In some embodiments, D1-D2 of cyno ILT2 comprises amino acids 27-220 of SEQ ID NO:166. In some embodiments, D2-D3 of cyno ILT2 comprises amino acids 115-311 of SEQ ID NO:166. In some embodiments, D3-D4 of cyno ILT2 comprises amino acids 221-408 of SEQ ID NO:166. In some embodiments, D1-D2-D3 of cyno ILT2 comprises amino acids 27-311 of SEQ ID NO:166. In some embodiments, D2-D3-D4 of cyno ILT2 comprises amino acids 115-408 of SEQ ID NO:166. In some embodiments, D4-stem of cyno ILT2 comprises amino acids 312-461 of SEQ ID NO:166. In some embodiments, D3-D4-stem of cyno ILT2 comprises amino acids 221-461 of SEQ ID NO:166. In some embodiments, D2- D3-D4-stem of cyno ILT2 comprises amino acids 115-461 of SEQ ID NO:166. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequence of SEQ ID NO:168. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequence of SEQ ID NO:169. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequence of SEQ ID NO:170. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequence of SEQ ID NO:171. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequence of SEQ ID NO:172. In some embodiments, a fragment of cyno ILT2 comprises the amino acid sequences of SEQ ID NO:169 and SEQ ID NO:170. In some embodiments, a fragment of human ILT2 comprises the amino acid sequence of SEQ ID NO:170 and SEQ ID NO:171. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:171 and SEQ ID NO:172. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:169, SEQ ID NO:170, and SEQ ID NO:171. In some embodiments, a fragment of human ILT2 comprises the amino acid sequences of SEQ ID NO:170, SEQ ID NO:171, and SEQ ID NO:172. [00165] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent disclosed herein binds a fragment of ILT2 (e.g., human ILT2, rhesus ILT2, and/or cyno ILT2). In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within a specific region of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds within the extracellular domain of ILT2. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds within the D1 domain of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D2 domain of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D3 domain of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D4 domain of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D4-stem region of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D1-D2 domains of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds within the D2-D3 domains of ILT2. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds within the D3-D4 domains of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds within the D1-D2-D3 domains of ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds within the D2-D3-D4 domains of ILT2. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds an epitope on ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a conformational epitope on ILT2. In some embodiments, the ILT2-binding agent does not bind other human LILRB proteins (e.g., ILT3, ILT4, ILT5, or LILRB5). In some embodiments, the ILT2/ILT4-binding agent does not bind other human LILRB proteins (e.g., ILT3, ILT5, or LILRB5). In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent does not bind one or more of the human LILRA proteins (e.g., LILRA1, LILRA2, LILRA4, LILRA5, or LILRA6). In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent does not bind LILRA2, LILRA4, LILRA5, or LILRA6. [00166] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent disclosed herein binds human ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds cyno ILT2 and/or rhesus ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds human ILT2, cyno ILT2, and rhesus ILT2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:3. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds a fragment comprising amino acids 24-461 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-115 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 116-221 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 222-312 of SEQ ID NO:1. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 313- 409 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-221 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 116-312 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 222-409 of SEQ ID NO:1. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:4. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:5. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:6. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds SEQ ID NO:7. [00167] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent disclosed herein binds SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:16. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:17. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 24-460 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-114 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 115-220 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds a fragment comprising amino acids 221-311 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 312-408 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-220 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 115-311 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 221-408 of SEQ ID NO:15. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:18. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:19. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:20. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:21. [00168] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent disclosed herein binds SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:167. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:168. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 24-461 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-114 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 115-220 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 221-311 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 312-408 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-220 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 115-311 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 221-408 of SEQ ID NO:166. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:169. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:170. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:171. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:172. [00169] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:3. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:4. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:5. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:6. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:7. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:16. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:17. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:18. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:19. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:20. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:21. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:167. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:168. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:169. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:170. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:171. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:172. [00170] In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent disclosed herein binds an epitope comprising amino acids within SEQ ID NO:2. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:3. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:4. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:5. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:6. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:7. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:16 In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:17. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:18. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:19. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:20. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:21. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:167 In some embodiments, the ILT2-binding agent or the ILT2/ILT4- binding agent binds an epitope comprising amino acids within SEQ ID NO:168. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:169. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:170. In some embodiments, the ILT2-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:171. In some embodiments, the ILT2- binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:172. [00171] In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds ILT4 or a fragment of ILT4. In some embodiments, a fragment of ILT4 comprises the extracellular domain of ILT4. In some embodiments, a fragment of ILT4 comprises one or more of the Ig-like C2 type domains (e.g., D1, D2, D3, and/or D4). In some embodiments, a fragment of ILT4 comprises D1 and D2. In some embodiments, a fragment of ILT4 comprises D2 and D3. In some embodiments, a fragment of ILT4 comprises D3 and D4. In some embodiments, a fragment of ILT4 comprises D1, D2, and D3. In some embodiments, a fragment of ILT4 comprises D2, D3, and D4. In some embodiments, a fragment of ILT4 comprises one or more of the Ig-like C2 type domains and the stem region. In some embodiments, a fragment of ILT4 comprises D4-stem, D3-D4-stem, or D2-D3-D4-stem. In some embodiments, the extracellular domain of human ILT4 comprises amino acids 22-461 of SEQ ID NO:8. In some embodiments, D1 of human ILT4 comprises amino acids 27-110 of SEQ ID NO:8. In some embodiments, D2 of human ILT4 comprises amino acids 111-229 of SEQ ID NO:8. In some embodiments, D3 of human ILT4 comprises amino acids 230-318 of SEQ ID NO:8. In some embodiments, D4 of human ILT4 comprises amino acids 330-419 of SEQ ID NO:8. In some embodiments, D1-D2 of human ILT4 comprises amino acids 27-229 of SEQ ID NO:8. In some embodiments, D2-D3 of human ILT4 comprises amino acids 111-318 of SEQ ID NO:8. In some embodiments, D3- D4 of human ILT4 comprises amino acids 230-419 of SEQ ID NO:8. In some embodiments, D1-D2-D3 of human ILT4 comprises amino acids 27-318 of SEQ ID NO:8. In some embodiments, D2-D3-D4 of human ILT4 comprises amino acids 111-419 of SEQ ID NO:8. In some embodiments, D4-stem of human ILT4 comprises amino acids 330-461 of SEQ ID NO:8. In some embodiments, D3-D4-stem of human ILT4 comprises amino acids 230-461 of SEQ ID NO:8. In some embodiments, D2-D3-D4-stem of human ILT4 comprises amino acids 111-461 of SEQ ID NO:8. [00172] In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within a specific region of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the extracellular domain of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D1 domain of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D2 domain of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D3 domain of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D4 domain of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D4-stem region of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds within the D1-D2 domains of ILT4. In some embodiments, the ILT4- binding agent or the ILT2/ILT4-binding agent binds within the D2-D3 domains of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds within the D3-D4 domains of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds within the D1-D2-D3 domains of ILT4. In some embodiments, the ILT4- binding agent or the ILT2/ILT4-binding agent binds within the D2-D3-D4 domains of ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds an epitope on ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a conformational epitope on ILT4. In some embodiments, the ILT4-binding agent does not bind other human LILRB proteins (e.g., ILT2, ILT3, ILT5, or LILRB5). In some embodiments, the ILT2/ILT4-binding agent does not bind other human LILRB proteins (e.g., ILT3, ILT5, or LILRB5). In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent does not bind one or more of the human LILRA proteins (e.g., LILRA1, LILRA2, LILRA4, LILRA5, or LILRA6). In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent does not bind LILRA2, LILRA4, LILRA5, or LILRA6. [00173] In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds human ILT4. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:9. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds SEQ ID NO:10. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 22-461 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-110 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 111-229 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 230-318 of SEQ ID NO:8. In some embodiments, the ILT4- binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 330- 419 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 27-229 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 111-318 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a fragment comprising amino acids 230-419 of SEQ ID NO:8. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:11. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:12. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:13. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds SEQ ID NO:14. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:11 and SEQ ID NO:12. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:12 and SEQ ID NO:13. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:13 and SEQ ID NO:14. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds SEQ ID NO:11, SEQ ID NO:12, and SEQ ID NO:13. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds SEQ ID NO:12, SEQ ID NO:13, and SEQ ID NO:14. [00174] In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:9. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:10. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:11. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:12. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:13. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds a polypeptide comprising the amino acid sequence of SEQ ID NO:14. [00175] In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:9. In some embodiments, the ILT4- binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:10. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:11. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:12. In some embodiments, the ILT4-binding agent or the ILT2/ILT4- binding agent binds an epitope comprising amino acids within SEQ ID NO:13. In some embodiments, the ILT4-binding agent or the ILT2/ILT4-binding agent binds an epitope comprising amino acids within SEQ ID NO:14. [00176] In some embodiments, the ILT-binding agent binds human ILT2, human ILT4, or both human ILT2/ILT4, and has at least one or more of the following properties: (i) binding rhesus ILT2; (ii) binding cyno ILT2; (iii) not binding ILT3, ILT5, and LILRB5; (iv) not binding LILRA2, LILRA4, LILRA5, and LILRA6; (v) being an ILT2 antagonist; (vi) being an ILT4 antagonist, (vii) inhibiting ILT2 activity; (viii) inhibiting ILT4 activity; (ix) inhibiting ILT2 signaling in cells that express ILT2; (x) inhibiting ILT4 signaling in cells that express ILT4; (xi) inhibiting binding of ILT2 to MHC I molecules; (xii) inhibiting binding of ILT4 to MHC I molecules; (xiii) inhibiting ILT2-induced suppression of myeloid cells; (xiv) inhibiting ILT4- induced suppression of myeloid cells; (xv) inhibiting ILT2-induced suppression of myeloid cell activity; (xvi) inhibiting ILT4-induced suppression of myeloid cell activity; (xvii) restoring FcR activation in myeloid cells; (xviii) enhancing NK cell activity; (xix) enhancing CTL activity; and/or (xx) enhancing macrophage phagocytosis. [00177] In some embodiments, the ILT-binding agent is an antibody. In some embodiments, the ILT2-binding agent is an antibody. In some embodiments, the ILT4-binding agent is an antibody. In some embodiments, the ILT2/ILT4-binding agent is an antibody. In some embodiments, the ILT-binding agent is an anti-ILT2 antibody. In some embodiments, the ILT- binding agent is an anti-ILT4 antibody. In some embodiments, the ILT-binding agent is an anti- ILT2/ILT4 antibody. In some embodiments, the antibody is a recombinant antibody. In some embodiments, the antibody is a monoclonal antibody. In some embodiments, the antibody is a chimeric antibody. In some embodiments, the antibody is a humanized antibody. In some embodiments, the antibody is a human antibody. In some embodiments, the antibody is an IgG antibody. In some embodiments, the antibody is an IgG1 antibody. In some embodiments, the antibody is an IgG2 antibody. In some embodiments, the antibody is an IgG3 antibody. In some embodiments, the antibody is an IgG4 antibody. In some embodiments, the antibody comprises an IgG heavy chain. In some embodiments, the antibody comprises an IgG1 heavy chain. In some embodiments, the antibody comprises an IgG2 heavy chain. In some embodiments, the antibody comprises an IgG4 heavy chain. In some embodiments, the antibody comprises a human IgG heavy chain. In some embodiments, the antibody comprises a human IgG1 heavy chain. In some embodiments, the antibody comprises a human IgG2 heavy chain. In some embodiments, the antibody comprises a human IgG4 heavy chain. In some embodiments, the antibody comprises a kappa light chain. In some embodiments, the antibody comprises a kappa light chain constant region. In some embodiments, the antibody comprises a human kappa light chain constant region. In some embodiments, the antibody comprises a lambda light chain. In some embodiments, the antibody comprises a lambda light chain constant region. In some embodiments, the antibody comprises a human lambda light chain constant region. In some embodiments, the antibody is an antibody fragment comprising at least one antigen-binding site. In some embodiments, the antibody is a scFv. In some embodiments, the antibody is a disulfide-linked scFv. In some embodiments, the antibody is a disulfide-linked sc(Fv) ₂ . In some embodiments, the antibody is a Fab, Fab′, or a F(ab) ₂ antibody. In some embodiments, the antibody is a diabody. In some embodiments, the antibody is a nanobody. In some embodiments, the antibody is a monospecific antibody. In some embodiments, the antibody is a bispecific antibody. In some embodiments, the antibody is a multispecific antibody. In some embodiments, the antibody is a monovalent antibody. In some embodiments, the antibody is a bivalent antibody. In some embodiments, the antibody is a tetravalent antibody. [00178] In some embodiments, the antibody is isolated. In some embodiments, the antibody is substantially pure. [00179] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) disclosed herein is a polyclonal antibody. Polyclonal antibodies can be prepared by any method known to those of skill in the art. In some embodiments, polyclonal antibodies are produced by immunizing an animal (e.g., a rabbit, rat, mouse, goat, donkey) with an antigen of interest (e.g., a purified peptide fragment, a recombinant protein, or a fusion protein) using multiple subcutaneous or intraperitoneal injections. In some embodiments, the antigen is conjugated to a carrier such as keyhole limpet hemocyanin (KLH), serum albumin, bovine thyroglobulin, or soybean trypsin inhibitor. The antigen (with or without a carrier protein) is diluted in sterile saline and usually combined with an adjuvant (e.g., Complete or Incomplete Freund's Adjuvant) to form a stable emulsion. After a period of time, polyclonal antibodies are recovered from the immunized animal (e.g., from blood or ascites). In some embodiments, the polyclonal antibodies are purified from serum or ascites according to standard methods in the art including, but not limited to, affinity chromatography, ion-exchange chromatography, gel electrophoresis, and/or dialysis. [00180] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) is a monoclonal antibody. Monoclonal antibodies can be prepared by any method known to those of skill in the art. In some embodiments, monoclonal antibodies are prepared using hybridoma methods known to one of skill in the art. For example, using a hybridoma method, a mouse, rat, rabbit, hamster, or other appropriate host animal, is immunized as described above. In some embodiments, lymphocytes are immunized in vitro. In some embodiments, the immunizing antigen is a human protein or a fragment thereof. In some embodiments, the immunizing antigen is a mouse protein or a fragment thereof. In some embodiments, the immunizing antigen is a rhesus protein or a fragment thereof. In some embodiments, the immunizing antigen is a cyno protein or a fragment thereof. In some embodiments, the immunizing antigen is a combination of two or more (e.g., 2, 3, 4) related proteins or fragments thereof. [00181] Following immunization, lymphocytes are isolated and fused with a suitable myeloma cell line using, for example, polyethylene glycol. The hybridoma cells are selected using specialized media as known in the art and unfused lymphocytes and myeloma cells do not survive the selection process. Hybridomas that produce monoclonal antibodies against a chosen antigen can be identified by a variety of methods including, but not limited to, immunoprecipitation, immunoblotting, and in vitro binding assays (e.g., flow cytometry, FACS, ELISA, SPR (e.g., Biacore), and radioimmunoassay). Once hybridoma cells that produce antibodies of the desired specificity, affinity, and/or activity are identified, the clones may be subcloned by limiting dilution techniques. In some embodiments, high-throughput methods are used to distribute single cell hybridoma cells into plates. The hybridomas can be propagated either in in vitro culture using standard methods or in vivo as ascites tumors in an animal. The monoclonal antibodies can be purified from the culture medium or ascites fluid according to standard methods in the art including, but not limited to, affinity chromatography, ion-exchange chromatography, gel electrophoresis, and dialysis. [00182] In some embodiments, monoclonal antibodies are made using recombinant DNA techniques as known to one skilled in the art. For example, the polynucleotides encoding an antibody are isolated from mature B-cells or hybridoma cells, such as by RT-PCR using oligonucleotide primers that specifically amplify the genes encoding the heavy and light chains of the antibody, and their sequence is determined using standard techniques. The isolated polynucleotides encoding the heavy and light chains are then cloned into suitable expression vectors which produce the monoclonal antibodies when transfected into host cells such as E. coli, simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin proteins. [00183] In some embodiments, recombinant monoclonal antibodies are isolated from phage display libraries expressing variable domains or CDRs of a desired species. Screening of phage libraries can be accomplished by various techniques known in the art. [00184] In some embodiments, a monoclonal antibody is modified by using recombinant DNA technology to generate alternative antibodies. In some embodiments, the constant domains of the light chain and heavy chain of a mouse monoclonal antibody are substituted for constant regions of a human antibody to generate a chimeric antibody. In some embodiments, the constant regions are truncated or removed to generate a desired antibody fragment of a monoclonal antibody. In some embodiments, site-directed or high-density mutagenesis of the variable region(s) is used to optimize specificity and affinity of a monoclonal antibody. [00185] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) is a humanized antibody. Various methods for generating humanized antibodies are known in the art. In some embodiments, a humanized antibody comprises one or more amino acid residues that have been introduced into it from a source that is non-human. In some embodiments, humanization is performed by substituting one or more non-human CDR sequences for the corresponding CDR sequences of a human antibody. In some embodiments, the humanized antibodies are constructed by substituting all six CDRs of a non-human antibody (e.g., a mouse antibody) for the corresponding CDRs of a human antibody. [00186] The choice of which human heavy chain variable region and/or light chain variable region to use for generating humanized antibodies can be made based on a variety of factors and by a variety of methods known in the art. In some embodiments, the “best-fit” method is used where the sequence of the variable region of a non-human (e.g., rodent) antibody is screened against the entire library of known human variable region sequences. The human sequence that is most similar to that of the non-human (e.g., rodent) sequence is selected as the human variable region framework for the humanized antibody. In some embodiments, a particular variable region framework derived from a consensus sequence of all human antibodies of a particular subgroup of light or heavy chains is selected as the variable region framework. In some embodiments, the variable region framework sequence is derived from the consensus sequences of the most abundant human subclasses. In some embodiments, human germline genes are used as the source of the variable region framework sequences. [00187] Other methods for humanization include, but are not limited to, a method called “superhumanization” which is described as the direct transfer of CDRs to a human germline framework, a method termed Human String Content (HSC) which is based on a metric of “antibody humanness”, methods based on generation of large libraries of humanized variants (including phage, ribosomal, and yeast display libraries), and methods based on framework region shuffling. [00188] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) is a human antibody. Human antibodies can be prepared using various techniques known in the art. In some embodiments, human antibodies are generated from immortalized human B lymphocytes immunized in vitro. In some embodiments, human antibodies are generated from lymphocytes isolated from an immunized individual. In any case, cells that produce an antibody directed against a target antigen can be generated and isolated. In some embodiments, a human antibody is selected from a phage library, where that phage library expresses human antibodies. Alternatively, phage display technology may be used to produce human antibodies and antibody fragments in vitro, from immunoglobulin variable region gene repertoires from unimmunized human donors. Techniques for the generation and use of antibody phage libraries are well known in the art. Once antibodies are identified, affinity maturation strategies known in the art, including but not limited to, chain shuffling and site-directed mutagenesis, may be employed to generate higher affinity human antibodies. In some embodiments, human antibodies are produced in transgenic mice that contain human immunoglobulin loci. Upon immunization these mice are capable of producing the full repertoire of human antibodies in the absence of endogenous immunoglobulin production. [00189] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) is an antibody fragment. As used herein, the term “antibody fragment” refers to a molecule other than an intact antibody that comprises a portion of an antibody and generally at least one antigen-binding site. Examples of antibody fragments include, but are not limited to, Fab, Fab′, F(ab′)2, Fv, single chain antibody molecules (e.g., scFv), disulfide-linked scFv (dsscFv), nanobodies, diabodies, tribodies, tetrabodies, minibodies, dual variable domain antibodies (DVD), single variable domain antibodies (e.g., camelid antibodies), and multispecific antibodies formed from antibody fragments. [00190] In some embodiments, the ILT-binding agent is a scFv antibody. In some embodiments, the scFv is a disulfide-linked scFv (dsscFv), which is a scFv comprising an engineered disulfide bond between the light chain variable region and heavy chain variable region of the scFv. In some embodiments, the disulfide bond increases stability of the scFv molecule. In some embodiments, the disulfide bond increases thermostability of the scFv molecule. [00191] In some embodiments, the ILT-binding agent is a Fv. In some embodiments, the ILT- binding agent is a Fab. In some embodiments, the ILT-binding agent is a F(ab′)2. In some embodiments, the ILT-binding agent is a F(ab′). [00192] Antibody fragments can be made by various techniques, including but not limited to proteolytic digestion of an intact antibody. The antibody fragments described herein can be produced using recombinant technologies known in the art (e.g., E.coli or phage expression). [00193] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) is a bispecific antibody. Bispecific antibodies are capable of recognizing and binding at least two different antigens or epitopes. The different epitopes can either be within the same molecule (e.g., two epitopes on ILT2) or on different molecules (e.g., one epitope on ILT2 and a second epitope on a different target). In some embodiments, a bispecific antibody has enhanced potency as compared to an individual antibody or to a combination of more than one antibody. In some embodiments, a bispecific antibody has reduced toxicity as compared to an individual antibody or to a combination of more than one antibody. It is known to those of skill in the art that any therapeutic agent may have unique pharmacokinetics (PK) (e.g., circulating half-life). In some embodiments, a bispecific antibody has the ability to synchronize the PK of two active binding agents wherein the two individual binding agents have different PK profiles. In some embodiments, a bispecific antibody has the ability to concentrate the actions of two agents in a common area (e.g., tissue) in a subject. In some embodiments, a bispecific antibody has the ability to concentrate the actions of two agents to a common target (e.g., a specific cell type). In some embodiments, a bispecific antibody has the ability to target the actions of two agents to more than one biological pathway or function. In some embodiments, a bispecific antibody has the ability to target two different cells and bring them closer together. [00194] In some embodiments, a bispecific antibody has decreased toxicity and/or side effects. In some embodiments, a bispecific antibody has decreased toxicity and/or side effects as compared to a mixture of the two individual antibodies or the antibodies as single agents. In some embodiments, a bispecific antibody has an increased therapeutic index. In some embodiments, a bispecific antibody has an increased therapeutic index as compared to a mixture of the two individual antibodies or the antibodies as single agents. [00195] Many techniques for making bispecific antibodies are known to those skilled in the art. In some embodiments, a bispecific antibody comprises heavy chain constant regions with modifications in the amino acids that are part of the interface between the two heavy chains. These modifications are made to enhance heterodimer formation and generally reduce or eliminate homodimer formation. In some embodiments, the bispecific antibody is generated using a knobs-into-holes (KIH) strategy. In some embodiments, the bispecific antibody comprises variant hinge regions incapable of forming disulfide linkages between identical heavy chains (e.g., reduce homodimer formation). In some embodiments, the bispecific antibody comprises heavy chains with changes in amino acids that result in altered electrostatic interactions. In some embodiments, the bispecific antibodies comprise heavy chains with changes in amino acids that result in altered hydrophobic/hydrophilic interactions. [00196] Bispecific antibodies can be intact antibodies or antibody fragments comprising antigen-binding sites. [00197] In some embodiments, the ILT-binding agent is an antibody that binds ILT2. In some embodiments, the anti-ILT antibody binds human ILT2. In some embodiments, the anti-ILT antibody binds cyno ILT2. In some embodiments, the anti-ILT antibody binds rhesus ILT2. In some embodiments, the anti-ILT antibody binds human ILT2 and cyno ILT2. In some embodiments, the anti-ILT antibody binds human ILT2 and rhesus ILT2. In some embodiments, the anti-ILT antibody binds human ILT2, rhesus ILT2, and cyno ILT2. In some embodiments, the anti-ILT2 antibody binds an ILT2 epitope. In some embodiments, the anti- ILT2 antibody binds an ILT2 epitope within the extracellular domain of human ILT2. In some embodiments, an anti-ILT2 antibody binds an ILT2 epitope within the extracellular domain of cyno ILT2. In some embodiments, the anti-ILT2 antibody binds an ILT2 epitope within the extracellular domain of rhesus ILT2. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 24- 461 of SEQ ID NO:1. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 27-115 of SEQ ID NO:1. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 116-221 of SEQ ID NO:1. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 222-312 of SEQ ID NO:1. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 313-409 of SEQ ID NO:1. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:3. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:4. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:5. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:6. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:7. In some embodiments, the anti- ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 24-460 of SEQ ID NO:15. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 27-114 of SEQ ID NO:15. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 115-220 of SEQ ID NO:15. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 221-311 of SEQ ID NO:15. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 312-408 of SEQ ID NO:15. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:17. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:18. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:19. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:20. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:21. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 24-461 of SEQ ID NO:166. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 27-114 of SEQ ID NO:166. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 115-220 of SEQ ID NO:166. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 221-311 of SEQ ID NO:166. In some embodiments, the anti-ILT2 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 312-408 of SEQ ID NO:166. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:168. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:169. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:170. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:171. In some embodiments, the anti-ILT2 antibody binds an epitope comprising amino acids within SEQ ID NO:172. In some embodiments, the epitope is a conformational epitope. In some embodiments, the epitope is a linear epitope. [00198] In some embodiments, the ILT-binding agent is an antibody that binds ILT4. In some embodiments, the anti-ILT antibody binds human ILT4. In some embodiments, the anti-ILT4 antibody binds an ILT4 epitope. In some embodiments, the anti-ILT4 antibody binds an ILT4 epitope within the extracellular domain of human ILT4. In some embodiments, the anti-ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 22-461 of SEQ ID NO:8. In some embodiments, the anti-ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 27- 110 of SEQ ID NO:8. In some embodiments, the anti-ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 111-229 of SEQ ID NO:8. In some embodiments, the anti-ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 230-318 of SEQ ID NO:8. In some embodiments, the anti-ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 330-419 of SEQ ID NO:8. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:9. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:10. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:11. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:12. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:13. In some embodiments, the anti-ILT4 antibody binds an epitope comprising amino acids within SEQ ID NO:14. In some embodiments, the epitope is a conformational epitope. In some embodiments, the epitope is a linear epitope. [00199] In some embodiments, the ILT-binding agent is an antibody that binds ILT2 and ILT4. It is understood by those of skill in the art that an antibody that binds ILT2 and ILT4, described as a dual binder, comprises at least one antigen-binding site that binds an epitope on both ILT2 and ILT4, in contrast to a bispecific antibody which would comprise one antigen-binding site that binds an epitope on ILT2 and a second antigen-binding site that binds a different epitope on ILT4. In some embodiments, the anti-ILT2/ILT4 antibody binds human ILT2 and human ILT4. In some embodiments, anti-ILT2/ILT4 antibody binds human ILT2, human ILT4, cyno ILT2, and rhesus ILT2. In some embodiments, the anti-ILT2/ILT4 antibody binds an ILT2 epitope and ILT4 epitope. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope within the extracellular domain of human ILT2 and an epitope within the extracellular domain of human ILT4, wherein the ILT2 epitope and the ILT4 epitope are the same or essentially the same. In some embodiments, the anti-ILT2/ILT4 antibody binds an ILT2 epitope within the extracellular domain of human ILT2, an ILT4 epitope within the extracellular domain of human ILT4, an ILT2 epitope within the extracellular domain of cyno ILT2, and an ILT2 epitope within the extracellular domain of rhesus ILT2. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 24-461 of SEQ ID NO:1 and the same or essentially the same epitope within amino acids 22-461 of SEQ ID NO:8. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 27-115 of SEQ ID NO:1 and the same or essentially the same epitope within amino acids 27-110 of SEQ ID NO:8. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 116-221 of SEQ ID NO:1 and the same or essentially the same epitope within amino acids 111-229 of SEQ ID NO:8. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 222-312 of SEQ ID NO:1 and the same or essentially the same epitope within amino acids 230-318 of SEQ ID NO:8. In some embodiments, the anti-ILT2/ILT4 antibody binds an epitope comprising at least one amino acid (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9) within amino acids 313-409 of SEQ ID NO:1 and the same or essentially the same epitope within amino acids 330-419 of SEQ ID NO:8. In some embodiments, the epitope is a conformational epitope. In some embodiments, the epitope is a linear epitope. [00200] In some embodiments, the ILT-binding agent is an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti-ILT2/ILT4 antibody described herein. In some embodiments, the ILT- binding agent is a variant of an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti-ILT2/ILT4 antibody described herein. In some embodiments, a variant of an anti-ILT antibody comprises one to thirty amino acid substitutions. In some embodiments, a variant of the anti-ILT antibody comprises one to twenty-five amino acid substitutions. In some embodiments, a variant of the anti-ILT antibody comprises one to twenty amino acid substitutions. In some embodiments, a variant of the anti-ILT antibody comprises one to fifteen amino acid substitutions. In some embodiments, a variant of the anti-ILT antibody comprises one to ten amino acid substitutions. In some embodiments, a variant of the anti-ILT antibody comprises one to five amino acid substitutions. In some embodiments, the variant of the anti-ILT antibody comprises one to three amino acid substitutions. In some embodiments, the amino acid substitution(s) is in a CDR of the antibody. In some embodiments, the amino acid substitution(s) is not in a CDR of the antibody. In some embodiments, the amino acid substitution(s) is in a framework region of the antibody. In some embodiments, the amino acid substitution(s) is a conservative amino acid substitution. [00201] CDRs of an antibody are defined using a variety of methods/systems by those skilled in the art. These systems and/or definitions have been developed and refined over a number of years and include Kabat, Chothia, IMGT, AbM, and Contact. The Kabat definition is based on sequence variability and is commonly used. The Chothia definition is based on the location of the structural loop regions. The IMGT system is based on sequence variability and location within the structure of the variable domain. The AbM definition is a compromise between Kabat and Chothia. The Contact definition is based on analyses of the available antibody crystal structures. An Exemplary system is a combination of Kabat and Chothia. Software programs (e.g., abYsis) are available and known to those of skill in the art for analysis of antibody sequence and determination of CDRs. [00202] The specific CDR sequences defined herein are generally based on a combination of Kabat and Chothia definitions (Exemplary definition). However, it will be understood that reference to a heavy chain variable region CDR or CDRs and/or a light chain variable region CDR or CDRs of a specific antibody will encompass all CDR definitions as known to those of skill in the art. [00203] In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the Kabat definition. In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the Chothia definition. In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the AbM definition. In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the IMGT definition. In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the Contact definition. In some embodiments, the anti-ILT antibody described herein comprises the six CDRs of antibody 27F9, 47C8, 48A5, 47H6, Hz47H6.v2, 51A1, 64A12, Hz64A12, 73C4, 73D1, or Hz73D1.v1 based on the Exemplary definition. [00204] In some embodiments, the ILT-binding agent is an anti-ILT antibody (e.g., an anti- ILT2 antibody, an anti-ILT4 antibody, or an anti-ILT2/ILT4 antibody) that comprises one, two, three, four, five, and/or six CDRs of any one of the antibodies described herein. In some embodiments, the anti-ILT2 antibody comprises (i) a heavy chain variable region (VH) comprising one, two, and/or three heavy chain variable region CDRs (VH-CDRs) from Table 1, and/or (ii) a light chain variable region (VL) comprising one, two, and/or three light chain variable region CDRs (VL-CDRs) from Table 1. In some embodiments, the anti-ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 2, and/or (ii) a light chain variable region comprising one, two, and/or three VL-CDRs from Table 2. In some embodiments, the anti-ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH- CDRs from Table 3, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 3. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 4A or Table 4B, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 4A or Table 4B. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 5, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 5. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 6A or Table 6B, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 6A or Table 6B. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 7, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 7. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising one, two, and/or three VH-CDRs from Table 8A or Table 8B, and/or (ii) a VL comprising one, two, and/or three VL-CDRs from Table 8A or Table 8B. In some embodiments, the anti-ILT2 antibody comprises (i) a VH comprising three VH-CDRs from Table 1, and (ii) a VL comprising three VL-CDRs from Table 1. In some embodiments, the anti-ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 2, and (ii) a VL comprising three VL-CDRs from Table 2. In some embodiments, the anti-ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 3, and (ii) a VL comprising three VL-CDRs from Table 3. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 4A, and (ii) a VL comprising three VL-CDRs from Table 4A. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 4B, and (ii) a VL comprising three VL-CDRs from Table 4B. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH- CDRs from Table 5, and (ii) a VL comprising three VL-CDRs from Table 5. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 6A, and (ii) a VL comprising three VL-CDRs from Table 6A. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 6B, and (ii) a VL comprising three VL-CDRs from Table 6B. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 7, and (ii) a VL comprising three VL-CDRs from Table 7. In some embodiments, the anti-ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 8A, and (ii) a VL comprising three VL-CDRs from Table 8B. In some embodiments, the anti- ILT2/ILT4 antibody comprises (i) a VH comprising three VH-CDRs from Table 8B, and (ii) a VL comprising three VL-CDRs from Table 8B.

Table 1: Anti-ILT2 Antibody 27F9 Sequences

Table 2: Anti-ILT4 Antibody 47C8 Sequences

Table 3: Anti-ILT4 Antibody 48A5 Sequences

Table 4A: Anti-ILT2/ILT4 Antibody 47H6 Sequences

Table 4B: Anti-ILT2/ILT4 Antibody Hz47H6.v2 Sequences

Table 5: Anti-ILT2/ILT4 Antibody 51A1 Sequences Table 6A: Anti-ILT2/ILT4 Antibody 64A12 Sequences

Table 6B: Anti-ILT2/ILT4 Antibody Hz64A12 Sequences Table 7: Anti-ILT2/ILT4 Antibody 73C4 Sequences

Table 8B: Anti-ILT2/ILT4 Antibody Hz73D1.v1 Sequences

[00205] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) comprises a VH-CDR1, a VH-CDR2, and a VH- CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from an antibody described herein. In some embodiments, the ILT-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH- CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from an antibody described herein. In some embodiments, the ILT-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH- CDR2, and a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from an antibody described herein. [00206] In some embodiments, the ILT-binding agent (e.g., the anti-ILT2 antibody, the anti- ILT4 antibody, or the anti-ILT2/ILT4 antibody) comprises one or more (e.g., 1, 2, 3, 4, etc.) amino acid substitutions in a CDR of an antibody described herein. In some embodiments, the amino acid substitutions are conservative substitutions. In some embodiments, a CDR comprises one amino acid substitution. In some embodiments, a CDR comprises two amino acid substitutions. In some embodiments, a CDR comprises three amino acid substitutions. In some embodiments, a CDR comprises four amino acid substitutions. In some embodiments, the CDR is a VH-CDR1. In some embodiments, the CDR is a VH-CDR2. In some embodiment, the CDR is a VH-CDR3. In some embodiments, the CDR is a VL-CDR1. In some embodiments, the CDR is a VL-CDR2. In some embodiments, the CDR is a VL-CDR3. In some embodiments, the substitutions are made as part of a humanization process. In some embodiments, the substitutions are made as part of a germline humanization process. In some embodiments, the substitutions are made as part of an affinity maturation process. In some embodiments, the substitutions are made as part of an optimization process. [00207] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) comprises one or more VH-CDRs or VL-CDRs that have been modified to reduce deamidation within the CDR sequence. Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine (Asn or N) or glutamine (Gln or Q) is removed or converted to another functional group. Generally, asparagine is converted to aspartic acid or isoaspartic acid and glutamine is converted to glutamic acid or polyglutamic acid. In some situations, deamidation may change the structure, function, and/or stability of a polypeptide, potentially resulting in decreased biological activity. In some embodiments, the VH-CDR1, VH-CDR2, and/or VH-CDR3 of an antibody described herein is modified to reduce deamidation. In some embodiments, the VL- CDR1, VL-CDR2, and/or VL-CDR3 of an antibody described herein is modified to reduce deamidation. [00208] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) comprises one or more VH-CDRs or VL-CDRs that have been modified to reduce isomerization. Isomerization is a chemical process by which a compound is transformed into any of its isomeric forms, i.e., forms with the same chemical composition but with different structure or configuration and, potentially with different physical and chemical properties. Studies have shown that asparatate (Asp or D) isomerization within a CDR can impact antibody binding and/or stability. In some embodiments, the VH-CDR1, VH- CDR2, and/or VH-CDR3 of an antibody described herein is modified to reduce isomerization. In some embodiments, the VL-CDR1, VL-CDR2, and/or VL-CDR3 is modified to reduce isomerization. [00209] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4 binding agent) comprises one or more VH-CDRs or VL-CDRs that have been modified to reduce oxidation. Oxidation is a chemical process by which an oxygen is added to an atom, for example, methionine is converted to methionine sulfoxide by addition of an oxygen to the sulfur atom. Oxidation of one or more amino acids can potentially affect the physical and chemical properties of a protein. Studies have shown that oxidation of methionine (Met or M) within a CDR has the potential to impact antibody binding and/or stability. In some embodiments, the VH-CDR1, VH-CDR2, and/or VH-CDR3 of an antibody described herein is modified to reduce oxidation (e.g., methionine oxidation). In some embodiments, the VL-CDR1, VL-CDR2, and/or VL-CDR3 of an antibody described herein is modified to reduce oxidation (e.g., methionine oxidation). [00210] In some embodiments, the ILT2-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 27F9, a humanized version thereof, or variants thereof. In some embodiments, the ILT2-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from antibody 27F9. In other embodiments, the ILT2-binding agent comprises a VL comprising a VL-CDR1, a VL- CDR2, and a VL-CDR3 from antibody 27F9 In some embodiments, the ILT2-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 27F9. In some embodiments, the ILT2-binding agent is a humanized version of antibody 27F9. In some embodiments, the ILT2-binding agent is a variant of antibody 27F9 or humanized 27F9. [00211] In some embodiments, the ILT2-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH- CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GFSLTNY (SEQ ID NO:28), a VH-CDR2 comprising the amino acid sequence WGDGS (SEQ ID NO:29), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTN (SEQ ID NO:30), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence NYGVS (SEQ ID NO:31), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TNYGVS (SEQ ID NO:32), a VH-CDR2 comprising the amino acid sequence WLGIIWGDGSTN (SEQ ID NO:33), and a VH-CDR3 comprising the amino acid sequence AKPNWDTYAMD (SEQ ID NO:34), and a VL comprising a VL-CDR1 comprising the amino acid sequence SNFLNWY (SEQ ID NO:35), a VL-CDR2 comprising the amino acid sequence LLIYCTSKLH (SEQ ID NO:36), and a VL-CDR3 comprising the amino acid sequence QQGNTLPP (SEQ ID NO:37). [00212] In some embodiments, the ILT2-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH- CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27). In some embodiments, the ILT2-binding agent comprises a VH comprising VH-CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24). In some embodiments, the ILT2-binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27). In some embodiments, the ILT2-binding agent comprises: (a) a VH comprising VH-CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27). [00213] In some embodiments, the anti-ILT2 binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 27F9 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:125 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 27F9 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:126. [00214] In some embodiments, the ILT2-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:125. In some embodiments, the ILT2-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:126. In some embodiments, the ILT2-binding agent comprises a VH comprising an amino acid sequence of SEQ ID NO:125. In some embodiments, the ILT2-binding agent comprises a VL comprising an amino acid sequence of SEQ ID NO:126. [00215] In some embodiments, the ILT2-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:125 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:126. In some embodiments, the ILT2-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:125 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:126. In some embodiments, the ILT2-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:125 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:126. In some embodiments, the ILT2-binding agent comprises a VH comprising an amino acid sequence of SEQ ID NO:125 and a VL comprising an amino acid sequence of SEQ ID NO:126. [00216] In some embodiments, the ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47C8, a humanized version thereof, or variants thereof. In some embodiments, the ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from antibody 47C8. In other embodiments, the ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL- CDR2, and a VL-CDR3 from antibody 47C8 In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47C8. In some embodiments, the ILT4-binding agent is a humanized version of antibody 47C8. In some embodiments, the ILT4-binding agent is a variant of antibody 47C8 or humanized 47C8. [00217] In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH- CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GYSFTGY (SEQ ID NO:44), a VH-CDR2 comprising the amino acid sequence YPNNGD (SEQ ID NO:45), and a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH- CDR2 comprising the amino acid sequence RVYPNNGDTS (SEQ ID NO:46), and a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence GYYMH (SEQ ID NO:47), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH- CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TGYYMH (SEQ ID NO:48), a VH-CDR2 comprising the amino acid sequence WIGRVYPNNGDTS (SEQ ID NO:49), and a VH-CDR3 comprising the amino acid sequence ARGATVVESLFA (SEQ ID NO:50), and a VL comprising a VL-CDR1 comprising the amino acid sequence DNYGNNFLHWY (SEQ ID NO:51), a VL-CDR2 comprising the amino acid sequence LLIYRTSNLE (SEQ ID NO:52), and a VL-CDR3 comprising the amino acid sequence QQSNEDPY (SEQ ID NO:53). [00218] In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH- CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43). In some embodiments, the ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40). In some embodiments, the ILT4- binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43). In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43). [00219] In some embodiments, the anti-ILT4 binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 47C8 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:127 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 47C8 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:128. [00220] In some embodiments, the ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:127. In some embodiments, the ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:128. In some embodiments, the ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:127. In some embodiments, the ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:128. [00221] In some embodiments, the ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:127 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:128. In some embodiments, the ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:127 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:128. In some embodiments, the ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:127 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:128. In some embodiments, the ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:127 and a VL comprising the amino acid sequence of SEQ ID NO:128. [00222] In some embodiments, the ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 48A5, a humanized version thereof, or variants thereof. In some embodiments, the ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from antibody 48A5. In other embodiments, the ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL- CDR2, and a VL-CDR3 from antibody 48A5 In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 48A5. In some embodiments, the ILT4-binding agent is a humanized version of antibody 48A5. In some embodiments, the ILT4-binding agent is a variant of antibody 48A5 or humanized 48A5. [00223] In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH- CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTNY (SEQ ID NO:60), a VH-CDR2 comprising the amino acid sequence NTYIGE (SEQ ID NO:61), and a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL- CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH- CDR2 comprising the amino acid sequence WINTYIGEPI (SEQ ID NO:62), and a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL- CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence NYGMN (SEQ ID NO:63), a VH- CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TNYGMN (SEQ ID NO:64), a VH-CDR2 comprising the amino acid sequence WMGWINTYIGEPI (SEQ ID NO:65), and a VH-CDR3 comprising the amino acid sequence ARRSDYDGYAMD (SEQ ID NO:66), and a VL comprising a VL-CDR1 comprising the amino acid sequence LYSGNQKNYLAWY (SEQ ID NO:67), a VL-CDR2 comprising the amino acid sequence LLIYWASTRE (SEQ ID NO:68), and a VL-CDR3 comprising the amino acid sequence QQHDSYP (SEQ ID NO:69). [00224] In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH- CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH- CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59). In some embodiments, the ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH- CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56). In some embodiments, the ILT4-binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59). In some embodiments, the ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59). [00225] In some embodiments, the anti-ILT4 binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 48A5 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:129 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 48A5 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:130. [00226] In some embodiments, the ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:129. In some embodiments, the ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:130. In some embodiments, the ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:129. In some embodiments, the ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:130. [00227] In some embodiments, the ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:129 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:130. In some embodiments, the ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:129 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:130. In some embodiments, the ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:129 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:130. In some embodiments, the ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:129 and a VL comprising the amino acid sequence of SEQ ID NO:130. [00228] In some embodiments, the ILT2/ILT4-binding agent (e.g., a dual binder) comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47H6, a humanized version thereof (e.g., Hz47H6.v2), or variants thereof. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from antibody 47H6 or antibody Hz47H6.v2. In other embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL- CDR2, and a VL-CDR3 from antibody 47H6 or antibody Hz47H6.v2. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH- CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47H6. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody Hz47H6.v2. In some embodiments, the ILT2/ILT4-binding agent is a humanized version of antibody 47H6. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody 47H6. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody Hz47H6.v2. [00229] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH- CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDY (SEQ ID NO:76), a VH-CDR2 comprising the amino acid sequence NPNNGG (SEQ ID NO:77) or the amino acid sequence NPNNAG (SEQ ID NO:119), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTT (SEQ ID NO:78) or the amino acid sequence DFNPNNAGTT (SEQ ID NO:120), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence DYYMN (SEQ ID NO:79), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TDYYMN (SEQ ID NO:80), a VH-CDR2 comprising the amino acid sequence WIGDFNPNNGGTT (SEQ ID NO:81) or the amino acid sequence WIGDFNPNNAGTT (SEQ ID NO:121), and a VH-CDR3 comprising the amino acid sequence ARGRFYYGSLYSFD (SEQ ID NO:82), and a VL comprising a VL-CDR1 comprising the amino acid sequence HNYLAWY (SEQ ID NO:83), a VL-CDR2 comprising the amino acid sequence LLVYNAKTLA (SEQ ID NO:84) or the amino acid sequence LLIYNAKTLA (SEQ ID NO:122), and a VL-CDR3 comprising the amino acid sequence QHFWTSI (SEQ ID NO:85). [00230] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH- CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, the ILT2/ILT4- binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72). In some embodiments, the ILT2/ILT4- binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72). In some embodiments, the ILT2/ILT4- binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). [00231] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 47H6 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:131 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 47H6 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:132. [00232] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:131. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:132. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:131. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:132. [00233] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:131 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:132. In some embodiments, an ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:131 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:132. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:131 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:132. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:131 and a VL comprising the amino acid sequence of SEQ ID NO:132. [00234] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody Hz47H6.v2 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:133 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody Hz47H6.v2 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:134. [00235] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:133. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:134. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:133. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:134. [00236] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:133 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:134. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:133 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:134. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:133 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:134. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:133 and a VL comprising the amino acid sequence of SEQ ID NO:134. [00237] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH-CDR1 comprising GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a light chain comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:148, and wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH- CDR1 comprising GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and a light chain comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75), wherein the heavy chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:148, and wherein the light chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4- binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:148 and (b) a light chain comprising a VL-CDR1 comprising RASGNIHNYLA (SEQ ID NO:73), a VL- CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75), wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:148 and (b) a light chain comprising a VL-CDR1 comprising RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising a VH-CDR1 comprising GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:148, and (b) a light chain comprising the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising a VH-CDR1 comprising GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a light chain comprising the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent is an antibody comprising a heavy chain comprising the amino acid sequence of SEQ ID NO:148 and a light chain comprising the amino acid sequence of SEQ ID NO:149. [00238] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:148. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:148 and a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:148. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:148 and a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:148. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain comprising the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:148 and a light chain comprising the amino acid sequence of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:148 and/or a light chain of SEQ ID NO:149. In some embodiments, the ILT2/ILT4- binding agent is an antibody that comprises a heavy chain of SEQ ID NO:148. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a light chain of SEQ ID NO:149. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:148 and a light chain of SEQ ID NO:149. [00239] In some embodiments, the ILT2/ILT4-binding agent (e.g., a dual binder) comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 51A1, a humanized version thereof, or variants thereof. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH- CDR3 from antibody 51A1. In other embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 51A1. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 51A1. In some embodiments, the ILT2/ILT4-binding agent is a humanized version of antibody 51A1. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody 51A1 or humanized 51A1. [00240] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH- CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTY (SEQ ID NO:92), a VH-CDR2 comprising the amino acid sequence RSKSSNYA (SEQ ID NO:93), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATY (SEQ ID NO:94), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence TYAMH (SEQ ID NO:95), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence NTYAMH (SEQ ID NO:96), a VH-CDR2 comprising the amino acid sequence WVARIRSKSSNYATY (SEQ ID NO:97), and a VH-CDR3 comprising the amino acid sequence VRDGIYYYGTMYYYAMD (SEQ ID NO:98), and a VL comprising a VL-CDR1 comprising the amino acid sequence DYYGNSFMYWY (SEQ ID NO:99), a VL-CDR2 comprising the amino acid sequence LLIYFASNLE (SEQ ID NO:100), and a VL-CDR3 comprising the amino acid sequence QQNNEDPW (SEQ ID NO:101). [00241] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH- CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88). In some embodiments, the ILT2/ILT4- binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). [00242] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 51A1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:135 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 51A1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:136. [00243] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:135. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:136. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:135. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:136. [00244] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:135 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:136. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:135 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:136. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:135 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:136. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:135 and a VL comprising the amino acid sequence of SEQ ID NO:136. [00245] In some embodiments, the ILT2/ILT4-binding agent (e.g., a dual binder) comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 64A12, a humanized version thereof (e.g., Hz64A12), or variants thereof. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from antibody 64A12 or Hz64A12. In other embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL-CDR2, and a VL- CDR3 from antibody 64A12 or Hz64A12. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 64A12 or Hz64A12. In some embodiments, the ILT2/ILT4-binding agent is a humanized version of antibody 64A12. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody 64A12. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody Hz64A12. [00246] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH- CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTY (SEQ ID NO:92), a VH-CDR2 comprising the amino acid sequence RSKSSNYA (SEQ ID NO:93), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATY (SEQ ID NO:94), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence TYAMH (SEQ ID NO:95), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence NTYAMH (SEQ ID NO:96), a VH-CDR2 comprising the amino acid sequence WVARIRSKSSNYATY (SEQ ID NO:97), and a VH-CDR3 comprising the amino acid sequence VRDGIYYYDTMYYYAMD (SEQ ID NO:104), and a VL comprising a VL-CDR1 comprising the amino acid sequence DYYGNSFIYWY (SEQ ID NO:105), a VL-CDR2 comprising the amino acid sequence LLIYFASNLE (SEQ ID NO:100), and a VL-CDR3 comprising the amino acid sequence QQNNEDPW (SEQ ID NO:101). [00247] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH- CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102). In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). [00248] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 64A12 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:137 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL- CDR3 of antibody 64A12 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:138. [00249] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:137. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:138. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:137. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:138. [00250] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:137 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:138. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:137 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:138. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:137 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:138. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:137 and a VL comprising the amino acid sequence of SEQ ID NO:138. [00251] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody Hz64A12 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:139 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL- CDR3 of antibody Hz64A12 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:140. [00252] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:139. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:140. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:139. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:140. [00253] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:139 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:140. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:139 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:140. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:139 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:140. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:139 and a VL comprising the amino acid sequence of SEQ ID NO:140. [00254] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a light chain comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:152, and wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and a light chain comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the heavy chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:152, and wherein the light chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:152 and (b) a light chain comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:152 and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:152, and (b) a light chain comprising the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and (b) a light chain comprising the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent is an antibody comprising a heavy chain comprising the amino acid sequence of SEQ ID NO:152 and a light chain comprising the amino acid sequence of SEQ ID NO:153. [00255] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:152. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:152 and a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:152. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:152 and a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:152. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain comprising the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:152 and a light chain comprising the amino acid sequence of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:152 and/or a light chain of SEQ ID NO:153. In some embodiments, the ILT2/ILT4- binding agent is an antibody that comprises a heavy chain of SEQ ID NO:152. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a light chain of SEQ ID NO:153. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:152 and a light chain of SEQ ID NO:153. [00256] In some embodiments, the ILT2/ILT4-binding agent (e.g., a dual binder) comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73C4, a humanized version thereof, or variants thereof. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH- CDR3 from antibody 73C4. In other embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73C4. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73C4. In some embodiments, the ILT2/ILT4-binding agent is a humanized version of antibody 73C4. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody 73C4 or humanized 73C4. [00257] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH- CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDY (SEQ ID NO:76), a VH-CDR2 comprising the amino acid sequence NPNNGG (SEQ ID NO:77), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTS (SEQ ID NO:108), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence DYYMN (SEQ ID NO:79), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TDYYMN (SEQ ID NO:80), a VH-CDR2 comprising the amino acid sequence WIGNVNPNNGGTS (SEQ ID NO:109), and a VH-CDR3 comprising the amino acid sequence ARREIYFYGTIYYYAMD (SEQ ID NO:110), and a VL comprising a VL-CDR1 comprising the amino acid sequence DYYGNSFMYWY (SEQ ID NO:99), a VL-CDR2 comprising the amino acid sequence LLIYFASNLE (SEQ ID NO:100), and a VL-CDR3 comprising the amino acid sequence QQNNEDPW (SEQ ID NO:101). [00258] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH- CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107). In some embodiments, the ILT2/ILT4- binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). [00259] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 73C4 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:141 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 73C4 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:142. [00260] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:141. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:141. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:142. [00261] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:141 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:141 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:141 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:141 and a VL comprising the amino acid sequence of SEQ ID NO:142. [00262] In some embodiments, the ILT2/ILT4-binding agent (e.g., a dual binder) comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and/or a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73D1, a humanized version thereof (e.g., Hz73D1), or variants thereof. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1, a VH- CDR2, and a VH-CDR3 from antibody 73D1 or antibody Hz73D1.v1. In other embodiments, the ILT2/ILT4-binding agent comprises a VL comprising a VL-CDR1, a VL-CDR2, and a VL- CDR3 from antibody 73D1 or antibody Hz73D1.v1. In some embodiments, the ILT2/ILT4- binding agent comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, a VH-CDR3; and (b) a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73D1 or antibody Hz73D1.v1. In some embodiments, the ILT2/ILT4-binding agent is a humanized version of antibody 73D1. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody 73D1. In some embodiments, the ILT2/ILT4-binding agent is a variant of antibody Hz73D1.v1. [00263] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH- CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (b) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDY (SEQ ID NO:76), a VH-CDR2 comprising the amino acid sequence NPNDGG (SEQ ID NO:113), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (c) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTT (SEQ ID NO:114), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); (d) a VH comprising a VH-CDR1 comprising the amino acid sequence DYYIN (SEQ ID NO:115), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91); or (e) a VH comprising a VH-CDR1 comprising the amino acid sequence TDYYIN (SEQ ID NO:116), a VH-CDR2 comprising the amino acid sequence WIGNVNPNDGGTT (SEQ ID NO:117) or the amino acid sequence WMGNVNPNDGGTT (SEQ ID NO:124), and a VH-CDR3 comprising the amino acid sequence ARREIYFYGTIYYYAMD (SEQ ID NO:110), and a VL comprising a VL-CDR1 comprising the amino acid sequence DYYGNSFMYWY (SEQ ID NO:99), a VL- CDR2 comprising the amino acid sequence LLIYFASNLE (SEQ ID NO:100), and a VL-CDR3 comprising the amino acid sequence QQNNEDPW (SEQ ID NO:101). [00264] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH- CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and/or (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107). In some embodiments, the ILT2/ILT4- binding agent comprises a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). [00265] In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions; a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions; and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions; and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions; a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions; and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), or a variant thereof comprising 1, 2, 3, or 4 amino acid substitutions. [00266] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody 73D1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:143 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody 73D1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:142. [00267] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:143. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:143. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:142. [00268] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:143 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:143 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:143 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:143 and a VL comprising the amino acid sequence of SEQ ID NO:142. [00269] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of VH-CDR1, VH-CDR2, and VH-CDR3 of antibody Hz73D1.v1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:144 and a VL comprising the amino acid sequence of VL-CDR1, VL-CDR2, and VL-CDR3 of antibody Hz73D1.v1 and which has at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:145. [00270] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:144. In some embodiments, the ILT2/ILT4-binding agent comprises a VL having at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO:145. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:144. In some embodiments, the ILT2/ILT4-binding agent comprises a VL comprising the amino acid sequence of SEQ ID NO:145. [00271] In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:144 and a VL having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:145. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:144 and a VL having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:145. In some embodiments, the ILT2/ILT4-binding agent comprises a VH having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:144 and a VL having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:145. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising the amino acid sequence of SEQ ID NO:144 and a VL comprising the amino acid sequence of SEQ ID NO:145. [00272] In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL- CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL- CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the VH comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98% identity to the amino acid sequence of SEQ ID NO:143, and wherein the VL comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98% identity to the amino acid sequence of SEQ ID NO:142. In some embodiments, the ILT2/ILT4-binding agent comprises a VH comprising a VH-CDR1 comprising GYTFTDYYIN (SEQ ID NO:111), a VH- CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the VH comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98% identity to the amino acid sequence of SEQ ID NO:144, and wherein the VL comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98% identity to the amino acid sequence of SEQ ID NO:145. [00273] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH-CDR1 comprising GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH- CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a light chain comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:156, and wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising a VH-CDR1 comprising GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and a light chain comprising a VL- CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL- CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the heavy chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:156, and wherein the light chain comprises at least 95% identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:156 and (b) a light chain comprising a VL-CDR1 comprising RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91), wherein the light chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises (a) a heavy chain comprising the amino acids of SEQ ID NO:156 and (b) a light chain comprising a VL-CDR1 comprising RASESVDYYGNSFMY (SEQ ID NO:89), a VL- CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a heavy chain comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), wherein the heavy chain comprises at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to the amino acid sequence of SEQ ID NO:156, and (b) a light chain comprising the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises: (a) a heavy chain comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a light chain comprising the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent is an antibody comprising a heavy chain comprising the amino acid sequence of SEQ ID NO:156 and a light chain comprising the amino acid sequence of SEQ ID NO:157. [00274] In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:156. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:156 and a light chain having at least 80%, at least 85%, at least 90%, or at least 95% identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:156. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain having at least 90% identity to the amino acid sequence of SEQ ID NO:156 and a light chain having at least 90% identity to the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:156. In some embodiments, the ILT2/ILT4-binding agent comprises a light chain comprising the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:156 and a light chain comprising the amino acid sequence of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:156 and/or a light chain of SEQ ID NO:157. In some embodiments, the ILT2/ILT4- binding agent is an antibody that comprises a heavy chain of SEQ ID NO:156. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a light chain of SEQ ID NO:157. In some embodiments, the ILT2/ILT4-binding agent is an antibody that comprises a heavy chain of SEQ ID NO:156 and a light chain of SEQ ID NO:157. [00275] In some embodiments, the ILT2/ILT4-binding agent is antibody 73D1. In some embodiments, the ILT2/ILT4-binding agent is antibody Hz73D1.v1. [00276] Provided herein are agents that compete with one or more of the binding agents described herein for binding to ILT2, ILT4, or both ILT2 and ILT4. In some embodiments, an agent competes with one or more of the antibodies described herein for binding to ILT2, ILT4, or both ILT2 and ILT4. In some embodiments, an agent that competes with one or more of the antibodies described herein is an antibody. In some embodiments, an agent binds the same epitope as one of the antibodies described herein. In some embodiments, an agent binds an epitope overlapping with an epitope bound by one of the antibodies described herein. Antibodies and antigen-binding fragments that compete with or bind the same epitope as the antibodies described herein are expected to show similar functional properties. [00277] In some embodiments, an agent competes for binding to human ILT2, ILT4, or both ILT2 and ILT4 with a reference antibody, wherein the reference antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, an agent competes for binding to human ILT2 with a reference antibody, wherein the reference antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). [00278] In some embodiments, an agent competes for binding to human ILT2, ILT4, or both ILT2 and ILT4 with a reference antibody, wherein the reference antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL- CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, an agent competes for binding to human ILT4 with a reference antibody, wherein the reference antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). [00279] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4, binding agent, or the ILT2/ILT4 binding agent) described herein comprises an antibody in which at least one or more of the constant regions of the antibody has been modified or deleted. In some embodiments, an antibody comprises one or more modifications to one or more of the three heavy chain constant regions (CH1, CH2 or CH3) and/or to the light chain constant region (CL). In some embodiments, an antibody comprises one or more modifications to the hinge region. In some embodiments, the heavy chain constant region of the modified antibody comprises at least one human constant region. In some embodiments, the heavy chain constant region of the modified antibody comprises more than one human constant region. In some embodiments, modifications to the constant region comprise additions, deletions, or substitutions of one or more amino acids in one or more regions. In some embodiments, one or more regions are partially or entirely deleted from the constant regions of a modified antibody. In some embodiments, the entire CH2 domain has been removed from an antibody (ΔCH2 constructs). In some embodiments, one or more regions are partially or entirely deleted from the hinge region of a modified antibody. In some embodiments, a deleted constant region is replaced by a short amino acid spacer that provides some of the molecular flexibility typically imparted by the absent constant region. In some embodiments, a deleted hinge region is replaced by a short amino acid spacer that provides some of the molecular flexibility typically imparted by the absent hinge region. In some embodiments, a modified antibody comprises a CH3 domain directly fused to the hinge region of the antibody. In some embodiments, a modified antibody comprises a peptide spacer inserted between the hinge region and modified CH2 and/or CH3 domains. [00280] It is known in the art that the constant region(s) of an antibody mediates several effector functions and these effector functions can vary depending on the isotype of the antibody. For example, binding of the C1 component of complement to the Fc region of IgG or IgM antibodies (bound to antigen) activates the complement system. Activation of complement is important in the opsonization and lysis of cell pathogens. The activation of complement also stimulates the inflammatory response and can be involved in autoimmune hypersensitivity. In addition, the Fc region of an antibody can bind a Fc receptor (FcR) on the surface of a cell. There are a number of Fc receptors that are specific for different classes of antibody, including IgG (gamma receptors), IgE (epsilon receptors), IgA (alpha receptors) and IgM (mu receptors). Binding of antibody to Fc receptors on cell surfaces triggers a number of important and diverse biological responses including engulfment and destruction of antibody-coated particles, clearance of immune complexes, lysis of antibody-coated target cells by killer cells (called antibody-dependent cell cytotoxicity or ADCC), release of inflammatory mediators, placental transfer, and control of immunoglobulin production. [00281] In some embodiments, the ILT-binding agent comprises a variant Fc region. The amino acid sequences of the Fc region of human IgG1, IgG2, IgG3, and IgG4 are known to those of ordinary skill in the art (e.g., a representative human IgG1 region is SEQ ID NO:158). In some cases, Fc regions with amino acid variations have been identified in native antibodies. In some embodiments, a variant Fc region is engineered with substitutions at specific amino acid positions as compared to a native Fc region. Variant Fc regions are well-known in the art and include, but are not limited to, SEQ ID NO:159, SEQ ID NO:160, SEQ ID NO:161, SEQ ID NO:162, and SEQ ID NO:163. [00282] In some embodiments, a modified antibody provides for altered effector functions that, in turn, affect the biological profile of the antibody. For example, in some embodiments, the deletion or inactivation (through point mutations or other means) of a constant region reduces Fc receptor binding of a modified antibody as it circulates. In some embodiments, constant region modifications increase the serum half-life of an antibody. In some embodiments, constant region modifications reduce the serum half-life of an antibody. In some embodiments, constant region modifications decrease or remove ADCC and/or complement-dependent cytotoxicity (CDC) of an antibody. In some embodiments, specific amino acid substitutions in a human IgG1 Fc region with corresponding IgG2 or IgG4 residues reduce effector functions (e.g., ADCC and CDC) in a modified antibody. In some embodiments, a modified antibody does not have one or more effector functions. In some embodiments, a modified antibody does not have any detectable effector functions (e.g., “effectorless” antibodies). In some embodiments, a modified antibody has no ADCC activity and/or no CDC activity. In some embodiments, a modified antibody does not bind an Fc receptor and/or complement factors. In some embodiments, a modified antibody has no effector function(s). In some embodiments, constant region modifications increase or enhance ADCC and/or CDC of an antibody. In some embodiments, the constant region is modified to eliminate disulfide linkages or oligosaccharide moieties. In some embodiments, the constant region is modified to add/substitute one or more amino acids to provide one or more cytotoxin, oligosaccharide, or carbohydrate attachment sites. [00283] Modifications to the constant region of antibodies described herein may be made using well-known biochemical or molecular engineering techniques. In some embodiments, antibody variants are prepared by introducing appropriate nucleotide changes into the encoding DNA, and/or by synthesis of the desired antibody or polypeptide. Using these engineering techniques to modify an antibody it may be possible to disrupt the activity or effector function provided by a specific sequence or region while substantially maintaining the structure, binding activity, and other desired characteristics of the modified antibody. [00284] The present disclosure further embraces additional variants and equivalents that are substantially homologous to the recombinant, monoclonal, chimeric, humanized, and human antibodies, or antibody fragments thereof, described herein. In some embodiments, it is desirable to improve the binding affinity of the antibody. In some embodiments, it is desirable to modulate biological properties of the antibody, including but not limited to, specificity, thermostability, expression level, effector function(s), glycosylation, immunogenicity, and/or solubility. Those skilled in the art will appreciate that amino acid changes may alter post- translational processes of an antibody, such as changing the number or position of glycosylation sites or altering membrane anchoring characteristics. [00285] Variations may be generated by the substitution, deletion, or insertion of one or more nucleotides into a polynucleotide encoding the antibody or polypeptide that results in a change in an amino acid or the amino acid sequence as compared with the native antibody or polypeptide sequence. In some embodiments, amino acid substitutions are the result of replacing one amino acid with another amino acid having similar structural and/or chemical properties, such as the replacement of a leucine with a serine (i.e., conservative amino acid replacements). In some embodiments, the substitution, deletion, or insertion includes less than 25 amino acid substitutions, less than 20 amino acid substitutions, less than 15 amino acid substitutions, less than 10 amino acid substitutions, less than 5 amino acid substitutions, less than 4 amino acid substitutions, less than 3 amino acid substitutions, or less than 2 amino acid substitutions relative to the parent molecule. In some embodiments, variations in the amino acid sequence that are biologically useful and/or relevant are determined by systematically making insertions, deletions, or substitutions in the sequence and testing the resulting variant proteins for activity as compared to the parental antibody. [00286] In some embodiments, variants may include addition of amino acid residues at the amino- and/or carboxyl-terminal end of the antibody or polypeptide. The length of additional amino acids residues may range from one residue to a hundred or more residues. In some embodiments, a variant comprises an N-terminal methionyl residue. In some embodiments, the variant comprises an additional polypeptide/protein to create a fusion protein. In some embodiments, a variant is engineered to be detectable and may comprise a detectable label and/or protein (e.g., a fluorescent tag, a fluorescent protein, or an enzyme). [00287] In some embodiments, a cysteine residue not involved in maintaining the proper conformation of an antibody is substituted or deleted to modulate the antibody’s characteristics, for example, to improve oxidative stability and/or prevent aberrant disulfide crosslinking. Conversely, in some embodiments, one or more cysteine residues are added to create disulfide bond(s) to improve stability. [00288] In some embodiments, an antibody of the present disclosure is “deimmunized”. The deimmunization of antibodies generally consists of introducing specific amino acid mutations (e.g., substitutions, deletions, additions) that result in removal of T-cell epitopes (known or predicted) without significantly reducing the binding affinity or other desired activities of the antibody. [00289] The variant antibodies or polypeptides described herein may be generated using methods known in the art, including but not limited to, site-directed mutagenesis, alanine scanning mutagenesis, and PCR mutagenesis. [00290] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4-binding agent) described herein is chemically modified. In some embodiments, the ILT-binding agent is (i) an anti-ILT2 antibody, (ii) an anti-ILT4 antibody, or (iii) an anti-ILT2/ILT4 antibody that is chemically modified by glycosylation, acetylation, pegylation, phosphorylation, amidation, derivatization by known protecting/blocking groups, proteolytic cleavage, and/or linkage to a cellular ligand or other protein. Any of numerous chemical modifications may be carried out by known techniques. In some embodiments, the ILT-binding agent is the antibody fragment (e.g., scFv, Fv, Fab, F(ab′)2, or F(ab′)), wherein the antibody fragment is attached (either directly or indirectly) to a half-life extending moiety including, but not limited to, polyethylene glycol (PEG), a PEG mimetic, XTEN®, serum albumin, polysialic acid, N-(2-hydroxypropyl)methacrylamide, or dextran. [00291] The present disclosure encompasses ILT-binding agents built upon non- immunoglobulin backbones, wherein the agents bind the same epitope or essentially the same epitope as an anti-ILT antibody disclosed herein. In some embodiments, a non- immunoglobulin-based binding agent is an agent that competes with (i) an anti-ILT2 antibody, (ii) an anti-ILT4 antibody, and/or (iii) an anti-ILT2/ILT4 antibody described herein in a competitive binding assay. In some embodiments, alternative ILT-binding agents comprise a scaffold protein. Generally, scaffold proteins can be assigned to one of three groups based on the architecture of their backbone (1) scaffolds consisting of α-helices; (2) small scaffolds with few secondary structures or an irregular architecture of α-helices and β-sheets; and (3) scaffolds consisting of predominantly β-sheets. Scaffold proteins include, but are not limited to, anticalins, which are based upon the lipocalin scaffold; adnectins, which are based on the 10 ^th domain of human fibronectin type 3; affibodies, which are based on the B-domain in the Ig- binding region of Staphylococcus aureus protein A; darpins, which are based on ankyrin repeat domain proteins; fynomers, which are based on the SH3 domain of the human Fyn protein kinase; affitins, which are based on Sac7d from Sulfolobus acidocaldarius; affilins, which are based on human γ-B-crystallin or human ubiquitin; avimers, which are based on the A-domains of membrane receptor proteins; knottins (cysteine knot miniproteins), which are based upon a stable 30-amino acid anti-parallel β-strand protein fold; and Kunitz domain inhibitor scaffolds, which are based upon a structure that contains three disulfide bonds and three loops. [00292] In some embodiments, the ILT2-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 1. In some embodiments, the ILT2-binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27). In some embodiments, the ILT2-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL- CDR1, a VL-CDR2, and a VL-CDR3 from antibody 27F9. [00293] In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 2. In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43). In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL- CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47C8. [00294] In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 3. In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59). In some embodiments, the ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL- CDR1, a VL-CDR2, and a VL-CDR3 from antibody 48A5. [00295] In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 4A or Table 4B. In some embodiments, the ILT2/ILT4- binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 47H6 or antibody Hz47H6.v2. [00296] In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 5. In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH- CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 51A1. [00297] In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 6A or Table 6B. In some embodiments, the ILT2/ILT4- binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 64A12. [00298] In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 7. In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH- CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73C4. [00299] In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 shown in Table 8A or Table 8B. In some embodiments, the ILT2/ILT4- binding agent comprises an engineered scaffold protein comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments, the ILT2/ILT4-binding agent comprises an engineered scaffold protein comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 from antibody 73D1 or antibody Hz73D1.v1. [00300] In some embodiments, a composition comprises an ILT-binding agent described herein. In some embodiments, a composition comprises an ILT2-binding agent described herein. In some embodiments, a composition comprises an ILT4-binding agent described herein. In some embodiments, a composition comprises an ILT2/ILT4-binding agent described herein. In some embodiments, a composition comprises an anti-ILT2 antibody described herein. In some embodiments, a composition comprises a monoclonal anti-ILT2 antibody described herein. In some embodiments, a composition comprises an anti-ILT4 antibody described herein. In some embodiments, a composition comprises a monoclonal anti-ILT4 antibody described herein. In some embodiments, a composition comprises an anti-ILT2/ILT4 antibody described herein. In some embodiments, a composition comprises a monoclonal anti-ILT2/ILT4 antibody described herein. In some embodiments, a composition comprises an antibody selected from the group consisting of: antibody 27F9, antibody 47C8, antibody 48A5, antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or humanized versions thereof. [00301] In some embodiments, a pharmaceutical composition comprises an ILT-binding agent described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an ILT2-binding agent described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an ILT4-binding agent described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an ILT2/ILT4-binding agent described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an anti-ILT2 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a composition comprises a monoclonal anti-ILT2 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an anti-ILT4 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a composition comprises a monoclonal anti-ILT4 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an anti-ILT2/ILT4 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a composition comprises a monoclonal anti-ILT2/ILT4 antibody described herein and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises an antibody selected from the group consisting of: antibody 27F9, antibody 47C8, antibody 48A5, antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or humanized versions thereof and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition comprises antibody Hz73D1.v1 and a pharmaceutically acceptable carrier. [00302] In some embodiments, the ILT-binding agent is isolated. In some embodiments, the ILT-binding agent is substantially pure. [00303] Generally speaking, antigen-antibody interactions are non-covalent and reversible, formed by a combination of hydrogen bonds, hydrophobic interactions, and electrostatic and van der Waals forces. When describing the strength of an antigen-antibody complex, the terms affinity and/or avidity are commonly used. The binding of an antibody to its antigen is a reversible process, and the affinity of the binding is typically reported as an equilibrium dissociation constant (K _D ). K _D is the ratio of an antibody dissociation rate (k _off ) (how quickly it dissociates from its antigen) to the antibody association rate (k _on ) (how quickly it binds to its antigen). In some embodiments, KD values are determined by measuring the kon and koff rates of a specific antibody/antigen interaction and then using a ratio of these values to calculate the K _D value. K _D values may be used to evaluate and rank order the strength of individual antibody/antigen interactions. The lower the KD of an antibody, the higher the affinity of the antibody for its target. In some embodiments, affinity is measured using SPR technology (e.g., using a Biacore system). Avidity gives a measure of the overall strength of an antibody-antigen complex. It is dependent on three major parameters: (i) affinity of the antibody for the target, (ii) valency of both the antibody and antigen, and (iii) structural arrangement of the parts that interact. [00304] In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a dissociation constant (KD) of 1 μM or less, 100 nM or less, 40 nM or less, 20 nM or less, 10 nM or less, 1 nM or less, 0.1 nM or less, 50 pM or less, 10 pM or less, or 1 pM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of about 20 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 10 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 5 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of 3 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of 2 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of 1 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of 0.5 nM or less. In some embodiments, the ILT- binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 0.1 nM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 50 pM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 25 pM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 10 pM or less. In some embodiments, the ILT- binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 1 pM or less. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 0.01 nM to 2.5 nM. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a KD of 0.1 nM to 5 nM. In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a K _D of 1 nM to 5 nM. In some embodiments, the dissociation constant of the binding agent for ILT2 and/or ILT4 is the dissociation constant determined using an ILT protein (e.g., ILT2 or ILT4) immobilized on a Biacore chip and the binding agent flowed over the chip. In some embodiments, the dissociation constant of the binding agent for ILT2 and/or ILT4 is the dissociation constant determined using the binding agent captured by an anti-human IgG antibody on a Biacore chip and soluble ILT2 or ILT4 flowed over the chip. [00305] In some embodiments, the ILT-binding agent binds ILT2, ILT4, or both ILT2 and ILT4 with a half maximal effective concentration (EC50) of 1 μM or less, 100 nM or less, 40 nM or less, 20 nM or less, 10 nM or less, 1 nM or less, or 0.1 nM or less. In some embodiments, the ILT-binding agent binds human ILT2, ILT4, or both ILT2 and ILT4 with an EC ₅₀ of 1 μM or less, 100 nM or less, 40 nM or less, 20 nM or less, 10 nM or less, 1 nM or less, or 0.1 nM or less. In some embodiments, the ILT-binding agent binds cyno or rhesus ILT2 with an EC50 of 40 nM or less, 20 nM or less, 10 nM or less, 1 nM or less or 0.1 nM or less. In some embodiments, the ILT-binding agent binds ILT2 and/or ILT4 with an EC50 of 0.1 nM to about 3 nM, 0.1 nM to 2 nM, 0.1 nM to 1 nM, 0.5 nM to 3 nM, 0.5 nM to 2 nM, or 0.5 nM to 1 nM. [00306] In some embodiments, the ILT-binding agent binds human ILT2 and human ILT4 and has at least one or more of the following properties: (i) binding rhesus ILT2/ILT4; (ii) binding cyno ILT2/4; (iii) not binding ILT3, ILT5, and LILRB5; (iv) not binding LILRA2, LILRA4, LILRA5, and LILRA6; (v) being an ILT2 antagonist; (vi) being an ILT4 antagonist, (vii) inhibits ILT2 activity; (viii) inhibiting ILT4 activity; (ix) inhibiting ILT2 signaling in cells that express ILT2; (x) inhibiting ILT4 signaling in cells that express ILT4; (xi) inhibiting binding of ILT2 to MHC I molecules; (xii) inhibiting binding of ILT4 to MHC I molecules; (xiii) inhibiting ILT2-induced suppression of myeloid cells; (xiv) inhibiting ILT4-induced suppression of myeloid cells; (xv) inhibiting ILT2-induced suppression of myeloid cell activity; (xvi) inhibiting ILT4-induced suppression of myeloid cell activity; (xvii) restoring FcR activation in myeloid cells; (xviii) enhancing NK cell activity; (xix) enhancing CTL activity; and/or (xx) enhancing macrophage phagocytosis. [00307] The ILT-binding agents (e.g., ILT2-binding agents, ILT4-binding agents, or ILT2/ILT4-binding agents) described herein can be produced by any suitable method known in the art. Such methods range from direct protein synthesis methods to constructing a DNA sequence encoding polypeptide sequences and expressing those sequences in a suitable host. In some embodiments, a DNA sequence is constructed using recombinant technology by isolating or synthesizing a DNA sequence encoding a wild-type protein of interest. Optionally, the sequence can be mutagenized by site-specific mutagenesis to provide functional variants thereof. In some embodiments, a DNA sequence encoding a polypeptide of interest is constructed by chemical synthesis using an oligonucleotide synthesizer. Oligonucleotides can be designed based on the amino acid sequence of the desired polypeptide and selecting those codons that are favored in the host cell in which the recombinant polypeptide of interest will be produced. Standard methods can be applied to synthesize a polynucleotide sequence encoding an isolated polypeptide of interest. For example, a complete amino acid sequence can be used to construct a back-translated gene. Further, a DNA oligomer containing a nucleotide sequence coding for the particular isolated polypeptide can be synthesized. For example, several small oligonucleotides coding for portions of the desired polypeptide can be synthesized and then ligated. The individual oligonucleotides typically contain 5′ or 3′ overhangs for complementary assembly. [00308] Once assembled (by synthesis, site-directed mutagenesis, or another method), the polynucleotide sequences encoding a particular polypeptide of interest can be inserted into an expression vector and operatively linked to an expression control sequence appropriate for expression of the protein in a desired host. Proper assembly can be confirmed by nucleotide sequencing, restriction enzyme mapping, and/or expression of a biologically active polypeptide in a suitable host. [00309] In some embodiments, recombinant expression vectors are used to amplify and express DNA encoding the ILT-binding agents described herein. For example, recombinant expression vectors can be replicable DNA constructs which have synthetic or cDNA-derived DNA fragments encoding a polypeptide chain of the ILT-binding agent, such as an anti-ILT2/ILT4 antibody, or antigen-binding fragment thereof, operatively linked to suitable transcriptional and/or translational regulatory elements derived from mammalian, microbial, viral, or insect genes. A transcriptional unit generally comprises an assembly of (1) a genetic element or elements having a regulatory role in gene expression, for example, transcriptional promoters and/or enhancers, (2) a structural or coding sequence that is transcribed into mRNA and translated into protein, and (3) appropriate transcription and translation initiation and termination sequences. Regulatory elements can include an operator sequence to control transcription. The ability to replicate in a host, usually conferred by an origin of replication, and a selection gene to facilitate recognition of transformants can additionally be incorporated. DNA regions are “operatively linked” when they are functionally related to each other. For example, DNA for a signal peptide (secretory leader) is operatively linked to DNA for a polypeptide if it is expressed as a precursor that participates in the secretion of the polypeptide; a promoter is operatively linked to a coding sequence if it controls the transcription of the sequence; or a ribosome binding site is operatively linked to a coding sequence if it is positioned so as to permit translation. In some embodiments, structural elements intended for use in yeast expression systems include a leader sequence enabling extracellular secretion of translated protein by a host cell. In some embodiments, in situations where recombinant protein is expressed without a leader or transport sequence, a polypeptide may include an N-terminal methionine residue. This residue can optionally be subsequently cleaved from the expressed recombinant protein to provide a final product. [00310] The choice of an expression control sequence and an expression vector generally depends upon the choice of host. A wide variety of expression host/vector combinations can be employed. Useful expression vectors for eukaryotic hosts include, for example, vectors comprising expression control sequences from SV40, bovine papilloma virus, adenovirus, and cytomegalovirus. Useful expression vectors for bacterial hosts include known bacterial plasmids, such as plasmids from E. coli, including pCR1, pBR322, pMB9 and their derivatives, and wider host range plasmids, such as M13 and other filamentous single-stranded DNA phages. [00311] In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4- binding agent, or the ILT2/ILT4-binding agent) of the present disclosure is expressed from one or more vectors. In some embodiments, a VH is expressed by one vector and a VL is expressed by a second vector. In some embodiments, a VH and a VL are expressed by one vector. In some embodiments, a vector encodes a VH of an ILT-binding agent described herein. In some embodiments, a vector encodes a VL of an ILT-binding agent described herein. In some embodiments, a vector encodes a VH and a VL of an ILT-binding agent described herein. In some embodiments, a heavy chain polypeptide is expressed by one vector and a light chain polypeptide is expressed by a second vector. In some embodiments, a heavy chain polypeptide and a light chain polypeptide are expressed by one vector. In some embodiments, a vector encodes a heavy chain polypeptide of an ILT-binding agent described herein. In some embodiments, a vector encodes a light chain polypeptide of an ILT-binding agent described herein. In some embodiments, a vector encodes a heavy chain polypeptide and a light chain polypeptide of an ILT-binding agent described herein. [00312] Suitable host cells for expression of the ILT-binding agent (e.g., ILT2-binding agents, ILT4-binding agents, or ILT2/ILT4-binding agents) or a ILT2 or ILT4 protein or fragment thereof to use as an antigen or immunogen include prokaryotes, yeast cells, insect cells, or higher eukaryotic cells under the control of appropriate promoters. Prokaryotes include gram- negative or gram-positive organisms, for example E. coli or Bacillus. Higher eukaryotic cells include established cell lines of mammalian origin as described herein. Cell-free translation systems may also be employed. Appropriate cloning vectors and expression vectors for use with bacterial, fungal, yeast, and mammalian cellular hosts, as well as methods of protein production, including antibody production are well known in the art. [00313] Various mammalian culture systems may be used to express recombinant polypeptides. Expression of recombinant proteins in mammalian cells may be desirable because these proteins are generally correctly folded, appropriately modified, and biologically functional. Examples of suitable mammalian host cell lines include, but are not limited to, COS-7 (monkey kidney- derived), L-929 (murine fibroblast-derived), C127 (murine mammary tumor-derived), 3T3 (murine fibroblast-derived), CHO (Chinese hamster ovary-derived), HeLa (human cervical cancer-derived), BHK (hamster kidney fibroblast-derived), HEK-293 (human embryonic kidney-derived) cell lines and variants thereof. Mammalian expression vectors can comprise non-transcribed elements such as an origin of replication, a suitable promoter and enhancer linked to the gene to be expressed, and other 5′ or 3′ flanking non-transcribed sequences, and 5′ or 3′ non-translated sequences, such as necessary ribosome binding sites, a polyadenylation site, splice donor and acceptor sites, and transcriptional termination sequences. [00314] Expression of recombinant proteins in insect cell culture systems (e.g., baculovirus) also offers a robust method for producing correctly folded and biologically functional proteins. Baculovirus systems for production of heterologous proteins in insect cells are well-known to those of skill in the art. [00315] Thus, the present disclosure provides cells comprising the ILT-binding agents described herein. In some embodiments, the cells produce the ILT-binding agents described herein. In some embodiments, the cells produce an antibody. In some embodiments, the cells produce an antibody that binds human ILT2. In some embodiments, the cells produce an antibody that binds human ILT4. In some embodiments, the cells produce an antibody that binds human ILT2 and ILT4. In some embodiments, the cells produce an antibody that binds human ILT2 and cyno ILT2. In some embodiments, the cells produce an anti-ILT2 antibody designated 27F9. In some embodiments, the cells produce an anti-ILT4 antibody designated 47C8. In some embodiments, the cells produce an anti-ILT4 antibody designated 48A5. In some embodiments, the cells produce an anti-ILT2/ILT4 antibody designated 47H6. In some embodiments, the cells produce a humanized anti-ILT2/ILT4 antibody designated Hz47H6.v2. In some embodiments, the cells produce an anti-ILT2/ILT4 antibody designated 51A1. In some embodiments, the cells produce an anti-ILT2/ILT4 antibody designated 64A12. In some embodiments, the cells produce a humanized anti-ILT2/ILT4 antibody designated Hz64A12. In some embodiments, the cells produce an anti-ILT2/ILT4 antibody designated 73C4. In some embodiments, the cells produce an anti-ILT2/ILT4 antibody designated 73D1. In some embodiments, the cells produce a humanized anti-ILT2/ILT4 antibody designated Hz73D1.v1. In some embodiments, the cell is a prokaryotic cell. In some embodiments, the cell is an eukaryotic cell. In some embodiments, the cell is a mammalian cell. In some embodiments, the cell is a hybridoma cell. [00316] Proteins produced by a host cell can be purified according to any suitable method. Standard methods include chromatography (e.g., ion exchange, affinity, and sizing column chromatography), centrifugation, differential solubility, or by any other standard technique for protein purification. Affinity tags such as hexahistidine (His6; SEQ ID NO:173), maltose binding domain, influenza coat sequence, and glutathione-S-transferase can be attached to the protein to allow easy purification by passage over an appropriate affinity column. Affinity chromatography methods used for purifying immunoglobulins can include, but are not limited to, Protein A, Protein G, and Protein L chromatography. Isolated proteins can be physically characterized using techniques that include, but are not limited to, proteolysis, size exclusion chromatography (SEC), mass spectrometry (MS), nuclear magnetic resonance (NMR), isoelectric focusing (IEF), high performance liquid chromatography (HPLC), and x-ray crystallography. The purity of isolated proteins can be determined using techniques known to those of skill in the art, including but not limited to, SDS-PAGE, SEC, capillary gel electrophoresis, IEF, and capillary isoelectric focusing (cIEF). [00317] In some embodiments, supernatants from expression systems that secrete recombinant protein into culture media are first concentrated using a commercially available protein concentration filter, for example, an Amicon® or Millipore Pellicon® ultrafiltration unit. Following the concentration step, the concentrate can be applied to a suitable purification matrix. In some embodiments, an anion exchange resin is employed, for example, a matrix or substrate having pendant diethylaminoethyl (DEAE) groups. The matrices can be acrylamide, agarose, dextran, cellulose, or other types commonly employed in protein purification. In some embodiments, a cation exchange step is employed. Suitable cation exchangers include various insoluble matrices comprising sulfopropyl or carboxymethyl groups. In some embodiments, a hydroxyapatite media is employed, including but not limited to, ceramic hydroxyapatite (CHT). In some embodiments, one or more reverse-phase HPLC steps employing hydrophobic RP- HPLC media, e.g., silica gel having pendant methyl or other aliphatic groups, are employed to further purify a recombinant protein. In some embodiments, hydrophobic interaction chromatography (HIC) is used to separate recombinant proteins based on their hydrophobicity. HIC is a useful separation technique for purifying proteins while maintaining biological activity due to the use of conditions and matrices that operate under less denaturing conditions than some other techniques. Some or all of the foregoing purification steps, in various combinations, can be employed to provide a homogeneous recombinant protein. [00318] ILT-binding agents (e.g., ILT2-binding agents, ILT4-binding agents, or ILT2/ILT4- binding agents) of the present disclosure may be analyzed for their physical/chemical properties and/or biological activities by various assays known in the art. In some embodiments, an anti- ILT2 antibody is tested for its ability to bind ILT2 (e.g., human ILT2 and/or cyno/rhesus ILT2). In some embodiments, an anti-ILT4 antibody is tested for its ability to bind ILT4 (e.g., human ILT4). In some embodiments, an anti-ILT2/ILT4 antibody is tested for its ability to bind ILT2 and ILT4 (e.g., human ILT2, human ILT4, and cyno/rhesus ILT2). Binding assays include, but are not limited to, SPR (e.g., Biacore), ELISA, and FACS. In some embodiments, an anti-ILT2 antibody is tested for its ability to inhibit, reduce, or block ILT2 binding to MHC class I antigens. In some embodiments, an anti-ILT4 antibody is tested for its ability to inhibit, reduce, or block ILT4 binding to MHC class I antigens. In some embodiments, an anti-ILT2/ILT4 antibody is tested for its ability to inhibit, reduce, or block ILT2 and ILT4 binding to MHC class I antigens. In addition, antibodies may be evaluated for solubility, stability, thermostability, viscosity, expression levels, expression quality, and/or purification efficiency. [00319] In some embodiments, monoclonal antibodies generated against ILT2, ILT4, or ILT2 and ILT4 are grouped based upon the epitope each individual antibody recognizes, a process known as “epitope binning”. Generally, antibodies are tested in a pairwise combinatorial manner and antibodies that compete with each other are grouped together into bins. For example, in a premix binning assay, a first antibody is immobilized on a surface and a premixed solution of a second antibody and antigen is flowed over the immobilized first antibody. In tandem, the antigen is immobilized on a surface and the two antibodies are flowed over the immobilized antigen and compete to bind. Using these techniques, antibodies that block one another can be identified. A competitive blocking profile is created for each antibody relative to the other antibodies. The blocking results determine which bin each antibody is placed in. High-throughput methods of epitope binning are known in the art and allow for screening and characterization of large numbers of antibodies within a short period of time. Antibodies that bind similar epitopes often share similar functions and/or capabilities. Conversely, antibodies that bind different epitopes may have different functional activities. [00320] In some embodiments, an epitope bin comprises at least one antibody from the group consisting of: 27F9, 47C8, 48A5, 47H6, 51A1, 64A12, 73C4, and 73D1. In some embodiments, an epitope bin comprises at least antibodies 27F9 and 73D1. In some embodiments, an epitope bin comprises at least antibodies 27F9, 73C4, and 73D1. In some embodiments, an epitope bin comprises at least antibodies 48A5 and 47H6. [00321] Epitope mapping is the process of identifying the binding site, or epitope on a target protein/antigen where an antibody (or other binding agent) binds. A variety of methods are known in the art for mapping epitopes on target proteins. These methods include (i) mutagenesis, including but not limited to, shotgun mutagenesis, site-directed mutagenesis, and alanine scanning; (ii) domain or fragment scanning; (iii) peptide scanning (e.g., Pepscan technology); (iv) display methods, including but not limited to, phage display, microbial display, and ribosome/mRNA display; (v) methods involving proteolysis and mass spectroscopy; (vi) methods involving amide hydrogen/deuterium exchange; and (vii) structural determination, including but not limited to, x-ray crystallography and NMR. [00322] In some embodiments, purified anti-ILT antibodies (e.g., anti-ILT2 antibodies, anti- ILT4 antibodies, or anti-ILT2/ILT4 antibodies) are characterized by assays including, but not limited to, N-terminal sequencing, amino acid analysis, HPLC, mass spectrometry, differential scanning fluorimetry (DSF), nanoDSF, capillary isoelectric focusing (cIEF), ion exchange chromatography, and papain digestion. [00323] In vitro assays that characterize immune cell function include, but are not limited to, cell activation assays (e.g., cell proliferation assays), cytotoxic T-cell (CTL) assays, T-cell suppression assays, MDSC assays, natural killer (NK) cell assays, mixed lymphocyte reaction (MLR) assays, cytokine/chemokine production assays, FcR binding assays, phagocytosis assays, and cell migration assays. In some embodiments, assays are provided for identifying anti-ILT antibodies that affect ILT activity. “Affect or affecting ILT activity” may include, for example, inhibiting, reducing, blocking, antagonizing, suppressing, and/or interfering with ILT2 activity, ILT4 activity, or ILT2 and ILT4 activity. As ILT2 and ILT4 generally act as negative regulator/inhibitory molecules, in some embodiments, inhibiting, reducing, blocking, antagonizing, suppressing, and/or interfering with ILT2 and/or ILT4 activity results in a blockade of ILT2-induced and/or ILT4-induced suppression of a biological function. Those of skill in the art may refer to this ability as “releasing the brake”, for example, anti-ILT antibodies described herein block the signaling of ILT2 and/or ILT4 that would otherwise send a suppressive message. Once the “brakes” are released, the immune system is able to mount a response or a stronger response to, for example, a tumor. [00324] As described herein, ILT2 is expressed on myeloid cells, such as monocytes, macrophages, dendritic cells (DCs), and APCs, as well as NK cells, B-cells, and CD8+ T-cells (CTLs). ILT2 activity or ILT2 signaling activity includes, but is not limited to, suppression of myeloid cells, suppression of myeloid cell activity, suppression of tumor-associated myeloid cells, suppression of NK cells, and suppression of cytolytic T-cells (CTLs). In some embodiments, inhibiting, reducing, blocking, antagonizing, suppressing, and/or interfering with ILT2 activity results in a release of ILT2-induced suppression of an activation signal. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disclosed herein inhibits ILT2 signaling. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody inhibits ILT2 signaling thereby reversing an ILT2-induced suppressive effect. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody inhibits an ILT2-induced extinction signal. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody increases myeloid cell activity. In some embodiments, the anti-ILT2 antibody or the anti- ILT2/ILT4 antibody increases APC activity. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody increases macrophage activity. In some embodiments, the anti- ILT2 antibody or the anti-ILT2/ILT4 antibody increases macrophage phagocytosis. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody increases NK cell activity. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody increases CTL activity. [00325] ILT4 is expressed on myeloid cells, such as monocytes, macrophages, dendritic cells (DCs), myeloid-derived suppressor cells (MDSCs), and APCs, as well as neutrophils and eosinophils. ILT4 activity or ILT4 signaling activity includes, but is not limited to, suppression of myeloid cells, suppression of myeloid cell activity, and suppression of tumor-associated myeloid cells. In some embodiments, inhibiting, reducing, blocking, antagonizing, suppressing, and/or interfering with ILT4 activity results in a release of ILT4-induced suppression of an activation signal. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody inhibits ILT4 signaling. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody inhibits ILT4 signaling thereby reversing an ILT4-induced suppressive effect. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody inhibits an ILT4-induced extinction signal. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody increases myeloid cell activity. In some embodiments, the anti-ILT4 antibody or the anti- ILT2/ILT4 antibody increases macrophage activity. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody decreases MDSCs. In some embodiments, the anti- ILT4 antibody or the anti-ILT2/ILT4 antibody decreases suppression by MDSCs. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody induces a switch of MDSCs to activated macrophages. [00326] In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway. In some embodiments, the anti-ILT2 antibody or the anti- ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and activates myeloid cells. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and activates APCs. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and activates dendritic cells. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and activates primary dendritic cells. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and increases NK cell activity. In some embodiments, the anti-ILT2 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and increases CTL activity. [00327] In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT4 signaling pathway. In some embodiments, the anti-ILT4 antibody or the anti- ILT2/ILT4 antibody disrupts the ILT4 signaling pathway and activates myeloid cells. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT4 signaling pathway and activates APCs. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT4 signaling pathway and activates dendritic cells. In some embodiments, the anti-ILT4 antibody or the anti-ILT2/ILT4 antibody disrupts the ILT4 signaling pathway and activates primary dendritic cells. [00328] In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and activates myeloid cells. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and activates APCs. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and activates dendritic cells. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and activates primary dendritic cells. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and increases myeloid cell activity. In some embodiments, the anti- ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and increases NK cell activity. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and increases CTL activity. In some embodiments, the anti-ILT2/ILT4 antibody disrupts the ILT2 signaling pathway and the ILT4 signaling pathway and decreases MDSC activity. [00329] In some embodiments, the terms “inhibiting”, “reducing”, “blocking”, “antagonizing”, “suppressing”, and “interfering” are relative to levels and/or activity in the absence of treatment with the ILT-binding agent. In some embodiments, the terms “inhibiting”, “reducing”, “blocking”, “antagonizing”, “suppressing”, and “interfering” are relative to levels and/or activity prior to treatment with the ILT-binding agent. [00330] In some embodiments, the terms “activating”, “promoting”, “increasing”, and “enhancing” are relative to levels and/or activity in the absence of treatment with the ILT- binding agent. In some embodiments, the terms “activating”, “promoting”, “increasing”, and “enhancing” are relative to levels and/or activity prior to treatment with the ILT-binding agent. [00331] In some embodiments, an anti-ILT2 antibody that inhibits ILT2 activity is antibody 27F9. In some embodiments, an anti-ILT4 antibody that inhibits ILT4 activity is antibody 47C8. In some embodiments, an anti-ILT4 antibody that inhibits ILT4 activity is antibody 48A5. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody 47H6. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody Hz47H6.v2. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody 51A1. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody 64A12. In some embodiments, an anti- ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody Hz64A12. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody 73C4. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody 73D1. In some embodiments, an anti-ILT2/ILT4 antibody that inhibits ILT2 and ILT4 activity is antibody Hz73D1.v1 [00332] The present disclosure also provides conjugates comprising an anti-ILT2, an anti-ILT4, or an anti-ILT2/ILT4 antibody described herein. In some embodiments, the antibody is attached to a second molecule. In some embodiments, the antibody is conjugated to a cytotoxic agent or moiety. In some embodiments, the antibody is conjugated to a cytotoxic agent to form an ADC (antibody-drug conjugate). In some embodiments, the cytotoxic agent is a chemotherapeutic agent including, but not limited to, methotrexate, adriamycin/doxorubicin, melphalan, mitomycin C, chlorambucil, duocarmycin, daunorubicin, pyrrolobenzodiazepines (PBDs), or other intercalating agents. In some embodiments, the cytotoxic agent is a microtubule inhibitor including, but not limited to, auristatins, maytansinoids (e.g., DM1 and DM4), and tubulysins. In some embodiments, the cytotoxic agent is an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof, including, but not limited to, diphtheria A chain, non-binding active fragments of diphtheria toxin, exotoxin A chain, ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), Momordica charantia inhibitor, curcin, crotin, Sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. In some embodiments, an antibody is conjugated to one or more small molecule toxins, such as calicheamicins, maytansinoids, trichothenes, and CC1065. A derivative of any one of these toxins may be used as long as the derivative retains the cytotoxic activity of the parent molecule. [00333] Conjugates comprising an anti-ILT antibody (e.g., an ILT2 antibody, an ILT4 antibody, or an ILT2/ILT4 antibody) described herein may be made using any suitable method known in the art. In some embodiments, conjugates are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyidithiol) propionate (SPDP), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCl), active esters (such as disuccinimidyl suberate), aldehydes (such as glutaraldehyde), bis-azido compounds (such as bis(p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as toluene 2,6-diisocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). [00334] In some embodiments, an anti-ILT antibody (e.g., an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti-ILT2/ILT4 antibody) described herein is conjugated to a detectable substance or molecule that allows the antibody to be used for diagnosis and/or detection. In some embodiments, a labeled anti-ILT antibody is used to monitor immune cells in a tumor or in the microenvironment of a tumor. In some embodiments, a labeled anti-ILT antibody is used to monitor immune cells in a tumor or in the microenvironment of a tumor after treatment. A detectable substance can include but is not limited to, enzymes, such as horseradish peroxidase, alkaline phosphatase, beta-galactosidase, and acetylcholinesterase; prosthetic groups, such as biotin and flavine(s); fluorescent materials, such as, umbelliferone, fluorescein, fluorescein isothiocyanate (FITC), rhodamine, tetramethylrhodamine isothiocyanate (TRITC), dichlorotriazinylamine fluorescein, dansyl chloride, cyanine (Cy3), and phycoerythrin; bioluminescent materials, such as luciferase; radioactive materials, such as ²¹² Bi, ¹⁴ C, ⁵⁷ Co, ⁵¹ Cr, ⁶⁷ Cu, ¹⁸ F, ⁶⁸ Ga, ⁶⁷ Ga, ¹⁵³ Gd, ¹⁵⁹ Gd, ⁶⁸ Ge, ³ H, ¹⁶⁶ Ho, ¹³¹ I, ¹²⁵ I, ¹²³ I, ¹²¹ I, ¹¹⁵ In, ¹¹³ In, ¹¹² In, ¹¹¹ In, ¹⁴⁰ La, ¹⁷⁷ Lu, ⁵⁴ Mn, ⁹⁹ Mo, ³² P, ¹⁰³ Pd, ¹⁴⁹ Pm, ¹⁴² Pr, ¹⁸⁶ Re, ¹⁸⁸ Re, ¹⁰⁵ Rh, ⁹⁷ Ru, ³⁵ S, ⁴⁷ Sc, ⁷⁵ Se, ¹⁵³ Sm, ¹¹³ Sn, ¹¹⁷ Sn, ⁸⁵ Sr, ^99m Tc, ²⁰¹ Ti, ¹³³ Xe, ⁹⁰ Y, ⁶⁹ Yb, ¹⁷⁵ Yb, ⁶⁵ Zn; positron emitting metals; and magnetic metal ions. [00335] In some embodiments, an anti-ILT antibody (e.g., an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti-ILT2/ILT4 antibody) described herein is used in an immunoassay. Immunoassays are known to those of skill in the art and include, but are not limited to, ELISA, SPR (e.g., Biacore), FACS, and immunohistochemistry (IHC). In some embodiments, an anti- ILT antibody described herein is used on a tissue sample or a tumor sample. [00336] An anti-ILT antibody (e.g., an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti- ILT2/ILT4 antibody) described herein can also be conjugated to a second antibody to form an antibody heteroconjugate. [00337] An anti-ILT antibody (e.g., an anti-ILT2 antibody, an anti-ILT4 antibody, or an anti- ILT2/ILT4 antibody) as described herein may be attached to a solid support. Such solid supports include, but are not limited to, glass, cellulose, polyacrylamide, nylon, polystyrene, polyvinyl chloride, or polypropylene. In some embodiments, immobilized anti-ILT antibodies are used in immunoassays. In some embodiments, immobilized anti-ILT antibodies are used in purification of the target antigen. 5.3. Polynucleotides [00338] In some embodiments, the disclosure encompasses polynucleotides comprising polynucleotides that encode a polypeptide (e.g., an ILT-binding agent) described herein. The term “polynucleotides that encode a polypeptide” encompasses a polynucleotide that includes only coding sequences for the polypeptide as well as a polynucleotide that includes additional coding and/or non-coding sequences. The polynucleotides of the disclosure can be in the form of RNA or in the form of DNA. DNA includes cDNA, genomic DNA, and synthetic DNA; and can be double-stranded or single-stranded, and if single stranded can be the coding strand or non-coding (anti-sense) strand. [00339] In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH and/or a VL of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VL of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT2-binding agent described herein and a polynucleotide encoding a VL of the ILT2-binding agent. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH and/or a VL of an ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VL of an ILT4- binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT4-binding agent described herein and a polynucleotide encoding a VL of the ILT4-binding agent. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH and/or a VL of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VL of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a VH of an ILT2/ILT4-binding agent described herein and a polynucleotide encoding a VL of the ILT2/ILT4-binding agent. [00340] In some embodiments, the polynucleotide comprises polynucleotide encoding a heavy chain and/or a light chain of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a light chain of an ILT2-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT2-binding agent described herein and a polynucleotide encoding a light chain of the ILT2-binding agent. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain and/or a light chain of an ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a light chain of an ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT4-binding agent described herein and a polynucleotide encoding a light chain of the ILT4-binding agent. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain and/or a light chain of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a light chain of an ILT2/ILT4-binding agent described herein. In some embodiments, the polynucleotide comprises a polynucleotide encoding a heavy chain of an ILT2/ILT4-binding agent described herein and a polynucleotide encoding a light chain of the ILT2/ILT4-binding agent. [00341] In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence selected from the group consisting of: SEQ ID NOs:125-145. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:125. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:126. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:127. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:128. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:129. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:130. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:131. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:132. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:133. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:134. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:135. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:136. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:137. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:138. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:139. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:140. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:141. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:142. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:143. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:144. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:145. [00342] In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence selected from the group consisting of: SEQ ID NOs:146-157. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:146. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:147. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:148. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:149. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:150. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:151. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:152. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:153. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:154. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:155. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:156. In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising an amino acid sequence of SEQ ID NO:157. [00343] In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising more than one amino acid sequence selected from the group consisting of: SEQ ID NOs:125-145. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:125 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:126. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:127 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:128. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:129 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:130. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:131 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:132. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:133 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:134. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:135 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:136. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:137 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:138. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:139 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:140. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:141 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:142. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:143 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:142. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:144 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:145. [00344] In some embodiments, the polynucleotide comprises a polynucleotide encoding a polypeptide comprising more than one amino acid sequence selected from the group consisting of: SEQ ID NOs:146-157. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:146 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:147. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:148 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:149. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:150 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:151. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:152 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:153. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:154 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:155. In some embodiments, the polynucleotide comprises a polynucleotide encoding (i) a polypeptide comprising an amino acid sequence of SEQ ID NO:156 and (ii) a polypeptide comprising an amino acid sequence of SEQ ID NO:157. [00345] The present disclosure also provides variants of the polynucleotides described herein, wherein a variant encodes, for example, a fragment, an analog, and/or a derivative of a polypeptide. In some embodiments, the present disclosure provides a polynucleotide comprising a polynucleotide having a nucleotide sequence at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, and in some embodiments, at least 96%, at least 97%, at least 98%, or at least 99% identical to a polynucleotide encoding a polypeptide described herein. [00346] In some embodiments, the polynucleotide comprises a polynucleotide having a nucleotide sequence at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, and in some embodiments, at least 96%, at least 97%, at least 98%, or at least 99% identical to a polynucleotide encoding an amino acid sequence selected from the group consisting of: SEQ ID NOs:125-157. Also provided is a polynucleotide that comprises a polynucleotide that hybridizes to a polynucleotide encoding an amino acid sequence selected from the group consisting of: SEQ ID NOs:125-157. In some embodiments, the hybridization is under conditions of high stringency as is known to those skilled in the art. [00347] As used herein, the phrase “a polynucleotide having a nucleotide sequence at least 95% identical to a polynucleotide sequence” is intended to mean that the nucleotide sequence of the polynucleotide is identical to a reference sequence except that the polynucleotide sequence can include up to five point mutations per each 100 nucleotides of the reference nucleotide sequence. In other words, to obtain a polynucleotide having a nucleotide sequence at least 95% identical to a reference nucleotide sequence, up to 5% of the nucleotides in the reference sequence can be deleted or substituted with another nucleotide, or a number of nucleotides up to 5% of the total nucleotides in the reference sequence can be inserted into the reference sequence. It is understood by those of skill in the art that an appropriate calculation would be made for other “% identical” statements, for example, 90% identical or 85% identical. The mutations of the reference sequence can occur at the 5′ or 3′ terminal positions of the reference nucleotide sequence or anywhere between those terminal positions, interspersed either individually among nucleotides in the reference sequence or in one or more contiguous groups within the reference sequence. [00348] The polynucleotide variants can contain alterations in the coding regions, non-coding regions, or both. In some embodiments, the polynucleotide variant contains alterations that produce silent substitutions, additions, or deletions, but does not alter the properties or activities of the encoded polypeptide. In some embodiments, the polynucleotide variant comprises silent substitutions that results in no change to the amino acid sequence of the polypeptide (due to the degeneracy of the genetic code). In some embodiments, the polynucleotide variant comprises one or more mutated codons comprising one or more (e.g., 1, 2, or 3) substitutions to the codon that change the amino acid encoded by that codon. Methods for introducing one or more substitutions into a codon are known in the art, including but not limited to, PCR mutagenesis and site-directed mutagenesis. Polynucleotide variants can be produced for a variety of reasons, for example, to optimize codon expression for a particular host (e.g., change codons in the human mRNA to those preferred by a bacterial host such as E. coli). In some embodiments, the polynucleotide variant comprises at least one silent mutation in a non-coding or a coding region of the sequence. [00349] In some embodiments, the polynucleotide variant is produced to modulate or alter expression (or expression levels) of the encoded polypeptide. In some embodiments, the polynucleotide variant is produced to increase expression of the encoded polypeptide. In some embodiments, the polynucleotide variant is produced to decrease expression of the encoded polypeptide. In some embodiments, the polynucleotide variant has increased expression of the encoded polypeptide as compared to a parental polynucleotide sequence. In some embodiments, the polynucleotide variant has decreased expression of the encoded polypeptide as compared to a parental polynucleotide sequence. [00350] In some embodiments, the polynucleotide comprises the coding sequence for a polypeptide fused in the same reading frame to a polynucleotide that aids in expression and secretion of a polypeptide from a host cell. In some embodiments, the polynucleotide that aids in expression and secretion is a leader sequence that functions as a secretory sequence for controlling transport of a polypeptide. In some embodiments, the polypeptide has a leader sequence cleaved by the host cell to form a “mature” form of the polypeptide. [00351] In some embodiments, the polynucleotide comprises the coding sequence for a polypeptide fused in the same reading frame to a marker or tag sequence. For example, In some embodiments, the marker sequence is a hexa-histidine tag (HIS-tag; SEQ ID NO:173) that allows for efficient purification of the polypeptide fused to the marker. In some embodiments, the marker sequence is a hemagglutinin (HA) tag derived from the influenza hemagglutinin protein when a mammalian host is used. In some embodiments, the marker sequence is a FLAG™ tag. In some embodiments, the marker may be used in conjunction with other markers or tags. [00352] In some embodiments, the polynucleotide is isolated. In some embodiments, the polynucleotide is substantially pure. [00353] Vectors and cells comprising each and every one of the polynucleotides described herein are also provided. In some embodiments, the vector comprises a polynucleotide molecule encoding an ILT-binding agent (e.g., an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent) described herein. In some embodiments, the vector comprises a polynucleotide molecule encoding a polypeptide that is part of an ILT-binding agent described herein. In some embodiments, the cell comprises a vector comprising a polynucleotide molecule encoding an ILT-binding agent described herein. In some embodiments, the cell comprises a vector comprising a polynucleotide molecule encoding a polypeptide that is part of an ILT- binding agent described herein. In some embodiments, the cell comprises a polynucleotide molecule encoding an ILT-binding agent described herein. In some embodiments, the cell comprises one or more polynucleotides encoding an ILT-binding agent described herein. In some embodiments, the cell comprises a single polynucleotide encoding an ILT-binding agent described herein. In some embodiments, the cell comprises a first polynucleotide encoding a VH of an ILT-binding agent described herein and a second polynucleotide encoding a VL of an ILT-binding agent described herein. In some embodiments, the cell comprises a polynucleotide encoding a VH and a VL of an ILT-binding agent described herein. In some embodiments, the cell comprises a first polynucleotide encoding a heavy chain of an ILT-binding agent described herein and a second polynucleotide encoding a light chain of an ILT-binding agent described herein. In some embodiments, the cell comprises a polynucleotide encoding a heavy chain and a light chain of an ILT-binding agent described herein. In some embodiments, the cell comprises one or more vectors encoding an ILT-binding agent described herein. In some embodiments, the cell comprises a vector encoding an ILT-binding agent described herein. In some embodiments, the cell comprises a first vector encoding a VH of an ILT-binding agent described herein and a second vector encoding a VL of an ILT-binding agent described herein. In some embodiments, the cell comprises a single vector encoding a VH and a VL of an ILT-binding agent described herein. In some embodiments, the cell comprises a first vector encoding a heavy chain of an ILT-binding agent described herein and a second vector encoding a light chain of an ILT-binding agent described herein. In some embodiments, the cell comprises a single vector encoding a heavy chain and a light chain of an ILT-binding agent described herein. 5.4. Methods of Making Binding Agents [00354] The disclosure provides methods for making the ILT-binding agents (e.g., ILT2- binding agents, ILT4-binding agents, or ILT2/ILT4-binding agents) described herein. In some embodiments, the method comprises providing a cell comprising one or more polynucleotides encoding a heavy chain and/or light chain of an ILT-binding agent described herein, culturing the cell under conditions that permit the expression of the binding agent, and isolating the binding agent. In some embodiments, the method further comprises purifying the binding agent. In some embodiments, the method further comprises formulating the binding gent as a pharmaceutical composition. [00355] In some embodiments, the cell comprises one or more polynucleotides encoding the heavy chain and the light chain of an ILT-binding agent described herein. In some embodiments, the cell comprises a first polynucleotide encoding the heavy chain of the ILT- binding agent and a second polynucleotide encoding the light chain of the ILT-binding agent. In other embodiments, a cell comprises a polynucleotide encoding the heavy chain and the light chain of the ILT-binding agent described herein. In some embodiments, the polynucleotide encoding the ILT-binding agent described herein is transiently transfected into a cell. In some embodiments, the polynucleotide encoding an ILT-binding agent described herein is stably transfected into a cell. [00356] In some embodiments, the cell comprises one or more vectors encoding the VH and the VL of an ILT-binding agent described herein. In some embodiments, the cell comprises a first vector encoding the VH of an ILT-binding agent and a second vector encoding the VL of an ILT-binding agent. In other embodiments, a cell comprises a vector encoding the VH and the VL of an ILT-binding agent. In some embodiments, the cell comprises one or more vectors encoding the heavy chain and the light chain of an ILT-binding agent described herein. In some embodiments, the cell comprises a first vector encoding the heavy chain of an ILT-binding agent and a second vector encoding the light chain of an ILT-binding agent. In other embodiments, a cell comprises a vector encoding the heavy chain and the light chain of an ILT-binding agent described herein. [00357] In some embodiments, an ILT-binding agent (e.g., the ILT2-binding agent, an ILT4- binding gent, or an ILT2/ILT4-binding agent) is an antibody fragment comprising at least one antigen-binding site and the method involves providing a cell comprising a polynucleotide encoding the fragment of the anti-ILT antibody, incubating the cell under conditions that permit the expression of the antibody fragment, and isolating the antibody fragment. In some embodiments, the cell comprises a polynucleotide encoding an antibody fragment described herein. In some embodiments, the cell comprises a vector encoding an antibody fragment described herein. In some embodiments, the method comprises purifying the antibody fragment. In some embodiments, the antibody fragment is a Fab, Fab′, F(ab′)2, Fv, scFv, (scFv)2, single chain antibody, dual variable region antibody, diabody, or nanobody. [00358] In some embodiments, the ILT-binding agent is a scFv and the method involves providing a cell comprising the scFv, incubating the cell under conditions that permit the expression of the scFv, and isolating the scFv. In some embodiments, the cell comprises a vector described herein encoding the scFv. In some embodiments, the cell comprises a polynucleotide described herein encoding the scFv. In some embodiments, the method comprises purifying the scFv. [00359] In some embodiments, the cell used to make an ILT-binding agent is a bacterial cell. In some embodiments, the cell used to make an ILT-binding agent is a yeast cell. In some embodiments, the cell used to make an ILT-binding agent is a mammalian cell. In some embodiments, the cell used to make an ILT-binding agent is a CHO cell. In other embodiments, the cell used to make an ILT-binding agent is a HEK-293 cell. 5.5. Methods of Use [00360] The ILT-binding agents (e.g., ILT2-binding agent, ILT4-binding agents, or ILT2/ILT4- binding agents) disclosed herein (see Section 5.2) are useful in a variety of applications including, but not limited to, therapeutic treatment methods, such as treatment of cancer. In some embodiments, the therapeutic treatment methods comprise immunotherapy for cancer. In some embodiments, an ILT-binding agent described herein is useful for activating, promoting, increasing, and/or enhancing an immune response to cancer or cancer cells. In some embodiments, an ILT-binding agent described herein is useful for activating, promoting, increasing, and/or enhancing an immune response to a tumor or tumor cells. The methods of use may be in vitro, ex vivo, or in vivo methods. [00361] The present disclosure provides methods of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking MHC I-induced ILT2 activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking ILT2-induced suppression of myeloid cells. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2- binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking of ILT2-induced suppression of myeloid cell activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules restores FcR signaling activity in myeloid cells. In some embodiments, the myeloid cell is a monocyte. In some embodiments, the myeloid cell is a macrophage. In some embodiments, the myeloid cell is a dendritic cell. In some embodiments, the myeloid cell is an APC. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2-binding agent described herein, wherein the method results in increasing NK cell activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT2-binding agent described herein, wherein the method results in increasing CTL activity. In some embodiments of the methods described herein, the MHC I molecule is a classical MHC I molecule. In some embodiments of the methods described herein, the MHC I molecule is a non-classical MHC I molecule. In some embodiments of the methods described herein, the MHC I molecule is HLA-A, HLA-B, HLA-C, HLA-E, and/or HLA-G. [00362] The present disclosure provides methods of disrupting, inhibiting, or blocking the binding of ILT4 to one or more MHC I molecules. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT4 to one or more MHC I molecules comprises contacting cells with an ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT4 to one or more MHC I molecules comprises contacting cells with an ILT4-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking MHC I-induced ILT4 activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT4 to one or more MHC I molecules comprises contacting cells with an ILT4-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking ILT4-induced suppression of myeloid cells. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 to one or more MHC I molecules comprises contacting cells with an ILT4- binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking of ILT4-induced suppression of myeloid cell activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT4 to one or more MHC I molecules restores FcR signaling activity in myeloid cells. In some embodiments, the myeloid cell is a monocyte. In some embodiments, the myeloid cell is a macrophage. In some embodiments, the myeloid cell is a dendritic cell. In some embodiments, the myeloid cell is an APC. In some embodiments of the methods described herein, the MHC I molecule is a classical MHC I molecule. In some embodiments of the methods described herein, the MHC I molecule is a non- classical MHC I molecule. In some embodiments of the methods described herein, the MHC I molecule is HLA-A, HLA-B, HLA-C, HLA-E, and/or HLA-G. [00363] The present disclosure provides methods of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking MHC I- induced ILT2 and/or ILT4 activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4-binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking ILT2-induced and/or ILT4-induced suppression of myeloid cells. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4- binding agent described herein, wherein the method results in disrupting, inhibiting, or blocking of ILT2-induced and/or ILT4-induced suppression of myeloid cell activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules restores FcR signaling activity in myeloid cells. In some embodiments, the myeloid cell is a monocyte. In some embodiments, the myeloid cell is a macrophage. In some embodiments, the myeloid cell is a dendritic cell. In some embodiments, the myeloid cell is an APC. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4-binding agent described herein, wherein the method results in increasing NK cell activity. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and ILT4 to one or more MHC I molecules comprises contacting cells with an ILT2/ILT4-binding agent described herein, wherein the method results in increasing CTL activity. [00364] The present disclosure provides methods of disrupting, inhibiting, or blocking the binding of ILT2 and/or ILT4 to MHC I molecules in a subject. In some embodiments, the method of disrupting, inhibiting, or blocking the binding of ILT2 and/or ILT4 to MHC I molecules in a subject, comprises administering to the subject an effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking MHC I-induced ILT2 and/or ILT4 activity in a subject comprises administering to the subject an effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking ILT2-induced and/or ILT4-induced suppression of myeloid cells in a subject comprises administering to the subject an effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking ILT2-induced and/or ILT4- induced suppression of myeloid cell activity in a subject comprises administering to the subject an effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting, inhibiting, or blocking ILT2-induced and/or ILT4-induced suppression of antigen-presenting cell activity in a subject restores FcR activity in myeloid cells. In some embodiments, the myeloid cell is a monocyte. In some embodiments, the myeloid cell is a macrophage. In some embodiments, the myeloid cell is a dendritic cell. In some embodiments, the myeloid cell is an APC. [00365] The present disclosure provides methods for activating an immune response in a subject using an ILT2/ILT4-binding agent described herein. In some embodiments, the disclosure provides methods for promoting an immune response in a subject using an ILT2/ILT4-binding agent described herein. In some embodiments, the disclosure provides methods for increasing an immune response in a subject using an ILT2/ILT4-binding agent described herein. In some embodiments, the disclosure provides methods for enhancing an immune response in a subject using an ILT2/ILT4-binding agent described herein. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises stimulating myeloid cells. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises stimulating monocytes. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises stimulating macrophages. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises stimulating dendritic cells. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises stimulating APCs. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises increasing cell-mediated immunity. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises increasing effector T-cell activity. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises increasing CTL activity. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises increasing NK cell activity. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises enhancing NK cell activity. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises inhibiting or decreasing the suppressive activity of Tregs. In some embodiments, the activating, promoting, increasing, and/or enhancing of an immune response comprises inhibiting or decreasing the suppressive activity of MDSCs. In some embodiments, the immune response is a result of antigenic stimulation. In some embodiments, the antigenic stimulation is a tumor cell. In some embodiments, the antigenic stimulation is cancer. [00366] The disclosure also provides methods of disrupting and/or inhibiting ILT2 and/or ILT4 signaling in a cell comprising contacting the cell with an effective amount of an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent described herein. In some embodiments, the method of disrupting and/or inhibiting ILT2 signaling in a cell comprises contacting the cell with an effective amount of antibody 27F9, antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or a humanized version thereof. In some embodiments, the method of disrupting and/or inhibiting ILT4 signaling in a cell comprises contacting the cell with an effective amount of antibody 47C8, antibody 48A5, antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or a humanized version thereof. In some embodiments, the method of disrupting and/or inhibiting ILT2 signaling and ILT4 signaling in a cell comprises contacting the cell with an effective amount of antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or a humanized version thereof. In some embodiments, the method of disrupting and/or inhibiting ILT2 signaling and ILT4 in a cell comprises contacting the cell with an effective amount of antibody Hz47H6.v2. In some embodiments, the method of disrupting and/or inhibiting ILT2 signaling and ILT4 in a cell comprises contacting the cell with an effective amount of antibody Hz64A12. In some embodiments, the method of disrupting and/or inhibiting ILT2 signaling and ILT4 in a cell comprises contacting the cell with an effective amount of antibody Hz73D1.v1. In some embodiments, the disclosure provides use of an ILT2-binding agent described herein in the manufacture or preparation of a medicament for disrupting and/or inhibiting ILT2 signaling in a cell. In some embodiments, the disclosure provides use of an ILT4-binding agent described herein in the manufacture or preparation of a medicament for disrupting and/or inhibiting ILT4 signaling in a cell. In some embodiments, the disclosure provides use of an ILT2/ILT4-binding agent described herein in the manufacture or preparation of a medicament for disrupting and/or inhibiting ILT2 signaling and ILT4 signaling in a cell. In some embodiments, the cell is a myeloid cell. In some embodiments, the cell is a monocyte. In some embodiments, the cell is a macrophage. In some embodiments, the cell is a dendritic cell. In some embodiments, the cell is an antigen-presenting cell. In some embodiments, the cells is a NK cell. In some embodiments, the cell is a CTL. In some embodiments, the method is an in vivo method wherein the step of contacting the cell with the agent comprises administering a therapeutically effective amount of an ILT-binding agent to a subject. In some embodiments, the method is an in vitro or ex vivo method. [00367] The present disclosure also provides methods for inhibiting growth of a tumor using an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent described herein. In some embodiments, the method of inhibiting growth of a tumor comprises using an ILT2- binding agent described herein. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody 27F9 or a humanized version thereof. In some embodiments, the method of inhibiting growth of a tumor comprises using an ILT4-binding agent described herein. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody 47C8 or antibody 48A5, or a humanized version thereof. In some embodiments, the method of inhibiting growth of a tumor comprises using an ILT2/ILT4-binding agent described herein. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or humanized versions thereof. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody Hz47H6.v2. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody Hz64A12. In some embodiments, the method of inhibiting growth of a tumor comprises using antibody Hz73D1.v1. In some embodiments, the method of inhibiting growth of a tumor comprises contacting a cell mixture with an ILT-binding agent in vitro. For example, an immortalized cell line or a cancer cell line mixed with immune cells (e.g., a myeloid cell) is cultured in medium to which is added a test agent that binds ILT2 and/or ILT4. In some embodiments, tumor cells are isolated from a patient sample such as, for example, a tissue biopsy, pleural effusion, or blood sample, mixed with immune cells (e.g., myeloid cells), and cultured in medium to which is added a test agent that binds ILT2 and/or ILT4. In some embodiments, the disclosure provides use of an ILT2-binding agent described herein in the manufacture or preparation of a medicament for inhibiting growth of a tumor or a tumor cell. In some embodiments, the disclosure provides use of an ILT4-binding agent described herein in the manufacture or preparation of a medicament for inhibiting growth of a tumor or a tumor cell. In some embodiments, the disclosure provides use of an ILT2/ILT4- binding agent described herein in the manufacture or preparation of a medicament for inhibiting growth of a tumor or a tumor cell. In some embodiments, the ILT2-binding agent increases, promotes, and/or enhances the activity of effector immune cells. In some embodiments, the ILT2-binding agent inhibits tumor cell growth by increasing, promoting, and/or enhancing the activity of effector immune cells. In some embodiments, an ILT4-binding agent increases, promotes, and/or enhances the activity of effector immune cells. In some embodiments, an ILT4-binding agent inhibits tumor cell growth by increasing, promoting, and/or enhancing the activity of effector immune cells. In some embodiments, an ILT2/ILT4-binding agent increases, promotes, and/or enhances the activity of effector immune cells. In some embodiments, an ILT2/ILT4-binding agent inhibits tumor cell growth by increasing, promoting, and/or enhancing the activity of effector immune cells. [00368] In some embodiments, the method of inhibiting tumor growth comprises contacting the tumor and/or tumor microenvironment with an ILT-binding agent (e.g., an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent) described herein in vivo. In some embodiments, contacting a tumor and/or tumor microenvironment with an ILT-binding agent described herein is undertaken in an animal model. For example, a test agent (e.g., an ILT2/ILT4-binding agent) may be administered to mice that have tumors. In some embodiments, the ILT2/ILT4-binding agent increases, promotes, and/or enhances the activity of immune cells in the mice. In some embodiments, the ILT2/ILT4-binding agent inhibits tumor growth. In some embodiments, the ILT2/ILT4-binding agent causes a tumor to regress. In some embodiments, the ILT2/ILT4-binding agent is administered at the same time or shortly after introduction of tumor cells into the animal to prevent tumor growth (“preventative model”). In some embodiments, the ILT2/ILT4-binding agent is administered after tumors have grown to a specified size or have become “established” for treatment (“therapeutic model”). In some embodiments, the ILT2/ILT4-binding agent is administered to a transgenic animal (e.g., a transgenic mouse) that expresses human ILT2 and/or ILT4, wherein the transgenic animal has a tumor derived from human cells. [00369] In some embodiments, the method of inhibiting tumor growth comprises administering to a subject a therapeutically effective amount of an ILT-binding agent (e.g., an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent) described herein. In some embodiments, the method of inhibiting tumor growth comprises administering to a subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of increasing or enhancing an immune response to a tumor or tumor cells in a subject comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of activating or enhancing a persistent or long-term immune response to a tumor or tumor cells in a subject comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4- binding agent described herein. In some embodiments, the method of inhibiting tumor relapse or tumor regrowth in a subject comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the method of inducing a persistent or long-term immunity that inhibits tumor relapse or tumor regrowth in a subject comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments of the methods described herein, the tumor is a solid tumor. In some embodiments, the tumor is a pancreatic tumor, a breast tumor, a lung tumor, a non-small cell lung tumor, a small cell lung tumor, a squamous cell carcinoma, a head and neck tumor, an esophageal cancer, a colorectal tumor, a prostate tumor, a skin tumor, a melanoma tumor, a stomach tumor, a gastric tumor, an intestinal tumor, an ovarian tumor, a cervical tumor, an uterine tumor, an endometrial tumor, a bladder tumor, a brain tumor, an esophageal tumor, a liver tumor, a kidney tumor, a renal cell carcinoma, a hepatocellular carcinoma, a biliary duct cancer, a thyroid tumor, a mesothelioma, a glioblastoma, or a testicular tumor. In some embodiments, the tumor is a hepatocellular carcinoma, a small cell lung tumor, a thyroid tumor, a mesothelioma, a glioblastoma, a renal cell carcinoma, a non-small cell lung tumor, a melanoma (skin cutaneous and uveal), a pancreatic ductal adenocarcinoma, a gastric tumor, a squamous cell carcinoma of the head and neck, a biliary duct tumor, a breast tumor, a triple-negative breast tumor, an ovarian tumor, a cervical tumor, an endocervical tumor, a colorectal tumor, an esophageal tumor, a gastroesophageal junction adenocarcinoma, a squamous cell carcinoma of head and neck, a bladder tumor, an uterine tumor, a cholangiocarcinoma, or a prostate tumor. In some embodiments, the tumor is a pancreatic tumor (e.g, a pancreatic ductal adenocarcinoma). In some embodiments, the tumor is a non-small cell lung tumor. In some embodiments, the tumor is a renal cell carcinoma (RCC). In some embodiments, the subject has a tumor or the subject had a tumor that was at least partially removed. In some embodiments of the methods described herein, the subject is a human. [00370] In some embodiments, the disclosure provides use of an ILT2-binding agent, an ILT4- binding agent, or an ILT2/ILT4-binding agent described herein in the manufacture or preparation of a medicament for inhibiting growth of a tumor or tumor cell. In some embodiments, the method of inhibiting growth of a tumor comprises administering to a subject a therapeutically effective amount of antibody 27F9, antibody 47C8, antibody 48A5, antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or humanized versions thereof. In some embodiments, the method of inhibiting growth of a tumor comprises administering to a subject a therapeutically effective amount of antibody Hz47H6.v2. In some embodiments, the method of inhibiting growth of a tumor comprises administering to a subject a therapeutically effective amount of antibody Hz64A12. In some embodiments, the method of inhibiting growth of a tumor comprises administering to a subject a therapeutically effective amount of antibody Hz73D1.v1. In some embodiments of the methods described herein, the subject is a human. [00371] The present disclosure provides methods of treating cancer. In some embodiments, the method of treating cancer comprises administering to a subject a therapeutically effective amount of an ILT2-binding agent described herein. In some embodiments, the method of treating cancer comprises administering to a subject a therapeutically effective amount of an ILT4-binding agent described herein. In some embodiments, the method of treating cancer comprises administering to a subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the ILT2/ILT4-binding agent binds ILT2 and/or ILT4 and inhibits or reduces growth of the cancer. In some embodiments, the ILT2/ILT4- binding agent binds human ILT2-expressing cells and/or ILT4-expressing cells, enhances an immune response to a cancer, and inhibits or reduces growth of the cancer. In some embodiments, the ILT2/ILT4-binding agent binds human ILT2-expressing cells and/or ILT4- expressing cells, activates myeloid cells, enhances an immune response to a cancer, and inhibits or reduces growth of the cancer. In some embodiments, the subject is a human. In some embodiments, the subject has a cancerous tumor. In some embodiments, the subject has had the cancer at least partially removed. [00372] In some embodiments, the disclosure provides use of an ILT2-binding agent described herein in the manufacture or preparation of a medicament for the treatment of cancer. In some embodiments, the disclosure provides use of an ILT4-binding agent described herein in the manufacture or preparation of a medicament for the treatment of cancer. In some embodiments, the disclosure provides use of an ILT2/ILT4-binding agent described herein in the manufacture or preparation of a medicament for the treatment of cancer. [00373] In some embodiments of the methods described herein, the cancer is pancreatic cancer, breast cancer (e.g., triple-negative breast cancer), lung cancer, non-small cell lung cancer (NSCLC), head and neck cancer, colorectal cancer, prostate cancer, skin cancer, melanoma, stomach cancer, gastric cancer, intestinal cancer, ovarian cancer, cervical cancer, uterine cancer, endometrial cancer, bladder cancer, brain cancer, esophageal cancer, liver cancer, kidney cancer, renal cell carcinoma (RCC), or testicular cancer. In some embodiments, the cancer is pancreatic cancer. In some embodiments, the cancer is breast cancer (e.g., triple-negative breast cancer). In some embodiments, the cancer is non-small cell lung cancer. In some embodiments, the cancer is renal cell carcinoma. [00374] In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody 27F9 or a humanized version thereof. In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody 47C8 or antibody 48A5, or a humanized version thereof. In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody 47H6, antibody 51A1, antibody 64A12, antibody 73C4, or antibody 73D1, or a humanized version thereof. In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody Hz47H6.v2. In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody Hz64A12. In some embodiments, the method for treating cancer in a subject comprises administering to the subject a therapeutically effective amount of antibody Hz73D1.v1. [00375] In other embodiments, the cancer is hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple-negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, or prostate cancer. In certain embodiments, the cancer is hepatocellular carcinoma. In certain embodiments, the cancer is small cell lung cancer. In certain embodiments, the cancer is thyroid cancer. [00376] In some embodiments, the tumor comprises a microsatellite instability – high (MSI-H) tumor. In some embodiments, the tumor comprises a deficient mismatch repair (dMMR) positive tumor. In other embodiments, the tumor is a small cell lung tumor, thyroid tumor, pancreatic tumor, a breast tumor, a lung tumor, a non-small cell lung tumor, a head and neck tumor, a colorectal tumor, a prostate tumor, a skin tumor, a melanoma, a gastric tumor, a colorectal tumor, an ovarian tumor, a cervical tumor, a uterine tumor, an endometrial tumor, an endocervical tumor, a bladder tumor, a brain tumor, an esophageal tumor, a liver tumor, a kidney tumor, a renal tumor, mesothelioma, glioblastoma, a biliary duct tumor, or a testicular tumor. In some embodiments, the tumor is a hepatocellular carcinoma, a small cell lung tumor, a thyroid tumor, a mesothelioma, a glioblastoma, a renal cell carcinoma, a non-small cell lung tumor, a melanoma (skin cutaneous and uveal), a pancreatic ductal adenocarcinoma, a gastric tumor, a squamous cell carcinoma of the head and neck, a biliary duct tumor, a breast tumor, a triple-negative breast tumor, an ovarian tumor, a cervical tumor, an endocervical tumor, a colorectal tumor, an esophageal tumor, a gastroesophageal junction adenocarcinoma, a squamous cell carcinoma of head and neck, a bladder tumor, an uterine tumor, a cholangiocarcinoma, or a prostate tumor. In certain embodiments, the tumor is a liver tumor. In certain embodiments, the tumor is a small cell lung tumor. In certain embodiments, the tumor is a thyroid tumor. [00377] Provided herein is use of the binding agent or antibody of the present disclosure for treatment of cancer. In certain embodiments, the cancer is hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple- negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, or prostate cancer. Provided herein is use of the binding agent or antibody of the present disclosure for treatment of hepatocellular cancer. Provided herein is use of the binding agent or antibody of the present disclosure for treatment of small cell lung cancer. Provided herein is use of the binding agent or antibody of the present disclosure for treatment of thyroid cancer. Provided herein is use of the binding agent or antibody of the present disclosure for treatment of a microsatellite instability – high (MSI-H) tumor. Provided herein in some embodiments is use of the binding agent or antibody of the present disclosure for treatment of a deficient mismatch repair (dMMR) positive tumor. [00378] In some embodiments, provided herein is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of cancer. In certain embodiments, the cancer is hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple-negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, or prostate cancer. Provided herein is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of hepatocellular cancer. Provided herein is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of small cell lung cancer. Provided herein is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of thyroid cancer. Provided herein is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of a microsatellite instability – high (MSI-H) tumor. Provided herein in some embodiments is use of the binding agent or antibody of the present disclosure in the manufacture of a medicament for treatment of a deficient mismatch repair (dMMR) positive tumor. [00379] In some embodiments, the disclosure provides methods of activating myeloid cells in the tumor microenvironment. In some embodiments, the method of activating myeloid cells in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent described herein. In some embodiments, the method of activating myeloid cells in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. In some embodiments, the myeloid cells are primary dendritic cells. In some embodiments, the myeloid cells are monocytes. In some embodiments, the myeloid cells are macrophages. In some embodiments, the myeloid cells are APCs. [00380] In some embodiments, the disclosure provides methods of activating NK cells in the tumor microenvironment. In some embodiments, the method of activating NK cells in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2-binding agent or an ILT2/ILT4-binding agent described herein. In some embodiments, the method of activating NK cells in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2-binding agent described herein. In some embodiments, the method of activating NK cells in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. [00381] In some embodiments, the disclosure provides methods of activating CTLs in the tumor microenvironment. In some embodiments, the method of activating CTLs in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2-binding agent or an ILT2/ILT4-binding agent described herein. In some embodiments, the method of activating CTLs in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2-binding agent described herein. In some embodiments, the method of activating CTLs in the tumor microenvironment in a subject with a tumor comprises administering to the subject a therapeutically effective amount of an ILT2/ILT4-binding agent described herein. [00382] In some embodiments of the methods described herein, the ILT2-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 27F9. [00383] In some embodiments of the method described herein, the ILT2-binding agent is an anti-ILT2 antibody. In some embodiments of the methods described herein, the anti-ILT2 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFSLTNYGVS (SEQ ID NO:22), a VH-CDR2 comprising the amino acid sequence IIWGDGSTNYHSALIS (SEQ ID NO:23), and a VH-CDR3 comprising the amino acid sequence PNWDTYAMDF (SEQ ID NO:24), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASQDISNFLN (SEQ ID NO:25), a VL-CDR2 comprising the amino acid sequence CTSKLHS (SEQ ID NO:26), and a VL-CDR3 comprising the amino acid sequence QQGNTLPPT (SEQ ID NO:27). In some embodiments of the methods described herein, the anti-ILT2 antibody comprises: (a) a VH of SEQ ID NO:125 and (b) a VL of SEQ ID NO:126. In some embodiments of the methods described herein, the anti-ILT2 antibody is antibody 27F9. In some embodiments of the methods described herein, the anti-ILT2 antibody is a humanized version of 27F9. [00384] In some embodiments of the methods described herein, the ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 47C8. [00385] In some embodiments of the method described herein, an ILT4-binding agent is an anti-ILT4 antibody. In some embodiments of the methods described herein, the anti-ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYSFTGYYMH (SEQ ID NO:38), a VH-CDR2 comprising the amino acid sequence RVYPNNGDTSYNQKFKV (SEQ ID NO:39), and a VH-CDR3 comprising the amino acid sequence GATVVESLFAY (SEQ ID NO:40), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDNYGNNFLH (SEQ ID NO:41), a VL-CDR2 comprising the amino acid sequence RTSNLES (SEQ ID NO:42), and a VL-CDR3 comprising the amino acid sequence QQSNEDPYT (SEQ ID NO:43. In some embodiments of the methods described herein, the anti-ILT4 antibody comprises: (a) a VH of SEQ ID NO:127 and (b) a VL of SEQ ID NO:128. In some embodiments of the methods described herein, the anti-ILT4 antibody is antibody 47C8. In some embodiments of the methods described herein, the anti-ILT4 antibody is a humanized version of antibody 47C8. [00386] In some embodiments of the methods described herein, the ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 48A5. [00387] In some embodiments of the method described herein, an ILT4-binding agent is an anti-ILT4 antibody. In some embodiments of the methods described herein, the anti-ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTNYGMN (SEQ ID NO:54), a VH-CDR2 comprising the amino acid sequence WINTYIGEPIYADDFKG (SEQ ID NO:55), and a VH-CDR3 comprising the amino acid sequence RSDYDGYAMDY (SEQ ID NO:56), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence KSSQSLLYSGNQKNYLA (SEQ ID NO:57), a VL-CDR2 comprising the amino acid sequence WASTRES (SEQ ID NO:58), and a VL-CDR3 comprising the amino acid sequence QQHDSYPT (SEQ ID NO:59). In some embodiments of the methods described herein, the anti-ILT4 antibody comprises: (a) a VH of SEQ ID NO:129 and (b) a VL of SEQ ID NO:130. In some embodiments of the methods described herein, the anti-ILT4 antibody is antibody 48A5. In some embodiments of the methods described herein, the anti- ILT4 antibody is a humanized version of antibody 48A5. [00388] In some embodiments of the methods described herein, the ILT2/ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 47H6 or antibody Hz47H6.v2. [00389] In some embodiments of the method described herein, an ILT2/ILT4-binding agent is an anti-ILT2/ILT4 antibody. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71) or DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNGGTTYNQKFEG (SEQ ID NO:71), and a VH-CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence DFNPNNAGTTYNQKFEG (SEQ ID NO:118), and a VH- CDR3 comprising the amino acid sequence GRFYYGSLYSFDY (SEQ ID NO:72), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASGNIHNYLA (SEQ ID NO:73), a VL-CDR2 comprising the amino acid sequence NAKTLAD (SEQ ID NO:74), and a VL-CDR3 comprising the amino acid sequence QHFWTSIT (SEQ ID NO:75). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:131 and (b) a VL of SEQ ID NO:132. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:133 and (b) a VL of SEQ ID NO:134. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a heavy chain of SEQ ID NO:148 and (b) a light chain of SEQ ID NO:149. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody 47H6. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody is a humanized version of antibody 47H6. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody Hz47H6.v2. [00390] In some embodiments of the methods described herein, the ILT2/ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 51A1 or a humanized version of antibody 51A1. [00391] In some embodiments of the method described herein, an ILT2/ILT4-binding agent is an anti-ILT2/ILT4 antibody. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYGTMYYYAMDY (SEQ ID NO:88), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:135 and (b) a VL of SEQ ID NO:136. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody 51A1. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is a humanized version of antibody 51A1. [00392] In some embodiments of the methods described herein, the ILT2/ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 64A12, a humanized version of antibody 64A12, or antibody Hz64A12. [00393] In some embodiments of the method described herein, an ILT2/ILT4-binding agent is an anti-ILT2/ILT4 antibody. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GFTFNTYAMH (SEQ ID NO:86), a VH-CDR2 comprising the amino acid sequence RIRSKSSNYATYYADSVKD (SEQ ID NO:87), and a VH-CDR3 comprising the amino acid sequence DGIYYYDTMYYYAMDY (SEQ ID NO:102), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFIY (SEQ ID NO:103), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:137 and (b) a VL of SEQ ID NO:138. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:139 and (b) a VL of SEQ ID NO:140. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a heavy chain of SEQ ID NO:152 and (b) a light chain of SEQ ID NO:153. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody 64A12. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is a humanized version of antibody 64A12. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody Hz64A12. [00394] In some embodiments of the methods described herein, the ILT2/ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 73C4 or a humanized version of antibody 73C4. [00395] In some embodiments of the method described herein, an ILT2/ILT4-binding agent is an anti-ILT2/ILT4 antibody. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYMN (SEQ ID NO:70), a VH-CDR2 comprising the amino acid sequence NVNPNNGGTSYNQKFKG (SEQ ID NO:106), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:141 and (b) a VL of SEQ ID NO:142. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody 73C4. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is a humanized version of antibody 73C4. [00396] In some embodiments of the methods described herein, the ILT2/ILT4-binding agent comprises a VH-CDR1, a VH-CDR2, and a VH-CDR3 and a VL-CDR1, a VL-CDR2, and a VL-CDR3 of antibody 73D1, a humanized version of antibody 73D1, or antibody Hz73D1.v1. [00397] In some embodiments of the method described herein, an ILT2/ILT4-binding agent is an anti-ILT2/ILT4 antibody. In some embodiments of the methods described herein, the anti- ILT2/ILT4 antibody comprises: (a) a VH comprising a VH-CDR1 comprising the amino acid sequence GYTFTDYYIN (SEQ ID NO:111), a VH-CDR2 comprising the amino acid sequence NVNPNDGGTTYNQKFKG (SEQ ID NO:112), and a VH-CDR3 comprising the amino acid sequence REIYFYGTIYYYAMDY (SEQ ID NO:107), and (b) a VL comprising a VL-CDR1 comprising the amino acid sequence RASESVDYYGNSFMY (SEQ ID NO:89), a VL-CDR2 comprising the amino acid sequence FASNLES (SEQ ID NO:90), and a VL-CDR3 comprising the amino acid sequence QQNNEDPWT (SEQ ID NO:91). In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:143 and (b) a VL of SEQ ID NO:142. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a VH of SEQ ID NO:144 and (b) a VL of SEQ ID NO:145. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody comprises: (a) a heavy chain of SEQ ID NO:156 and (b) a light chain of SEQ ID NO:157. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody 73D1. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is a humanized version of antibody 73D1. In some embodiments of the methods described herein, the anti-ILT2/ILT4 antibody is antibody Hz73D1.v1. (a) Dosing Regimens [00398] For the treatment of a disease, the appropriate dosage of an ILT-binding agent (e.g., an ILT2-binding agent, an ILT4-binding agent, or an ILT2/ILT4-binding agent) of the present disclosure depends on the disorder or disease to be treated, the severity and course of the disorder or disease, the responsiveness of the disorder or disease, whether the agent is administered for therapeutic or preventative purposes, previous therapy, the patient's clinical history, and so on. An ILT-binding agent can be administered one time or over a series of treatments lasting from several days to several months, or until a cure is affected or a diminution of the disease state is achieved. [00399] In some embodiments of the method or use, the binding agent is administered at a dose of about 1 mg, about 3 mg, about 5 mg, about 6 mg, about 20 mg, about 60 mg, about 200 mg, about 600 mg, about 1200 mg, about 1500 mg, about 1800 mg, about 2100 mg, or about 2400 mg. [00400] In some embodiments of the method or use, the binding agent is administered at a dose of between about 50 mg and about 2000 mg. In some embodiments of the method or use, the binding agent is administered at a dose of between about 60 mg and about 1800 mg, between about 60 mg and about 1500 mg, between about 60 mg and about 1200 mg, between about 60 mg and about 900 mg, between about 60 mg and about 800 mg, between about 60 mg and about 600 mg, between about 60 mg and about 400 mg, between about 60 mg and about 200 mg, between about 200 mg and about 1800 mg, between about 200 mg and about 1500 mg, between about 200 mg and about 1200 mg, between about 200 mg and about 900 mg, between about 200 mg and about 800 mg, between about 200 mg and about 600 mg, between about 200 mg and about 400 mg, between about 400 mg and about 1800 mg, between about 400 mg and about 1500 mg, between about 400 mg and about 1200 mg, between about 400 mg and about 900 mg, between about 400 mg and about 800 mg, between about 400 mg and about 600 mg, between about 600 mg and about 1800 mg, between about 600 mg and about 1500 mg, between about 600 mg and about 1200 mg, between about 600 mg and about 900 mg, between about 800 mg and about 1800 mg, between about 800 mg and about 1500 mg, between about 800 mg and about 1200 mg, between about 800 mg and about 1000 mg, between about 900 mg and about 1800 mg, between about 900 mg and about 1500 mg, between about 900 mg and about 1200 mg, between about 1200 mg and about 1800 mg, or between about 1200 mg and about 1500 mg. In some embodiments of the method or use, the binding agent is administered at a dose of between about 400 mg and about 700 mg, between about 500 mg and about 800 mg, or between about 500 mg and about 700 mg. In some embodiments of the method or use, the binding agent is administered at a dose of about 600 mg. In some embodiments of the method or use, the binding agent is administered at a dose of between about 1000 mg and about 1300 mg, between about 1100 mg and about 1400 mg, or between about 1100 mg and about 1300 mg. In some embodiments of the method or use, the binding agent is administered at a dose of about 1200 mg. In certain embodiment, wherein the binding agent is administered at a dose of about 200 mg, about 300 mg, about 400 mg, about 500 mg, about 600 mg, about 700 mg, about 800 mg, about 900 mg, about 1000 mg, about 1100 mg, about 1200 mg, about 1300 mg, about 1400 mg, about 1500 mg, about 1600 mg, about 1700 mg, or about 1800 mg. In some embodiments of the method or use, the dose is a flat dose. [00401] In some embodiments of the method or use, the binding agent is administered at a dose of between about 1 mg/kg and about 100 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of between about 1 mg/kg and about 30 mg/kg, between about 5 mg/kg and about 30 mg/kg, between about 10 mg/kg and about 30 mg/kg, between about 15 mg/kg and about 30 mg/kg, between about 20 mg/kg and about 30 mg/kg, between about 25 mg/kg and about 30 mg/kg, between about 1 mg/kg and about 25 mg/kg, between about 5 mg/kg and about 25 mg/kg, between about 10 mg/kg and about 25 mg/kg, between about 15 mg/kg and about 25 mg/kg, between about 20 mg/kg and about 25 mg/kg, between about 1 mg/kg and about 20 mg/kg, between about 5 mg/kg and about 20 mg/kg, between about 10 mg/kg and about 20 mg/kg, between about 15 mg/kg and about 20 mg/kg, between about 1 mg/kg and about 15 mg/kg, between about 5 mg/kg and about 15 mg/kg, between about 10 mg/kg and about 15 mg/kg, between about 1 mg/kg and about 10 mg/kg, or between about 5 mg/kg and about 10 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of between about 5 mg/kg and about 15 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of about 10 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of between about 15 mg/kg and about 25 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of about 20 mg/kg of body weight. In some embodiments of the method or use, the binding agent is administered at a dose of about 10 mg/kg, about 12 mg/kg, about 14 mg/kg, about 16 mg/kg, about 18 mg/kg, about 20 mg/kg, about 22 mg/kg, about 24 mg/kg, about 26 mg/kg, about 28 mg/kg, or about 30 mg/kg. In some embodiments of the method or use, the dose is a body weight-based dose. [00402] In some embodiments of the method or use, the binding agent is administered once or sequentially. [00403] In some embodiments of the method or use, the binding agent is administered once every week (e.g., every 5-9, 6-9, 7-9, 5-8, 5-7, 6-8, 6-7, 7-8 days, or every 7 days), every 2 weeks (e.g., every 2-16, 13-16, 14-16, 12-15, 12-14, 13-15, 13-14, or 14-15 days, or every 14 days), every 3 weeks (e.g., every 19-23, 20-23, 21-23, 19-22, 19-21, 20-22, 20-21, 21-22 days, or every 21 days), every 4 weeks (e.g., every 26-30, 27-30, 28-30, 26-29, 26-28, 27-29, 27-28, 28-29 days, or every 28 days), every 5 weeks (e.g., every 33-37, 34-37, 35-37, 34-36, 34-36, 35- 37, 36-37, 35-36 days, or every 35 days), or every 6 weeks (e.g., every 40-44, 40-43, 40-42, 40- 41, 41-44, 41-43, 41-42, 42-44, 42-43, 43-44 days, or every 42 days). In some embodiments, the binding agent is administered once every 3 weeks. In some embodiments, the binding agent is administered once every 21 days. In some embodiments, the binding agent is administered once every 6 weeks. In some embodiments, the binding agent is administered once every 42 days. [00404] In some embodiments of the method or use, the binding agent is administered over about 30 minutes, about 60 minutes, or about 90 minutes. In some embodiments of the method or use, the binding agent is administered over about 30 minutes at a dose of ≤ 600 mg (e.g., about 200 mg, about 300 mg, about 400 mg, about 500 mg, about 600 mg). In some embodiments of the method or use, the binding agent is administered over about 60 minutes at a dose of ≥ 600 mg (e.g., about 600 mg, about 800 mg, about 1000 mg, about 1200 mg, about 1400 mg, about 1600 mg, and about 1800 mg). In some embodiments of the method or use, the binding agent is administered over about 90 minutes at a dose of ≥ 1800 mg. [00405] In some embodiments of the method or use, the dose comprises a starting dose. In some embodiments of the method or use, the dose is modified relative to the starting dose. In some embodiments of the method or use, the dose is modified to be about two thirds of the starting dose. In some embodiments of the method or use, the dose is modified to be about one half of the starting dose. In some embodiments of the method or use, the dose is modified to be about one third of the starting dose. [00406] In some embodiments of the method or use, the binding agent is administered intravenously, subcutaneously, or intra-peritoneally. In some embodiments of the method or use, the binding agent is administered intravenously. [00407] In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 600 mg. In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 1200 mg. In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 600 mg, once every 3 weeks (e.g., every 21 days). In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 1200 mg, once every 3 weeks (e.g., every 21 days). In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 600 mg over about 30 minutes, once every 3 weeks (e.g., every 21 days). In some embodiments of the method or use, the binding agent is administered intravenously at a dose of about 1200 mg over about 60 minutes, once every 3 weeks (e.g., every 21 days). [00408] In some embodiments of the method or use, the binding agent is administered intravenously at a dose of between about 200 mg and about 1800 mg, once every 6 weeks (e.g., every 42 days). (b) Methods for Determining Receptor Occupancy [00409] In some embodiments, provided herein is a method for determining receptor occupancy, said method comprising the steps of: a. collecting a first sample (e.g., a blood sample or a tissue biopsy) from a subject treated with the binding agent or antibody of the present disclosure; b. contacting the first sample with a detection agent, wherein optionally the detection agent comprises an antibody or antigen binding fragment thereof, that binds at least one molecule of the binding agent or antibody of the present disclosure; c. collecting a second sample (e.g., a blood sample or a tissue biopsy) from the subject; d. contacting the second sample with the binding agent or antibody of the present disclosure ex vivo; e. contacting the second sample with the detection agent; and f. determining receptor occupancy by comparing the amount of detection agent in the first sample to the amount of detection agent in the second sample. [00410] In some embodiments, the receptor occupancy is determined between about 20 days and about 30 days after treating the subject with the binding agent or antibody. In some embodiments, the receptor occupancy is determined between 7 days and 21 days after treating the subject with the binding agent or antibody. In some embodiments, the receptor occupancy is determined 7 days, 14 days or 21 days after treating the subject with the binding agent or antibody. [00411] In some embodiments, provided herein is a method for determining receptor occupancy, said method comprising the steps of: a. collecting a sample (e.g., a blood sample or a tissue biopsy)from a subject treated with the binding agent or antibody of the present disclosure; b. contacting the sample (e.g., a blood sample or a tissue biopsy) with a first detection agent, wherein the detection agent comprises the binding agent or antibody of the present disclosure; c. contacting the sample (e.g., a blood sample or a tissue biopsy) with a second detection agent, wherein the second detection agent comprises an antibody or antigen binding fragment thereof, that binds at least one molecule of the binding agent or antibody of the present disclosure and the second detection agent does not compete with the first detection agent; and d. determining receptor occupancy by comparing the amount of first detection agent to the amount of second detection agent. [00412] In some embodiments, the receptor occupancy is determined between about 20 days and about 30 days after treating the subject with the binding agent or antibody. In some embodiments, the receptor occupancy is determined between 7 days and 21 days after treating the subject with the binding agent or antibody. In some embodiments, the receptor occupancy is determined 7 days, 14 days or 21 days after treating the subject with the binding agent or antibody. [00413] In certain embodiments, the sample is a peripheral blood sample. In certain embodiments, the sample is a tissue biopsy. In certain embodiments, the sample is a tumor biopsy. [00414] In certain embodiments, the sample is labeled with markers for certain cell types (e.g., immune cells, e.g., monocytes, myeloid derived suppressor cells (MDSCs), pan-myeloid cells, CD33+ myeloid cells). In certain embodiments, the sample is co-stained with competitive and non-competitive binding agents that bind to IL2 and/or IL4 to determine the receptor occupancy. [00415] In some embodiments of the method for determining receptor occupancy, the subject is treated with a single dose of the binding agent or antibody at between about 1 mg/kg and about 100 mg/kg. In some embodiments, the subject is treated with a single dose of the binding agent or antibody at between about 1 mg/kg and about 30 mg/kg, between about 5 mg/kg and about 30 mg/kg, between about 10 mg/kg and about 30 mg/kg, between about 15 mg/kg and about 30 mg/kg, between about 20 mg/kg and about 30 mg/kg, between about 25 mg/kg and about 30 mg/kg, between about 1 mg/kg and about 25 mg/kg, between about 5 mg/kg and about 25 mg/kg, between about 10 mg/kg and about 25 mg/kg, between about 15 mg/kg and about 25 mg/kg, between about 20 mg/kg and about 25 mg/kg, between about 1 mg/kg and about 20 mg/kg, between about 5 mg/kg and about 20 mg/kg, between about 10 mg/kg and about 20 mg/kg, between about 15 mg/kg and about 20 mg/kg between about 1 mg/kg and about 15 mg/kg, between about 5 mg/kg and about 15 mg/kg, between about 10 mg/kg and about 15 mg/kg, between about 1 mg/kg and about 10 mg/kg, or between about 5 mg/kg and about 10 mg/kg. In some embodiments, the subject is treated with a single dose of the binding agent or antibody at about 10 mg/kg. In some embodiments, the subject is treated with a single dose of the binding agent or antibody at about 20 mg/kg. In some embodiments, the subject is treated with a single dose of the binding agent or antibody at 4 mg/kg. In some embodiments, the dose is a body weight-based dose. [00416] In some embodiments of the method for determining receptor occupancy, the subject is treated with a single dose of between about 60 mg and about 1800 mg, between about 60 mg and about 1500 mg, between about 60 mg and about 1200 mg, between about 60 mg and about 900 mg, between about 60 mg and about 800 mg, between about 60 mg and about 600 mg, between about 60 mg and about 400 mg, between about 60 mg and about 200 mg, between about 200 mg and about 1800 mg, between about 200 mg and about 1500 mg, between about 200 mg and about 1200 mg, between about 200 mg and about 900 mg, between about 200 mg and about 800 mg, between about 200 mg and about 600 mg, between about 200 mg and about 400 mg, between about 400 mg and about 1800 mg, between about 400 mg and about 1500 mg, between about 400 mg and about 1200 mg, between about 400 mg and about 900 mg, between about 400 mg and about 800 mg, between about 400 mg and about 600 mg, between about 600 mg and about 1800 mg, between about 600 mg and about 1500 mg, between about 600 mg and about 1200 mg, between about 600 mg and about 900 mg, between about 800 mg and about 1800 mg, between about 800 mg and about 1500 mg, between about 800 mg and about 1200 mg, between about 800 mg and about 1000 mg, between about 900 mg and about 1800 mg, between about 900 mg and about 1500 mg, between about 900 mg and about 1200 mg, between about 1200 mg and about 1800 mg, or between about 1200 mg and about 1500 mg. In some embodiments, the subject is treated with a single dose of about 1 mg, about 3 mg, about 5 mg, about 6 mg, about 20 mg, about 60 mg, about 200 mg, about 600 mg, about 1200 mg, about 1500 mg, about 1800 mg, about 2100 mg, or about 2400 mg. In some embodiments, the subject is treated with a single dose of between about 400 mg and about 700 mg, between about 500 mg and about 800 mg, or between about 500 mg and about 700 mg. In some embodiments, the subject is treated with a single dose of about 600 mg. In some embodiments, the subject is treated with a single dose of between about 1000 mg and about 1300 mg, between about 1100 mg and about 1400 mg, or between about 1100 mg and about 1300 mg. In some embodiments, the subject is treated with a single dose of about 1200 mg. In some embodiments of the method or use, the dose is a flat dose. [00417] In some embodiments, at least one sample (e.g., a blood sample or a tissue biopsy) is collected prior to administration of the binding agent to the subject. In other embodiments, at least one sample (e.g., a blood sample or a tissue biopsy) is collected immediately following the end of infusion into the subject of the binding agent, or a 4 hours, 24 hours, 72 hours, 168 hours, or 336 hours following the end of infusion. In other embodiments, at least one sample (e.g., a blood sample or a tissue biopsy) is collected immediately prior to infusion of a second, third, fourth, or subsequent infusion into the subject of the binding agent. In specific examples, second and subsequent infusions of the binding agent are administered about 14 days, 21 days, 28 days, or 35 days after the previous infusion of binding agent. [00418] In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve between 1% and 99% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 1% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 5% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 15% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 20% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 25% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 30% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 35% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 40% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 45% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 50% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 55% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 60% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 65% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 70% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or is administered at a dose that achieves or can achieve at least 75% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 80% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 85% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 90% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 95% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 96% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 97% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 98% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least 99% receptor occupancy in immune cells. In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve 100% receptor occupancy in immune cells. [00419] In some embodiments, the binding agent or antibody is administered at a dose that achieves or can achieve at least about 95% (e.g., 95%, 96%, 97%, 98%, 99%, 100%) receptor occupancy in immune cells. In certain embodiment, the binding agent is administered at a dose that achieves at least about 95% of receptor occupancy in immune cells within 1 hour, within 2 hours, within 3 hours, within 4 hour, within 5 hour, within 6 hour, within 8 hour, within 10 hour, within 12 hour, within 14 hour, within 16 hour, within 18 hour, within 20 hour, within 22 hour, or within 24 hour of administration. In certain embodiment, the binding agent is administered at a dose that achieves at least about 95% of receptor occupancy in immune cells within 24 hours of administration. [00420] In certain embodiment, the binding agent is administered at a dose that achieves at least about 75% (e.g., at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or more) receptor occupancy in immune cells. In certain embodiment, the binding agent is administered at a dose that achieves at least about 75% receptor occupancy in immune cells 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, or 25 days after administration. In certain embodiment, the binding agent is administered at a dose that achieves at least about 75% receptor occupancy in immune cells 21 days after administration. In certain embodiment, the binding agent is administered at a dose that achieves at least about 75% receptor occupancy in immune cells 3 weeks after administration. [00421] In certain embodiments, the immune cells are monocytes. In certain embodiments, the immune cells are myeloid derived suppressor cells (MDSCs). In certain embodiments, the immune cells are pan-myeloid cells. In certain embodiments, the immune cells are CD33+ myeloid cells. [00422] In certain embodiments, the immune cells are B cells. In certain embodiments, the immune cells are T cells. In certain embodiments, the immune cells are natural killer cells. In certain embodiments, the immune cells are granulocytes. In certain embodiments, the immune cells are myeloid antigen presenting cells. 5.6. Pharmaceutical Compositions [00423] The present disclosure provides pharmaceutical compositions comprising an ILT- binding agent described herein and a pharmaceutically acceptable vehicle. The present disclosure also provides pharmaceutical compositions comprising an ILT2-binding agent described herein and a pharmaceutically acceptable vehicle. The present disclosure also provides pharmaceutical compositions comprising an ILT4-binding agent described herein and a pharmaceutically acceptable vehicle. The present disclosure also provides pharmaceutical compositions comprising an ILT2/ILT4-binding agent described herein and a pharmaceutically acceptable vehicle. [00424] Formulations are prepared for storage and use by combining a purified antibody or agent of the present disclosure with a pharmaceutically acceptable vehicle (e.g., a carrier or excipient). Those of skill in the art generally consider pharmaceutically acceptable carriers, excipients, and/or stabilizers to be inactive ingredients of a formulation or pharmaceutical composition. [00425] Suitable pharmaceutically acceptable vehicles include, but are not limited to, nontoxic buffers such as phosphate, citrate, and other organic acids; salts such as sodium chloride; antioxidants including ascorbic acid and methionine; preservatives such as octadecyldimethylbenzyl ammonium chloride, hexamethonium chloride, benzalkonium chloride, benzethonium chloride, phenol, butyl or benzyl alcohol, alkyl parabens, such as methyl or propyl paraben, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol; low molecular weight polypeptides (e.g., less than about 10 amino acid residues); proteins such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; carbohydrates such as monosaccharides, disaccharides, glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; metal complexes such as Zn-protein complexes; and non-ionic surfactants such as TWEEN or polyethylene glycol. (Remington: The Science and Practice of Pharmacy, 22 ^nd Edition, 2012, Pharmaceutical Press, London.). In some embodiments, the formulation is in the form of an aqueous solution. In some embodiments, the formulation is stored in a lyophilized or in an alternative dried form. [00426] The ILT-binding agents of the present disclosure can be formulated in any suitable form for delivery to a target cell/tissue. In some embodiments, the ILT-binding agent (e.g., the ILT2-binding agent, the ILT4-binding agent, or the ILT2/ILT4-binding agent) can be formulated as a liposome, microparticle, microcapsule, albumin microsphere, microemulsion, nanoparticle, nanocapsule, or macroemulsion. [00427] In some embodiments, an ILT-binding agent (e.g., the ILT2-binding agent, an ILT4- binding agent, or an ILT2/ILT4-binding agent) is formulated with liposomes. Methods to produce liposomes are known to those of skill in the art. For example, some liposomes can be generated by reverse phase evaporation with a lipid composition comprising phosphatidylcholine, cholesterol, and PEG-derivatized phosphatidylethanolamine (PEG-PE). [00428] In some embodiments, an ILT-binding agent (e.g., the ILT2-binding agent, an ILT4- binding agent, or an ILT2/ILT4-binding agent) is formulated as a sustained-release preparation. Suitable examples of sustained-release preparations include semi-permeable matrices of solid hydrophobic polymers containing an agent, where the matrices are in the form of shaped articles (e.g., films or microcapsules). Sustained-release matrices include but are not limited to polyesters, hydrogels such as poly(2-hydroxyethyl-methacrylate) or poly(vinyl alcohol), polylactides, copolymers of L-glutamic acid and 7 ethyl-L-glutamate, non-degradable ethylene- vinyl acetate, degradable lactic acid-glycolic acid copolymers such as the LUPRON DEPOT™ (injectable microspheres composed of lactic acid-glycolic acid copolymer and leuprolide acetate), sucrose acetate isobutyrate, and poly-D-(-)-3-hydroxybutyric acid. [00429] The pharmaceutical compositions or formulations of the present disclosure can be administered in any number of ways for either local or systemic treatment. Administration can be topical by epidermal or transdermal patches, ointments, lotions, creams, gels, drops, suppositories, sprays, liquids and powders; pulmonary by inhalation or insufflation of powders or aerosols, including by nebulizer, intratracheal, and intranasal; oral; or parenteral including intravenous, intraarterial, intratumoral, subcutaneous, intraperitoneal, intramuscular (e.g., injection or infusion), or intracranial (e.g., intrathecal or intraventricular). 5.7. Biomarkers [00430] The present disclosure further provides methods for predicting a subject’s responsiveness to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4 (e.g., a binding agent disclosed in Section 5.2 herein), where the subject (e.g., a human subject) has a cancer or a tumor. The present disclosure further provides methods for determining the efficacy of a therapy in a subject (e.g., a human subject) having a cancer or a tumor, where the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4 (e.g., a binding agent disclosed in Section 5.2 herein). It is based on the discovery that reduction of CD163 expression can be used as a biomarker for assessing efficacy and/or clinical benefits from the presently disclosed therapies (see e.g., Example 24). [00431] CD163 (Cluster of Differentiation 163) also known as M130, MM130, and SCARI1, is a protein that is encoded by the CD163 gene in human. CD163 functions as an innate immune sensor for gram-positive and gram-negative bacteria [00432] In certain embodiments, the present disclosure provides a method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, wherein the method comprises: comparing the expression level of CD163 in a sample obtained from the subject before receiving the therapy to a CD163 reference level, wherein the subject is identified as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. In certain embodiments, the method further comprises administering the therapy to the subject identified as more likely to respond to the therapy. [00433] In certain embodiments, the present disclosure provides a method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, where the method comprises: (a) measuring the expression level of CD163 in a sample obtained from the subject before receiving the therapy; (b) comparing the expression level of CD163 in (a) to a CD163 reference level; and (c) identifying the subject as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. In certain embodiments, the method further comprises administering the therapy to the subject identified as more likely to respond to the therapy. [00434] In certain embodiments, the present disclosure provides a method for treating a subject having a cancer or a tumor, comprising: (a) comparing the expression level of CD163 in a sample obtained from the subject before receiving a therapy to a CD163 reference level, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; and (b) administering the therapy to the subject if the expression level of CD163 is higher than the CD163 reference level. [00435] In certain embodiments, the present disclosure provides a method for treating a subject having a cancer or a tumor, comprising: (a) measuring the expression level of CD163 in a sample obtained from the subject before receiving a therapy, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; (b) comparing the expression level of CD163 to a CD163 reference level; and (c) administering the therapy to the subject if the expression level of CD163 is higher than the CD163 reference level. [00436] In another aspect, the present disclosure provides a method for selectively treating a cancer or a tumor in a subject identified to have a higher expression level of CD163 than a CD163 reference level, the method comprising administering a therapeutically effective amount of a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4 to said subject. [00437] In certain embodiments, the CD163 reference level is the expression level of CD163 in a sample from a healthy and/or non-diseased part of the body (e.g., tissue or cells) of the same subject. In certain embodiments, the CD163 reference level is the expression level of CD163 in a sample from the same subject collected prior to having the cancer or tumor. In certain embodiments, the CD163 reference level is the expression level of CD163 in a sample from a healthy or non-diseased subject. In certain embodiments, the CD163 reference level is the expression level of CD163 (e.g., a median or a mean value) in samples from healthy or non- diseased subjects. In certain embodiments, the CD163 reference level is a predetermined value based on the expression levels of CD163 in health or non-diseased populations. In certain embodiments, the sample for generating the CD163 reference level is from the same tissue (e.g., both are blood samples, liver samples, pancreas samples) as the sample of the subject having the cancer or tumor. [00438] In certain embodiments, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: comparing (a) the expression level of CD163 in a sample obtained from the subject before receiving the therapy and (b) the expression level of CD163 in a sample obtained from the subject after receiving the therapy, wherein the therapy is determined to be effective if the expression level of CD163 in (b) is reduced as compared to the expression level of CD163 in (a). In certain embodiments, the method further comprises continuing administering to the subject the therapy determined to be effective. [00439] In certain embodiments, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) measuring (i) the expression level of CD163 in a sample obtained from the subject before receiving the therapy, and (ii) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a- i) to the expression level of CD163 in (a-ii); and (c) determining the therapy is effective if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). In certain embodiments, the method further comprises continuing administering to the subject the therapy determined to be effective. [00440] In certain embodiments, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: comprises comparing (a) the expression level of CD163 in a sample obtained from the subject before receiving the therapy and (b) the expression level of CD163 in a sample obtained from the subject after receiving the therapy, wherein the therapy is determined to be not effective if the expression level of CD163 in (b) is not reduced (e.g., increased) as compared to the expression level of CD163 in (a). In certain embodiments, the method further comprises increasing the dose or dosing frequency of the binding agent where the therapy is determined to be not effective. [00441] In certain embodiments, the present disclosure provides a method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) measuring (i) the expression level of CD163 in a sample obtained from the subject before receiving the therapy, and (ii) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a- i) to the expression level of CD163 in (a-ii); and (c) determining the therapy is not effective if the expression level of CD163 in (a-ii) is not reduced (e.g., increased) as compared to the expression level of CD163 in (a-i). In certain embodiments, the method further comprises increasing the dose or dosing frequency of the binding agent where the therapy is determined to be not effective. [00442] The present disclosure further provides a method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: comparing (a) the expression level of CD163 in a sample obtained from the subject before receiving the therapy and (b) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; and continuing administering the therapy to the subject if the expression level of CD163 in (b) is reduced as compared to the expression level of CD163 in (a). [00443] The present disclosure further provides a method of treating a subject having a cancer or a tumor, comprising: (a) measuring (i) the expression level of CD163 in a sample obtained from the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a- i) to the expression level of CD163 in (a-ii); and (c) continuing administering the therapy to the subject if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). [00444] The present disclosure further provides a method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: comparing (a) the expression level of CD163 in a sample obtained from the subject before receiving the therapy and (b) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; and increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (b) is not reduced (e.g., increased) as compared to the expression level of CD163 in (a). [00445] The present disclosure further provides a method of treating a subject having a cancer or a tumor, comprising; (a) measuring (i) the expression level of CD163 in a sample obtained from the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample obtained from the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a- i) to the expression level of CD163 in (a-ii); and (c) increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (a-ii) is not reduced (e.g., increased) as compared to the expression level of CD163 in (a-i). [00446] In certain embodiments, the sample is a peripheral blood sample. In certain embodiments, the sample is a tissue biopsy. In certain embodiments, the sample is a tumor biopsy. In certain embodiments, the sample is a whole blood lysate. [00447] In certain embodiments, the sample comprises cells isolated from peripheral blood or a tissue biopsy (e.g., tumor biopsy) of the subject. In certain embodiments, the isolated cells are selected from the group consisting of monocytes, MDSCs, pan-myeloid cells, pan-dendritic cells, and combinations thereof. In certain embodiments, the monocytes are selected from the group consisting of classical monocytes (CD14 ⁺ CD16-), non-classical monocytes (CD14- CD16 ⁺ ), intermediate monocytes (CD14 ⁺ CD16 ⁺ ), and combinations thereof. In certain embodiments, the pan-myeloid cells are selected from the group consisting of CD11b ⁺ CD15- cells, CD19-HLA.DR ⁺ cells, CD3-CD19-CD56-CD15-cells, and combinations thereof. In certain embodiments, the pan dendritic cells are selected from the group consisting of D1 cells, D2 cells, and combinations thereof. In certain embodiments, the expression level of CD163 is a protein expression level of CD163. In certain embodiments, the expression level of CD163 is an mRNA expression level of CD163. [00448] Any suitable methods known in the art can be used with the presently disclosed subject matter for measuring the expression level of CD163. The protein expression level of CD163 can be measured by methods including, but not limited to, flow cytometry, immunohistochemistry, Western Blot, and enzyme-linked immunosorbent assay (ELISA). The mRNA expression level can be measured by methods including, but not limited to, PCR, qPCR, quantitative reverse- transcriptase PCR (RT-qPCR), microarray, Northern blot, and RNA sequencing. [00449] In certain embodiments, the therapy comprises a dosing regimen comprising administering to the subject multiple doses of the binding agent (e.g., a dosing regimen disclosed in Section V of the present disclosure). [00450] In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received one dose (e.g., a first dose) of the binding agent. In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received multiple doses (e.g., one, two, three, four, five, six, or more doses) of the binding agent. [00451] In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received a first dose of the binding agent. In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received a second dose of the binding agent. [00452] In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained between 1 day and 40 days after the subject received a dose (e.g., a first dose) of the binding agent. In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained from the subject between 15 days and 36 days after the subject receiving a dose (e.g., a first dose) of the binding agent. In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained from the subject between 15 days after the subject receiving the first dose and 15 days after the subject receiving the second dose (e.g., between 15 days and 36 days after the subject receiving a first dose of the binding agent when the agent is administered once every 21 days). [00453] In certain embodiments, the sample obtained from the subject after receiving the therapy is a sample obtained at least 7 days (e.g., 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 31 days, 32 days, 33 days, 34 days, 35 days, 36 days, 37 days, 38 days, 39 days, 40 days, or more) after the subject received a dose (e.g., a first dose) of the binding agent. [00454] In certain embodiments, the sample obtained from the subject before receiving the therapy is a sample obtained from the subject before receiving any dose of the binding agent. In certain embodiments, the sample obtained from the subject before receiving the therapy is a sample obtained from the subject before receiving a first dose of the binding agent. In certain embodiments, the sample obtained from the subject before receiving the therapy is a sample obtained from the subject before receiving a dose of the binding agent but after the subject has received a prior dose of the binding agent. [00455] In certain embodiments, the subject is a human subject. In certain embodiments, the subject having a cancer selected from the group consisting of hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple-negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, and prostate cancer. In certain embodiments, the subject having a tumor selected from the group consisting of a hepatocellular carcinoma, a small cell lung tumor, a thyroid tumor, a mesothelioma, a glioblastoma, a renal cell carcinoma, a non-small cell lung tumor, a melanoma (skin cutaneous and uveal), a pancreatic ductal adenocarcinoma, a gastric tumor, a squamous cell carcinoma of the head and neck, a biliary duct tumor, a breast tumor, a triple-negative breast tumor, an ovarian tumor, a cervical tumor, an endocervical tumor, a colorectal tumor, an esophageal tumor, a gastroesophageal junction adenocarcinoma, a squamous cell carcinoma of head and neck, a bladder tumor, an uterine tumor, a cholangiocarcinoma, or a prostate tumor. 6. EMBODIMENTS [00456] The present disclosure provide the following non-limiting embodiments: 1. A method of treating cancer in a subject, the method comprising administering to the subject a therapeutically effective amount of (a) a binding agent comprising (i) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145; or (ii) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:143; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:142; wherein the binding agent is administered at a dose of between about 200 mg and about 1800 mg. 2. The method of embodiment 1, wherein the cancer is hepatocellular carcinoma, small cell lung cancer, thyroid cancer, mesothelioma, glioblastoma, renal cell carcinoma, non-small cell lung cancer, melanoma (skin cutaneous and uveal), pancreatic ductal adenocarcinoma, gastric cancer, squamous cell carcinoma of the head and neck, biliary duct cancer, breast cancer, triple- negative breast cancer, ovarian cancer, cervical cancer, endocervical cancer, colorectal cancer, esophageal cancer, gastroesophageal junction adenocarcinoma, squamous cell carcinoma of head and neck, bladder cancer, uterine cancer, cholangiocarcinoma, or prostate cancer. 3. The method of embodiment 1 or 2, wherein the cancer is a microsatellite instability – high (MSI-H) tumor or a deficient mismatch repair (dMMR) positive tumor. 4. The method of any one of embodiments 1-3, wherein the binding agent is administered at a dose of about 600 mg. 5. The method of any one of embodiments 1-3, wherein the binding agent is administered at a dose of about 1200 mg. 6. The method of any one of embodiments 1-3, wherein the binding agent is administered at a dose of about 1800 mg. 7. The method of any one of embodiments 1-6, wherein the binding agent is administered at a dose that achieves at least about 95% of receptor occupancy in immune cells within 24 hours of administration. 8. The method of any one of embodiments 1-7, wherein the binding agent is administered at a dose that achieves at least about 75% receptor occupancy in immune cells three weeks after administration. 9. The method of embodiment 7 or 8, wherein the immune cells are selected from the group consisting of granulocytes, myeloid antigen presenting cells, natural killer cells, monocytes, CD33 ⁺ myeloid cells, T cells, and B cells. 10. The method of any one of embodiments 1-9, wherein the binding agent is administered once every week, 2 weeks, 3 weeks, or 4 weeks. 11. The method of embodiment 10, wherein the binding agent is administered once every 3 weeks. 12. The method of any one of embodiments 1-11, wherein the binding agent is administered over about 30 minutes, about 60 minutes or about 90 minutes. 13. The method of any one of embodiments 1-3, wherein the binding agent is administered over about 30 minutes at a dose of ≤ 600 mg. 14. The method of any one of embodiments 1-3, wherein the binding agent is administered over about 60 minutes at a dose of ≥ 600 mg. 15. The method of any one of embodiments 1-14, wherein the binding agent is administered intravenously. 16. The method of any one of embodiments 1-3, wherein the binding agent is administered intravenously at a dose of about 600 mg once every 3 weeks. 17. The method of any one of embodiments 1-3, wherein the binding agent is administered intravenously at a dose of about 1200 mg once every 3 weeks. 18. The method of any one of embodiments 1-3, wherein the binding agent is administered intravenously at a dose of about 1800 mg once every 3 weeks. 19. The method of any one of embodiments 1-18, wherein: (1) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:115, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (2) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (3) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:76, the VH-CDR2 having the amino acid sequence of SEQ ID NO:113, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (4) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:114, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; or (5) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:116, the VH-CDR2 having the amino acid sequence of SEQ ID NO:124, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:110; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:99, the VL-CDR2 having the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:101. 20. The method of any one of embodiments 1-18, wherein: (1) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8A; or (2) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8B. 21. The method of any one of embodiments 1-18, wherein: (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:145; or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:144 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:145. 22. The method of any one of embodiments 1-18, wherein (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145. 23. The method of any one of embodiments 1-18 and 20, wherein (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142. 24. The method of any one of embodiments 1-18 and 20, wherein (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142. 25. A method for: (a) inhibiting tumor growth in a subject; (b) increasing or enhancing an immune response to a tumor or tumor cells in a subject; (c) activating or enhancing a persistent or long-term immune response to a tumor or tumor cells in a subject; (d) inhibiting tumor relapse or tumor regrowth in a subject; or (e) inducing a persistent or long-term immunity that inhibits tumor relapse or tumor regrowth in a subject; the method comprising administering to the subject a therapeutically effective amount of a binding agent comprising (i) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145; or (ii) a heavy chain variable region comprising a heavy chain variable region CDR1 (VH-CDR1), a heavy chain variable region CDR2 (VH-CDR2), and a heavy chain variable region CDR3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:143; and a light chain variable region comprising a light chain variable region CDR1 (VL-CDR1), a light chain variable region CDR2 (VL-CDR2), and a light chain variable region CDR3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:142; wherein the binding agent is administered at a dose of between about 200 mg and about 1800 mg. 26. The method of embodiment 25, wherein: (1) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:115, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (2) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:112, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (3) the heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:76, the VH-CDR2 having the amino acid sequence of SEQ ID NO:113, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; (4) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:111, the VH-CDR2 having the amino acid sequence of SEQ ID NO:114, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:107; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:89, the VL-CDR2 having the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:91; or (5) a heavy chain variable region of the binding agent comprises the VH-CDR1 having the amino acid sequence of SEQ ID NO:116, the VH-CDR2 having the amino acid sequence of SEQ ID NO:124, and the VH-CDR3 having the amino acid sequence of SEQ ID NO:110; and the light chain variable region of the binding agent comprises the VL-CDR1 having the amino acid sequence of SEQ ID NO:99, the VL-CDR2 having the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 having the amino acid sequence of SEQ ID NO:101. 27. The method of embodiment 25, wherein: (1) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8A; or (2) the heavy chain variable region of the binding agent comprises the VH-CDR1, the VH-CDR2, the VH-CDR3, the VL-CDR1, the VL-CDR2, and the VL-CDR3 comprising amino acid sequences of any one of the five CDR definitions set forth in Table 8B. 28. The method of embodiment 25 or 26, wherein: (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence set forth in SEQ ID NO:145; or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:144 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to SEQ ID NO:145. 29. The method of embodiment 25 or 26, wherein (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:144 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:145. 30. The method of embodiment 25 or 27, wherein (a) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises an amino acid sequence having at least 80% sequence identity to the sequence of SEQ ID NO:142. 31. The method of embodiment 25 or 27, wherein (a) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143; (b) the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142; and/or (c) the heavy chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:143 and the light chain variable region of the binding agent comprises the amino acid sequence of SEQ ID NO:142. 32. The method of any one of embodiments 25-31, wherein the tumor comprises a microsatellite instability – high (MSI-H) tumor or a deficient mismatch repair (dMMR) positive tumor. 33. The method of any one of embodiments 25-32, wherein the tumor is a hepatocellular carcinoma, a small cell lung tumor, a thyroid tumor, a mesothelioma, a glioblastoma, a renal cell carcinoma, a non-small cell lung tumor, a melanoma (skin cutaneous and uveal), a pancreatic ductal adenocarcinoma, a gastric tumor, a squamous cell carcinoma of the head and neck, a biliary duct tumor, a breast tumor, a triple-negative breast tumor, an ovarian tumor, a cervical tumor, an endocervical tumor, a colorectal tumor, an esophageal tumor, a gastroesophageal junction adenocarcinoma, a squamous cell carcinoma of head and neck, a bladder tumor, an uterine tumor, a cholangiocarcinoma, or a prostate tumor. 34. The method of any one of embodiments 1-33, wherein the binding agent is (a) an antibody; (b) a recombinant antibody; (c) an antibody fragment comprising at least one antigen-binding site; (d) a chimeric antibody; (e) a humanized antibody; (f) a bispecific or multispecific antibody; or (g) attached to a half-life extending moiety. 35. The method of embodiment 34, wherein the binding agent is an IgG1 antibody, an IgG2 antibody, or an IgG4 antibody; optionally wherein the binding agent is a human IgG1 antibody, a human IgG2 antibody, or a human IgG4 antibody; further optionally the human IgG1 antibody has reduced or no effector function. 36. The method of embodiment 34 or 35, wherein the binding agent comprises a kappa light chain or a lambda light chain, optionally wherein the antibody comprises a human kappa light chain or a human lambda light chain. 37. The method of embodiment 34, the antibody fragment is a Fab, a Fab’, a F(ab’)2, a Fv, a scFv, a (scFv)2, a single chain antibody, a dual variable region antibody, a diabody, or a nanobody. 38. The method of any one of embodiments 1-37, wherein the binding agent comprises a heavy chain comprising an amino acid sequence with 80% identity to the sequence of SEQ ID NO:156 and a light chain comprising an amino acid sequence with 80% identity to the sequence of SEQ ID NO:157. 39. The method of embodiment 38, wherein the binding agent comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:156 and a light chain comprising the amino acid sequence of SEQ ID NO:157. 40. The method of any one of embodiments 1-39, wherein the binding agent has one or more of the following properties: (1) binds rhesus ILT2; (2) binds cyno ILT2; (3) does not bind ILT3, ILT5, and LILRB5; (4) does not bind LILRA2, LILRA4, LILRA5, and LILRA6; (5) is an ILT2 antagonist; (6) is an ILT4 antagonist, (7) inhibits ILT2 activity; (8) inhibits ILT4 activity; (9) inhibits ILT2 signaling in cells that express ILT2; (10) inhibits ILT4 signaling in cells that express ILT4; (11) inhibits binding of ILT2 to MHC I molecules; (12) inhibits binding of ILT4 to MHC I molecules; (13) inhibits ILT2-induced suppression of myeloid cells; (14) inhibits ILT4-induced suppression of myeloid cells; (15) inhibits ILT2-induced suppression of myeloid cell activity; (16) inhibits ILT4-induced suppression of myeloid cell activity; (17) restores FcR activation in myeloid cells; (18) enhances NK cell activity; (19) enhances CTL activity; (20) enhances macrophage phagocytosis; and (21) inhibits MDSC mediated suppression of immune cells. 41. The method of embodiments 1-40, wherein the subject is a human. 42. A method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, the method comprising comparing the expression level of CD163 in a sample of the subject before receiving the therapy to a CD163 reference level, wherein the subject is identified as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. 43. A method for identifying a subject having a cancer or a tumor as more likely to respond to a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, the method comprising: (a) measuring the expression level of CD163 in a sample of the subject before receiving the therapy; (b) comparing the expression level of CD163 in (a) to a CD163 reference level; and (c) identifying the subject as more likely to respond to the therapy if the expression level of CD163 is higher than the CD163 reference level. 44. A method for selectively treating a cancer or a tumor in a subject identified to have a higher expression level of CD163 than a CD163 reference level, the method comprising administering a therapeutically effective amount of a binding agent specifically binding to human ILT2 and/or human ILT4 to the subject. 45. A method for treating a subject having a cancer or a tumor, comprising: (a) comparing the expression level of CD163 in a sample of the subject before receiving a therapy to a CD163 reference level, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; and (b) administering a therapeutically effective amount of the binding agent to the subject if the expression level of CD163 is higher than the CD163 reference level. 46. A method for treating a subject having a cancer or a tumor, comprising: (a) measuring the expression level of CD163 in a sample obtained from the subject before receiving a therapy, wherein the therapy comprises a binding agent specifically binding to human ILT2 and/or human ILT4; (b) comparing the expression level of CD163 to a CD163 reference level; and (c) administering the therapy to the subject if the expression level of CD163 is higher than the CD163 reference level. 47. The method of any one of embodiments 42-46, wherein the CD163 reference level is the expression level of CD163 in a sample from a healthy or non-diseased subject, or the expression level of CD163 in samples from a population of healthy or non-diseased subjects, wherein the sample from the healthy or non-diseased subject or the samples from a population of healthy or non-diseased subjects are from the same source as the sample from the subject having the cancer or tumor. 48. A method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, the method comprising comparing (a) the expression level of CD163 in a sample of the subject before receiving the therapy and (b) the expression level of CD163 in a sample of the subject after receiving the therapy, wherein the therapy is determined to be effective if the expression level of CD163 in (b) is reduced as compared to the expression level of CD163 in (a). 49. A method for determining the efficacy of a therapy in a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, the method comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving the therapy, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) determining the therapy is effective if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). 50. A method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) comparing (i) the expression level of CD163 in a sample of the subject before receiving the therapy and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; and (b) continuing administering the therapy to the subject if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). 51. A method of treating a subject having a cancer or a tumor, comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) continuing administering the therapy to the subject if the expression level of CD163 in (a-ii) is reduced as compared to the expression level of CD163 in (a-i). 52. A method of treating a subject having a cancer or a tumor, wherein the therapy comprises a binding agent that specifically binds to human ILT2 and/or human ILT4, and the method comprises: (a) comparing (i) the expression level of CD163 in a sample of the subject before receiving the therapy and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; and (b) increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (a-ii) is not reduced as compared to the expression level of CD163 in (a-i). 53. A method of treating a subject having a cancer or a tumor, comprising: (a) measuring (i) the expression level of CD163 in a sample of the subject before receiving a therapy comprising a binding agent specifically binding to human ILT2 and/or human ILT4, and (ii) the expression level of CD163 in a sample of the subject after receiving the therapy; (b) comparing the expression level of CD163 in (a-i) to the expression level of CD163 in (a-ii); and (c) increasing the dose or dosing frequency of the binding agent if the expression level of CD163 in (a-ii) is not reduced as compared to the expression level of CD163 in (a-i). 54. The method of any one of embodiments 42-53, wherein the sample is a peripheral blood sample or a tumor biopsy. 55. The method of any one of embodiments 42-54, wherein the sample comprises cells isolated from peripheral blood or a tumor biopsy of the subject. 56. The method of embodiment 55, wherein the isolated cells are selected from the group consisting of monocytes, MDSCs, pan-myeloid cells, pan-dendritic cells, and combinations thereof. 57. The method of any one of embodiments 42-56, wherein the expression level of CD163 is a protein expression level of CD163. 58. The method of embodiment 57, wherein the protein expression level is measured by flow cytometry, immunohistochemistry, Western Blot, or enzyme-linked immunosorbent assay (ELISA). 59. The method of any one of embodiments 42-56, wherein the expression level of CD163 is an mRNA expression level of CD163. 60. The method of embodiment 59, wherein the mRNA expression level is measured by quantitative reverse-transcriptase PCR (RT-qPCR), microarray, Northern blot, or RNA sequencing. 61. The method of any one of embodiments 48-60, wherein the sample obtained from the subject after receiving the therapy is a sample obtained after the subject received one dose or multiple doses of the binding agent. 62. The method of any one of embodiments 48-61, wherein the sample obtained from the subject after receiving the therapy is a sample obtained from the subject between 15 days after the subject received a first dose of the binding agent and 15 days after the subject received a second dose of the binding agent. 63. The method of any one of embodiments 48-62, wherein the antigen-binding domain binds specifically to both human ILT2 and human ILT4 and comprises a heavy chain variable region (VH) comprising a heavy chain complementarity-determining region 1 (VH-CDR1), a heavy chain complementarity-determining region 2 (VH-CDR2), and a heavy chain complementarity-determining region 3 (VH-CDR3) from the amino acid sequence of SEQ ID NO:144; and a light chain variable region (VL) comprising a light chain complementarity- determining region 1 (VL-CDR1), a light chain complementarity-determining region 2 (VL- CDR2), and a light chain complementarity-determining region 3 (VL-CDR3) from the amino acid sequence of SEQ ID NO:145. 64. The method of embodiment 63, wherein: (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:115, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:113, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:114, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:116, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:124, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101. 65. The method of embodiment 63 or 64, wherein (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:144, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:145; or (b) the VH comprises the amino acid sequence of SEQ ID NO:144, and/or the VL comprises the amino acid sequence of SEQ ID NO:145. 66. The method of any one of embodiments 63-65, wherein the antigen-binding domain comprises (a) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:156, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:157; or (b) a heavy chain comprising the amino acid sequence of SEQ ID NO:156, and/or a light chain comprising the amino acid sequence of SEQ ID NO:157. 67. The method of any one of embodiments 48-62, wherein the antigen-binding domain binds specifically to both human ILT2 and human ILT4 and comprises: (i) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:139; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:140; (ii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:133; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:134; (iii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:143; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:142; (iv) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:131; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:132; (v) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:137; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:138; (vi) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:135; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:136; or (vii) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:141; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:142. 68. The method of embodiment 67, wherein (i) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:139; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:140, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:123, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:105, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (ii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:133; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:134, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:118, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:118, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:119, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:120, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:121, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:82, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:83, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:122, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:85; or (iii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:143; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:142, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:115, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:112, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:113, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:111, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:114, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:116, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:117, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (iv) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:131; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:132, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:71, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:71, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:77, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:78, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:72, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:73, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:74, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:75; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:81, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:82, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:83, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:84, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:85; or (v) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:137; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:138, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:102, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:103, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:104, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:105, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (vi) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:135; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:136, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:95, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:87, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:92, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:93, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:86, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:94, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:88, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:96, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:97, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:98, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101; or (vii) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:141; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:142, and wherein (a) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:79, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:106, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (b) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:106, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (c) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:76, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:77, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; (d) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:70, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:108, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:107, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:89, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:90, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:91; or (e) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:80, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:109, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:110, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:99, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:100, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:101. 69. The method of embodiment 67 or 68, wherein (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:139, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:140; or the VH comprises the amino acid sequence of SEQ ID NO:139, and/or the VL comprises the amino acid sequence of SEQ ID NO:140, (b) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:133, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:134; or the VH comprises the amino acid sequence of SEQ ID NO:133, and/or the VL comprises the amino acid sequence of SEQ ID NO:134, (c) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:143, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142; or the VH comprises the amino acid sequence of SEQ ID NO:143, and/or the VL comprises the amino acid sequence of SEQ ID NO:142, (d) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:131, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:132; or the VH comprises the amino acid sequence of SEQ ID NO:131, and/or the VL comprises the amino acid sequence of SEQ ID NO:132, (e) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:137, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:138; or the VH comprises the amino acid sequence of SEQ ID NO:137, and/or the VL comprises the amino acid sequence of SEQ ID NO:138, (f) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:135, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:136; or the VH comprises the amino acid sequence of SEQ ID NO:135, and/or the VL comprises the amino acid sequence of SEQ ID NO:136, or (g) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:141, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:142; or the VH comprises the amino acid sequence of SEQ ID NO:141, and/or the VL comprises the amino acid sequence of SEQ ID NO:142. 70. The method of any one of embodiments 67-69, wherein the antigen-binding domain comprises: (a) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:148, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:149; (b) a heavy chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:152, and/or a light chain comprising an amino acid sequence having at least 80% sequence identity to the amino acid sequence of SEQ ID NO:153; (c) a heavy chain comprising the amino acid sequence of SEQ ID NO:148, and/or a light chain comprising the amino acid sequence of SEQ ID NO:149; or (d) a heavy chain comprising the amino acid sequence of SEQ ID NO:152, and/or a light chain comprising the amino acid sequence of SEQ ID NO:153. 71. The method of any one of embodiments 48-62, wherein the antigen-binding domain binds specifically to human ILT2 and comprises a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:125; and a VL comprising a VL- CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:126. 72. The method of embodiment 71, wherein: (i) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:31, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:23, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (ii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:22, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:23, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (iii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:28, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:29, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:22, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:30, the VH-CDR3 the amino acid sequence of SEQ ID NO:24, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:25, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:26, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:27; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:32, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:33, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:34, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:35, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:36, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:37. 73. The method of embodiment 71 or 72, wherein: (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:125, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:126; or (b) the VH comprises the amino acid sequence of SEQ ID NO:125, and/or the VL comprises the amino acid sequence of SEQ ID NO:126. 74. The method of any one of embodiments 48-62, wherein the antigen-binding domain binds specifically to human ILT4 and comprises: (a) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:129; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:130; or (b) a VH comprising a VH-CDR1, a VH-CDR2, and a VH-CDR3 from the amino acid sequence of SEQ ID NO:127; and a VL comprising a VL-CDR1, a VL-CDR2, and a VL-CDR3 from the amino acid sequence of SEQ ID NO:128. 75. The method of embodiment 74, wherein: (a) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:129; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:130, and wherein (i) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:63, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:55, and the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56,the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (ii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:54, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:55, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (iii) the VH comprises the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:60, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:61, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:54, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:62, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:56, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:57, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:58, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:59; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:64, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:65, and the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:66, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:67, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:68, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:69; or (b) the VH comprises the VH-CDR1, the VH-CDR2, and the VH-CDR3 from the amino acid sequence of SEQ ID NO:127; and the VL comprises the VL-CDR1, the VL-CDR2, and the VL-CDR3 from the amino acid sequence of SEQ ID NO:128, and wherein (i) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:47, the VH- CDR2 comprises the amino acid sequence of SEQ ID NO:39, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (ii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:38, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:39, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (iii) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:44, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:45, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; (iv) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:38, the VH-CDR2 comprising the amino acid sequence of SEQ ID NO:46, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:40, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:41, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:42, and the VL-CDR3 comprises the amino acid sequence of SEQ ID NO:43; or (v) the VH-CDR1 comprises the amino acid sequence of SEQ ID NO:48, the VH-CDR2 comprises the amino acid sequence of SEQ ID NO:49, the VH-CDR3 comprises the amino acid sequence of SEQ ID NO:50, the VL-CDR1 comprises the amino acid sequence of SEQ ID NO:51, the VL-CDR2 comprises the amino acid sequence of SEQ ID NO:52, and the VL-CDR3 comprises an amino acid sequence of SEQ ID NO:53. 76. The method of embodiment 74 or 75, wherein: (a) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:129, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:130; (b) the VH has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:127, and/or the VL has at least 80% sequence identity to the amino acid sequence of SEQ ID NO:128; (c) the VH comprises the amino acid sequence of SEQ ID NO:129, and/or the VL comprises the amino acid sequence of SEQ ID NO:130; or (d) the VH comprises the amino acid sequence of SEQ ID NO:127, and/or the VL comprises the amino acid sequence of SEQ ID NO:128. 7. EXAMPLES 7.1 Example 1: Generation of Antibodies and Screening of Antibodies [00457] Anti-ILT antibodies were generated using the extracellular domain of human ILT2, the extracellular domain of human ILT4, and/or the extracellular domain of rhesus ILT2 as the immunogen. For examples, anti-ILT2 antibodies were generated using the extracellular domain of human ILT2. Similarly, anti-ILT4 antibodies were generated using the extracellular domain of human ILT4. Anti-ILT2/ILT4 antibodies were generated using a mixture of the extracellular domain of human ILT2, the extracellular domain of human ILT4, and the extracellular domain of rhesus ILT2. Single cell suspensions of lymphocytes were obtained from the spleens and lymph nodes of immunized mice after the individual animals had been determined to have suitable antibody titers. Lymphocytes were fused with murine myeloma cells by standard methods. Hybridoma fusions were plated onto semi-solid media for HAT selection. After 5-7 days, single colonies were selected using a ClonePix™ system and plated into 96-well plates. [00458] ELISA assays were used to screen antibodies against human ILT2, human ILT4, and rhesus ILT2. Antibodies that bound to human ILT2 only, human ILT4 only, or human ILT2, human ILT4 and rhesus ILT2 were selected. 7.2 Example 2: Synteny Between Human and Cynomolgus Monkey ILT2 and ILT4 Genes [00459] In rodents, paired Ig-like receptor B (PirB) and gp49B1 have been described as the potential orthologues of human LILRB family of receptors (Kang X, et al. Cell Cycle. (2016);15(1):25-40). However, PirB and gp49B1 show less than 50% identity to both human ILT2 and human ILT4. Further, marked differences exist in the receptor/ligand pairing among the rodent and human LILRB family members and the biological function of the rodent receptors are unclear. Thus, rodents are not considered relevant species to test the biological effects of anti-ILT antibodies. [00460] An analysis of genomic structure (synteny) was used to identify candidate orthologs of both human ILT2 and ILT4 in cynomolgus monkey. The genomic organization of the locus that contains the LILR family members in human (hg38) and cynomolgus monkey (Macaca fascicularis v5.0.95, “cyno”) were compared using the gene annotations provided by Ensembl. In cases where annotations were not found, manual analysis of the intervening sequence was used to confirm lack of an open reading frame. The predicted protein sequence of genes in cynomolgus monkey without pre-annotated gene symbols was compared to all human genes using blastp tools on UniProt to find the most likely human ortholog based on the identity score. [00461] It was found that the cynomolgus monkey genomic organization is missing a gene at the same genome location as human LILRB2 (ILT4), while retaining a gene at the same location as human LILRB1 (ILT2). A similar organization was observed with rhesus macaque. The sequence identity between human ILT2, human ILT4 and cyno ILT2 ranges from 73%-80%. The sequence identity between human ILT2 and cyno ILT2 is 73%, while sequence identity between human ILT4 and cyno ILT2 is 78%. In comparison, the sequence identity between human ILT2 and human ILT4 is 80%. 7.3 Example 3: Binding Characteristics of Anti-human ILT2, ILT4, and ILT2/ILT4 Antibodies [00462] The binding affinities of anti-ILT2 and anti-ILT4 antibodies were measured using a Biacore system (GE Healthcare LifeSciences). Equilibrium dissociation constant (K _D ) measurements were carried out with purified antibodies to evaluate their binding to human ILT2, human ILT4, and rhesus ILT2. Briefly, purified anti-ILT2 antibody 27F9, anti-ILT4 antibodies 47C8 and 48A5, and anti-ILT2/ILT4 antibodies 47H6, 51A1, 64A12, 73C4, and 73D1 were captured on a Sensor Chip Protein A (GE HealthCare). The surface of the Biacore Sensor Chip Protein A consists of a carboxymethylated dextran matrix with a recombinant Protein A variant covalently attached. Soluble human ILT2-ECD, human ILT4-ECD, or rhesus ILT2-ECD were injected at a flow rate of 30 µL/min at 25°C. The ILT2 or ILT4 proteins were used at concentrations ranging from 1.6 - 200 nM in PBS-P buffer with 2 fold dilutions. Kinetic data were collected over time and fit using the simultaneous global fit equation to yield affinity constants (K _D values) for each antibody. [00463] Binding data is shown in Tables 9A and 9B. Table 9A 1 - Binding assay was performed under low resolution parameters Table 9B 1 - Binding assay was performed under low resolution parameters 7.4 Example 4: Sequence Analyses of Anti-ILT2, Anti-ILT4, and Anti-ILT2/ILT4 Antibodies [00464] Representative anti-ILT2 antibody 27F9, anti-ILT4 antibodies 47C8 and 48A5, and anti-ILT2/ILT4 antibodies 47H6, 51A1, 64A12, 73C4, and 73D1 were sequenced and the VH and VL amino acid sequences are disclosed herein and summarized in Table 10. Table 10 [00465] The heavy chain and VL-CDRs for the individual antibodies are disclosed in Tables 1- 8 and as SEQ ID NOs:22-124. 7.5 Example 5: Generation of Humanized Antibodies [00466] Several of the anti-ILT2/ILT4 antibodies, i.e., 47H6, 64A12, and 73D1, were humanized by methods known to those skilled in the art. These humanized antibodies are referred to herein as Hz47H6.v2, Hz64A12, and Hz73D1.v1, respectively. During the humanization process for antibody 47H6, the VH-CDR2 was modified from DFNPNNGGTTYNQKFEG (SEQ ID NO:71) to DFNPNNAGTTYNQKFEG (SEQ ID NO:118). The VH sequence of Hz47H6.v2 is SEQ ID NO:133 and the VL sequence of Hz47H6.v2 is SEQ ID NO:134; the VH sequence of Hz64A12 is SEQ ID NO:139 and the VL sequence of Hz64A12 is SEQ ID NO:140; and the VH sequence of Hz73D1.v1 is SEQ ID NO:144 and the VL sequence of Hz73D1.v1 is SEQ ID NO:145. [00467] The binding affinities of the humanized antibodies to human ILT2 and human ILT4 were measured using a Biacore system as described herein. The binding affinities of antibodies Hz47H6.v2, Hz64A12, and Hz73D1.v1 are shown in Table 11 as compared with the parental antibodies. Table 11 1 - Binding assay was performed under low resolution parameters [00468] These results demonstrated that the humanization process for exemplary anti- ILT2/ILT4 antibodies did not have a significant effect on the antibodies’ binding capabilities to human ILT2 or human ILT4. [00469] Cross-reactivity of humanized anti-ILT2/ILT4 antibodies with cynomolgus monkey (“cyno”, Macaca fascicularis) ILT2 were also assayed. Similar to anti-ILT2/ILT4 antibodies, humanized anti-ILT2/ILT4 antibodies bind to cyno ILT2. Binding affinities of an exemplary clone Hz73D1.v1 measured by a Biacore system are shown in Table 12. In the Biacore system, a humanized anti-ILT2/ILT4 antibody was captured on a Protein A chip. ILT proteins were injected at different concentrations into the flow cells to evaluate kinetic parameters at 25°C. The binding affinity (KD) of Hz73D1.v1 to human ILT2 and ILT4 was determined to be 1.03 and 0.205 nM, respectively. The KD of Hz73D1.v1 to cyno ILT2 was determined to be 19.1 nM. Table 12 Species of ILT KD (nM) kon (1/Ms) koff (1/s) Human ILT2 1.03 4.72 × 10 ⁴ 4.85 × 10 ^-5 Human ILT4 0.205 2.2 × 10 ⁵ 4.6 × 10 ^-5 Cynomolgus monkey ILT2 19.1 3.4 × 10 ⁶ 0.06 7.6 Example 6: ILT2 and ILT4 Expression in Subsets of Immune Cells [00470] ILT2 and ILT4 expression has been described on various cells of hematopoietic origin, including myeloid cells, granulocytes, and lymphocytes (Colonna M et al. J Exp Med. (1997) Dec 1; 186(11): 1809–1818; Colonna M et al., J Immunol (1998), 160(7): 3096-3100). Anti-ILT antibodies described herein were used to further elucidate the expression of ILT2 and ILT4 on subsets of human and cyno immune cells. [00471] Flow cytometry analysis of blood immune cells was performed on human and cyno PBMC and whole blood. PBMC were prepared from a leukopak (Allcells Inc.) by centrifugation through ficoll, washing with PBS and freezing in cryopreservation buffer in liquid nitrogen until use. Whole blood (Allcells Inc.) was obtained fresh and red blood cells (RBC) depleted using ammonium chloride RBC lysing solution (Biolegend). PBMC or whole blood samples were stained with a fluorescently labeled antibody panel to distinguish various immune subsets (monocytes, B cells, NK cells, CD4+ and CD8+ T cells, neutrophils and eosinophils). Samples were further stained with fluorescently labeled isotype, 27F9 (ILT2 specific), 48A5 (ILT4 specific), 73D1, and Hz73D1.v1. The number of ILT2 and ILT4 molecules per cell of each immune subset was estimated by incubation with Quantum Simply Cellular microspheres followed by flow cytometry analysis. [00472] As shown in Table 13 and Figure 1, high expression of ILT2 was observed on monocytes, B cells, a subset of NK cells (5-20% total NK cells), and a subset of CD8+ T cells (5-20% total CD8+ T cells). High expression of ILT4 was observed on monocytes, eosinophils and neutrophils. The results showed that cynomolgus monkey peripheral immune cells expressed ILT2 protein with a level of expression and immune cell distribution comparable with the combination of ILT2 and ILT4 in human peripheral blood. Table 13 CD8 NK Cell T Cell Antigen Monocyte Neutrophil B Cell (Subset) (Subset) Human ILT2 5.0 × 10 ⁴ 0 2.0 × 10 ⁴ 4.0 × 10 ³ 5.5 × 10 ³ Human ILT4 5.0 × 10 ⁴ 2.5 × 10 ⁴ 0 0 0 Cynomolgus monkey ^{1.3 × 105} 5.0 × 10 ⁴ 2.0 × 10 ³ 8.0 × 10 ³ 5.0 × 10 ³ 7.7 Example 7: Inhibition of the Interaction Between ILT2 or ILT4 and MHC I Molecules by Anti-ILT Antibodies [00473] As part of the characterization process, the ability of exemplary antibodies to inhibit or block the interaction of ILT2 or ILT4 with their natural ligands was evaluated in competition experiments using a Biacore system. As described herein, the natural ligands of ILT2 and ILT4 include, but are not limited to, HLA class I molecules, including HLA-A, HLA-B, HLA-C, HLA-E, and HLA-G. Biotinylated HLA-A*1101 was captured in high amounts on a NeutrAvidin chip surface. Antigen-antibody complexes were prepared with (i) ILT2-ECD and anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, or anti-ILT2/ILT4 antibody Hz73D1.v1 and (ii) ILT4-ECD and anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, or anti-ILT2/ILT4 antibody Hz73D1.v1. The antibody concentration of each antibody was titrated from 0.09 - 100 nM and the concentration of human ILT2-ECD or ILT4-ECD was kept constant at 20 nM. The complexes were mixed in a 96-well microplate and each was injected onto the HLA-A-coated chip surface. The measured signal (response unit, RU) was plotted against the antibody concentration. [00474] The results are shown in Figure 2. A decrease in binding of ILT2 to HLA-A was observed with increasing concentrations of anti-ILT2 antibody 27F9 and anti-ILT2/ILT4 antibody Hz73D1.v1 in a dose-dependent manner. In contrast, anti-ILT4 antibody 48A5 had no effect on the binding of ILT2 to HLA-A. Similarly, a decrease in binding of ILT4 to HLA-A was observed with increasing concentrations of anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibody Hz73D1.v1, with no effect by anti-ILT2 antibody 27F9. The antibodies were observed to inhibit the interactions at IC50s in the nanomolar range. Another set of experiments was carried out using a HLA-G-coated chip surface with similar results. [00475] These data demonstrate that anti-ILT2 and anti-ILT2/ILT4 antibodies described herein inhibit the interactions between ILT2 and its natural ligands. In addition, anti-ILT4 and anti- ILT2/ILT4 antibodies described herein inhibit the interactions between ILT4 and its natural ligands. Importantly, this experiment also showed that the anti-ILT2/ILT4 antibody not only bound to both targets, i.e., ILT2 and ILT4, but was biologically functional in blocking the interactions of both targets with their ligands. These results show that anti-ILT2/ILT4 antibodies may be a potential therapeutic for blocking ILT2-induced and ILT4-induced suppression of immune responses. 7.8 Example 8: Binding of Anti-ILT2/ILT4 Antibody to Cells [00476] The binding of anti-ILT2/ILT4 antibodies to monocytes was evaluated. The binding of exemplary anti-ILT2/ILT4 antibody 73D1 and the humanized version Hz73D1.v1 to the CD14+ monocyte population of human and cyno PBMC were determined by flow cytometry analysis. Briefly, human or cyno PBMCs (from 2 donors each) were thawed, washed in media (RPMI, 10% FBS, L-glutamine, pen/strep), and resuspended in fresh media. PBMCs were stained with a cocktail of labeled antibodies to differentiate between the different cell types.1 × 10 ⁶ cells/well were stained with fluorescently-labelled 73D1 or Hz73D1.v1 antibody and incubated on ice. The cells were washed with ice-cold reagents and immediately analyzed by flow cytometry. The geometric mean fluorescence intensity for CD14+ monocytes was calculated for each sample. As shown in Figure 3, an increase in fluorescence was observed at increasing concentrations of antibodies 73D1 and Hz73D1.v1 in both human cells and cyno cells. Furthermore, binding of the antibodies to human cells and cyno cells was comparable. For example, the 50% effective concentration (EC50) of Hz73D1.v1 was 8.8 nM with human monocytes and 1.8 nM with cyno monocytes. Cells stained with a control antibody showed no shift in fluorescence. These results demonstrate that anti-ILT2/ILT4 antibodies recognize ILT2 and/or ILT4 on intact cells, i.e., primary monocytes. Importantly, these results show that there is comparable binding to both human and cyno monocytes, suggesting that monkeys will be a suitable model for future studies. Further, no binding of anti-ILT2/ILT4 antibodies described herein was observed to monocytes and other immune cells from rat and mouse, confirming that rodents are not an appropriate species for nonclinical testing. [00477] In addition to binding to ILT2 and ILT4, anti-ILT2/ILT4 antibodies show cross-reactivity with LILRA1, but not with ILLRB3, ILLRB4, ILLRB5, ILLRA2, ILLRA4, ILLRA5, and ILLRA6. Binding of anti-ILT2/ILT4 antibodies to ILT family members was evaluated by fluorescent-activated cell sorting (FACS) using 293T cells expressing human and cynomolgus monkey ILT2, ILT4, LILRA1, ILLRB3, ILLRB4, ILLRB5, ILLRA2, ILLRA4, ILLRA5, and ILLRA6 respectively. The binding affinities of an exemplary anti-ILT2/ILT4 antibody Hz73D1.v1 to human ILT2, human ILT4, human LILRA1, and cyno LILRA1 expressed on 293T cells and measured by flow cytometry are shown to be 1.2nM, 1.4nM, 2.64nM and 1.97 nM respectively. 7.9 Example 9: Inhibition of the Interaction Between ILT2 or ILT4 and MHC I Molecules by Anti-ILT Antibodies [00478] The ability of anti-ILT2/ILT4 antibodies to inhibit the interaction between ILT2 and/or ILT4 and MHC I molecules was evaluated using a reporter cell system. The Raji cell line was established over 50 years ago from a Burkitt lymphoma and has been shown to express MHC I and MHC II molecules. The lymphoblastoid cell line (LCL) 721.221 is a mutant of parent LCL 721, wherein LCL 721.221 does not express any MHC I molecules. LCL 721.221 cells were transfected with the non-classical MHC I molecule HLA-G and a stable cell line was established, referred to herein as 721.221-HLA-G. Raji cells or 721.221-HLA-G cells were co- cultured with cells expressing a stable reporter system and a cell surface receptor of interest ("reporter cells"). In this chimeric receptor system, the extracellular domain of the receptor of interest (e.g., ILT2 or ILT4) is fused with the transmembrane/intracellular domain of PILRβ that associates with the adaptor protein DAP12. When the chimeric receptor (e.g., ILT2 or ILT-4) is activated by binding to a ligand (e.g., MHC I molecule), DAP12 becomes phosphorylated and activates an NFAT-responsive promoter which drives GFP expression (see, e.g., Deng et al., 2014, Blood, 124:924-935). [00479] ILT2 and ILT4 reporter cells (expressing human ILT2 or human ILT4) were stained with CellTracker Deep Red (ThermoFisher) to distinguish them from Raji or 721.221-HLA-G cells upon analysis. Reporter cells were washed after staining and resuspended at 1 × 10 ⁶ cells/ml in X-VIVO™ 15 media (Lonza). Raji cells or 721.221-HLA-G cells were washed and resuspended in X-VIVO™ 15 media at 1 × 10 ⁶ cell/ml. For assays with Raji cells: anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibody 73D1 and Hz73D1.v1, and a control antibody were serially diluted and 50 µl was added to each well of a 96-well flat-bottom cell culture plate. For assays with 721.221-HLA-G cells: anti-ILT4 antibody 48A5, anti- ILT2/ILT4 antibody Hz73D1.v1, and a control antibody were serially diluted and 50 µl was added to each well of a 96-well flat-bottom cell culture plate. ILT2-expressing or ILT4- expressing reporter cells (100 µl/well) were co-cultured with Raji cells or 721.221-HLA-G cells (100 µl/well). The plates were incubated overnight at 37°C. The next day, reporter cells were assayed for GFP expression by FACS. [00480] As shown in Figure 4A, expression of GFP was induced when ILT2 or ILT4 was expressed on the surface of the reporter cells in the presence of Raji cells. With reporter cells expressing ILT2 on their cell surface, an increasing concentration of anti-ILT2 antibody 27F9 and anti-ILT2/ILT4 antibody 73D1 or Hz73D1.v1 was observed to inhibit GFP expression in a dose-dependent manner (expressed as the % GFP-positive cells). Anti-ILT4 antibody was seen to have no inhibitory effect. Similarly, with reporter cells expressing ILT4 on their cell surface, an increasing concentration of anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibody 73D1 or Hz73D1.v1, was observed to inhibit GFP expression in a dose-dependent manner and the anti- ILT2 antibody had no effect. As shown in Figure 4B, expression of GFP was induced when ILT2 or ILT4 was expressed on the surface of the reporter cells in the presence of 721.221- HLA-G cells. With reporter cells expressing ILT2 on their cell surface, an increasing concentration of anti-ILT2/ILT4 antibody Hz73D1.v1 was observed to inhibit GFP expression in a dose-dependent manner. With reporter cells expressing ILT4 on their cell surface, an increasing concentration of anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibody Hz73D1.v1 was observed to inhibit GFP expression in a dose-dependent manner. Table 14 shows IC ₅₀ of Hz73D1.v1 for blocking the interaction of human ILT2, human ILT4, and cyno ILT2 with MHC I molecules on Raji cells. Table 15 shows IC50 of Hz73D1.v1 for blocking the interaction of human ILT2, human ILT4 with HLA-G expressed on 721.221 cells. Table 14 Table 15 [00481] These results show that anti-ILT2 or anti-ILT2/ILT4 antibodies are able to inhibit and/or block the functional interaction between ILT2 and classical MHC I molecules to a high level. In parallel, these results show that anti-ILT4 or anti-ILT2/ILT4 antibodies are able to inhibit and/or block the functional interaction between ILT4 and classical and non-classical MHC I molecules (e.g., HLA-G) to a high level. These results support the idea that an antibody that binds ILT2 and ILT4 would modulate pathways induced by both of these molecules. Therefore, an anti-ILT2/ILT4 antibody may be a stronger therapeutic agent than an antibody that targets only ILT2 or only ILT4. [00482] An additional study was undertaken with reporter cells expressing cyno ILT2. As described above, cyno ILT2 reporter cells were stained with CellTracker Deep Red, washed, and resuspended at 1 × 10 ⁶ cells/ml in X-VIVO™ 15 media (Lonza). Raji cells were washed and resuspended in X-VIVO™ 15 media at 1 × 10 ⁶ cell/ml. Anti-ILT2/ILT4 antibody 73D1 and Hz73D1.v1 and a control antibody were serially diluted and 50 µl was added to each well of a 96-well flat-bottom cell culture plate. ILT2-expressing reporter cells (100 µl/well) were co- cultured with Raji cells (100 µl/well). The plates were incubated overnight at 37°C. The next day, reporter cells were assayed for GFP expression by FACS. [00483] As shown in Figure 5, expression of GFP was induced when cyno ILT2/4 was expressed on the surface of the reporter cells in the presence of Raji cells. In the presence of an increasing concentration of anti-ILT2/ILT4 antibody 73D1 or Hz73D1.v1, the percentage of GFP-expressing cells was decreased in a dose-dependent manner. Table 14 shows IC ₅₀ of Hz73D1.v1 for blocking the interaction of cyno ILT2 with MHC I molecules on Raji cells. These results are further evidence that monkeys would be a good model for testing. [00484] In addition to the reporter cell system, the inhibitory activity of anti-ILT2/ILT4 antibodies towards the interaction between ILT2 and MHC I molecules, and the interaction between ILT4 and MHC I molecules was evaluated using the Biacore system. Human ILT2-Fc and ILT4-Fc were used as target receptors and their interaction with an exemplary MHC- I molecule (HLA-A) was assayed in the presence or absence of an exemplary anti-ILT2/ILT4 antibody Hz73D1.v1 at 25°C. Anti-human ILT2 (clone 27F9) or ILT4 (clone 48A5) antibodies were used as tool reagents to dissect ILT2- and ILT4-specific blocking activities. Anti-IL2/ILT4 antibodies produced a dose-dependent reduction in the interaction between ILT2 and HLA-A, as well as between ILT4 and HLA-A. IC50s of the antibodies tested are shown in Table 16. Table 16 7.10 Example 10: Effect of Anti-ILT Antibodies on Activity of NK Cells [00485] NKL is a human natural killer (NK) cell line established from the peripheral blood of a patient with large granular lymphocyte (LGL) leukemia and kindly provided by Dr. Louis Lanier. As disclosed herein, NK cells express ILT2 but generally do not express ILT4.721.221 cells were transfected with plasmids expressing either HLA-G or HLA-A*0201 and high- expressing pools were enriched by antibiotic selection, generating 721.221-HLA-G and 721.221-A*0201 cell lines.721.221-HLA-G cells (described herein) or 721.221-HLA-A*0201 cells are used as targets in cytolytic cell assays. The target cells were labeled with CellTracker Deep Red (ThermoFisher) to distinguish them from NKL cells (after co-culture) and then resuspended at 5 × 10 ⁵ cells/ml in assay media (RPMI with 10% FBS, penicillin/streptomycin, L-glutamine, 5% human serum and recombinant human IL-2 (rhIL-2) at 20 ng/ml). NKL cells were suspended at 7.5 × 10 ⁶ cells/ml in assay media. Serial dilutions of anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 73D1 or Hz73D1.v1, and a control isotype antibody were prepared in assay media and 50 µl was added to wells of a V-bottom 96- well plate. NKL cells (50 µl) were added to each well, followed by target cells (50 µl), resulting in a target to NK ratio of 1:15. Plates were cultured for 3.5 hours at 37°C followed by centrifugation at 360 × g for 8 minutes at room temperature and removal of media. Cells were then resuspended in PBS containing a 1:1,000 dilution of Sytox Blue (ThermoFisher). Sytox Blue will stain cells with compromised cell membranes allowing live cells to be distinguished from dead or damaged cells. Cells were analyzed by FACS and the percent target cell killing was calculated based on the value of a positive control well of target cells permeabilized with detergent (100% lysis). [00486] As shown in Figure 6, anti-ILT2 antibody 27F9 and anti-ILT2/ILT4 antibodies 73D1 and Hz73D1.v1 enhanced NK cytolytic activity in a dose-dependent manner. EC ₅₀ values for Hz73D1.v1 were 2.4 nM for HLA-G expressing target cells and 0.13 nM for HLA-A*0201 expressing target cells. In comparison, EC50 for 27F9 was 0.064 nM for HLA-G expressing target cells. Anti-ILT4 antibody 48A5 had little to no effect on NK cell activity. These results show that anti-ILT2 antibodies and anti-ILT2/ILT4 antibodies are able to block the functional interaction between ILT2 on NK cells and MHC I molecules on the surface of target cells, leading to the enhancement of cytolytic activity. This supports the theory that anti-ILT2/ILT4 antibodies could enhance killing of tumor cells by inhibiting ILT2-induced suppression of NK cells. [00487] Similar experiments were undertaken using human primary NK cells. Briefly, NK cells were isolated from PBMC by negative selection, washed in assay media (RPMI with 10% FBS, pen/strep, 5% human serum, rhIL-2 (40 ng/ml), and IL-15 (50 ng/ml)), and resuspended at 7.5 × 10 ⁶ cells/ml in assay media.721.221-HLA-G target cells were labeled with CellTracker Deep Red (ThermoFisher) and resuspended at 5 × 10 ⁵ cells/ml in assay media. Target cells and NK cells (50 µl each) were combined in each well of a V-bottom plate. Anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, or anti-ILT2/ILT4 antibodies 47H6, 73D1, or 64A12 were added to wells at a final concentration of 1 µg/ml. Plates were cultured overnight at 37°C followed by centrifugation at 360 × g for 8 minutes at room temperature and removal of media. Cells were then resuspended in PBS containing a 1:1,000 dilution of Sytox Blue (ThermoFisher). Cells were analyzed by FACS and the percent target cell killing was calculated based on the value of a positive control well of target cells permeabilized with detergent (100% lysis). [00488] As shown in Figure 7, the presence of anti-ILT2 antibody 27F9 or anti-ILT2/ILT4 antibodies 47H6, 73D1, and 64A12, enhanced killing by primary NK cells. In agreement with other experiments described herein, these results show that ILT2 mediates suppression of primary NK cells and this suppression can be reversed with antagonist antibodies inhibiting or blocking ILT2/MHC I interactions. [00489] Further experiments were performed to evaluate NK cell cytolytic activity via analysis of CD137 expression, a marker that is upregulated on NK cells during cytolysis. NK cells were isolated from PBMC and cultured with a K562 cell line transfected to express the non-classical MHC-I molecule HLA-G. NK cell cytolytic activity was evaluated by FACS analysis of expression of activation marker CD137, gating on the CD3 negative, CD56 positive NK population. CD57 staining was performed to enrich for memory (adaptive) NK cells known to preferentially express ILT2 (Lopez-Vergès S et al, Proc.Natl. Acad. Sci. (2011), 108 (36) 14725- 14732). CD137 is upregulated on NK cells during cytolysis, providing a surrogate measure of cell killing. Hz73D1.v1 or anti-ILT2 (27F9), but not anti-ILT4 (48A5), significantly increased the CD137+ population (Figure 8). This effect was most pronounced in the CD57+ memory NK cell population. These data suggest that anti-IL2/ILT4 antibodies are able to block the interaction of ILT2 on primary NK cells with MHC-I on target cells, leading to enhanced activation and cytolytic activity. [00490] To evaluate activity of anti-IL2/ILT4 antibodies on killing of target cells naturally expressing HLA-A/B/C (classic MHC-I), an antibody dependent cellular cytotoxicity (ADCC) assay was performed. NK cells were isolated from PBMC and cultured with the CAL-27 squamous cell carcinoma cell line which expresses high levels of HLA-A, HLA-B, HLA-C and the NKG2A ligand HLA-E (data not shown). Anti-EGFR antibody was added to induce ADCC of these EGFR+ CAL-27 cells. CD137 was upregulated on NK cells during cytolysis, providing a surrogate measure of cell killing. Hz73D1.v1 or anti-ILT227F9, but not anti-ILT448A5, significantly increased the percent CD137+ NK cells in the CD57+ population (Figure 9). By comparison, an anti-NKG2A antibody significantly increased percent CD137+ in the CD57-, but not the CD57+ population. Both antibodies induced a comparable fold increase in activation (Hz73D1.v1 increased percent CD137+ cells 1.8-fold while anti-NKG2A antibody increased percent CD137+ cells 2.1-fold). An anti-KIR2DL antibody showed no activity in this assay. These data suggest that anti-ILT2/ILT4 antibodies are able to block the interaction of ILT2 on primary NK cells with classic MHC-I on target cells, leading to enhanced activation and cytolytic activity of NK cells. 7.11 Example 11: Effect of Anti-ILT Antibodies on MDSC Activity in MLR Assay [00491] Myeloid-derived suppressor cells (MDSC) have been shown to be critical in regulating immune responses by suppressing antigen presenting cells (APC) and T-cells. Furthermore, they have been observed to have a negative effect on anti-tumor activity by immune cells. The effect of anti-ILT antibodies on MDSC activity was investigated using a mixed lymphocyte reaction assay (MLR). To generate MDSC-like cells, human peripheral monocytes were grown in pre-conditioned X-VIVO™ 15 media (Lonza). Pre-conditioned media was generated by culture with the OVISE cell line. The OVISE cell line is an ovarian clear cell adenocarcinoma which secretes a large number of factors into its growth media. Monocytes were cultured in media consisting of 50% OVISE-conditioned media and 50% fresh X-VIVO™ 15 for 5 days; the resulting MDSC-like cells are referred to as ovMDSCs. These MDSC-like cells show MDSC functional characteristics, including increased Arg1 and IDO and suppression of T cell proliferation and pro-inflammatory cytokines in MLR (Mixed Lymphocyte Reaction) assays when compared to monocyte derived dendritic cells (data not shown). As a positive control for the assays, monocyte-derived dendritic cells (moDC) were generated by culture of human peripheral monocytes with GM-CSF and IL-4 for 5 days. To perform the MLR assay, 1 × 10 ⁵ allogeneic T-cells were co-cultured with 2.5 × 10 ⁴ ovMDSCs or moDCs in a 96-well round bottom cell culture plate. The cells were co-cultured in the presence of anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 47H6 or 73D1, or an isotype control antibody (each at 10 µg/ml). Controls included T-cells only, moDCs only, moDCs with T-cells (positive MLR), ovMDSCs only, and ovMDSCs with T-cells. Cells were incubated at 37°C and after 5 days 50 µl of media containing ³ H-Thymidine was added to each well. After 18 hours of incubation, the cells from each well were harvested and analyzed for thymidine incorporation as a marker for proliferation, and the supernatants were analyzed for cytokine secretion by multiplex bead array. [00492] As shown in Figure 10, T-cell proliferation was suppressed by co-culture with ovMDSCs. The presence of anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibodies 47H6 and 73D1 increased proliferation of T-cells cultured with ovMDSC to a level equivalent to the MLR response of T-cells with moDCs. Anti-ILT2 antibody 27F9 showed no ability to enhance T-cell proliferation. [00493] Another MLR assay was set up wherein 1 × 10 ⁵ allogeneic T-cells were co-cultured with 2.5 × 10 ⁴ ovMDSCs in a 96-well round bottom cell culture plate. The cells were co- cultured in the presence of serial dilutions of anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 73D1 or Hz73D1.v1, or a control isotype antibody. Cells were incubated at 37°C and after 5 days 50 µl of supernatant was harvested from each well for cytokine analysis using a Luminex system. Subsequently, 50 µl of media containing ³ H- Thymidine was added to each well. After 18 hours of incubation, the cells from each well were harvested and analyzed for thymidine incorporation. [00494] Similar to results described above, anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibodies 73D1 and Hz73D1.v1 were shown to increase T-cell proliferation (Figure 11A). In addition, it was determined that TNF-α secretion and GM-CSF secretion were increased in a dose-dependent manner in the presence of anti-ILT4 and anti-ILT2/ILT4 antibodies (Figures 11B-11C). As in the previous experiment, no effect was seen with anti-ILT2 antibodies. [00495] These results show that anti-ILT4 and anti-ILT2/ILT4 antibodies are able to inhibit and/or block the functional interaction between ILT4 on MDSCs and MHC I molecules on neighboring cells (e.g., APCs), leading to the reversal of MDSC suppression and the enhancement of T-cell activation. The reversal of MDSC-induced suppression also appears to lead to the increased secretion of pro-inflammatory cytokines such as TNF-α and GM-CSF. 7.12 Example 12: Effect of Anti-ILT2/4 Antibodies on LPS-Mediated Stimulation of Cells [00496] Lipopolysaccharide (LPS) stimulates innate immune responses on myeloid cells via toll-like receptors 2 and 4 (TLR2 and TLR4). To determine whether anti-ILT2 and/or anti-ILT4 antibodies can enhance LPS-mediated stimulation, a PBMC/LPS assay was performed. Briefly, frozen human PBMCs were thawed, washed in media (RPMI with 10% FBS, L-glutamine and pen/strep) and counted. Anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 73D1 and Hz73D1.v1, and a control isotype antibody were serially diluted in media and 50 µl added to each well of a 96-well round bottom tissue culture plate. PBMCs were added at 1 × 10 ⁶ cells/ml in a volume of 100 µl and the plate was incubated at 37°C for 30 minutes. LPS was added in 50 µl of media (final concentration of 30 ng/ml) and the plate were incubated at 37°C for 2 days. Cell supernatants were removed for analysis of cytokines using a Luminex® system. [00497] As shown in Figure 12, the presence of anti-ILT4 and anti-ILT2/ILT4 antibodies resulted in the increased production of GM-CSF and TNFα in a dose-dependent manner. For example, the EC ₅₀ values of Hz73D1.v1 were 0.76 nM for TNFα secretion and 1.5 nM for GM- CSF secretion. Anti-ILT2 antibody 27F9 and the control antibody showed little GM-CSF and TNFα secretion (approximately 20-40 pg/ml). These results show that the expression of ILT4 on myeloid cells in the PBMC culture can strongly suppress the production of pro-inflammatory cytokines induced by LPS, and importantly, that the suppression can be reversed by inhibiting and/or blocking ILT4/MHC I interactions. [00498] A similar experiment was set up using cyno PMBCs. Briefly, cyno PBMCs were washed in media (RPMI with 10% FBS, L-glutamine and pen/strep) and counted. Anti- ILT2/ILT4 antibody Hz73D1.v1 or a control antibody was serially diluted in media and 50 µl added to each well of a 96-well round bottom tissue culture plate. PMBCs were added at 2 × 10 ⁶ cells/ml in 100 µl and plates were incubated at 37°C for 30 minutes. LPS was added in 50 µl of media (final concentration of 50 ng/ml) and plates were incubated at 37°C for 2 days. Cell supernatants were removed for analysis of cytokines using a Luminex® system. [00499] Similar to the results with human PBMCs, anti-ILT2/4 antibody Hz73D1.v1 enhanced GM-CSF secretion from cyno PBMCs (Figure 13). EC50 was determined to be 14 nM. These results show that anti-ILT2/ILT4 antibodies had a similar biological effect on cyno immune cells and human immune cells. [00500] To further evaluate the effect of anti-ILT antibodies on cells involved in suppression of immune responses to tumor cells, a LPS assay with tolerogenic dendritic cells (tolDC) was set up. Briefly, isolated human monocytes were plated onto 10 cm tissue culture dishes at 4 × 10 ⁶ cells/dish in a volume of 20 ml media (X-VIVO™ 15 media (Lonza) supplemented with 50 ng/mL each of recombinant GM-CSF and IL-4 (Peprotech)). The monocytes were incubated for 5-7 days at 37°C and then the cells were harvested. For the assay, the in vitro generated DCs were suspended in fresh media containing 1:50 dilution of Fc Block (Biolegend) at a concentration of 6 × 10 ⁵ cells/ml. DCs were seeded in 96-well tissue culture plates at 50 µl/well and anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibody Hz73D1.v1, or a control antibody were added in serial dilutions at 50 µl/well. LPS was added (6 µg/ml final concentration) together with one of a variety of tolerizing agents in a volume of 50 µl media. The tolerizing agents included: vitamin D3/dexamethasone (VitD3/Dex) at 100 nM and 10 nM respectively, cyclosporin A at 750 ng/ml, rapamycin at 100 ng/ml, prostaglandin E2 (PGE2) at 1 µg/ml, IL-6 at 20 ng/ml, IL-10 at 20 ng/ml or TGFα at 20 ng/ml. Plates were incubated at 37°C for 2 days and supernatants were harvested for analysis using a Luminex® system. [00501] As shown in Figure 14, anti-ILT4 and anti-ILT2/ILT4 antibodies enhanced LPS- mediated cytokine (e.g.,TNFα) secretion in a dose-dependent manner. The EC50 values of Hz73D1.v1 induced TNFa secretion in the presence of LPS and an additional tolerizing agent are shown in table 17. In contrast, there was no increase of TNF-α in tolDCs treated with a control antibody and anti-ILT2 antibody (data not shown). These data show that tolDCs present within a patient’s tumor would be responsive to reactivation by the presence of anti- ILT4 and/or anti-ILT2/ILT4 antibodies that inhibit or block ILT4 and MHC I molecule interactions. Table 17 7.13 Example 13: Effect of Anti-ILT Antibodies on HMGB1, STING and/or Anti-CD3 Stimulation of PBMCs [00502] High mobility group protein B1 (HMGB1) is a nuclear protein that can be released from cells and binds to TLRs. HMGB1 has been shown to be present at high concentrations in necrotic tumor tissue, providing a potential source of innate stimulation of tumor infiltrating DC, monocytes, and macrophages (see, e.g., Guerriero et al., 2011, J. Immunol., 186:3517-3526). Experiments were designed to determine whether anti-ILT antibodies could enhance pro- inflammatory cytokine secretion from PBMCs treated with HMGB1. Briefly, anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 47H6, 73D1 and 64A12, and a control isotype antibody were serially diluted in media and 50 µl added to each well of a 96-well round bottom tissue culture plate. PBMCs were added at 1 × 10 ⁶ cells/ml in a volume of 100 µl and the plate was incubated at 37°C for 30 minutes. Recombinant HMGB1 (Biolegend) was added at a concentration of 2.5 µg/ml (a concentration anticipated to be present in the microenvironment of a tumor) and the plate was incubated at 37°C for 2 days. Cell supernatants were removed for analysis of cytokines using a Luminex® system. [00503] As shown in Figure 15, anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibodies 47H6, 73D1, and 64A12 enhanced secretion of TNF-α. These data show that anti-ILT4 and anti- ILT2/ILT4 antibodies will enhance the pro-inflammatory function of infiltrating monocytes within a tumor. [00504] Similarly, tumor cell necrosis and/or tumor cell death from radiotherapy results in the release of nuclear DNA. Free nuclear DNA can lead to myeloid cell stimulation via STING (stimulator of interferon genes) signaling. Experiments were designed to determine whether anti-ILT antibodies could enhance inflammatory cytokine production from PBMCs treated with a STING agonist. Briefly, PBMCs were plated in 96-well round bottom tissue culture plates and anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, and a control isotype antibody were added. After a 30-minute incubation, STING agonist 2'3'-cGAMP (Invivogen) was added at a concentration of 10 µg/ml (a concentration anticipated to be present in the microenvironment of a necrotic tumor). Cells were incubated for two days and supernatants were analyzed using a Luminex® system. [00505] As shown in Figure 16, exemplary anti-ILT4 antibody 48A5 enhanced secretion of IFNγ, TNF-α, and IL-1β. These data show that anti-ILT4 and anti-ILT2/ILT4 antibodies will enhance the pro-inflammatory functions of tumor infiltrating monocytes. [00506] In addition to suppression of innate immune activators, ILT2 or ILT4 may play a role in suppression of T-cell-mediated stimulation of myeloid cells. To evaluate T-cell stimulation of myeloid cells, PBMCs were activated with an anti-CD3 antibody and recombinant IL-2. Briefly, anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 47H6 and 64A12, and a control isotype antibody were serially diluted in media and 50 µl added to each well of a 96-well round bottom tissue culture plate. PBMCs were added at 1 × 10 ⁶ cells/ml in a volume of 100 µl and the plate was incubated at 37°C for 30 minutes. Anti-CD3 antibody clone HIT3a (eBioscience) was added at a concentration of 10 ng/ml and recombinant IL-2 was added at a concentration of 100 U/ml (Peprotech). Cells were incubated for two days and supernatants were analyzed using a Luminex® system. [00507] As shown in Figure 17, anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibodies 47H6 and 64A12 enhanced TNF-α secretion in a dose-dependent manner. Anti-ILT2 antibody 27F9 did not have any effect of cytokine production. These data show that ILT4 blockade enhances the immune response (i.e., pro-inflammatory cytokine secretion) resulting from interaction between activated T-cells and myeloid cells. 7.14 Example 14: Effect of Anti-ILT Antibodies on Macrophage Phagocytosis [00508] Phagocytosis assays were performed to further characterize the effect of anti-ILT2, anti-ILT4, and anti-ILT2/ILT4 antibodies on macrophage functions. Macrophages were generated by culture of isolated monocytes in media (RPMI with 10% FBS, L-glutamine and pen/strep) containing 50ng/ml recombinant M-CSF (Peprotech) for 5 days at 37° C in 12-well tissue culture plates. Macrophages were removed from the plate with a cell scraper and plated at 20,000 cells/well in 100 µl media in a flat bottom 96-well tissue culture plate. Macrophages were incubated overnight at 37° C. The next day, antibody was added to the macrophages at a concentration of 2.5 µg/ml together with 2.5 µg/ml of anti-CD47 antibody to induce antibody dependent phagocytosis. Raji cells were stained for 1 hour with a 1:4,000 dilution of pH Rodo Red Dye (Essen Bioscience), washed in media and added at 50,000 cells/well to macrophages. Phagocytosis was measured by mean red fluorescence on an Incucyte machine at 45 minute intervals. Test antibody was compared to isotype control antibody at the peak response timepoint (3 hours). [00509] As shown in Figure 18, anti-ILT2/ILT4 antibodies (e.g., Hz73D1.v1) and anti-ILT2 antibodies (e.g., 27F9) enhanced phagocytic activity of macrophages against Raji tumor cells opsonized with anti-CD47 antibody. Anti-ILT4 antibodies (e.g., 48A5) had no effect on phagocytosis by macrophages. To control for ILT2 expression by Raji cells, antibody 24E7, an ILT2 binder unable to block MHC-I interaction, was used. These data show that anti-ILT2 and anti-ILT2/ILT4 antibodies are able to enhance macrophage phagocytosis by blocking macrophage ILT2 interaction with MHC-I on tumor cells, and inhibiting ILT-2 induced suppression of macrophages, thus increasing macrophage phagocytosis of tumors. This activity of anti-ILT2 and anti-ILT2/ILT4 antibodies is specific to blocking ILT2/MHC-I interaction but not ILT4/MHC-1 interaction despite ILT4 expression on macrophages. 7.15 Example 15: Effect of Anti-ILT Antibodies on Dendritic Cells [00510] It is believed that ILT2 and/or ILT4 act as suppressors of myeloid cell activation and that inhibition or blocking of ILT2 and/or ILT4 would inhibit ILT2 and/or ILT4-induced suppression. [00511] Activation of myeloid cells can be achieved by the crosslinking of Fc receptors (FcR) on the cell surface and the crosslinking results in cytokine production; this is used as the basis for a myeloid cell activation assay. Dendritic cells were generated as described herein. Briefly, isolated human monocytes were plated on 10 cm tissue culture dishes with 4 × 10 ⁶ cells per dish in a volume of 20 ml media (Lonza) supplemented with 50 ng/mL each of recombinant GM- CSF and IL-4 (Peprotech). The monocytes were incubated for 5 - 7 days at 37°C and the resulting dendritic cells were harvested. Maxisorp 96-well ELISA plates were coated with anti- KLH antibody (5 µg/mL) and incubated overnight at 4°C. The anti-KLH antibody contains an Fc domain capable of binding Fc receptors on the dendritic cells. The plates were washed and blocked with X-VIVO™ 15 media for one hour. Dendritic cells were added at 7 × 10 ⁴ cells/well. Anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, a combination of antibodies 27F9 and 48A5, anti-ILT2/ILT4 antibody Hz73D1.v1 or a control antibody were added at serial dilutions and plates incubated at 37°C for 2 days. Supernatants were collected and analyzed for TNF-α secretion using a Luminex® system. [00512] As shown in Figure 19, a combination of anti-ILT2 antibody 27F9 and anti-ILT4 antibody 48A5 and anti-ILT2/ILT4 antibody 73D1 enhanced TNF-α secretion from dendritic cells in a dose-dependent manner. Anti-ILT2 antibody 27F9 as a single agent and anti-ILT4 antibody 48H6 as a single agent had only a small effect on increasing cytokine production. Thus the strong increase in cytokine secretion by the combination of anti-ILT2 antibody 27F9 with anti-ILT4 antibody 48A5 was surprising. This response was mirrored with the dual binding anti-ILT2/ILT4 antibody Hz73D1.v1. These data show that both ILT2 and ILT4 inhibit Fc- receptor-mediated activation of dendritic cells and that these effects are non-redundant. These data show that inhibiting the suppression of dendritic cells with agents that target both ILT2 and ILT4 (i.e., a dual binding anti-ILT2/ILT4 antibody) may result in a much better therapeutic effect than therapy with mono-specific antibodies. 7.16 Example 16: Effect of Anti-ILT Antibodies on Cytokine Secretion from Human and Cyno Blood Cells [00513] To investigate the potential for toxicity related to cytokine release (i.e., a “cytokine storm”), a variety of antibodies were cultured with human or cyno blood cells and cytokine production was analyzed. Briefly, antibodies were added at 10 µg/ml to 96-well flat-bottom plates and shaken at room temperature for 1 hour. The antibodies tested included anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibodies 47H6, 73D1, and Hz73D1.v1, superagonist anti- CD28 antibody clone 5D10 (Ancell), polyclonal anti-ILT2 antibody (R&D Systems), polyclonal anti-ILT4 antibody (R&D Systems), anti-LILRA1 antibody (R&D Systems), anti-CD3 antibody, and a control antibody. Plates were washed and blocked with culture media (RPMI with 10% FBS, L-glutamine and pen/strep) for 1 hour with shaking. Blood was obtained from healthy human donors and cyno monkeys. Red blood cells were removed from blood by lysis in RBC lysis buffer (eBioscience), followed by centrifugation, and the remaining cells were washed with culture media. 5 × 10 ⁵ cells were added per well, with LPS added to replicate wells as a positive control, and plates incubated at 37°C for 24 hours. Supernatants were collected and assayed for cytokine secretion using a Luminex® system. [00514] As shown in Figure 20, incubation of human blood cells with soluble LPS or plate- coated anti-CD28 antibody induced a significant increase in many cytokines including TNF-α, GM-CSF, MIP-1α, IL-6, IL-1β, and IL-10. In contrast, polyclonal anti-ILT2 antibody, polyclonal anti-ILT4 antibody, anti-LILRA1 antibody, anti-ILT4 antibody 48A5, and anti- ILT2/ILT4 antibodies 73D1 and Hz73D1.v1 failed to induce cytokine levels above isotype control antibody from the human blood cells. As shown in Figure 21, incubation of cyno blood cells with soluble LPS induced a significant increase in cytokines such as TNF-α, IL-1β, MIP- 1α, IL-6 and MIP-1β. Similar to the human blood cell assay, polyclonal anti-ILT2 antibody, polyclonal anti-ILT4 antibody, anti-LILRA1 antibody, anti-CD3 antibody, and anti-ILT2/ILT4 antibodies 47H6, 73D1, and Hz73D1.v1 failed to induce cytokine levels above the level seen with the isotype control antibody from the cyno blood cells. These data show that the potential of anti-ILT2 antibodies, ILT-4 antibodies, and anti-ILT2/ILT4 antibodies to produce a toxic immune response, such as a cytokine storm, is low. [00515] A further in vitro cytokine release assay was performed to evaluate the capacity of anti- ILT2/ILT4 antibodies to induce pro-inflammatory cytokines IL-2, TNF-α, IL-6 and IFN-γ. Whole blood samples for 10 healthy donors were used. Anti-ILT2/ILT4 antibodies were compared with a number of positive and negative controls. An anti-KLH isotype control antibody was used as a negative control. A super-agonist anti-CD28 antibody (clone ANC28.1) was used as a positive control (Walker 2011). In addition, Staphylococcus enterotoxin B (SEB) was used as a positive control for soluble antibody cultures. Two assay formats were used. In the first format, cells were cultured with an antibody (Hz73D1.v1, an isotype control antibody or anti-CD28 antibdy) or SEB at increasing concentrations. Antibodies were tested at 0.1, 1, 10 and 100 µg/ml. SEB was tested at 0.01, 0.1 and 1 µg/ml. In the second format, 96-well tissue culture plates were pre-incubated with an antibody overnight at 4° C, washed and then cells were added and cultured. Cell culture supernatant was then collected and tested for cytokine levels by cytometric bead array assay. [00516] In the first assay format, SEB at 1 µg/mL induced high levels of all cytokines evaluated (IL-2, IL-6, TNFα and IFNγ), with cytokine levels above isotype control for all 10 donors. Soluble anti-CD28 antibody at 100 µg/mL induced cytokine levels above isotype control for IL-6, TNFα and IFNγ. Median values with Hz73D1.v1 were comparable with the isotype control (Table 18). In the second assay format, the positive control of plate-coated anti-CD28 (100 µg/ml) induced IL-6 in 5 of 10 donors. In contrast, plate-coated Hz73D1.v1 did not induce any of the 4 cytokines to a level above that of isotype control (Table 19). Table 18 Anti-CD28 SEB (μg/mL) Isotype (μg/mL) Hz73D1.v1 (μg/mL) (μg/mL) 10 100 0.1 1 10 100 10 100 IL-6 1115 8934 571 1422 7 5 3 6 IL-2 44 48 1309 3418 19 21 17 20 TNFα 52 605 614 1452 4 7 6 10 IFNγ 35 343 208 704 5 6 5 5 Table 19 Anti-CD28 (μg/mL) Isotype (μg/mL) Hz73D1.v1 (μg/mL) 10 100 10 100 10 100 I ^L-6 _{17 93 10 9 9 7} I ^L-2 _{33 45 40 38 28 32} TNFα 18 26 17 19 16 12 7.17 Example 17: Effect of Anti-ILT Antibodies on T cell Activity [00517] ILT2 expression is known to be enriched on a population of effector memory CD45RA+ CD8+ T cells (CD8+ TEMRA cells) (Gustafson 2017). This population is only a small proportion of CD8+ T cells in healthy donors, making bulk CD8+ T cell cell-killing assays challenging. Therefore, to characterize the cytolytic activity of ILT2+ CD8 T cells, primary CD8+ T cells were transduced with ILT2 and expanded in vitro to generate sufficient numbers of ILT2+ CD8+ T cells. Cytolytic activity was then evaluated in a CD8+ T cell killing assay using fluorescently labeled 721.221-HLA-G target cells. Briefly, frozen PBMC were thawed, washed in media (RPMI with 10% FBS, L-glutamine and pen/strep) and CD8+ T cells were isolated using a CD8+ T cell positive selection kit. Isolated CD8+ T cells were cultured in basic media (Xvivo15 media with 10mM HEPES, 2mM Glutamine, pen/strep and 5% normal human serum) and stimulated for 24 hours at 37° C with CD3/28 beads adding 5µl beads per million cells. Activated T cells (2 × 10 ⁵ ) were then harvested and resuspended in 1 ml of Lentivirus expressing human ILT2 at a viral concentration of 1 × 10 ⁷ PFU/ml in the presence of polybrene to infect cells. Infected cells were then resuspended in T cell media (basic media supplemented with 5 ng/ml IL-7, 5 ng/ml IL-15 and 25 ng/ml IL-2) and allowed to expand for two weeks. Cells were then FACS sorted for the ILT2+ population and expanded for an additional 6 weeks to generated sufficient cells for the study. For evaluation of cytolytic activity, 2.5 × 10 ⁴ CellTracker deep red-labelled 721.221-HLAG cells were mixed with 2.5 × 10 ⁵ ILT2-transduced CD8+ T cells at a 10:1 T cell:Target ratio and 0.1 µg/ml anti-CD3/CD19 bispecific antibody in RPMI-10% FBS media. Anti-ILT antibodies or control antibodies were added to the cells at a concentration of 10µg/ml and incubated for 18 hours. Target cells were analyzed by FACS and percent target cell killing was calculated as the number of dead target cells divided by the total number of target cells. [00518] As shown in Figure 22, anti-ILT2/ILT4 antibodies (e.g., Hz73D1.v1) and anti-ILT2 antibodies (e.g., 27F9), but not anti-ILT4 antibodies (e.g., 48A5), enhanced cytolytic activity of CD8+ T cells against 721.221-HLA-G target cells. These data show that anti-ILT2 and anti- ILT2/ILT4 antibodies enhance CD8+ T cell cytolytic activity by blocking CD8+ T cell ILT2 interaction with MHC-I on target cells. As such, anti-ILT2 and anti-ILT2/ILT4 antibodies disrupt the immune suppressive activity of ILT2 on cytolytic lymphocytes, in particular effector memory T cells known to be involved in anti-tumor cell killing. 7.18 Example 18: Anti-ILT2/ILT4 Antibodies Induce M2-like to M1-like Polarization of Monocyte-derived Macrophages [00519] Macrophages are traditionally characterized as either pro-inflammatory (M1) or immune suppressive (M2) based on surface expression markers CD80, CD86 (M1), CD163, CD204, and CD206 (M2). Anti-IL2/ILT4 antibodies as well as anti-IL2 and anti-ILT4 antibodies were evaluated for their ability to polarize macrophages toward an M1-like or M2-like phenotype. [00520] Macrophages were generated by culture of monocytes in media (RPMI with 10% FBS, L-glutamine and pen/strep) containing Hz73D1.v1, 27F9, 48A5 or isotype control antibody (1 ug/ml) and 50 ng/ml recombinant M-CSF (Peprotech) for 5 days at 37° C in 48-well tissue culture plates. On day 5 samples were analyzed by flow cytometry for various surface markers indicative of an M1-like or M2-like phenotype. [00521] As shown in Figure 23, Hz73D1.v1 induced a decrease in M2-like macrophage phenotypic markers CD163, CD204, and CD206 and additional M2-like markers CD14 and CD209, consistent with an M2-like to M1-like polarization of the monocytes during differentiation. Anti-ILT4 specific antibody 48A5, but not anti-ILT2 specific antibody 27F9, induced an increase in M1-like marker CD86 and a decrease in M2-like markers CD163, CD204, and CD206, and additional M2-like markers CD14, CD209, and CCR5, consistent with an M2-like to M1-like polarization with ILT4 blockade. Overall, these data demonstrate that anti-ILT2/ILT4 antibodies induce a more pro-inflammatory M1-like phenotype during macrophage differentiation, and this response is mediated by inhibition of ILT4 interaction with MHC-I. 7.19 Example 19: Hz73D1.v1 (NGM707) Strongly Inhibits Tumor Growth in a CD34 Humanized Mouse Melanoma Model [00522] A CD34 Humanized mouse tumor model was established to evaluate the effect of hz73D1.v1 (NGM707) on growth of human tumors in the presence of human myeloid and lymphoid immune cells. [00523] NOG-EXL immunodeficient female mice were purchased from Taconic pre-engrafted with human CD34+ stem cells from cord blood. Mice (12-14 weeks of age) were injected subcutaneously with 5 million A375 human melanoma tumor cells on the right flank and tumors allowed to grow to 100-200 mm ³ and randomized into two groups. Group 1 was treated with isotype control antibody while Group 2 was treated with hz73D1.v1 (NGM707). All animals received antibody at 10mg/kg at days 25, 29, 33, and 39. [00524] As shown in Figure 24, hz73D1.v1 (NGM707) significantly inhibited tumor growth with a mean tumor growth inhibition of 70% compared to isotype at day 47 post tumor implantation. These results indicate that hz73D1.v1 (NGM707) induces a robust anti-tumor immune response in animals engrafted with a human immune system. 7.20 Example 20: Blockade of ILT2 and ILT4 Inhibits Tumor Growth Individually and in Combination [00525] A human PBMC-engrafted mouse tumor model was established to evaluate the individual and combined effect of anti-ILT2, anti-ILT4, anti-PD1, and hz73D1.v1 (NGM707) on tumor growth. [00526] Female NSG mice were purchased from Jackson Laboratories. As illustrated in Figure 25, at 8-10 weeks of age, the animals were injected subcutaneously with A375 melanoma tumor cells. A week later, the animals were irradiated at 1.8gy using an X-ray irradiator and injected intraperitoneally with 5 million PBMC. The tumors reached 80-100 mm ³ five days later. In a first experiment, groups of animals (n=5) were treated approximately bi-weekly (on days 15, 18, 22, 24, 28, and 31) with 10 mg/kg (i.e., total weekly does of 20 mg/kg) of isotype control, anti- ILT2, anti-ILT4, or hz73D1.v1 (NGM707) for a total of six doses. [00527] As shown in Figure 26, a modest but not statistically significant reducing in tumor volume was observed in animals treated with anti-ILT2; however, statistically significant tumor volume reductions of about 64% were observed in animals treated with anti-ILT4 and hz73D1.v1 (NGM707). [00528] Taken together, these results indicate that hz73D1.v1 (NGM707) is superior to anti- ILT2 alone. 7.21 Example 21: Ligation Using Plate-coated HLA-G (MHC-I) Revealed an Additive Role for ILT2 and ILT4 blockade on Monocyte LPS Activation [00529] Lipopolysaccharide (LPS) stimulates innate immune responses on myeloid cells via toll-like receptors 2 and 4 (TLR2 and TLR4). To determine whether anti-ILT2 and/or anti-ILT4 antibodies can enhance LPS-mediated stimulation, a Monocyte/LPS assay was performed. To optimally engage both ILT2 and ILT4, the assay was performed on culture plates previously coated with HLA-G tetramers. Maxisorp 96 well flat bottom plates were coated overnight with anti-Streptavidin polyclonal antibody at 10 µg/ml in PBS at 4°C. Plate was then washed twice in X-Vivo 15 media and coated for 2 hours with HLA-G tetramer (provided by Fred Hutchinson Cancer Center Tetramer Core) at 10 µg/ml in X-Vivo 15 media. Plates were washed twice with media before addition of cells. Isolated human monocytes were washed in media (RPMI with 10% FBS, L-glutamine and pen/strep) and counted. Anti-ILT2 antibody 27F9, anti-ILT4 antibody 48A5, anti-ILT2/ILT4 antibody hz73D1.v1 (NGM707), and a control isotype antibody were added at 1 µg/ml final concentration. Monocytes were added at 1 × 10 ⁶ cells/ml in a volume of 100 µl and the plate was incubated at 37°C for 30 minutes. LPS was added in 50 µl of media (final concentration of 30 ng/ml) and the plate were incubated at 37°C for 2 days. Cell supernatants were removed for analysis of cytokines using a Luminex system. [00530] As shown in Figure 27, the combination of either anti-ILT2 (27F9) and anti-ILT4 (48A5), or hz73D1.v1 (NGM707), resulted in a significant decrease in the production of IL-10. Anti-ILT2 antibody 27F9 alone and the control antibody showed no decrease in the secretion of IL-10, while anti-ILT4 antibody 48A5 alone showed a modest decrease in IL-10 secretion. [00531] These results suggest that a combination of ILT2 and ILT4 blockade is required to strongly reduce the production of the immune suppressive cytokine IL-10 by human monocytes. 7.22 Example 22: Hz73D1.v1 (NGM707) Synergistically Activates the Immune System In Vivo by Blocking Both ILT2 and ILT4 [00532] CX3CR1 tumor infiltrating T cells have been characterized as a highly cytolytic cell population critical for anti-tumor immune responses. CX3CR1 membrane expression was evaluated by FACS on splenocytes of humanized mice treated with hz73D1.v1 or various controls. [00533] Spleens were dissected from mice at the conclusion of the A375 tumor study described above (Figure 26). A single cell suspension was prepared by crushing the spleen tissue through a 70 µm filter using the head of a 5 ml syringe. Suspension cells were then stained with a FACS panel. Cells characterized as CD8+ T effector memory CD45RA+ (Temra) cells were analyzed for Geometric Mean Fluorescence Intensity (MFI) of CX3CR1. As shown in Figure 28, hz73D1.v1(NGM707)-treated mice showed a significant increase in CX3CR1 MFI on Temra cells compared to all other groups tested. These results demonstrate that dual inhibition of ILT2 and ILT4 by hz73D1.v1 (NGM707) treatment increases the cytolytic capacity of this effector memory population, whereas, treatment with anti-PD1 alone, ILT2 monotherapy, or ILT4 monotherapy does not. [00534] Interferon gamma secretion is another characteristic of anti-tumor immunity. Plasma from animals in a separate study following the same protocol was analyzed for secretion of cytokines. As shown in Figure 29, a significant increase in interferon gamma was observed between isotype and hz73D1.v1 (NGM707) treated animals. Anti-PD1 and anti-ILT4 treatment did not induce interferon gamma secretion above isotype control levels. These results indicate that hz73D1.v1 (NGM707) is inducing interferon gamma secretion which may be responsible for enhancing anti-tumor immune responses in these animals. 7.23 Example 23: Hz73D1.v1 (NGM707) Reverses a Suppressive Myeloid Phenotype Induced by Cancer Associated Fibroblasts [00535] Cancer associated fibroblasts (CAF) are a critical component of the tumor stroma and contribute to immune suppression in the tumor microenvironment. To evaluate the ability of hz73D1.v1 (NGM707) to impact this immune suppression, a CAF cell line was co-cultured with monocyte derived dendritic cells. Isolated human monocytes were plated onto 10 cm tissue culture dishes at 4 × 10 ⁶ cells/dish in a volume of 20 ml media (X-VIVO™ 15 media (Lonza) supplemented with 50 ng/mL each of recombinant GM-CSF and IL-4 (Peprotech)). The monocytes were incubated for 5-7 days at 37°C and then the cells were harvested. For the assay, these in vitro generated DCs were co-cultured with a CAF cell line in X-VIVO 15 media for 4 days in 12 well plates. DCs, alone or with CAF, were cultured in the presence of either hz73D1.v1 (NGM707) or isotype control. Cells were then removed from the culture wells and stained for FACS analysis of the immune suppression marker CD163 and the immune activation marker CD86. The proportion of cells that were CD163 low and CD86 high was calculated for each culture and treatment condition. [00536] As shown in Figure 30, CAF coculture strongly reduced the percentage of CD163 low/CD86 high dendritic cells, while the addition of hz73D1.v1 (NGM707) allowed the cells to retain their CD163 low CD86 high phenotype. [00537] These results demonstrate that hz73D1.v1 (NGM707) enables dendritic cells to maintain their immune-stimulatory activity within the tumor stroma despite close contact with immuno-suppressive fibroblast cells. 7.24 Example 24: Monotherapy Using Hz73D1.v1 (NGM707) [00538] A multicenter phase 1a human trial was designed to evaluate NGM707 as a monotherapy for various types of ILT2 and ILT4 high expressing cancer, including ovarian cancer, melanoma, gastric cancer, pancreatic cancer, renal cell carcinoma (RCC), rectal cancer, colorectal cancer (CRC), rectosigmoid adenocarcinoma, cholangiocarcinoma, non-small cell lung cancer (NSCLC), cervical cancer, breast cancer (including triple-negative breast cancer), pancreatic ductal adenocarcinoma (PDAC), and head and neck squamous cell carcinomas (HNSCCs). An escalation of NGM707 doses (6 mg, 20 mg, 60 mg, 200 mg, 600 mg, 1200 mg or 1800 mg) was administered intravenously to 34 human subjects once every 3 weeks. All 34 subjects had received a median of 4 prior therapies (ranging from 1-11) and all had metastatic disease. 1. Safety [00539] Treatment-related adverse events (AE) were characterized by type, frequency, severity (graded by NCI CTCAE v5.0), timing, seriousness, and relationship to the study drug. Laboratory abnormalities in the subjects were characterized by type, frequency, severity (graded by NCI CTCAE v5.0), and timing. Treatment-related adverse events and serious treatment- related adverse events are shown in Table 20. A maximum tolerated dose was not reached in this trial. Table 20 200 600 1200 1800 6 mg 20 mg 60 mg mg mg mg mg Total System Organ Class (N=2) (N=2) (N=3) (N=4) (N=9) (N=4) (N=8) (N=32) Preferred Term n (%) n (%) n (%) n (%) n (%) n (%) n (%) ^{n (%)} Subjects with at least one TEAE 1 2 2 2 2 0 5 14 related to NGM707 (50.0) (100) (66.7) (50.0) (22.2) (62.5) (43.8) Gastrointestinal disorders 0 0 1 1 1 0 2 5 (15.6) (33.3) (25.0) (11.1) (25.0) Nausea 0 0 1 1 1 0 1 4 (12.5) (33.3) (25.0) (11.1) (12.5) Abdominal pain 0 0 0 0 0 0 Diarrhoea 0 0 0 0 0 0 Dyspepsia 0 0 0 0 0 0 Vomiting 0 0 0 0 1 0 0 1 (3.1) (11.1) General disorders and 0 1 1 1 1 0 1 5 (15.6) administration site conditions (50.0) (33.3) (25.0) (11.1) (12.5) Fatigue 0 1 0 1 1 0 1 4 (12.5) (50.0) (25.0) (11.1) (12.5) Pyrexia 0 0 1 0 0 0 1 2 (6.3) (33.3) (12.5) Investigations 0 0 0 1 1 0 1 3 (9.4) (25.0) (11.1) (12.5) Aspartate aminotransferase 0 0 0 0 1 0 0 1 (3.1) increased (11.1) Blood bilirubin increased 0 0 0 0 0 0 1 1 (3.1) (12.5) Platelet count decreased 0 0 0 1 0 0 0 1 (3.1) (25.0) Skin and subcutaneous tissue 0 1 0 0 0 0 2 3 (9.4) disorders (50.0) (25.0) Pruritus 0 1 0 0 0 0 2 3 (9.4) (50.0) (25.0) Musculoskeletal and connective 1 1 0 0 0 0 0 2 (6.3) tissue disorders (50.0) (50.0) Arthralgia 1 1 0 0 0 0 0 2 (6.3) (50.0) (50.0) Blood and lymphatic system 0 0 0 0 0 0 1 1 (3.1) disorders (12.5) Anaemia 0 0 0 0 0 0 1 1 (3.1) (12.5) Injury, poisoning and procedural 0 1 0 0 0 0 0 1 (3.1) complications (50.0) Infusion related reaction 0 1 0 0 0 0 0 1 (3.1) (50.0) Metabolism and nutrition disorders 0 0 0 0 1 0 0 1 (3.1) (11.1) Hyponatraemia 0 0 0 0 1 0 0 1 (3.1) (11.1) Nervous system disorders 0 0 0 0 0 0 1 1 (3.1) (12.5) Headache 0 0 0 0 0 0 Respiratory, thoracic and 0 0 0 0 1 0 0 1 (3.1) mediastinal disorders (11.1) Pneumonitis 0 0 0 0 1 0 0 1 (3.1) (11.1) Serious Treatment-Related Adverse Events Subjects with at least one 0 0 0 0 1 (11.1) 0 0 1 (3.1) serious TEAE related to NGM707 Respiratory, thoracic and 0 0 0 0 1 (11.1) 0 0 1 (3.1) mediastinal disorders Pneumonitis 0 0 0 0 1 (11.1) 0 0 1 (3.1) 2. Anti-Tumor Activity [00540] Tumor progression in the subjects was assessed according to the criteria set out from RECIST 1.1. Of 24 response-evaluable subjects, best overall responses were partial response in one subject (1800 mg; metastatic melanoma), stable disease in six subjects and non-complete response/non-progressive disease in one subject. Six subjects had reduced target cancer lesion size, and the maximum reduction of lesion size was observed in one subject reaching 70%. Maximum treatment duration to date was six months, and five subjects remained on study. Objective responses over time and lesion assessment in the subjects are shown in Figure 31. [00541] The profile of chemokines associated with T cell and myeloid cell recruitment was evaluated in the subject showing a partial response. As shown in Figures 37A&37B, CXCL9, CXCL10, CXCL11, and CCL3 were evaluated at cycle 1 day 4, day 8, and day 15, cycle 2 day 1, and cycle 2 day 3. Each of these cytokines showed a time-dependent and statistically significant increase over the course of therapy. Together, these results are consistent with an NGM707-driven basis for the observed clinical response. [00542] The inflammatory immune status and cell proliferation signature was evaluated in biopsy samples obtained from all NGM707 monotherapy patients with evidence of disease control. Inflammatory immune status was evaluated using the 18-gene T Cell Inflammation Signature ("TIS;" Ayers et al., JCI, 2017). The proliferation signature was evaluated using a 10- gene tumor cell panel including ANLN, CCNB1, CDC25C, CDKN1C, CENPF, CEP55, MELK, MKI67, RRM2, and TYMS. The data in Figure 38 demonstrates that patients showing a response of stable disease or better (i.e., stable disease (“SD”), non-complete response/non- progressive disease (“NPD/NCR”) or partial response (“PR”) had a significantly elevated TIS score and significantly reduced tumor cell proliferation score relative to those with progressive disease (“PD”). 3. Pharmacokinetic Analysis [00543] During NGM707 treatment, blood samples from the subjects were collected for measurement of the serum concentrations of NGM707 on day 0 (pre-dosing), day 7 (post- dosing), day 14 (post-dosing) and day 21 (post-dosing) for the first three cycles. The concentrations were determined using an electrochemiluminescence immunoassay on the Meso Scale Diagnostics (MSD) platform. Briefly, a biotinylated monoclonal anti-idiotype antibody of the anti-NGM707 antibody was captured onto a streptavidin coated plate. The plate was then incubated with the serum of the subjects. After thorough washing of the plate to remove the unbound antibodies, a ruthenylated anti-idiotype antibody was added to the plate. Electrochemiluminescence signals were measured after adding the substrate to the plate. The concentration of NGM707 in the serum of each subject was calculated based on the standard curve generated using the same platform. Mean serum NGM707 concentration-time data by dose level are shown in Figures 32A and 32B. Mean values represent n=2, 2, 3, 7, 14, 8, and 11 for NGM707 doses of 6 mg, 20 mg, 60 mg, 200 mg, 600 mg, 1200 mg, and 1800 mg, respectively. A linear relationship between NGM707 serum concentration and the dose administered to human subjects was observed at doses ≥200 mg. 4. Receptor Occupancy [00544] Receptor ILT2 and ILT4 occupancy was analyzed in peripheral immune cells isolated from the subjects administered with different doses of NGM707. Briefly, blood from the patients was drawn into Cyto-Chex BCT direct draw tubes (Streck, Inc.; La Vista, NE, USA) and analyzed within 4 days of collection. A panel of 10 fluorochrome-labeled antibodies was used to identify major blood immune cell populations, including monocytes, CD4+ T cells, CD8+ T cells, total T cells, NK cells, B cells, granulocytes, and total CD33+ myeloid cells. In addition to cell-type specific markers, the antibody panel included two fluorochrome-labeled antibodies specific for each target: 1) a competing antibody that only binds free target, and 2) a non- competing antibody that binds all target molecules (independent of NGM707 presence). RO of ILT2 and ILT4 were each calculated based on the relative mean fluorescence intensities of the competing and non-competing antibodies, adjusted for their relative intensities at the baseline (RO measured prior to treatment). As shown in Figure 33, dose-dependent receptor occupancy (RO) was observed for both ILT2 and ILT4. At the 200 mg dose level, NGM707 fully occupied both receptors in most patients during the entire dosing interval. At >200mg dose levels, full occupancy of both receptors was reached. It was observed that immune cells upregulate ILT2 and ILT4 on surface after administration of NGM707 in a dose dependent manner (data not shown). Despite target upregulation, full receptor occupancy was maintained on ILT2 and ILT4 for the entire dosing interval at dose levels of 200mg and above. 5. Biomarker Identification [00545] To identify biomarkers associated with NGM707 treatment in cancer patients, blood was collected from the patients between D15 of cycle 1 and D15 of cycle 2 of dosing with NGM707. CD163 expression on various immune cells was assayed by flow cytometry using an antibody panel. Reduction of CD163 on various immunes cells including classical monocytes non-classical monocytes, myeloid derived suppressor cells (MDSCs), CD33+ pan myeloid cells, and pan dendritic cells was found to correlates with patients experiencing clinical benefit from NGM707 monotherapy treatment. As shown in Figures 34A and 34B, CD163 expression level on peripheral non-classical monocytes was significantly reduced in patients that showed clinical benefits (stable diseases or better) from NGM707 treatment. [00546] Paired tumor core needle biopsies (baseline and on-treatment) were collected from two colorectal cancer patients (patients 11002 and 11004) on day 20-21 after starting the treatment with 600 mg of NGM707. The samples were fixed on slides and stained using standard chromogenic immunohistochemistry on the Leica Bond platform. The assay for CD163 used the commercial reagent clone D6U1J from Cell Signaling Technologies (Danvers, MA). The percent area positive for each marker was quantified in the viable portions of the samples. Figures 35A and 35B showed a ~50% decrease of CD163 expression in the on-treatment biopsy sample compared with the baseline biopsy sample. [00547] These clinical data are consistent with in vitro observations. Peripheral blood mononuclear cells (PBMCs) from healthy blood donors were cultured in vitro for 3 days with 5 μg/mL of NGM707 or anti-KLH control antibody in the presence of plate-bound IgG (to provide FcR stimulation). After treatment, the cells were stained with a panel of fluorochrome-labeled antibodies including CD14, CD16, and CD163. The Mean Fluorescence Intensity (MFI) of CD163 was assessed on CD14 ^low CD16+ non-classical monocytes. As illustrated in Figure 36, in vitro treatment with NGM707 reduced CD163 expression on non-classical monocytes. [00548] CD163 is a marker of suppressive M2 macrophages, and these results evidence myeloid reprogramming in response to NGM707 treatment. The results have identified reduction of CD163 expression as a biomarker for assessing efficacy and/or clinical benefits from NGM707 treatment. The results also suggest that CD163 is a predictive marker for efficacy and/or clinical benefits from NGM707 treatment. [00549] Although the foregoing present disclosure has been described in some detail by way of illustration and example for purposes of clarity of understanding, the descriptions and examples should not be construed as limiting the scope of the present disclosure. The embodiments of the present disclosure described herein are intended to be merely exemplary, and those skilled in the art will recognize numerous equivalents to the specific procedures described herein. All such equivalents are considered to be within the scope of the present disclosure and are covered by the embodiments. [00550] All publications, patents, patent applications, internet sites, and accession numbers/database sequences including both polynucleotide and polypeptide sequences cited herein are hereby incorporated by reference in their entirety for all purposes to the same extent as if each individual publication, patent, patent application, internet site, or accession number/database sequence were specifically and individually indicated to be so incorporated by reference. SEQUENCES [00551] Following are sequences disclosed in the application. CDR sequences are listed in Tables 1-8. Human ILT2 amino acid sequence with predicted signal sequence underlined (SEQ ID NO:1) MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRL YREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTG AYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRA IFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEE TLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGA HNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKE GAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVS GPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLF LILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQ PEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMD TEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH Human ILT2 amino acid sequence without predicted signal sequence (SEQ ID NO:2) GHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQF PIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVIL QCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSN SPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGER DFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFY DRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFP MGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQP LTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQH PAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYA EVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLR REA TEPPPSQEGPSPAVPSIYATLAIH Human ILT2 extracellular domain (aa 24-461) (SEQ ID NO:3) GHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQF PIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVIL QCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSN SPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGER DFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFY DRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFP MGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQP LTPTGSDPQSGLGRHLGV Human ILT2 Ig-like C2-type domain 1 amino acid sequence (aa 27-115) (SEQ ID NO:4) PKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIP SITWEHAGRYRCYYGSDTAGRSESSDPLE Human ILT2 Ig-like C2-type domain 2 amino acid sequence (aa 116-221) (SEQ ID NO:5) LVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHAR GSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLG Human ILT2 Ig-like C2-type domain 3 amino acid sequence (aa 222-312) (SEQ ID NO:6) VSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQAN FTLGPVSRSYGGQYRCYGAHNLSSEWSAPSD Human ILT2 Ig-like C2-type domain 4 amino acid sequence (aa 313-409) (SEQ ID NO:7) PLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRST YQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLT Human ILT4 amino acid sequence with predicted signal sequence underlined (SEQ ID NO:8) MTPIVTVLICLGLSLGPRTHVQTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRL YREKKSASWITRIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGA YPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEEEHPQCLNSQPHARGSSRAI FSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVVAPGES LTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAH NLSSECSAPSDPLDILITGQIRGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAG AADAPLRLRSIHEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSG PSMGSSPPPTGPISTPAGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLF LILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQ PEDGVEMDTRAAASEAPQDVTYAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH Human ILT4 amino acid sequence without predicted signal sequence (SEQ ID NO:9) QTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNG QFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVT LQCESQVAFGGFILCKEGEEEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDL NSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVVAPGESLTLQCVSDVGYDRFVLYKEGE RDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQI RGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEF PMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPAGPED QPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLFLILRHRRQGKHWTSTQRKADF QHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQPEDGVEMDTRAAASEAPQDVT YAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH Human ILT4 extracellular domain (aa 22-461) (SEQ ID NO:10) QTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNG QFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVT LQCESQVAFGGFILCKEGEEEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDL NSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVVAPGESLTLQCVSDVGYDRFVLYKEGE RDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQI RGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEF PMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPAGPED QPLTPTGSDPQSGLGRHLGV Human ILT4 Ig-like C2-type domain 1 amino acid sequence (aa 27-110) (SEQ ID NO:11) PKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQFHIP SITWEHTGRYGCQYYSRARWSELS Human ILT4 Ig-like C2-type domain 2 amino acid sequence (aa 111-229) (SEQ ID NO:12) DPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEEEHPQCLNSQ PHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSV Human ILT4 Ig-like C2-type domain 3 amino acid sequence (aa 230-318) (SEQ ID NO:13) QPGPVVAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRS YGGQYRCYGAHNLSSECSAPSDPLDILIT Human ILT4 Ig-like C2-type domain 4 amino acid sequence (aa 330-419) (SEQ ID NO:14) QPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSA HAGTYRCYGSLNSDPYLLSHPSEPLELVVS Rhesus ILT2 amino acid sequence with predicted signal sequence underlined (SEQ ID NO:15) MTPILMVLICLGLSLGSRTRVQAGTFPKPTLWAEPGSMISKGSPVTLRCQGSLPVQDYRL QREKKTASWVRRIQQELVKKGYFPIASITSEHAGQYRCQYYSHSWWSEPSDPLELVVTGA YSKPTLSALPSPVVASGGNVTLQCDSQVAXGGFVLCKEGEDEHPQCLNSQPHTRGSSRAV FSVGPVSPSRRWSYRCYGYDSRSPYVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDK LTLQCGSDAGYNRFALYKEGERDFLQRPGRQPQAGLSQANFLLDPVRRSHGGQYRCSGAH NLSSEWSAPSDPLDILIAGQIRGRPSLLVQPGPTVVSGENVTLLCQSSWQFHVFLLTQAG AADAHLHLRSMYKYPKYQAEFPMSPVTSAHAGTYRCYGSHSSDSYLLSIPSDPLELVVSG PSGGPSSPTTGPTSTCGPEDQPLTPTGSDPQSGLGRHLGVVTGVLVAFVLLLFLLLLLFL VLRHRRQGKRWTSAQRKADFQHPAGAVEPEPRDRGLQRRSSPAANTQEENLYAAVKDTQP EDGVELDSRSPHDEDPQAVTYARVKHSRPRREMASPPSPLSEEFLDTKDTQAAASEDPQD VTYAQLQSLTLRRETTEPPPSQEREPPVESSIYATLTIH Rhesus ILT2 amino acid sequence without predicted signal sequence (SEQ ID NO:16) GTFPKPTLWAEPGSMISKGSPVTLRCQGSLPVQDYRLQREKKTASWVRRIQQELVKKGYF PIASITSEHAGQYRCQYYSHSWWSEPSDPLELVVTGAYSKPTLSALPSPVVASGGNVTLQ CDSQVAXGGFVLCKEGEDEHPQCLNSQPHTRGSSRAVFSVGPVSPSRRWSYRCYGYDSRS PYVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYNRFALYKEGERD FLQRPGRQPQAGLSQANFLLDPVRRSHGGQYRCSGAHNLSSEWSAPSDPLDILIAGQIRG RPSLLVQPGPTVVSGENVTLLCQSSWQFHVFLLTQAGAADAHLHLRSMYKYPKYQAEFPM SPVTSAHAGTYRCYGSHSSDSYLLSIPSDPLELVVSGPSGGPSSPTTGPTSTCGPEDQPL TPTGSDPQSGLGRHLGVVTGVLVAFVLLLFLLLLLFLVLRHRRQGKRWTSAQRKADFQHP AGAVEPEPRDRGLQRRSSPAANTQEENLYAAVKDTQPEDGVELDSRSPHDEDPQAVTYAR VKHSRPRREMASPPSPLSEEFLDTKDTQAAASEDPQDVTYAQLQSLTLRRETTEPPPSQE REPPVESSIYATLTIH Rhesus ILT2 extracellular domain (aa 24-460) (SEQ ID NO:17) GTFPKPTLWAEPGSMISKGSPVTLRCQGSLPVQDYRLQREKKTASWVRRIQQELVKKGYF PIASITSEHAGQYRCQYYSHSWWSEPSDPLELVVTGAYSKPTLSALPSPVVASGGNVTLQ CDSQVAXGGFVLCKEGEDEHPQCLNSQPHTRGSSRAVFSVGPVSPSRRWSYRCYGYDSRS PYVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYNRFALYKEGERD FLQRPGRQPQAGLSQANFLLDPVRRSHGGQYRCSGAHNLSSEWSAPSDPLDILIAGQIRG RPSLLVQPGPTVVSGENVTLLCQSSWQFHVFLLTQAGAADAHLHLRSMYKYPKYQAEFPM SPVTSAHAGTYRCYGSHSSDSYLLSIPSDPLELVVSGPSGGPSSPTTGPTSTCGPEDQPL TPTGSDPQSGLGRHLGV Rhesus ILT2 Ig-like C2-type domain 1 amino acid sequence (aa 27-114) (SEQ ID NO:18) PKPTLWAEPGSMISKGSPVTLRCQGSLPVQDYRLQREKKTASWVRRIQQELVKKGYFPIA SITSEHAGQYRCQYYSHSWWSEPSDPLE Rhesus ILT2 Ig-like C2-type domain 2 amino acid sequence n (aa 115-220) (SEQ ID NO:19) LVVTGAYSKPTLSALPSPVVASGGNVTLQCDSQVAXGGFVLCKEGEDEHPQCLNSQPHTR GSSRAVFSVGPVSPSRRWSYRCYGYDSRSPYVWSLPSDLLELLVPG Rhesus ILT2 Ig-like C2-type domain 3 amino acid sequence n (aa 221-311) (SEQ ID NO:20) VSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYNRFALYKEGERDFLQRPGRQPQAGLSQAN FLLDPVRRSHGGQYRCSGAHNLSSEWSAPSD Rhesus ILT2 Ig-like C2-type domain 4 amino acid sequence n (aa 312-408) (SEQ ID NO:21) PLDILIAGQIRGRPSLLVQPGPTVVSGENVTLLCQSSWQFHVFLLTQAGAADAHLHLRSM YKYPKYQAEFPMSPVTSAHAGTYRCYGSHSSDSYLLS 27F9 Heavy chain variable region amino acid sequence (SEQ ID NO:125) QVQLKESGPGLVAPSQSLSITCTVSGFSLTNYGVSWVRQPPGKGLEWLGIIWGDGSTNYH SALISRLSISKDNSKSQVFLKLNSLQADDTATYYCAKPNWDTYAMDFWGQGTSVTVSS 27F9 Light chain variable region amino acid sequence (SEQ ID NO:126) DIQMTQTTSSLSASLGDRVTISCRASQDISNFLNWYQQKPDGTVKLLIYCTSKLHSGVPS RFSGSGSETDYSLTISNLEQEDIATYFCQQGNTLPPTFGGGTKLEII 47C8 Heavy chain variable region amino acid sequence (SEQ ID NO:127) EVQLQQSGPDLVKPGASVKISCKASGYSFTGYYMHWVKQSHGKSLEWIGRVYPNNGDTSY NQKFKVKAILTVDKSSSTAYMELRSLTSEDSAVYYCARGATVVESLFAYWGQGTLVTVSA 47C8 Light chain variable region amino acid sequence (SEQ ID NO:128) DIVLTQSPASLAVSLGQRATISCRASESVDNYGNNFLHWYQQKPGQPPKLLIYRTSNLES GIPARFSGSGSRTDFTLTINPVEADDVATYYCQQSNEDPYTFGGGTKLEIK 48A5 Heavy chain variable region amino acid sequence (SEQ ID NO:129) QIQLVQSGPELKKPGETVKISCKASGYTFTNYGMNWVKQAPGKGLKWMGWINTYIGEPIY ADDFKGRFAFSLETSASTAYLQINNLKNEDMATYFCARRSDYDGYAMDYWGQGTSVTVSS 48A5 Light chain variable region amino acid sequence (SEQ ID NO:130) DIVMSQSPSSLAVSVGERVTMSCKSSQSLLYSGNQKNYLAWYQQKPGQSPKLLIYWASTR ESGVPDRFTGSGSGTDFTLTISSVKAEDLAVYYCQQHDSYPTFGGGSRLEIK 47H6 Heavy chain variable region amino acid sequence (SEQ ID NO:131) EVQLQQSGPELVKPGASVKISCKASGYTFTDYYMNWVKQSHGKSLEWIGDFNPNNGGTTY NQKFEGKATLTVDKSSNTAYMDLRSLTSEDSAVYYCARGRFYYGSLYSFDYWGQGTTLTV SS 47H6 Light chain variable region amino acid sequence (SEQ ID NO:132) DIQMTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPHLLVYNAKTLADGVPS RFSGSGSGTQYSLKINNLQPEDFGSYYCQHFWTSITFGAGTKLDLK Hz47H6.v2 Heavy chain variable region amino acid sequence (SEQ ID NO:133) QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYMNWVRQAPGQRLEWIGDFNPNNAGTTY N QKFEGRVTITVDKSASTAYMELSSLRSEDTAVYYCARGRFYYGSLYSFDYWGQGTLVTVS S Hz47H6.v2 Light chain variable region amino acid sequence (SEQ ID NO:134) DIQMTQSPSSLSASVGDRVTITCRASGNIHNYLAWYQQKPGKAPKLLIYNAKTLADGVPS R FSGSGSGTDFTLTISSLQPEDFATYYCQHFWTSITFGPGTKVDIK 51A1 Heavy chain variable region amino acid sequence (SEQ ID NO:135) EVQLVESGGGLVQPKGSLKLSCAASGFTFNTYAMHWVRQAPGKGLEWVARIRSKSSNYAT YYADSVKDRFTISRDDSQSMLYLQMNNLKTEDTAMYYCVRDGIYYYGTMYYYAMDYWGQG TSVTVSS 51A1 Light chain variable region amino acid sequence (SEQ ID NO:136) NIVLTQSPASLAVSLGQRATISCRASESVDYYGNSFMYWYQQKPGQPPKLLIYFASNLES GVPARFSGSGSRTDFTLTIDPVEAADAASYYCQQNNEDPWTFGGGTKLEIK 64A12 Heavy chain variable region amino acid sequence (SEQ ID NO:137) EVQLVESGGGLVQPKGSLKLSCAASGFTFNTYAMHWVRQAPGKGLEWVARIRSKSSNYAT YYADSVKDRFTISRDDSQSMLYLQMNNLKTEDTAMYYCVRDGIYYYDTMYYYAMDYWGQG TSVTVSS 64A12 Light chain variable region amino acid sequence (SEQ ID NO:138) NIVLTQSPASLAVSLGQRATISCRASESVDYYGNSFIYWYQQKPGQPPKLLIYFASNLES GVPARFSGSGSRTDFTLTIDPVEAADAASYYCQQNNEDPWTFGGGTKLEIK Hz64A12 Heavy chain variable region amino acid sequence (SEQ ID NO:139) EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMHWVRQAPGKGLEWVARIRSKSSNYAT YYADSVKDRFTISRDDAKNSLYLQMNSLRAEDTAVYYCARDGIYYYDTMYYYAMDYWGQG TLVTVSS Hz64A12 Light chain variable region amino acid sequence (SEQ ID NO:140) NIVLTQSPDSLAVSLGERATINCRASESVDYYGNSFIYWYQQKPGQPPKLLIYFASNLES GVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQNNEDPWTFGGGTKVEIK 73C4 Heavy chain variable region amino acid sequence (SEQ ID NO:141) AVQLQQSGPELVKPGASVKISCKASGYTFTDYYMNWVKQSHGKSLEWIGNVNPNNGGTSY NQKFKGKATLTVDKSSSTAYMELRSLTSEDSAVYYCARREIYFYGTIYYYAMDYWGQGTS VTVSS 73C4 and 73D1 Light chain variable region amino acid sequence (SEQ ID NO:142) DIVLTQSPASLAVSLGQRATISCRASESVDYYGNSFMYWYQQKPGRPPNLLIYFASNLES GVPARFSGSGSRTDFTLTIDPVEADDAATYYCQQNNEDPWTFGGGTKLEIK 73D1 Heavy chain variable region amino acid sequence (SEQ ID NO:143) AVQLQQSGPELVKPGASVKISCKASGYTFTDYYINWVKQSHGKSLQWIGNVNPNDGGTTY NQKFKGKATLTVDKSSSTAYMELRSLTSEDSAVYYCARREIYFYGTIYYYAMDYWGQGTS VTVSS Hz73D1.v1 Heavy chain variable region amino acid sequence (SEQ ID NO:144) QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYINWVRQAPGQGLEWMGNVNPNDGGTTY NQKFKGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARREIYFYGTIYYYAMDYWGQGTL VTVSS Hz73D1.v1 Light chain variable region amino acid sequence (SEQ ID NO:145) DIQLTQSPSFLSASVGDRVTITCRASESVDYYGNSFMYWYQQKPGKAPKLLIYFASNLES GVPSRFSGSGSGTEFTLTISSLQPEDFATYYCQQNNEDPWTFGGGTKVEIK Hz47H6.v2 Heavy chain amino acid sequence with signal sequence underlined (SEQ ID NO:146) MDMRVPAQLLGLLLLWLRGARCQVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYMNWVR QAPGQRLEWIGDFNPNNAGTTYNQKFEGRVTITVDKSASTAYMELSSLRSEDTAVYYCAR GRFYYGSLYSFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEP VTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDK KVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKT TPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz47H6.v2 Light chain amino acid sequence with signal sequence underlined (SEQ ID NO:147) MDMRVPAQLLGLLLLWLRGARCDIQMTQSPSSLSASVGDRVTITCRASGNIHNYLAWYQQ KPGKAPKLLIYNAKTLADGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQHFWTSITFG PGTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Hz47H6.v2 Heavy chain amino acid sequence without signal sequence (SEQ ID NO:148) QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYMNWVRQAPGQRLEWIGDFNPNNAGTTY NQKFEGRVTITVDKSASTAYMELSSLRSEDTAVYYCARGRFYYGSLYSFDYWGQGTLVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELL GGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQ YGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR EEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz47H6.v2 Light chain amino acid sequence without signal sequence (SEQ ID NO:149) DIQMTQSPSSLSASVGDRVTITCRASGNIHNYLAWYQQKPGKAPKLLIYNAKTLADGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQHFWTSITFGPGTKVDIKRTVAAPSVFIFPPS DEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTL SKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Hz64A12 Heavy chain amino acid sequence with signal sequence underlined (SEQ ID NO:150) MDMRVPAQLLGLLLLWLRGARCEVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMHWVR QAPGKGLEWVARIRSKSSNYATYYADSVKDRFTISRDDAKNSLYLQMNSLRAEDTAVYYC ARDGIYYYDTMYYYAMDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKD YFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSN TKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSH EDPEVKFNWYVDGVEVHNAKTKPREEQYGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKAL PAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPE NNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz64A12 Light chain amino acid sequence with signal sequence underlined (SEQ ID NO:151) MDMRVPAQLLGLLLLWLRGARCNIVLTQSPDSLAVSLGERATINCRASESVDYYGNSFIY WYQQKPGQPPKLLIYFASNLESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQNNED PWTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Hz64A12 Heavy chain amino acid sequence without signal sequence (SEQ ID NO:152) EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMHWVRQAPGKGLEWVARIRSKSSNYAT YYADSVKDRFTISRDDAKNSLYLQMNSLRAEDTAVYYCARDGIYYYDTMYYYAMDYWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCP APELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTK PREEQYGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYT LPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKL TVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz64A12 Light chain amino acid sequence without signal sequence (SEQ ID NO:153) NIVLTQSPDSLAVSLGERATINCRASESVDYYGNSFIYWYQQKPGQPPKLLIYFASNLES GVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQNNEDPWTFGGGTKVEIKRTVAAPSVF IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Hz73D1.v1 Heavy chain amino acid sequence with signal sequence underlined (SEQ ID NO:154) MDMRVPAQLLGLLLLWLRGARCQVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYINWVR QAPGQGLEWMGNVNPNDGGTTYNQKFKGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCAR REIYFYGTIYYYAMDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTK VDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHED PEVKFNWYVDGVEVHNAKTKPREEQYGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPA PIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz73D1.v1 Light chain amino acid sequence with signal sequence underlined (SEQ ID NO:155) MDMRVPAQLLGLLLLWLRGARCDIQLTQSPSFLSASVGDRVTITCRASESVDYYGNSFMY WYQQKPGKAPKLLIYFASNLESGVPSRFSGSGSGTEFTLTISSLQPEDFATYYCQQNNED PWTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Hz73D1.v1 Heavy chain amino acid sequence without signal sequence (SEQ ID NO:156) QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYINWVRQAPGQGLEWMGNVNPNDGGTTY NQKFKGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARREIYFYGTIYYYAMDYWGQGTL VTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAP ELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR EEQYGSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLP PSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTV DKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Hz73D1.v1 Light chain amino acid sequence without signal sequence (SEQ ID NO:157) DIQLTQSPSFLSASVGDRVTITCRASESVDYYGNSFMYWYQQKPGKAPKLLIYFASNLES GVPSRFSGSGSGTEFTLTISSLQPEDFATYYCQQNNEDPWTFGGGTKVEIKRTVAAPSVF IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Human IgG1 constant region (SEQ ID NO:158) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREE MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human IgG1 constant region E233A/L235A (SEQ ID NO:159) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPALAGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREE MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human IgG1 constant region L234A/L235A (SEQ ID NO:160) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPEAAGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQY NSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR EEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human IgG1 constant region L234A/L235A/P329G (SEQ ID NO:161) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPEAAGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQY NSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALGAPIEKTISKAKGQPREPQVYTLPPSR EEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDK SRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human IgG1 constant region N297G (SEQ ID NO:162) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYG STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREE MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human IgG1 constant region N297G/H310A (SEQ ID NO:163) ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYG STYRVVSVLTVLAQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREE MTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK Human Kappa light chain constant region (SEQ ID NO:164) RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Human Lambda light chain constant region (SEQ ID NO:165) GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSK QSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS Cyno ILT2 amino acid sequence with predicted signal sequence underlined (SEQ ID NO:166) MTPILMVLICLGLSLGPRTHVQAGILPKPTLWAEPGSMISEGSPVTLRCQGSLQVQEYRL YREKKPASWVRRIQQELVKKGYFAIGFITWEHTGQYRCQYYSHSWWSEPSDPLELVVTGA YSKPTLSALPSPVVASGGNVTLQCDSQVAFDSFTLCKEGEDEHPQRLNCQSHARGWSWAV FSVGPVSPSRRWSYRCYGYISSAPNVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDK LTLQCGSDAGYDRFALYKEGEGDFLQRPVRQPQAGLSQANFLLGPVSRSHGGQYRCSGAH NLSSEWSAPSDPLDILIAGQIRGRPFLSVQPGPKVVSGENVTLLCQSSWQFHAFLLTQAG AADAHLHLRSMYKYPKYQAEFPMSPVTSAHAGTYRCYGSRSSNPYLLSVPSDPLELVVSG PSGGPSSPTTGPTSTCAGPEDQPLTPTGSDPQSGLGRHLGVVTGILVAFVLLLFLLLLLF LVLRHQRQGKHWTSAQRKADFQHPAGAVEPEPRDRGLQRRSSPAADTQEENLYAAVKDTQ PEDGVELDSRQRPHDEDPQAVTYARVKHSRPRREMASPPSPLSEEFLDTKDTQAEEDRQM DTEAAASEDPQDVTYAQLQSLTLRRETTEPPPSQERAPPVESSIYATLTIH Cyno ILT2 amino acid sequence without predicted signal sequence (SEQ ID NO:167) GILPKPTLWAEPGSMISEGSPVTLRCQGSLQVQEYRLYREKKPASWVRRIQQELVKKGYF AIGFITWEHTGQYRCQYYSHSWWSEPSDPLELVVTGAYSKPTLSALPSPVVASGGNVTLQ CDSQVAFDSFTLCKEGEDEHPQRLNCQSHARGWSWAVFSVGPVSPSRRWSYRCYGYISSA PNVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYDRFALYKEGEGD FLQRPVRQPQAGLSQANFLLGPVSRSHGGQYRCSGAHNLSSEWSAPSDPLDILIAGQIRG RPFLSVQPGPKVVSGENVTLLCQSSWQFHAFLLTQAGAADAHLHLRSMYKYPKYQAEFPM SPVTSAHAGTYRCYGSRSSNPYLLSVPSDPLELVVSGPSGGPSSPTTGPTSTCAGPEDQP LTPTGSDPQSGLGRHLGVVTGILVAFVLLLFLLLLLFLVLRHQRQGKHWTSAQRKADFQH PAGAVEPEPRDRGLQRRSSPAADTQEENLYAAVKDTQPEDGVELDSRQRPHDEDPQAVTY ARVKHSRPRREMASPPSPLSEEFLDTKDTQAEEDRQMDTEAAASEDPQDVTYAQLQSLTL RRETTEPPPSQERAPPVESSIYATLTIH Cyno ILT2 extracellular domain (aa 24-461) (SEQ ID NO:168) GILPKPTLWAEPGSMISEGSPVTLRCQGSLQVQEYRLYREKKPASWVRRIQQELVKKGYF AIGFITWEHTGQYRCQYYSHSWWSEPSDPLELVVTGAYSKPTLSALPSPVVASGGNVTLQ CDSQVAFDSFTLCKEGEDEHPQRLNCQSHARGWSWAVFSVGPVSPSRRWSYRCYGYISSA PNVWSLPSDLLELLVPGVSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYDRFALYKEGEGD FLQRPVRQPQAGLSQANFLLGPVSRSHGGQYRCSGAHNLSSEWSAPSDPLDILIAGQIRG RPFLSVQPGPKVVSGENVTLLCQSSWQFHAFLLTQAGAADAHLHLRSMYKYPKYQAEFPM SPVTSAHAGTYRCYGSRSSNPYLLSVPSDPLELVVSGPSGGPSSPTTGPTSTCAGPEDQP LTPTGSDPQSGLGRHLGV Cyno ILT2 Ig-like C2-type domain 1 amino acid sequence (aa 27-114) (SEQ ID NO:169) PKPTLWAEPGSMISEGSPVTLRCQGSLQVQEYRLYREKKPASWVRRIQQELVKKGYFAIG FITWEHTGQYRCQYYSHSWWSEPSDPLE Cyno ILT2 Ig-like C2-type domain 2 amino acid sequence n (aa 115-220) (SEQ ID NO:170) LVVTGAYSKPTLSALPSPVVASGGNVTLQCDSQVAFDSFTLCKEGEDEHPQRLNCQSHAR GWSWAVFSVGPVSPSRRWSYRCYGYISSAPNVWSLPSDLLELLVPG Cyno ILT2 Ig-like C2-type domain 3 amino acid sequence n (aa 221-311) (SEQ ID NO:171) VSKKPSLSVQPGPVVAPGDKLTLQCGSDAGYDRFALYKEGEGDFLQRPVRQPQAGLSQAN FLLGPVSRSHGGQYRCSGAHNLSSEWSAPSD Cyno ILT2 Ig-like C2-type domain 4 amino acid sequence n (aa 312-408) (SEQ ID NO:172) PLDILIAGQIRGRPFLSVQPGPKVVSGENVTLLCQSSWQFHAFLLTQAGAADAHLHLRSM Y KYPKYQAEFPMSPVTSAHAGTYRCYGSRSSNPYLLS Hexahistidine peptide tag (SEQ ID NO:173) HHHHHH