TEM-1-TARGETED RADIOIMMUNOCONJUGATES AND USES THEREOF RELATED APPLICATIONS [0001] The present application claims priority to U.S. Provisional Patent Application No. 63/006,040, filed April 6, 2020, the entire contents of which are hereby incorporated by reference for all purposes. SEQUENCE LISTING [0002] The present specification makes reference to a Sequence Listing (submitted electronically as a .txt file named “FPI_007_Sequence_Listing.txt” on April 6, 2021). The .txt file was generated on March 29, 2021 and is 23,661 bytes in size. The entire contents of the Sequence Listing are herein incorporated by reference. BACKGROUND [0003] TEM-1 (tumor epithelial marker-1) (also known as endosialin or CD248) has been identified as a target for cancer therapeutics as a result of its expression across the stroma of many human tumors and because of its low or absent expression in normal tissues. Thus far, there are only a handful of therapeutics that are being developed using TEM-1 as a target. For example, ontuxizumab (MORAb-004 by Morphotek), a TEM-1 monoclonal antibody, is being investigated as a therapeutic for a variety of cancers. These therapeutics seek to treat the cancer by virtue of direct mediation of cell killing resulting from the antibody bound directly to the cancerous cells. [0004] Radiotherapy has been pursued as a treatment for cancer for many years, far longer than immunotherapy. Despite excellent reductions in tumor volume seen with some radiotherapeutics, the clinical use of radiotherapy has been limited by the toxicity caused by harmful radiation near or in healthy tissues, which are exposed to radiation that generally continues until, ultimately, the radionuclide decays. As a result of these “off target” effects on healthy tissue, dose reductions may be necessary, reducing efficacy; otherwise, severe side- effects, including permanent organ or tissue damage, are clinical risks. [0005] Thus, there remains a need for improved therapeutics (e.g., cancer therapeutics). Improvements to radiotherapeutics which make them clinically effective (e.g., excellent specificity for cancerous versus healthy tissue combined with tolerable side effects) would be a significant advance in cancer therapy. SUMMARY [0006] The present invention includes the discovery of an effective therapy for TEM-1 expressing cancerous cells. The invention employs the administration of radioimmunoconjugates that target TEM-1 (e.g., human TEM-1). Surprisingly, the radioimmunoconjugates of the invention exhibit dramatic and specific TEM-1 tumor killing and yet demonstrate lower, not higher, off target effects. This is a seemingly contradictory combination of high efficacy and reduced toxicity. The treatment effect is unexpected for TEM-1 tumors, relative to a) TEM-1 antibodies alone or b) radiotherapeutics employing alternative structural combinations, relative to those of the invention. It is the combination of the specificity for the TEM-1-expressing tumor cells and improved excretion of the radioimmunoconjugates provided by the structural combinations of the invention that allow for therapeutics that are uniquely effective for treating TEM-1-associated cancer cells. In essence, the lowered total radiation resident in the treated subject’s healthy tissue as a result of the radioimmunoconjugates of the invention lowers the deleterious “off target” effects but also allows for a level of dosing that delivers a high degree of therapeutic efficacy. As a result of the dramatic combination of anti-tumor efficacy and the absence of significant side effects, the invention provides unparalleled therapeutics for the treatment of TEM-1- associated cancers. [0007] In one aspect, provided are radioimmunoconjugate comprising the following structure: A-L-B (Formula I-a) or a pharmaceutically acceptable salt thereof, wherein: A is a chelating moiety or metal complex thereof; B is a TEM-1 targeting moiety; and L is a linker. [0008] In some embodiments, the chelating moiety is selected from the group consisting of: DOTA, DOTMA, DOTAM, DOTPA, DO3AM-acetic acid, DOTA-GA anhydride, DOTP, DOTMP, DOTA-4AMP, CB-TE2A, NOTA, NOTP, TETPA, TETA, HEHA, PEPA, H ₄ octapa, H ₂ dedpa, H ₆ phospa, TTHA, DO2P, HP-DO3A, EDTA, Deferoxamine, DTPA, DTPA-BMA, octadentate-HOPO, and porphyrins. In some embodiments, A is a metal complex of a chelating moiety. In some such embodiments, the metal complex comprises a radionuclide. In some embodiments, the radionuclide is an alpha emitter, e.g., an alpha emitter selected from the group consisting of Astatine-211 ( ²¹¹ At), Bismuth-212 ( ²¹² Bi), Bismuth-213 ( ²¹³ Bi), Actinium-225 ( ²²⁵ Ac), Radium-223 ( ²²³ Ra), Lead-212 ( ²¹² Pb), Thorium- 227 ( ²²⁷ Th), and Terbium-149 ( ¹⁴⁹ Tb), or a progeny thereof. In some embodiments, the radionuclide is ²²⁵ Ac or a progeny thereof. [0009] In some embodiments, L is has the structure -L ¹ -(L ² )n-, as shown within Formula I-b: A-L ¹ -(L ² ) _n -B (Formula I-b) wherein: A is a chelating moiety or metal complex thereof; B is a TEM-1 targeting moiety; L ¹ is a bond, optionally substituted C1-C6 alkyl, optionally substituted C1-C6 heteroalkyl, or optionally substituted aryl or heteroaryl; n is an integer between 1 and 5 (inclusive); and each L ² , independently, has the structure: -X ¹ -L ³ -Z ¹ - (Formula III) wherein: X ¹ is C=O(NR ¹ ), C=S(NR ¹ ), OC=O(NR ¹ ), NR ¹ C=O(O), NR ¹ C=O(NR ¹ ), - CH2PhC=O(NR ¹ ), -CH2Ph(NH)C=S(NR ¹ ) , O, or NR ¹ ; and each R ¹ independently is H, optionally substituted C ₁ -C ₆ alkyl, optionally substituted C ₁ -C ₆ heteroalkyl, or optionally substituted aryl or heteroaryl, in which C1-C6 alkyl can be substituted by oxo (=O), heteroaryl, or a combination thereof; L ³ is optionally substituted C ₁ -C ₅₀ alkyl or optionally substituted C ₁ -C ₅₀ heteroalkyl; and Z ¹ is CH ₂ , C=O, C=S, OC=O, NR ¹ C=O, or NR ¹ , wherein R ¹ is a hydrogen or optionally substituted C1-C6 alkyl or pyrrolidine-2,5-dione. [0010] In some embodiments, L ³ is C ₅ -C ₂₀ polyethylene glycol. In some embodiments, L ³ is (CH ₂ CH ₂ O) _m (CH ₂ ) _w , and m and w are independently an integer between 0 and 10 (inclusive). [0011] In some embodiments, the radioimmunoconjugate or a pharmaceutically acceptable salt thereof comprises the following structure: , wherein B is a TEM-1 targeting moiety. [0012] In some embodiments, L has the structure -L ¹ -(L ² ) _n -, as shown within Formula I- b: A-L ¹ -(L ² )n-B (Formula I-b) wherein: A is DOTA, or metal complex thereof; B is a TEM-1 targeting moiety; L ¹ is a bond or C ₁ -C ₆ alkyl; n is 1; and L ² has the structure: -X ¹ -L ³ -Z ¹ - (Formula III) wherein: X ¹ is C=O(NR ¹ ), and R ¹ is H or C ₁ -C ₆ alkyl; L ³ is (CH ₂ CH ₂ O) _m (CH ₂ ) _w , and m and w are independently an integer between 0 and 10 (inclusive); and Z ¹ is C=O. [0013] In some embodiments, the TEM-1 targeting moiety is at least 100 kDa in size, e.g., at least 150 kDa in size, at least 200 kDa in size, at least 250 kDa in size, or at least 300 kDa in size. [0014] In some embodiments, the TEM-1 targeting moiety is capable of binding to human TEM-1. [0015] In some embodiments, the TEM-1 targeting moiety comprises an antibody or antigen-binding fragment thereof. In some embodiments, the antibody or antigen-binding fragment thereof is humanized. In some embodiments, the antibody or antigen-binding fragment thereof is capable of binding an epitope comprising an amino acid sequence of SRDHQIPVIAAN (SEQ ID NO: 2). [0016] In some embodiments, the antibody or antigen-binding fragment thereof comprises at least one complementarity determining region (CDR) selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0017] In some embodiments, the antibody or antigen-binding fragment thereof comprises at least two CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0018] In some embodiments, the antibody or antigen-binding fragment thereof comprises at least three CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0019] In some embodiments, the antibody or antigen-binding fragment thereof comprises at least four CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0020] In some embodiments, the antibody or antigen-binding fragment thereof comprises at least five CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0021] In some embodiments, the antibody or antigen-binding fragment thereof comprises: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; or CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0022] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising at least one CDR selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and (ii) a light chain variable domain comprising at least one CDR selected from the group consisting of: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0023] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising at least one CDR selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6; and (ii) a light chain variable domain comprising at least one CDR selected from the group consisting of: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9. [0024] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising at least two CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and (ii) a light chain variable domain comprising at least two CDRs selected from the group consisting of: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0025] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising at least two CDRs selected from the group consisting of: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6; and (ii) a light chain variable domain comprising at least two CDRs selected from the group consisting of: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9. [0026] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4, or an amino acid sequence differing in 1 or 2 amino acids from SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and (ii) a light chain variable domain comprising: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7, or an amino acid sequence differing in 1 or 2 amino acids therefrom; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8, or an amino acid sequence differing in 1 or 2 amino acids therefrom; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9, or an amino acid sequence differing in 1 or 2 amino acids therefrom. [0027] In some embodiments, the antibody or antigen-binding fragment thereof comprises (i) a heavy chain variable domain comprising: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5; CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6; and (ii) a light chain variable domain comprising: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9. [0028] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain having an amino acid sequence with at least 85% identity with the amino acid sequence of SEQ ID NO: 16; and (ii) a light chain variable domain having an amino acid sequence with at least 85% identity with the amino acid sequence of SEQ ID NO: 21. [0029] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain having an amino acid sequence with at least 90% identity with the amino acid sequence of SEQ ID NO: 16; and (ii) a light chain variable domain having an amino acid sequence with at least 90% identity with the amino acid sequence of SEQ ID NO: 21. [0030] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain having an amino acid sequence with at least 95% identity with the amino acid sequence of SEQ ID NO: 16; and (ii) a light chain variable domain having an amino acid sequence with at least 95% identity with the amino acid sequence of SEQ ID NO: 21. [0031] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain variable domain comprising the amino acid sequence of SEQ ID NO: 16; and (ii) a light chain variable domain comprising the amino acid sequence of SEQ ID NO: 21. [0032] In some embodiments, the antibody is hMP-E-8.3. [0033] In some embodiments, after administration of the radioimmunoconjugate or a composition thereof to a mammal, the proportion of radiation excreted by the intestinal routes, renal route, or both routes is at least 2-fold greater than the proportion of radiation excreted by the same route(s) by a comparable mammal that has been administered a reference radioimmunoconjugate. [0034] In some embodiments, after administration of the radioimmunoconjugate or a composition thereof to a mammal, the proportion of radiation excreted by the intestinal routes, renal route, or both routes is at least 3-fold greater than the proportion of radiation excreted by the same route(s) by a comparable mammal that has been administered a reference radioimmunoconjugate. [0035] In some embodiments, A-L- is a metal complex of a moiety selected from the group consisting of:

[0036] In some embodiments, A-L- is a metal complex of Moiety 1: [0037] In some embodiments, A-L- is a metal complex of Moiety 1:

wherein the metal complex comprises a radionuclide, such as an alpha emitter (e.g., Astatine- 211 ( ²¹¹ At), Bismuth-212 ( ²¹² Bi), Bismuth-213 ( ²¹³ Bi), Actinium-225 ( ²²⁵ Ac), Radium-223 ( ²²³ Ra), Lead-212 ( ²¹² Pb), Thorium-227 ( ²²⁷ Th), and Terbium-149 ( ¹⁴⁹ Tb), or a progeny thereof). In some embodiments, the TEM-1 targeting moiety comprises an antibody or antigen- binding fragment thereof (e.g., a humanized antibody or antigen-binding fragment thereof). [0038] In some embodiments, A-L- is a metal complex of Moiety 1: wherein the metal complex comprises ²²⁵ Ac or a progeny thereof, and the TEM-1 targeting moiety is hMP-E-8.3 or an antigen-binding fragment thereof. In some embodiments, the TEM-1 targeting moiety is an antibody or antigen-binding fragment thereof comprising (i) a heavy chain variable domain comprising: CDR-H1 comprising the amino acid sequence of SEQ ID NO: 3 or 4; CDR-H2 comprising the amino acid sequence of SEQ ID NO: 5; and CDR-H3 comprising the amino acid sequence of SEQ ID NO: 6; and (ii) a light chain variable domain comprising: CDR-L1 comprising the amino acid sequence of SEQ ID NO: 7; CDR-L2 comprising the amino acid sequence of SEQ ID NO: 8; and CDR-L3 comprising the amino acid sequence of SEQ ID NO: 9. [0039] In some embodiments, A-L- is a metal complex of Moiety 1:

wherein the metal complex comprises ²²⁵ Ac or a progeny thereof, and the TEM-1 targeting moiety is hMP-E-8.3 or an antigen-binding fragment thereof. In some embodiments, the TEM-1 targeting moiety is hMP-E-8.3. [0040] In some embodiments, the radioimmunoconjugate or a pharmaceutically acceptable salt thereof comprises the following structure: , wherein is hMP-E-8.3. [0041] In another aspect, provided are pharmaceutical compositions comprising a radioimmunoconjugate or a pharmaceutically acceptable salt thereof as described herein and a pharmaceutically acceptable carrier. [0042] In another aspect, provided are methods of treating cancer, the method comprising administering to a subject in need thereof a pharmaceutical composition comprising an effective amount of a radioimmunoconjugate or a pharmaceutically acceptable salt thereof as described herein. [0043] In some embodiments, the subject is a mammal, e.g., a human. [0044] In some embodiments, tumor stromal cells associated with the cancer express TEM-1. [0045] In some embodiments, the cancer comprises cells that express TEM-1. [0046] In some embodiments, the cancer is a solid tumor cancer. For example, the solid tumor cancer may be a sarcoma, e.g., a sarcoma is selected from the group consisting of angiosarcoma or hemangioendothelioma, astrocytoma, chondrosarcoma, Ewing’s sarcoma, fibrosarcoma, glioma, leiomyosarcoma, liposarcoma, malignant fibrous histiocytoma (MFH), mesenchymous or mixed mesodermal tumor, mesothelial sarcoma or mesothelioma, myxosarcoma, osteosarcoma, rhabdomyosarcoma, and synovial sarcoma. In some embodiments, the sarcoma is osteosarcoma. In some embodiments, the sarcoma is a Ewing’s sarcoma. [0047] In some embodiments, the solid tumor cancer is a carcinoma, e.g., a carcinoma is selected from the group consisting of adenoid cystic carcinoma, adrenocortical carcinoma, bladder cancer, breast cancer, cervical cancer, colorectal cancer, endometrial cancer, gallbladder carcinoma, gastric cancer, head and neck cancer, lung cancer (e.g., small cell lung cancer or non-small cell lung cancer, or adenocarcinoma of the lung), neuroblastoma, neuroendocrine cancer, ovarian cancer, pancreatic cancer, prostate cancer, renal cancer, testicular cancer. [0048] In some embodiments, the solid tumor cancer is pancreatic cancer. [0049] In some embodiments, the solid tumor cancer is breast cancer. [0050] In some embodiments, the solid tumor cancer is head and neck cancer. [0051] In some embodiments, the solid tumor cancer is liver cancer. [0052] In some embodiments, the solid tumor cancer is lung cancer. [0053] In some embodiments, the solid tumor cancer is a brain cancer. [0054] In some embodiments, the solid tumor cancer is neuroblastoma. [0055] In some embodiments, the solid tumor cancer is melanoma. [0056] In some embodiments, the pharmaceutical composition is administered systemically. For example, in some embodiments, the pharmaceutical composition is administered parenterally, e.g., intravenously, intraarterially, intraperitoneally, subcutaneously, or intradermally. In some embodiments, the pharmaceutical composition is administered enterically, e.g., trans-gastrointestinally or orally. [0057] In some embodiments, the pharmaceutical composition is administered locally, e.g., by peritumoral injection or by intratumoral injection. BRIEF DESCRIPTION OF THE DRAWINGS [0058] FIG.1A is a schematic depicting the general structure of a bifunctional chelate comprising a chelate, a linker, and a cross-linking group. FIG.1B is a schematic depicting the general structure of a bifunctional conjugate comprising a chelate, a linker, and a targeting moiety. [0059] FIG.2 is a schematic depicting the synthesis of the bifunctional chelate, 4-{[11- oxo-11-(2,3,5,6-tetrafluorophenoxy)undecyl]carbamoyl}-2-[4,7 ,10-tris(carboxymethyl)- 1,4,7,10-tetraazacyclododecan-1-yl]butanoic acid (Compound B). Synthesis of Compound B is described in Example 2. (See Example 2.) [0060] FIG.3 is a schematic depicting the synthesis of the bifunctional chelate, 4-{[2-(2- {2-[3-oxo-3-(2,3,5,6-tetrafluorophenoxy)propoxy]ethoxy}ethox y)ethyl]carbamoyl}-2- [4,7,10-tris(carboxymethyl)-1,4,7,10-tetraazacyclododecan-1- yl]butanoic acid (Compound C). Synthesis of Compound C is described in Example 4. (See Example 4.) [0061] FIG.4A and FIG.4B show flow cytometry results for SK-N-AS (neuroblastoma) cells and SJSA-1 (osteosarcoma) cells, respectively, stained with a commercially available anti-human TEM-1 (CD248) antibody. The left-most peaks in Figs.4A and 4B represent cells stained with an isotype-matched control antibody instead of anti-human TEM-1. (See Example 6.) [0062] FIG.5 shows flow cytometry results from SJSA-1 cells stained with 1) hMP-E- 8.3 from an original stock solution; 2) hMP-E-8.3 from a re-purified stock solution; 3) Compound C-hMP-E-8.3 conjugate; or 4) an isotype-matched control antibody, then stained with a FITC-labeled secondary antibody. The left-most peak indicates unstained ells. (See Example 6.) [0063] FIG.6 shows results from saturation binding study using SJSA-1 cells to determine the binding affinity for [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3. (See Example 6.) [0064] FIG.7 shows results from a biodistribution study in an SJSA-1 osteosarcoma mouse model. Mice were injected with [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 and sacrificed at 4 h, 24 h, 48 h, 96 h, or 168 h. The percentage of injected dose/ gram (%ID/g) was assessed in blood, bone, heart, intestines, kidneys + adrenals, liver + gall bladder, lungs, muscle, pancreas, spleen, stomach, or tumor. (See Example 7.) [0065] FIG.8 shows tumor growth curves in an SJSA-1 osteosarcoma mouse model for mice injected with [ ²²⁵ Ac]-Compound C-hMP-E-8.3 (10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi) or with vehicle or antibody controls. (See Example 8.) [0066] FIG.9 shows tumor growth curves in an SK-N-AS neuroblastoma mouse model for mice injected with [ ²²⁵ Ac]-Compound C-hMP-E-8.3 (10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi) or with vehicle or antibody controls. (See Example 9.) [0067] FIG.10 shows tumor growth curves in an A673 Ewing’s sarcoma mouse model for mice injected with [ ²²⁵ Ac]-Compound C-hMP-E-8.3 (10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi) or with vehicle or antibody controls. (See Example 10.) DETAILED DESCRIPTION [0068] Radioimmunoconjugates are designed to target a protein or receptor that is upregulated in a disease state to deliver a radioactive payload to damage and kill cells of interest (radioimmunotherapy). The process of delivering such a payload, via radioactive decay, produces an alpha, beta, or gamma particle or Auger electron that can cause direct effects to DNA (such as single or double stranded DNA breaks) or indirect effects such as by- stander or crossfire effects. [0069] Radioimmunoconjugates typically contain a biological targeting moiety (e.g., an antibody or antigen binding fragment thereof that is capable of specifically binding to human TEM-1), a radioisotope, and a molecule that links the two. Conjugates are formed when a bifunctional chelate is appended to the biological targeting molecule so that structural alterations are minimal while maintaining target affinity. Once radiolabelled, the final radioimmunoconjugate is formed. [0070] Bifunctional chelates structurally contain a chelate, the linker, and a cross-linking group (FIG.1A). When developing new bifunctional chelates, most efforts focus around the chelating portion of the molecule. Several examples of bifunctional chelates have been described with various cyclic and acyclic structures conjugated to a targeted moiety. [Bioconjugate Chem.2000, 11, 510-519; Bioconjugate Chem.2012, 23, 1029-1039; Mol Imaging Biol.2011, 13, 215-221; Bioconjugate Chem.2002, 13, 110-115.] [0071] One of the key factors of developing safe and effective radioimmunoconjugates is maximizing efficacy while minimizing off-target toxicity in normal tissue. While this statement is one of the core tenets of developing new drugs, the application to radioimmunotherapeutics presents new challenges. Radioimmunoconjugates do not need to block a receptor, as needed with a therapeutic antibody, or release the cytotoxic payload intracellularly, as required with an antibody drug conjugate, in order to have therapeutic efficacy. However, the emission of the toxic particle is an event that occurs as a result of first-order (radioactive) decay and can occur at random anywhere inside the body after administration. Once the emission occurs, damage could occur to surrounding cells within the range of the emission leading to the potential of off-target toxicity. Therefore, limiting exposure of these emissions to normal tissue is the key to developing new drugs. [0072] One potential method for reducing off-target exposure is to remove the radioactivity more effectively from the body (e.g., from normal tissue in the body). One mechanism is to increase the rate of clearance of the biological targeting agent. This approach likely requires identifying ways to shorten the half-life of the biological targeting agent, which is not well described for biological targeting agents. Regardless of the mechanism, increasing drug clearance will also negatively impact the pharmacodynamics/efficacy in that the more rapid removal of drug from the body will lower the effective concentration at the site of action, which, in turn, would require a higher total dose and would not achieve the desired results of reducing total radioactive dose to normal tissue. [0073] Other efforts have focused on accelerating the metabolism of the portion of the molecule that contains the radioactive moiety. To this end, some efforts have been made to increase the rate of cleavage of the radioactivity from the biological targeting agents using what have been termed “cleavable linkers”. Cleavable linkers, however, have been taken on different meaning as it relates to radioimmunoconjugates. Cornelissen, et al. has described cleavable linkers as those by which the bifunctional chelate attaches to the biologic targeting agent through a reduced cysteine, whereas others have described the use of enzyme-cleavable systems that require the co-administration of the radioimmunoconjugate with a cleaving agent/enzyme to release [Mol Cancer Ther.2013, 12(11), 2472-2482; Methods Mol Biol. 2009, 539, 191-211; Bioconjug Chem.2003, 14(5), 927-933]. These methods either change the nature of the biological targeting moiety, in the case of the cysteine linkage, or are not practical from a drug development perspective (enzyme cleavable systems) since, in the case of the citations provided, require the administration of two agents. [0074] The present disclosure provides, among other things, radioimmunoconjugates that are more effectively eliminated from the body after catabolism and/or metabolism, while maintain therapeutic efficacy. Disclosed immunoconjugates may, in some embodiments, achieve a reduction of total body radioactivity, for example, by increasing the extent of excretion of the catabolic/metabolic products while maintaining the pharmacokinetics of the intact molecule when compared to known bifunctional conjugates. In some embodiments, this reduction in radioactivity results from the clearance of catabolic/metabolic by-products without impacting other in vitro and in vivo properties such as binding specificity (in vitro binding), cellular retention, and tumor uptake in vivo. Thus, in some embodiments, provided radioimmunoconjugates achieve reduced radioactivity in the human body while maintaining on-target activity. Definitions [0075] As used herein, “antibody” refers to a polypeptide whose amino acid sequence includes immunoglobulins and fragments thereof which specifically bind to a designated antigen, or fragments thereof. Antibodies in accordance with the present invention may be of any type (e.g., IgA, IgD, IgE, IgG, or IgM) or subtype (e.g., IgA1, IgA2, IgG1, IgG2, IgG3, or IgG4). Those of ordinary skill in the art will appreciate that a characteristic sequence or portion of an antibody may include amino acids found in one or more regions of an antibody (e.g., variable region, hypervariable region, constant region, heavy chain, light chain, and combinations thereof). Moreover, those of ordinary skill in the art will appreciate that a characteristic sequence or portion of an antibody may include one or more polypeptide chains, and may include sequence elements found in the same polypeptide chain or in different polypeptide chains. [0076] As used herein, “antigen-binding fragment” refers to a portion of an antibody that retains the binding characteristics of the parent antibody. [0077] As used herein, the term “bind” or “binding” of a targeting moiety means an at least temporary interaction or association with or to a target molecule, e.g., to human TEM-1, e.g., wild type or mutant TEM-1 as described herein. [0078] The term “bifunctional chelate,” as used herein, refers to a compound that comprises a chelate, a linker, and a cross-linking group. See, e.g., FIG.1A. A “cross-linking group” is a reactive group that is capable of joining two or more molecules, e.g., joining a bifunctional chelate and a targeting moiety, by a covalent bond. [0079] The term “bifunctional conjugate,” as used herein, refers to a compound that comprises a chelate or metal complex thereof, a linker, and a targeting moiety, e.g., an antibody or antigen-binding fragment thereof. See, e.g., Formula I-a or FIG.1B. [0080] The term “cancer” refers to any cancer caused by the proliferation of malignant neoplastic cells, such as tumors, neoplasms, carcinomas, sarcomas, leukemias, and lymphomas. A “solid tumor cancer” is a cancer comprising an abnormal mass of tissue, e.g., sarcomas, carcinomas, and lymphomas. A “hematological cancer” or “liquid cancer,” as used interchangeably herein, is a cancer present in a body fluid, e.g., lymphomas and leukemias. [0081] The term “chelate” as used herein, refers to an organic compound or portion thereof that can be bonded to a central metal or radiometal atom at two or more points. [0082] The term “conjugate,” as used herein, refers to a molecule that contains a chelating group or metal complex thereof, a linker group, and which optionally contains a targeting moiety, e.g., an antibody or antigen-binding fragment thereof. [0083] As used herein, the term “compound,” is meant to include all stereoisomers, geometric isomers, and tautomers of the structures depicted. [0084] The compounds recited or described herein can be asymmetric (e.g., having one or more stereocenters). All stereoisomers, such as enantiomers and diastereomers, are intended unless otherwise indicated. Compounds discussed in the present disclosure that contain asymmetrically substituted carbon atoms can be isolated in optically active or racemic forms. Methods on how to prepare optically active forms from optically active starting materials are known in the art, such as by resolution of racemic mixtures or by stereoselective synthesis. [0085] As used herein “detection agent” refers to a molecule or atom which is useful in diagnosing a disease by locating the cells containing the antigen. Various methods of labeling polypeptides with detection agents are known in the art. Examples of detection agents include, but are not limited to, radioisotopes and radionuclides, dyes (such as with the biotin-streptavidin complex), contrast agents, luminescent agents (e.g., fluorescein isothiocyanate or FITC, rhodamine, lanthanide phosphors, cyanine, and near IR dyes), and magnetic agents, such as gadolinium chelates. [0086] As used herein, the term “radionuclide,” refers to an atom capable of undergoing radioactive decay (e.g., ³ H, ¹⁴ C, ¹⁵ N, ¹⁸ F, ³⁵ S, ⁴⁷ Sc, ⁵⁵ Co, ⁶⁰ Cu, ⁶¹ Cu, ⁶² Cu, ⁶⁴ Cu, ⁶⁷ Cu, ⁷⁵ Br, ⁷⁶ Br , ⁷⁷ Br , ⁸⁹ Zr, ⁸⁶ Y, ⁸⁷ Y, ⁹⁰ Y, ⁹⁷ Ru, ⁹⁹ Tc, ^99m Tc ¹⁰⁵ Rh, ¹⁰⁹ Pd, ¹¹¹ In, ¹²³ I, ¹²⁴ I, ¹²⁵ I, ¹³¹ I, ¹⁴⁹ Pm, ¹⁴⁹ Tb, ¹⁵³ Sm, ¹⁶⁶ Ho, ¹⁷⁷ Lu, ¹⁸⁶ Re, ¹⁸⁸ Re, ¹⁹⁸ Au, ¹⁹⁹ Au, ²⁰³ Pb, ²¹¹ At, ²¹² Pb , ²¹² Bi, ²¹³ Bi, ²²³ Ra, ²²⁵ Ac, ²²⁷ Th, ^229Th , ⁶⁶ Ga, ⁶⁷ Ga, ⁶⁸ Ga, ⁸² Rb, ^117m Sn, ²⁰¹ Tl). The terms radioactive nuclide, radioisotope, or radioactive isotope may also be used to describe a radionuclide. Radionuclides may be used as detection agents, as described herein. In some embodiments, the radionuclide may be an alpha-emitting radionuclide. [0087] The term an “effective amount” of an agent (e.g., any of the foregoing conjugates), as used herein, is that amount sufficient to effect beneficial or desired results, such as clinical results, and, as such, an “effective amount” depends upon the context in which it is being applied. For example, in therapeutic applications, an “effective amount” may be an amount sufficient to cure or at least partially arrest the symptoms of the disorder and its complications, and/or to substantially improve at least one symptom associated with the disease or a medical condition. For example, in the treatment of cancer, an agent or compound that decreases, prevents, delays, suppresses, or arrests any symptom of the disease or condition would be therapeutically effective. A therapeutically effective amount of an agent or compound is not required to cure a disease or condition but may, for example, provide a treatment for a disease or condition such that the onset of the disease or condition is delayed, hindered, or prevented, such that the disease or condition symptoms are ameliorated, or such that the term of the disease or condition is changed. For example, the disease or condition may become less severe and/or recovery is accelerated in an individual. An effective amount may be administered by administering a single dose or multiple (e.g., at least two, at least three, at least four, at least five, or at least six) doses. [0088] The term “immunoconjugate,” as used herein, refers to a conjugate that includes a targeting moiety, such as an antibody (or antigen-binding fragment thereof), nanobody, affibody, or a consensus sequence from Fibronectin type III domain. In some embodiments, the immunoconjugate comprises an average of at least 0.10 conjugates per targeting moiety (e.g., an average of at least 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 2, 4, 5, or 8 conjugates per targeting moiety). [0089] The term “radioconjugate,” as used herein, refers to any conjugate that includes a radioisotope or radionuclide, such as any of the radioisotopes or radionuclides described herein. [0090] The term “radioimmunoconjugate,” as used herein, refers to any immunoconjugate that includes a radioisotope or radionuclide, such as any of the radioisotopes or radionuclides described herein. A radioimmunoconjugate provided in the present disclosure typically refers to a bifunctional conjugate that comprises a metal complex formed from a radioisotope or radionuclide. [0091] The term “radioimmunotherapy,” as used herein, refers a method of using a radioimmunoconjugate to produce a therapeutic effect. In some embodiments, radioimmunotherapy may include administration of a radioimmunoconjugate to a subject in need thereof, wherein administration of the radioimmunoconjugate produces a therapeutic effect in the subject. In some embodiments, radioimmunotherapy may include administration of a radioimmunoconjugate to a cell, wherein administration of the radioimmunoconjugate kills the cell. Wherein radioimmunotherapy involves the selective killing of a cell, in some embodiments the cell is a cancer cell in a subject having cancer. [0092] The term “pharmaceutical composition,” as used herein, represents a composition containing a radioimmunoconjugate described herein formulated with a pharmaceutically acceptable excipient. In some embodiments, the pharmaceutical composition is manufactured or sold with the approval of a governmental regulatory agency as part of a therapeutic regimen for the treatment of disease in a mammal. Pharmaceutical compositions can be formulated, for example, for oral administration in unit dosage form (e.g., a tablet, capsule, caplet, gelcap, or syrup); for topical administration (e.g., as a cream, gel, lotion, or ointment); for intravenous administration (e.g., as a sterile solution free of particulate emboli and in a solvent system suitable for intravenous use); or in any other formulation described herein. [0093] A “pharmaceutically acceptable excipient,” as used herein, refers any ingredient other than the compounds described herein (for example, a vehicle capable of suspending or dissolving the active compound) and having the properties of being nontoxic and non- inflammatory in a patient. Excipients may include, for example: antiadherents, antioxidants, binders, coatings, compression aids, disintegrants, dyes (colors), emollients, emulsifiers, fillers (diluents), film formers or coatings, flavors, fragrances, glidants (flow enhancers), lubricants, preservatives, printing inks, radioprotectants, sorbents, suspending or dispersing agents, sweeteners, or waters of hydration. Exemplary excipients include, but are not limited to: ascorbic acid, histidine, phosphate buffer, butylated hydroxytoluene (BHT), calcium carbonate, calcium phosphate (dibasic), calcium stearate, croscarmellose, crosslinked polyvinyl pyrrolidone, citric acid, crospovidone, cysteine, ethylcellulose, gelatin, hydroxypropyl cellulose, hydroxypropyl methylcellulose, lactose, magnesium stearate, maltitol, mannitol, methionine, methylcellulose, methyl paraben, microcrystalline cellulose, polyethylene glycol, polyvinyl pyrrolidone, povidone, pregelatinized starch, propyl paraben, retinyl palmitate, shellac, silicon dioxide, sodium carboxymethyl cellulose, sodium citrate, sodium starch glycolate, sorbitol, starch (corn), stearic acid, stearic acid, sucrose, talc, titanium dioxide, vitamin A, vitamin E, vitamin C, and xylitol. [0094] The term “pharmaceutically acceptable salt,” as use herein, represents those salts of the compounds described here that are, within the scope of sound medical judgment, suitable for use in contact with the tissues of humans and animals without undue toxicity, irritation, or allergic response. Pharmaceutically acceptable salts are well known in the art. For example, pharmaceutically acceptable salts are described in: Berge et al., J. Pharmaceutical Sciences 66:1-19, 1977 and in Pharmaceutical Salts: Properties, Selection, and Use, (Eds. P.H. Stahl and C.G. Wermuth), Wiley-VCH, 2008. Salts can be prepared in situ during the final isolation and purification of the compounds described herein or separately by reacting the free base group with a suitable organic acid. [0095] The compounds of the invention may have ionizable groups so as to be capable of preparation as pharmaceutically acceptable salts. These salts may be acid addition salts involving inorganic or organic acids or the salts may, in the case of acidic forms of the compounds of the invention be prepared from inorganic or organic bases. Frequently, the compounds are prepared or used as pharmaceutically acceptable salts prepared as addition products of pharmaceutically acceptable acids or bases. Suitable pharmaceutically acceptable acids and bases are well-known in the art, such as hydrochloric, sulphuric, hydrobromic, acetic, lactic, citric, or tartaric acids for forming acid addition salts, and potassium hydroxide, sodium hydroxide, ammonium hydroxide, caffeine, various amines for forming basic salts. Methods for preparation of the appropriate salts are well-established in the art. [0096] Representative acid addition salts include acetate, adipate, alginate, ascorbate, aspartate, benzenesulfonate, benzoate, bisulfate, borate, butyrate, camphorate, camphorsulfonate, citrate, cyclopentanepropionate, digluconate, dodecylsulfate, ethanesulfonate, fumarate, glucoheptonate, glycerophosphate, hemisulfate, heptonate, hexanoate, hydrobromide, hydrochloride, hydroiodide, 2-hydroxy-ethanesulfonate, lactobionate, lactate, laurate, lauryl sulfate, malate, maleate, malonate, methanesulfonate, 2- naphthalenesulfonate, nicotinate, nitrate, oleate, oxalate, palmitate, pamoate, pectinate, persulfate, 3-phenylpropionate, phosphate, picrate, pivalate, propionate, stearate, succinate, sulfate, tartrate, thiocyanate, toluenesulfonate, undecanoate, valerate salts, among others. Representative alkali or alkaline earth metal salts include sodium, lithium, potassium, calcium, and magnesium, as well as nontoxic ammonium, quaternary ammonium, and amine cations, including, but not limited to ammonium, tetramethylammonium, tetraethylammonium, methylamine, dimethylamine, trimethylamine, triethylamine, and ethylamine. [0097] The term “polypeptide” as used herein refers to a string of at least two amino acids attached to one another by a peptide bond. In some embodiments, a polypeptide may include at least 3-5 amino acids, each of which is attached to others by way of at least one peptide bond. Those of ordinary skill in the art will appreciate that polypeptides can include one or more “non-natural” amino acids or other entities that nonetheless are capable of integrating into a polypeptide chain. In some embodiments, a polypeptide may be glycosylated, e.g., a polypeptide may contain one or more covalently linked sugar moieties. In some embodiments, a single “polypeptide” (e.g., an antibody polypeptide) may comprise two or more individual polypeptide chains, which may in some cases be linked to one another, for example by one or more disulfide bonds or other means. [0098] By “subject” is meant a human or non-human animal (e.g., a mammal). [0099] By “substantial identity” or “substantially identical” is meant a polypeptide sequence that has the same polypeptide sequence, respectively, as a reference sequence, or has a specified percentage of amino acid residues, respectively, that are the same at the corresponding location within a reference sequence when the two sequences are optimally aligned. For example, an amino acid sequence that is “substantially identical” to a reference sequence has at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the reference amino acid sequence. For polypeptides, the length of comparison sequences will generally be at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 50, 75, 90, 100, 150, 200, 250, 300, or 350 contiguous amino acids (e.g., a full- length sequence). Sequence identity may be measured using sequence analysis software on the default setting (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, WI 53705). Such software may match similar sequences by assigning degrees of homology to various substitutions, deletions, and other modifications. [0100] As used herein, the term “targeting moiety” refers to any molecule or any part of a molecule that is capable of binding to a given target. The term, “TEM-1 targeting moiety” refers to a targeting moiety that is capable of binding a TEM-1 molecule, e.g., a human TEM- 1 molecule, e.g., a wild type or mutant TEM-1 molecule. [0101] As used herein, and as well understood in the art, “to treat” a condition or “treatment” of the condition (e.g., the conditions described herein such as cancer) is an approach for obtaining beneficial or desired results, such as clinical results. Beneficial or desired results can include, but are not limited to, alleviation or amelioration of one or more symptoms or conditions; diminishment of extent of disease, disorder, or condition; stabilized (i.e., not worsening) state of disease, disorder, or condition; preventing spread of disease, disorder, or condition; delay or slowing the progress of the disease, disorder, or condition; amelioration or palliation of the disease, disorder, or condition; and remission (whether partial or total), whether detectable or undetectable. “Palliating” a disease, disorder, or condition means that the extent and/or undesirable clinical manifestations of the disease, disorder, or condition are lessened and/or time course of the progression is slowed or lengthened, as compared to the extent or time course in the absence of treatment. [0102] As used herein, the term “about” or “approximately,” when used in reference to a quantitative value, includes the recited quantitative value itself, unless specifically stated otherwise. As used herein, the term “about” or “approximately” refers to a ±10% variation from the recited quantitative value unless otherwise indicated or inferred from the context. Radioimmunoconjugates [0103] In one aspect, the present disclosure provides radioimmunoconjugates having structure of Formula I-a: A-L-B (Formula I-a) wherein A is a chelating moiety or metal complex thereof, wherein B is a TEM-1 targeting moiety, and wherein L is a linker. [0104] In some embodiments, the radioimmunoconjugate has or comprises the structure shown in Formula II: , (Formula II) wherein B is the TEM-1 targeting moiety. [0105] In some embodiments, A-L- is a metal complex of a moiety selected from the group consisting of:

[0106] In some embodiments, as further described herein, the radioimmunoconjugate comprises a chelating moiety or metal complex thereof, which metal complex may comprise a radionuclide. In some such radioimmunoconjugates, the average ratio or median ratio of the chelating moiety to the TEM-1 targeting moiety is eight or less, seven or less, six or less, five or less, four or less, three or less, two or less, or about one. In some radioimmunoconjugates, the average ratio or median ratio of the chelating moiety to the TEM-1 targeting moiety is about one. [0107] In some embodiments, after the radioimmunoconjugate is administered to a mammal, the proportion of radiation (of the total amount of radiation that is administered) that is excreted by the intestinal route, the renal route, or both is greater than the proportion of radiation excreted by a comparable mammal that has been administered a reference radioimmunoconjugate. By “reference immunoconjugate” it is meant a known radioimmunoconjugate that differs from a radioimmunoconjugate described herein at least by (1) having a different linker; (2) having a targeting moiety of a different size and/or (3) lacking a targeting moiety. In some embodiments, the reference radioimmunoconjugate is selected from the group consisting of [ ⁹⁰ Y]-ibritumomab tiuxetan (Zevalin (90Y)) and [ ¹¹¹ In]- ibritumomab tiuxetan (Zevalin ( ¹¹¹ In)). [0108] In some embodiments, the proportion of radiation excreted by a given route or set of routes) is at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or at least 95% greater than the proportion of radiation excreted by the same route(s) by a comparable mammal that has been administered a reference radioimmunoconjugate. In some embodiments, the proportion of radiation excreted is at least 1.5-fold, at least 2-fold, at least 2.5-fold, at least 3-fold, at least 3.5 fold, at least 4-fold, at least 4.5 fold, at least 5 fold, at least 6-fold, at least 7-fold, at least 8-fold, at least 9-fold, or at least 10-fold greater than proportion of radiation excreted by a comparable mammal that has been administered a reference radioimmunoconjugate. The extent of excretion can be measured by methods known in the art, e.g., by measuring radioactivity in urine and/or feces and/or by measuring total body radioactivity over a period time. See also, e.g., International Patent Publication WO 2018/024869. [0109] In some embodiments, the extent of excretion is measured at a time period of at least or about 12 hours after administration, at least or about 24 hours after administration, at least or about 2 days after administration, at least or about 3 days after administration, at least or about 4 days after administration, at least or about 5 days after administration, at least or about 6 days after administration, or at least or about 7 days, after administration. [0110] In some embodiments, after a radioimmunoconjugate has been administered to a mammal, the radioimmunoconjugate exhibits decreased off-target binding effects (e.g., toxicities) as compared to a reference conjugate (e.g., a reference immunoconjugate such as a reference radioimmunoconjugate). In some embodiments, this decreased off-target binding effect is a feature of a radioimmunoconjugate that also exhibits a greater excretion rate as described herein. Targeting moieties [0111] Targeting moieties include any molecule or any part of a molecule that is capable of binding to a given target, e.g., TEM-1. In some embodiments, the targeting moiety is capable of binding to an epitope within human TEM-1, an exemplary sequence for which is shown in SEQ ID NO: 1: (SEQ ID NO: 1) [0112] In some embodiments, the targeting moiety comprises a protein or polypeptide. In some embodiments, the targeting moiety is selected from the group consisting of antibodies or antigen binding fragments thereof, nanobodies, affibodies, and consensus sequences from Fibronectin type III domains (e.g., Centyrins or Adnectins). In some embodiments, a moiety is both a targeting and a therapeutic moiety, i.e., the moiety is capable of binding to a given target and also confers a therapeutic benefit. In some embodiments, the targeting moiety comprises a small molecule. [0113] In some embodiments, the targeting moiety has a molecular weight of at least 50 kDa, at least 75 kDa, at least 100 kDa, at least 125 kDa, at least 150 kDa, at least 175 kDa, at least 200 kDa, at least 225 kDa, at least 250 kDa, at least 275 kDa, or at least 300 kDa. [0114] Typically, the targeting moiety is capable of binding to TEM-1, e.g., wild type and/or mutant TEM-1. In some embodiments, the targeting moiety is capable of binding to human TEM-1, e.g., wild type and/or mutant human TEM-1. [0115] In some embodiments, the targeting moiety is capable of binding specifically to TEM-1 (e.g., is capable of binding to TEM-1 while exhibiting comparatively little or no binding to other proteins, such as other C-lectin family proteins). [0116] In some embodiments, the targeting moiety is capable of binding to an extracellular region of TEM-1, e.g., the C-type lectin domain, the Sushi-like domain, one of the three EGF repeat domains, or the mucin domain. In some embodiments, the targeting moiety is capable of binding to a portion of the extracellular region that is not the C-type lectin domain (e.g., a Sushi-like domain, an EGF repeat domain, or the mucin domain). [0117] In some embodiments, the targeting moiety inhibits TEM-1. By “inhibits,” it is meant that the targeting moiety at least partially inhibits one or more functions of TEM-1 (e.g., human TEM-1). In some embodiments, the targeting moiety at least partially inhibits one or more functions of wild type TEM-1, e.g., wild type human TEM-1. [0118] In some embodiments, the targeting moiety blocks binding of TEM-1 to one or more of its protein binding partner. For example, in some embodiments, the targeting moiety blocks binding of TEM-1 to an extracellular matrix protein (e.g., an extracellular matrix protein that mediates cell adhesion and migration, such as fibronectin or collagen I). In some embodiments, the targeting moiety blocks binding of TEM-1 to LGALS3BP6. [0119] In some embodiments, the targeting moiety impairs signaling downstream of TEM-1. Antibodies [0120] Antibodies typically comprise two identical light polypeptide chains and two identical heavy polypeptide chains linked together by disulfide bonds. The first domain located at the amino terminus of each chain is variable in amino acid sequence, providing the antibody-binding specificities of each individual antibody. These are known as variable heavy (VH) and variable light (VL) regions. The other domains of each chain are relatively invariant in amino acid sequence and are known as constant heavy (CH) and constant light (CL) regions. Light chains typically comprise one variable region (VL) and one constant region (CL). An IgG heavy chain includes a variable region (VH), a first constant region (CH1), a hinge region, a second constant region (CH2), and a third constant region (CH3). In IgE and IgM antibodies, the heavy chain includes an additional constant region (CH4). [0121] Antibodies suitable for use with the present disclosure can include, for example, monoclonal antibodies, polyclonal antibodies, multispecific antibodies, human antibodies, humanized antibodies, camelid antibodies, chimeric antibodies, single-chain Fvs (scFv), disulfide-linked Fvs (sdFv), and anti-idiotypic (anti-Id) antibodies, and antigen-binding fragments of any of the above. In some embodiments, the antibody or antigen-binding fragment thereof is humanized. In some embodiments, the antibody or antigen-binding fragment thereof is chimeric. Antibodies can be of any type (e.g., IgG, IgE, IgM, IgD, IgA and IgY), class (e.g., IgG1, IgG2, IgG3, IgG4, IgA1 and IgA2) or subclass. [0122] The term “antigen binding fragment” of an antibody, as used herein, refers to one or more fragments of an antibody that retain the ability to specifically bind to an antigen. Examples of binding fragments encompassed within the term “antigen binding fragment” of an antibody include a Fab fragment, a F(ab')2 fragment, a Fd fragment, a Fv fragment, a scFv fragment, a dAb fragment (Ward et al., (1989) Nature 341:544-546), and an isolated complementarity determining region (CDR). In some embodiments, an “antigen binding fragment” comprises a heavy chain variable region and a light chain variable region. These antibody fragments can be obtained using conventional techniques known to those with skill in the art, and the fragments can be screened for utility in the same manner as are intact antibodies. [0123] Antibodies or antigen-binding fragments described herein can be produced by any method known in the art for the synthesis of antibodies (see, e.g., Harlow et al., Antibodies: A Laboratory Manual (Cold Spring Harbor Laboratory Press, 2nd ed.1988); Brinkman et al., 1995, J. Immunol. Methods 182:41-50; WO 92/22324; WO 98/46645). Chimeric antibodies can be produced using the methods described in, e.g., Morrison, 1985, Science 229:1202, and humanized antibodies by methods described in, e.g., U.S. Pat. No.6,180,370. [0124] Additional antibodies described herein are bispecific antibodies and multivalent antibodies, as described in, e.g., Segal et al., J. Immunol. Methods 248:1-6 (2001); and Tutt et al., J. Immunol.147: 60 (1991), or any of the molecules described herein. [0125] “Avimer” relates to a multimeric binding protein or peptide engineered using, for example, in vitro exon shuffling and phage display. Multiple binding domains are linked, resulting in greater affinity and specificity compared to single epitope immunoglobin domains. [0126] “Nanobodies” are antibody fragments consisting of a single monomeric variable antibody domain. Nanobodies may also be referred to as single-domain antibodies. Like antibodies, nanobodies bind selectively to a specific antigen. Nanobodies may be heavy- chain variable domains or light chain domains. Nanobodies may occur naturally or be the product of biological engineering. Nanobodies may be biologically engineered by site- directed mutagenesis or mutagenic screening (e.g., phage display, yeast display, bacterial display, mRNA display, ribosome display).“Affibodies” are polypeptides or proteins engineered to bind to a specific antigen. As such, affibodies may be considered to mimic certain functions of antibodies. [0127] Affibodies may be engineered variants of the B-domain in the immunoglobulin- binding region of staphylococcal protein A. Affibodies may be engineered variants of the Z- domain, a B-domain that has lower affinity for the Fab region. Affibodies may be biologically engineered by site-directed mutagenesis or mutagenic screening (e.g., phage display, yeast display, bacterial display, mRNA display, ribosome display). [0128] Affibody molecules showing specific binding to a variety of different proteins (e.g. insulin, fibrinogen, transferrin, tumor necrosis factor-α, IL-8, gp120, CD28, human serum albumin, IgA, IgE, IgM, HER2 and EGFR) have been generated, demonstrating affinities (Kd) in the μM to pM range. “Diabodies” are antibody fragments with two antigen- binding sites that may be bivalent or bispecific. See for example Hudson et al., (2003). Single-chain antibodies are antibody fragments comprising all or a portion of the heavy chain variable domain or all, or a portion of the light chain variable domain of an antibody. Antibody fragments can be made by various techniques including but not limited to proteolytic digestion of an intact antibody as well as production by recombinant hosts (e.g., E. coli or phage) as described herein. [0129] In certain embodiments, the antibody or antigen-binding fragment thereof is a multispecific, e.g. bispecific. Multispecific antibodies (or antigen-binding fragments thereof) include monoclonal antibodies (or antigen-binding fragments thereof) that have binding specificities for at least two different sites. [0130] In certain embodiments, amino acid sequence variants of antibodies or antigen- binding fragments thereof are contemplated; e.g., variants that bind to TEM-1, e.g., human TEM-1. For example, it may be desirable to improve the binding affinity and/or other biological properties of the antibody or antigen-binding fragment thereof. Amino acid sequence variants of an antibody or antigen-binding fragment thereof may be prepared by introducing appropriate modifications into the nucleotide sequence encoding the antibody or antigen-binding fragment thereof, or by peptide synthesis. Such modifications include, for example, deletions from and/or insertions into and/or substitutions of residues within the amino acid sequences of the antibody or antigen-binding fragment thereof. Any combination of deletion, insertion and substitution can be made to arrive at the final construct, provided that the final construct possesses desired characteristics, e.g. antigen binding. [0131] In some embodiments, the antibody or antigen binding fragment thereof is an inhibitory antibody (also called “antagonistic antibody”) or antigen-binding fragment thereof, e.g., the antibody or antigen binding fragment thereof at least partially inhibits one or more functions of the target molecule (e.g., TEM-1) as explained further herein. [0132] Non-limiting examples of inhibitory antibodies include humanized monoclonal antibodies such as hMP-E-8.3 (Mediapharma), ontuxizumab (also known as MORAb-004) (Morphotek), and anti-TEM-1 antibodies from Kirin Brewery. (See, e.g., U.S. Pat. No. 8,895,000, and International Patent Publication Nos. WO 2017/134234 A1 and WO 2006/017759 A2.) [0133] In some embodiments, the antibody or antigen binding fragment thereof is an agonistic antibody (also known as stimulatory antibody). [0134] In some embodiments, the antibody or antigen binding fragment thereof is neither agonistic or antagonistic, or has not been characterized as either agonistic or antagonistic. [0135] Additional known TEM-1 antibodies include, for example, humanized antibodies such as humanized FB5; mouse monoclonal antibodies such as, for example, mMP-E-8.3 (Mediapharma) (see, e.g., WO 2017/134234), FB5, 1F9B4 (Proteintech Group), G-9 (sc- 377221) (Santa Cruz Biotechnology), and B1/35 (MilliporeSigma); rat monoclonal antibodies such as, e.g., 9G5, 16D2, 7H12, 15F8, 9A5, 11D1, 15D10, 7D3, or 16D2 from Morphotek (see, e.g., WO 2013/148250), clone 458606 (R&D systems), CBFYE-0326 (Creative Biolabs); rabbit monoclonal antibodies such as EPR17081 (Abcam); and chimeric antibodies such as cMP-E-8.3 (Mediapharma) (see, e.g., WO 2017/134234). [0136] In some embodiments, the TEM-1 antibody or antigen-binding fragment thereof is capable of binding an epitope comprising an amino acid sequence of SRDHQIPVIAAN (SEQ ID NO: 2). [0137] In certain embodiments of the present disclosure, the antibody or antigen-binding fragment thereof comprises specific heavy chain complementarity determining regions CDR- H1, CDR-H2 and/or CDR-H3 as described herein. In some embodiments, the complementarity determining regions (CDRs) of the antibody or antigen-binding fragment thereof are flanked by framework regions. A heavy or light chain of an antibody or antigen- binding fragment thereof containing three CDRs typically contains four framework regions. [0138] In some embodiments, the heavy chain variable region of the TEM-1 antibody or antibody-binding fragment thereof comprises one, two, or three complementarity determining regions (CDRs) CDR-H1, CDR-H2, and/or CDR-H3, with amino acid sequences shown below,, or CDR region(s) having an amino acid sequence(s) differing in 1 or 2 amino acids therefrom: [0139] In some embodiments, the light chain variable region of the TEM-1 antibody or antibody-binding fragment thereof comprises one, two, or three complementarity determining regions (CDRs) CDR-L1, CDR-L2, and/or CDR-L3. with amino acid sequences as shown below, or CDR region(s) having an amino acid sequence(s) differing in 1 or 2 amino acids therefrom: [0140] In some embodiments, the antibody or antigen-binding fragment thereof comprises: (i) a heavy chain comprising: a heavy chain complementarity determining region 1 (CDR-H1) having the amino acid sequence as shown in SEQ ID NO: 3 or an amino acid sequence differing in 1 or 2 amino acids therefrom, a heavy chain complementarity determining region 2 (CDR-H2) having the amino acid sequence as shown in SEQ ID NO: 5 or an amino acid sequence differing in 1 or 2 amino acids therefrom, and a heavy chain complementarity determining region 3 (CDR-H3) having the amino acid sequence as shown in SEQ ID NO: 6 or an amino acid sequence differing in 1 or 2 amino acids therefrom, and (ii) a light chain comprising: a light chain complementarity determining region 1 (CDR-L1) having the amino acid sequence as shown in SEQ ID NO: 7 or an amino acid sequence differing in 1 or 2 amino acids therefrom, a light chain complementarity determining region 2 (CDR-L2) having the amino acid sequence as shown in SEQ ID NO: 8 or an amino acid sequence differing in 1 or 2 amino acids therefrom, and a light chain complementarity determining region 3 (CDR-L3) having the amino acid sequence as shown in SEQ ID NO: 9 or an amino acid sequence differing in 1 or 2 amino acids therefrom, or a monoclonal antibody recognizing the same epitope (e.g., an epitope having the sequence of SEQ ID NO: 2) on human TEM-1. [0141] In some embodiments, the antibody or antigen-binding fragment thereof has CDR sequences having amino acid sequences of SEQ ID NOs: 3 and 5-9 without any variation. For example, in some embodiments, the antibody or antigen-binding fragment thereof comprises heavy chain complementary determining regions CDR-H1, CDR-H2, and CDR-H3 having the amino acid sequences of SEQ ID NOs: 3, 5, and 6, and the chain complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 having the amino acid sequences of SEQ ID NOs: 7, 8, and 9. [0142] In some embodiments, the antibody or antigen-binding fragment thereof has CDR sequences having amino acid sequences of SEQ ID NOs: 4-9 without any variation. For example, in some embodiments, the antibody or antigen-binding fragment thereof comprises heavy chain complementary determining regions CDR-H1, CDR-H2, and CDR-H3 having the amino acid sequences of SEQ ID NOs: 4, 5, and 6, and the chain complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 having the amino acid sequences of SEQ ID NOs: 7, 8, and 9. [0143] In some embodiments, the heavy chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence of SEQ ID NO: 10 or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 10: (SEQ ID NO: 10) [0144] In some embodiments, the light chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence of SEQ ID NO: 11 or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 11: (SEQ ID NO: 11) [0145] In some embodiments, the heavy chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence of SEQ ID NO: 12 or 13 or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 12 or 13: (SEQ ID NO: 12) (SEQ ID NO: 13) [0146] In some embodiments, the light chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence of SEQ ID NO: 14 or 15 or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 14 or 15: (SEQ ID NO: 14) (SEQ ID NO: 15) [0147] In some embodiments, the TEM-1 antibody or antigen-binding fragment thereof is a humanized antibody or antigen-binding fragment thereof. [0148] In some embodiments, the heavy chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 16, 17, 18, and 19, or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 16, 17, 18, and 19: Humanized VH1: (SEQ ID NO: 16) Humanized VH2: (SEQ ID NO: 17) Humanized VH3: (SEQ ID NO: 18) Humanized VH4: (SEQ ID NO: 19) [0149] In some embodiments, the light chain variable region of the TEM-1 antibody or antigen-binding fragment thereof comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 20, 21, 22, and 23, or an amino acid sequence differing in 1, 2, 3, or 4 amino acids therefrom, or an amino acid sequence having at least 85%, at least 90%, at least 95%, at least 97%, or at least 99% identity to SEQ ID NO: 20, 21, 22, and 23: Humanized VL1: (SEQ ID NO: 20) Humanized VL2: (SEQ ID NO: 21) Humanized VL3: (SEQ ID NO: 22) Humanized VL4: (SEQ ID NO: 23). [0150] In some embodiments, the antibody, or antibody-binding fragment thereof, comprises a heavy chain variable domain comprising the amino acid sequence of SEQ ID NO: 16, and a light chain variable domain comprising the amino acid sequence of SEQ ID NO: 21. [0151] In certain embodiments, the antibody or antigen-binding fragment thereof has a dissociation constant (Kd) of ≤ 1 µM, ≤ 100 nM, ≤ 10 nM, ≤ 1 nM, ≤ 0.1 nM, ≤ 0.01 nM, or ≤ 0.001 nM. In some embodiments, the antibody or antigen-binding fragment thereof has a dissociation constant (Kd) of between 1 nM and 10 nM (inclusive of endpoints) or between 0.1 nM and 1 nM (inclusive of endpoints). [0152] In one embodiment, Kd is measured by a radio-labeled antigen binding assay (radioimmunoassay, RIA) performed with the Fab version of an antibody or antigen-binding fragment thereof of interest and its antigen. [0153] According to another embodiment, Kd is measured using surface plasmon resonance assays with immobilized antigen. In some embodiments, the antibodies or antigen- binding fragments thereof are human monoclonal antibodies directed against an epitope of TEM-1, e.g., human TEM-1. [0154] The antibody or antigen-binding fragment thereof may be any antibody or antigen-binding fragment thereof of natural and/or synthetic origin, e.g. an antibody of mammalian origin. In some embodiments, the constant domain, if present, is a human constant domain. In some embodiments, the variable domain is a mammalian variable domain, e.g., a humanized or a human variable domain. [0155] In some embodiments, antibodies used in accordance with this disclosure are monoclonal antibodies. In some embodiments, antibodies are recombinant murine antibodies, chimeric, humanized or fully human antibodies, multispecific antibodies (e.g., bispecific antibodies), or antigen-binding fragments thereof. [0156] In some embodiments, are further coupled to other moieties for, e.g., drug targeting and imaging applications. [0157] In some embodiments, e.g., for diagnostic purposes, the antibody or antigen- binding fragment thereof is labelled, i.e. coupled to a labelling group. Non-limiting examples of suitable labels include radioactive labels, fluorescent labels, suitable dye groups, enzyme labels, chromogenes, chemiluminescent groups, biotinyl groups, predetermined polypeptide epitopes recognized by a secondary reporter etc. In some embodiments, one or more labels are covalently bound to the antibody or antigen-binding fragment thereof. [0158] Those labelled antibodies or antigen-binding fragments thereof (also referred to as "antibody conjugates") may in particular be used in immunohistochemistry assays or for molecular imaging in vivo. [0159] In some embodiments, e.g., for therapeutic purposes, the antibody or antigen- binding fragment thereof is further conjugated with an effector group, in particular, a therapeutic effector group such as a cytotoxic agent or a radioactive group agent. Polypeptides [0160] Polypeptides include, for example, any of a variety of hematologic agents (including, for instance, erythropoietin, blood-clotting factors, etc.), interferons, colony stimulating factors, antibodies, enzymes, and hormones. The identity of a particular polypeptide is not intended to limit the present disclosure, and any polypeptide of interest can be a polypeptide in the present methods. [0161] A reference polypeptide described herein can include a target-binding domain that is capable of binding to a target of interest (e.g., capable of binding to an antigen, e.g., TEM- 1). For example, a polypeptide, such as an antibody, can be capable of binding to a transmembrane polypeptide (e.g., receptor) or ligand (e.g., a growth factor). Modified polypeptides [0162] Polypeptides suitable for use with compositions and methods of the present disclosure may have a modified amino acid sequence. Modified polypeptides may be substantially identical to the corresponding reference polypeptide (e.g., the amino acid sequence of the modified polypeptide may have at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the amino acid sequence of the reference polypeptide). In certain embodiments, the modification does not destroy significantly a desired biological activity (e.g., binding to TEM-1). The modification may reduce (e.g., by at least 5%, 10%, 20%, 25%, 35%, 50%, 60%, 70%, 75%, 80%, 90%, or 95%), may have no effect, or may increase (e.g., by at least 5%, 10%, 25%, 50%, 100%, 200%, 500%, or 1000%) the biological activity of the original polypeptide. The modified polypeptide may have or may optimize a characteristic of a polypeptide, such as in vivo stability, bioavailability, toxicity, immunological activity, immunological identity, and conjugation properties. [0163] Modifications include those by natural processes, such as post-translational processing, or by chemical modification techniques known in the art. Modifications may occur anywhere in a polypeptide including the polypeptide backbone, the amino acid side chains and the amino- or carboxy-terminus. The same type of modification may be present in the same or varying degrees at several sites in a given polypeptide, and a polypeptide may contain more than one type of modification. Polypeptides may be branched as a result of ubiquitination, and they may be cyclic, with or without branching. Cyclic, branched, and branched cyclic polypeptides may result from post-translational natural processes or may be made synthetically. Other modifications include pegylation, acetylation, acylation, addition of acetomidomethyl (Acm) group, ADP-ribosylation, alkylation, amidation, biotinylation, carbamoylation, carboxyethylation, esterification, covalent attachment to flavin, covalent attachment to a heme moiety, covalent attachment of a nucleotide or nucleotide derivative, covalent attachment of drug, covalent attachment of a marker (e.g., fluorescent or radioactive), covalent attachment of a lipid or lipid derivative, covalent attachment of phosphatidylinositol, cross-linking, cyclization, disulfide bond formation, demethylation, formation of covalent crosslinks, formation of cystine, formation of pyroglutamate, formylation, gamma-carboxylation, glycosylation, GPI anchor formation, hydroxylation, iodination, methylation, myristoylation, oxidation, proteolytic processing, phosphorylation, prenylation, racemization, selenoylation, sulfation, transfer-RNA mediated addition of amino acids to proteins such as arginylation and ubiquitination. [0164] A modified polypeptide can also include an amino acid insertion, deletion, or substitution, either conservative or non-conservative (e.g., D-amino acids, desamino acids) in the polypeptide sequence (e.g., where such changes do not substantially alter the biological activity of the polypeptide). In particular, the addition of one or more cysteine residues to the amino or carboxy-terminus of a polypeptide herein can facilitate conjugation of these polypeptides by, e.g., disulfide bonding. For example, a polypeptide can be modified to include a single cysteine residue at the amino-terminus or a single cysteine residue at the carboxy-terminus. Amino acid substitutions can be conservative (i.e., wherein a residue is replaced by another of the same general type or group) or non-conservative (i.e., wherein a residue is replaced by an amino acid of another type). In addition, a naturally occurring amino acid can be substituted for a non-naturally occurring amino acid (i.e., non-naturally occurring conservative amino acid substitution or a non-naturally occurring non-conservative amino acid substitution). [0165] Polypeptides made synthetically can include substitutions of amino acids not naturally encoded by DNA (e.g., non-naturally occurring or unnatural amino acid). Examples of non-naturally occurring amino acids include D-amino acids, N-protected amino acids, an amino acid having an acetylaminomethyl group attached to a sulfur atom of a cysteine, a pegylated amino acid, the omega amino acids of the formula NH ₂ (CH ₂ ) _n COOH wherein n is 2-6, neutral nonpolar amino acids, such as sarcosine, t-butyl alanine, t-butyl glycine, N- methyl isoleucine, and norleucine. Phenylglycine may substitute for Trp, Tyr, or Phe; citrulline and methionine sulfoxide are neutral nonpolar, cysteic acid is acidic, and ornithine is basic. Proline may be substituted with hydroxyproline and retain the conformation conferring properties. [0166] Analogs may be generated by substitutional mutagenesis and retain the biological activity of the original polypeptide. Examples of substitutions identified as “conservative substitutions” are shown in Table 1. If such substitutions result in a change not desired, then other type of substitutions, denominated “exemplary substitutions” in Table 1, or as further described herein in reference to amino acid classes, are introduced and the products screened. [0167] Table 1: Amino acid substitutions [0168] Substantial modifications in function or immunological identity are accomplished by selecting substitutions that differ significantly in their effect on maintaining (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a sheet or helical conformation, (b) the charge or hydrophobicity of the molecule at the target site, and/or (c) the bulk of the side chain. Chelating moiety or metal complex thereof: Chelating moieties [0169] Examples of suitable chelating moieties include, but are not limited to, DOTA (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid), DOTMA (1R,4R,7R,10R)-α, α’, α”, α’”-tetramethyl-1,4,7,10-tetraazacyclododecane-1,4,7,10 -tetraacetic acid, DOTAM (1,4,7,10-tetrakis(carbamoylmethyl)-1,4,7,10-tetraazacyclodo decane), DOTPA (1,4,7,10- tetraazacyclododecane-1,4,7,10-tetra propionic acid), DO3AM-acetic acid (2-(4,7,10-tris(2- amino-2-oxoethyl)-1,4,7,10-tetraazacyclododecan-1-yl)acetic acid), DOTA-GA anhydride (2,2’,2”-(10-(2,6-dioxotetrahydro-2H-pyran-3-yl)-1,4,7,1 0-tetraazacyclododecane-1,4,7- triyl)triacetic acid, DOTP (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetra(methylene phosphonic acid)), DOTMP (1,4,6,10-tetraazacyclodecane-1,4,7,10-tetramethylene phosphonic acid, DOTA-4AMP (1,4,7,10-tetraazacyclododecane-1,4,7,10- tetrakis(acetamido-methylenephosphonic acid), CB-TE2A (1,4,8,11- tetraazabicyclo[6.6.2]hexadecane-4,11-diacetic acid), NOTA (1,4,7-triazacyclononane-1,4,7- triacetic acid), NOTP (1,4,7-triazacyclononane-1,4,7-tri(methylene phosphonic acid), TETPA (1,4,8,11-tetraazacyclotetradecane-1,4,8,11-tetrapropionic acid), TETA (1,4,8,11- tetraazacyclotetradecane-1,4,8,11-tetra acetic acid), HEHA (1,4,7,10,13,16- hexaazacyclohexadecane-1,4,7,10,13,16-hexaacetic acid), PEPA (1,4,7,10,13- pentaazacyclopentadecane-N,N’,N”,N’’’, N’’’’-pentaacetic acid), H ₄ octapa (N,N’-bis(6- carboxy-2-pyridylmethyl)-ethylenediamine-N,N’-diacetic acid), H2dedpa (1,2-[[6-(carboxy)- pyridin-2-yl]-methylamino]ethane), H6phospa (N,N’-(methylenephosphonate)-N,N’-[6- (methoxycarbonyl)pyridin-2-yl]-methyl-1,2-diaminoethane), TTHA (triethylenetetramine- N,N,N’,N”,N’’’, N’’’-hexaacetic acid), DO2P (tetraazacyclododecane dimethanephosphonic acid), HP-DO3A (hydroxypropyltetraazacyclododecanetriacetic acid), EDTA (ethylenediaminetetraacetic acid), Deferoxamine, DTPA (diethylenetriaminepentaacetic acid), DTPA-BMA (diethylenetriaminepentaacetic acid-bismethylamide), octadentate-HOPO (octadentate hydroxypyridinones), or porphyrins. [0170] In some embodiments, radioimmunoconjugates comprise a metal complex of a chelating moiety. For example, chelating groups may be used in metal chelate combinations with metals, such as manganese, iron, and gadolinium and isotopes (e.g., isotopes in the general energy range of 60 to 10,000 keV), such as any of the radioisotopes and radionuclides discussed herein. [0171] In some embodiments, chelating moieties are useful as detection agents, and radioimmunoconjugates comprising such detectable chelating moieties can therefore be used as diagnostic or theranostic agents. Radioisotopes and Radionuclides [0172] In some embodiments, the metal complex comprises a radionuclide. Examples of suitable radioisotopes and radionuclides include, but are not limited to, ³ H, ¹⁴ C, ¹⁵ N, ¹⁸ F, ³⁵ S, ⁴⁷ Sc, ⁵⁵ Co, ⁶⁰ Cu, ⁶¹ Cu, ⁶² Cu, ⁶⁴ Cu, ⁶⁶ Ga, ⁶⁷ Ga, ⁶⁷ Cu, ⁶⁸ Ga, ⁷⁵ Br, ⁷⁶ Br , ⁷⁷ Br , ⁸² Rb, ⁸⁹ Zr, ⁸⁶ Y, ⁸⁷ Y, ⁹⁰ Y, ⁹⁷ Ru, ⁹⁹ Tc, ^99m Tc, ¹⁰⁵ Rh, ¹⁰⁹ Pd, ¹¹¹ In, ¹²³ I, ¹²⁴ I, ¹²⁵ I, ¹³¹ I, ¹⁴⁹ Pm, ¹⁴⁹ Tb, ¹⁵³ Sm, ¹⁶⁶ Ho, ¹⁷⁷ Lu, ^117m Sn, ¹⁸⁶ Re, ¹⁸⁸ Re, ¹⁹⁸ Au, ¹⁹⁹ Au, ²⁰¹ Tl, ²⁰³ Pb, ²¹¹ At, ²¹² Pb , ²¹² Bi, ²¹³ Bi, ²²³ Ra, ²²⁵ Ac, ²²⁷ Th, and ²²⁹ Th. [0173] In some embodiments, the radionuclide is an alpha emitter, e.g., Astatine-211 ( ²¹¹ At), Bismuth-212 ( ²¹² Bi), Bismuth-213 ( ²¹³ Bi), Actinium-225 ( ²²⁵ Ac), Radium-223 ( ²²³ Ra), Lead-212 ( ²¹² Pb), Thorium-227 ( ²²⁷ Th), or Terbium-149 ( ¹⁴⁹ Tb), or a progeny thereof. In some embodiments, the alpha-emitter is Actinium-225 ( ²²⁵ Ac), or a progeny thereof. Linker [0174] In some embodiments, the linker is as shown within the structure of Formula I-b, as that part of Formula I-b absent A and B: A-L ¹ -(L ² )n-B (Formula I-b) (A and B are as defined in Formula I-a.) [0175] Thus, in some embodiments, the linker is -L ¹ -(L ² )n-, wherein: L ¹ is a bond, optionally substituted C ₁ -C ₆ alkyl, optionally substituted C ₁ -C ₆ heteroalkyl, or optionally substituted aryl or heteroaryl; n is an integer between 1 and 5 (inclusive); and each L ² , independently, has the structure: -X ¹ -L ³ -Z ¹ - (Formula III) wherein X ¹ is C=O(NR ¹ ), C=S(NR ¹ ), OC=O(NR ¹ ), NR ¹ C=O(O), NR ¹ C=O(NR ¹ ), -CH ₂ PhC=O(NR ¹ ), -CH ₂ Ph(NH)C=S(NR ¹ ) , O, or NR ¹ ; and each R ¹ independently is H, optionally substituted C1-C6 alkyl, optionally substituted C1-C6 heteroalkyl, or optionally substituted aryl or heteroaryl, in which C1-C6 alkyl can be substituted by oxo (=O), heteroaryl, or a combination thereof; L ³ is optionally substituted C ₁ -C ₅₀ alkyl or optionally substituted C ₁ -C ₅₀ heteroalkyl (e.g., C5-C20 polyethylene glycol); and Z ¹ is CH ₂ , C=O, C=S, OC=O, NR ¹ C=O, or NR ¹ , wherein R ¹ is a hydrogen or optionally substituted C ₁ -C ₆ alkyl or pyrrolidine-2,5-dione. [0176] In some embodiments, L ¹ is substituted C1-C6 alkyl or substituted C1-C6 heteroalkyl, the substituent comprising a heteroaryl group (e.g., six-membered nitrogen- containing heteroaryl). [0177] In some embodiments, L ³ is substituted C1-C50 alkyl or substituted C1-C50 heteroalkyl, the substituent comprising a heteroaryl group (e.g., six-membered nitrogen- containing heteroaryl). In some embodiments, L ³ is C ₁ -C ₅₀ heteroalkyl. In some embodiments, L ³ is C ₅ -C ₂₀ polyethylene glycol. In some embodiments, L ³ is (CH2CH2O)m(CH2)w, and m and w are independently an integer between 0 and 10 (inclusive). [0178] In some embodiments, A is a macrocyclic chelating moiety comprising one or more heteroaryl groups (e.g., six-membered nitrogen-containing heteroaryl). Cross-linking groups [0179] In some embodiments, radioimmunoconjugates are synthesized using bifunctional chelates that comprise a chelate, a linker, and a cross-linking group. Once the radioimmunoconjugate is formed, the cross-linking group may be absent from the radioimmunoconjugate. [0180] In some embodiments, radioimmunoconjugates comprise a cross-linking group instead of or in addition to the targeting moiety (e.g., in some embodiments, B in Formula I comprises a cross-linking group). [0181] A cross-linking group is a reactive group that is able to join two or more molecules by a covalent bond. Cross-linking groups may be used to attach the linker and chelating moiety to a therapeutic or targeting moiety. Cross-linking groups may also be used to attach the linker and chelating moiety to a target in vivo. In some embodiments, the cross- linking group is an amino-reactive, methionine reactive or thiol-reactive cross-linking group, or comprises a sortase recognition sequence. In some embodiments, the amino-reactive or thiol-reactive cross-linking group comprises an activated ester such as a hydroxysuccinimide ester, 2,3,5,6-tetrafluorophenol ester, 4-nitrophenol ester or an imidate, anhydride, thiol, disulfide, maleimide, azide, alkyne, strained alkyne, strained alkene, halogen, sulfonate, haloacetyl, amine, hydrazide, diazirine, phosphine, tetrazine, isothiocyanate, or oxaziridine. In some embodiments, the sortase recognition sequence may comprise of a terminal glycine- glycine-glycine (GGG) and/or LPTXG amino acid sequence, where X is any amino acid. A person having ordinary skill in the art will understand that the use of cross-linking groups is not limited to the specific constructs disclosed herein, but rather may include other known cross-linking groups. Pharmaceutical compositions [0182] In one aspect, the present disclosure provides pharmaceutical compositions comprising radioimmunoconjugates disclosed herein. Such pharmaceutical compositions can be formulated for use in a variety of drug delivery systems. One or more physiologically acceptable excipients or carriers can also be included in a pharmaceutical composition for proper formulation. Non-limiting examples of suitable formulations compatible for use with the present disclosure include those described in Remington’s Pharmaceutical Sciences, Mack Publishing Company, Philadelphia, PA, 17th ed., 1985. For a brief review of methods for drug delivery, see, e.g., Langer (Science.249:1527-1533, 1990). [0183] Pharmaceutical compositions may be formulated for any of a variety of routes of administration discussed herein (see, e.g., the “Administration and Dosage” subsection herein), Sustained release administration is contemplated, by such means as depot injections or erodible implants or components. Thus, the present disclosure provides pharmaceutical compositions that include agents disclosed herein (e.g., radioimmunoconjugates) dissolved or suspended in an acceptable carrier, preferably an aqueous carrier, e.g., water, buffered water, saline, or PBS, among others. In some embodiments, pharmaceutical compositions contain pharmaceutically acceptable auxiliary substances to approximate physiological conditions, such as pH adjusting and buffering agents, tonicity adjusting agents, wetting agents, or detergents, among others. In some embodiments, pharmaceutical compositions are formulated for oral delivery and may optionally contain inert ingredients such as binders or fillers for the formulation of a unit dosage form, such as a tablet or a capsule. In some embodiments, pharmaceutical compositions are formulated for local administration and may optionally contain inert ingredients such as solvents or emulsifiers for the formulation of a cream, an ointment, a gel, a paste, or an eye drop. [0184] In some embodiments, provided pharmaceutical compositions are sterilized by conventional sterilization techniques, e.g., may be sterile filtered. Resulting aqueous solutions may be packaged for use as is, or lyophilized. Lyophilized preparations can be, for example, combined with a sterile aqueous carrier prior to administration. The pH of preparations typically will be between 3 and 11, more preferably between 5 and 9 or between 6 and 8, and most preferably between 6 and 7, such as 6 to 6.5. Resulting compositions in solid form may be packaged, for example, in multiple single dose units, each containing a fixed amount of the above-mentioned agent or agents, such as in a sealed package of tablets or capsules. Pharmaceutical compositions in solid form can also be packaged in a container for a flexible quantity, such as in a squeezable tube designed for a topically applicable cream or ointment. Methods of treatment [0185] In one aspect, the present disclosure provides methods of treatment comprising a subject a radioimmunoconjugate as disclosed herein. Subjects [0186] In some disclosed methods, a therapy (e.g., comprising a therapeutic agent) is administered to a subject. In some embodiments, the subject is a mammal, e.g., a human. [0187] In some embodiments, the subject has cancer or is at risk of developing cancer. For example, the subject may have been diagnosed with cancer. For example, the cancer may be a primary cancer or a metastatic cancer. Subjects may have any stage of cancer, e.g., stage I, stage II, stage III, or stage IV with or without lymph node involvement and with or without metastases. Provided radioimmunoconjugates and compositions may prevent or reduce further growth of the cancer and/or otherwise ameliorate the cancer (e.g., prevent or reduce metastases). In some embodiments, the subject does not have cancer but has been determined to be at risk of developing cancer, e.g., because of the presence of one or more risk factors such as environmental exposure, presence of one or more genetic mutations or variants, family history, etc. In some embodiments, the subject has not been diagnosed with cancer. [0188] In many embodiments, the cancer is associated with TEM-1 expression. For example, in some embodiments, TEM-1 is expressed in tumor stromal cells (e.g., pericytes, myofibroblasts, or epithelial cells such as vascular epithelial cells). In some embodiments, the cancer comprises cancer cells that themselves express TEM-1. [0189] In some embodiments, the cancer is a solid tumor cancer, e.g., a carcinoma, sarcoma, melanoma, or lymphoma. [0190] In some embodiments, the solid tumor cancer is a carcinoma, e.g., adenocarcinoma, squamous cell carcinoma, or adenosquamous carcinoma. Non-limiting examples of carcinomas include adenoid cystic carcinoma, adrenocortical carcinoma, bladder cancer, breast cancer, cervical cancer, colorectal cancer, endometrial cancer, gallbladder carcinoma, gastric cancer, head and neck cancer, lung cancer (e.g., small cell lung cancer or non-small cell lung cancer, or adenocarcinoma of the lung), neuroblastoma, neuroendocrine cancer, ovarian cancer, pancreatic cancer, prostate cancer, renal cancer, testicular cancer. [0191] In some embodiments, the solid tumor cancer is a sarcoma. Non-limiting examples of sarcomas include angiosarcoma or hemangioendothelioma, astrocytoma, chondrosarcoma, Ewing’s sarcoma, fibrosarcoma, glioma, leiomyosarcoma, liposarcoma, malignant fibrous histiocytoma (MFH), mesenchymous or mixed mesodermal tumor, mesothelial sarcoma or mesothelioma, myxosarcoma, osteosarcoma, rhabdomyosarcoma, and synovial sarcoma. [0192] In some embodiments, the cancer is neuroblastoma. [0193] In some embodiments, the cancer is a brain cancer. In some embodiments, the cancer is a glioma. [0194] In some embodiments, the cancer is melanoma. [0195] In some embodiments, the cancer is a non-solid tumor cancer, e.g., a liquid cancer or hematologic cancer. In some embodiments, the cancer is a myeloma, e.g., multiple myeloma. In some embodiments, the cancer is a leukemia, e.g., acute myeloid leukemia. [0196] In some embodiments, the cancer is a mixed type cancer, e.g., mixed mesodermal tumor, carcinosarcoma, or teratocarcinoma. Administration and dosage [0197] Radioimmunoconjugates and pharmaceutical compositions thereof disclosed herein may be administered by any of a variety of routes of administration, including systemic and local routes of administration [0198] Systemic routes of administration include parenteral routes and enteral routes. In some embodiments, radioimmunoconjugates or pharmaceutical compositions thereof are administered by a parenteral route, for example, intravenously, intraarterially, intraperitoneally, subcutaneously, or intradermally. In some embodiments, radioimmunoconjugates or pharmaceutical compositions thereof are administered intravenously. In some embodiments, radioimmunoconjugates or pharmaceutical compositions thereof are administered by an enteral route of administration, for example, trans-gastrointestinal, or orally. [0199] Local routes of administration include, but are not limited to, peritumoral injections and intratumoral injections. [0200] Pharmaceutical compositions can be administered for radiation treatment planning, diagnostic, and/or therapeutic treatments. When administered for radiation treatment planning or diagnostic purposes, the radioimmunoconjugate may be administered to a subject in a diagnostically effective dose and/or an amount effective to determine the therapeutically effective dose. In therapeutic applications, pharmaceutical compositions may be administered to a subject (e.g., a human) already suffering from a condition (e.g., cancer) in an amount sufficient to cure or at least partially arrest the symptoms of the disorder and its complications. An amount adequate to accomplish this purpose is defined as a “therapeutically effective amount,” an amount of a compound sufficient to substantially improve at least one symptom associated with the disease or a medical condition. For example, in the treatment of cancer, an agent or compound that decreases, prevents, delays, suppresses, or arrests any symptom of the disease or condition would be therapeutically effective. A therapeutically effective amount of an agent or compound is not required to cure a disease or condition but may, for example, provide a treatment for a disease or condition such that the onset of the disease or condition is delayed, hindered, or prevented, such that the disease or condition symptoms are ameliorated, or such that the term of the disease or condition is changed. For example, the disease or condition may become less severe and/or recovery is accelerated in an individual. In some embodiments, a subject is administered a first dose of a radioimmunoconjugate or composition in an amount effective for radiation treatment planning, then administered a second dose or set of doses of the radioimmunoconjugate or composition in a therapeutically effective amount. [0201] Effective amounts may depend on the severity of the disease or condition and other characteristics of the subject (e.g., weight). Therapeutically effective amounts of disclosed radioimmunoconjugates and compositions for subjects (e.g., mammals such as humans) can be determined by the ordinarily-skilled artisan with consideration of individual differences (e.g., differences in age, weight, and the condition of the subject. [0202] In some embodiments, disclosed radioimmunoconjugates exhibit an enhanced ability to target cancer cells. In some embodiments, effective amount of disclosed radioimmunoconjugates are lower than (e.g., less than or equal to about 90%, 75%, 50%, 40%, 30%, 20%, 15%, 12%, 10%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, 0.5%, or 0.1% of) the equivalent dose for a therapeutic effect of the unconjugated, and/or non-radiolabeled targeting moiety. [0203] Single or multiple administrations of pharmaceutical compositions disclosed herein including an effective amount can be carried out with dose levels and pattern being selected by the treating physician. Dose and administration schedule can be determined and adjusted based on the severity of the disease or condition in the subject, which may be monitored throughout the course of treatment according to the methods commonly practiced by clinicians or those described herein. [0204] The following specific examples are to be construed as merely illustrative, and not limitative of the remainder of the disclosure in any way whatsoever. EXAMPLES Example 1. General materials and methods [0205] Lutetium-177 can be obtained from Perkin Elmer as lutetium trichloride in a 0.05 N hydrochloric acid solution; indium-111, as a trichloride salt, can be obtained from BWX Technologies and actinium-225 can be obtained as actinium-225 trinitrate from Oak Ridge National Laboratories. [0206] Analytical HPLC-MS can be performed using a Waters Acquity HPLC-MS system comprised of a Waters Acquity Binary Solvent Manager, a Waters Acquity Sample Manager (samples cooled to 10˚C), a Water Acquity Column Manager (column temperature 30˚C), a Waters Acquity Photodiode Array Detector (monitoring at 254 nm and 214 nm), a Waters Acquity TQD with electrospray ionization and a Waters Acquity BEH C18, 2.1×50 (1.7 μm) column. Preparative HPLC can be performed using a Waters HPLC system comprised of a Waters 1525 Binary HPLC pump, a Waters 2489 UV/Visible Detector (monitoring at 254 nm and 214 nm) and a Waters XBridge Prep phenyl or C1819×100 mm (5 μm) column. [0207] HPLC elution method 1: Waters Acquity BEH C182.1×50 mm (1.7 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate = 0.3 mL/min; initial = 90% A, 3-3.5 min = 0% A, 4 min = 90% A, 5 min = 90% A. [0208] HPLC elution method 2: Waters XBridge Prep Phenyl 19×100 mm (5 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 80% A, 13 min = 0% A. [0209] HPLC elution method 3: Waters Acquity BEH C182.1×50 mm (1.7 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate = 0.3 mL/min; initial = 90% A, 8 min = 0% A, 10 min = 0% A, 11 min = 90% A, 12 min = 90% A. [0210] HPLC elution method 4: Waters XBridge Prep C18 OBD 19×100 mm (5 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 80% A, 3 min = 80% A, 13 min = 20% A, 18 min = 0% A. [0211] HPLC elution method 5: Waters XBridge Prep C18 OBD 19×100 mm (5 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 90% A, 3 min = 90% A, 13 min = 0% A, 20 min = 0% A. [0212] HPLC elution method 6: Waters XBridge Prep C18 OBD 19×100 mm (5 μm) column; mobile phase A: H ₂ O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 75% A, 13 min = 0% A, 15 min = 0% A. [0213] HPLC elution method 7: Waters XBridge Prep C18 OBD 19×100 mm (5 μm) column; mobile phase A: H2O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 80% A, 12 min = 0% A, 15 min = 0% A. [0214] HPLC elution method 8: Waters XBridge Prep C18 OBD 19×100 mm (5 μm) column; mobile phase A: H2O (0.1% v/v TFA); mobile phase B: acetonitrile (0.1% v/v TFA); flow rate: 10 mL/min; initial = 90% A, 12 min = 0% A, 15 min = 0% A. [0215] Analytical Size Exclusion Chromatography (SEC) can be performed using a Waters system comprised of a Waters 1525 Binary HPLC pump, a Waters 2489 UV/Visible Detector (monitoring at 280 nm), a Bioscan Flow Count radiodetector (FC-3300) and TOSOH TSKgel G3000SWxl, 7.8×300 mm column. The isocratic SEC method can have a flow rate of, e.g., mL/min, with a mobile phase of 0.1 M phosphate, 0.6 M NaCl, 0.025% sodium azide, pH = 7. [0216] MALDI-MS (positive ion) can be performed using a MALDI Bruker Ultraflextreme Spectrometer. [0217] Radio thin-layer chromatography (radioTLC) can be performed with Bioscan AR- 2000 Imaging Scanner, and can be carried out on iTLC-SG glass microfiber chromatography paper (Agilent Technologies, SGI0001) plates using citrate buffer (0.1 M, pH 5.5). Example 2. Synthesis of 4-{[11-oxo-11-(2,3,5,6-tetrafluorophenoxy)undecyl]carbamoyl} -2- [4,7,10-tris(carboxymethyl)-1,4,7,10-tetraazacyclododecan-1- yl]butanoic acid (Compound B) [0218] A bifunctional chelate, 4-{[11-oxo-11-(2,3,5,6- tetrafluorophenoxy)undecyl]carbamoyl}-2-[4,7,10-tris(carboxy methyl)-1,4,7,10- tetraazacyclododecan-1-yl]butanoic acid (Compound B), can be synthesized according to the scheme provided in FIG.2. To a solution of 5-(tert-butoxy)-5-oxo-4-(4,7,10-tris(2-(tert- butoxy)-2-oxoethyl)-1,4,7,10-tetraazacyclododecan-1-yl)penta noic acid (DOTA-GA-(tBu)4, 50 mg, 0.07 mmol) in ACN (2.0 mL), DSC (50 mg, 0.21 mmol) is added, followed by pyridine, (0.20 mL, 2.48 mmol). The reaction is stirred at room temperature for 1 hour. To the reaction mixture is added 11-aminoundecanoic acid, (70 mg, 0.36 mmol) followed by PBS solution (1.0 mL) at room temperature. The reaction is stirred for 72 hours at room temperature. The reaction mixture is filtered with a syringe filter and purified directly by Prep-HPLC using method 6 to yield Intermediate 2-A. [0219] To a solution of Intermediate 2-A (40 mg, 0.03 mmol), TFP (90 mg, 0.54 mmol) and EDC (40 mg, 0.27 mmol) in ACN (1.0 mL) is added pyridine (0.05 mL, 50 mg, 0.62 mmol) at room temperature. The solution is stirred at room temperature for 24 hours. The reaction is purified directly by Prep-HPLC using method 7 to provide Intermediate 2-B as a wax after concentration using a Biotage V10 Rapid Evaporator. [0220] Intermediate 2-B is dissolved in DCM / TFA (1.0 mL / 2.0 mL) and allowed to stir at room temperature for 24 hours. The reaction is concentrated by air stream and purified directly by Prep-HPLC using method 8 to yield Compound B as a clear wax after concentration. Example 3. Synthesis of [ ²²⁵ Ac]-Compound B-hMP-E-8.3 ([ ²²⁵ Ac]-hMP-E-8.3 conjugate 1) [0221] Compound B (1 μmole) is dissolved in a hydrochloric acid solution (0.001 M). An aliquot of Compound B solution (5 μL, 70 nmole) is added to a solution containing MP-hE- 8.3 (1.8 nmoles), a humanized anti-TEM-1 monoclonal antibody, in a phosphate buffer (pH 8). After 3 hours at ambient temperature, the resulting immunoconjugate is purified via a Sephadex G-50 resin packed column. The immunoconjugate Compound B-hMP-E-8.3 is eluted from the column with acetate buffer (pH 6.5). (Throughout, the name “Compound B- hMP-E-8.3” refers to the conjugate formed after reacting Compound B, which contains a crosslinking moiety, with hMP-E-8.3. The conjugate does not contain the cross-linking moiety.) [0222] Ac-225 (15 μCi, 10 μL) is added to a solution of Compound B-hMP-E-8.3 (300 μg in acetate buffer (pH 6.5). The radiolabeling reaction is incubated at 30° C for 1 hour. The crude product, [ ²²⁵ Ac]-Compound B-anti-hMP-E-8.3 is purified via a Sephadex G-50 resin packed column eluted with acetate buffer. Example 4. Synthesis of 4-{[2-(2-{2-[3-oxo-3-(2,3,5,6-tetrafluorophenoxy)propoxy] ethoxy}ethoxy)ethyl]carbamoyl}-2-[4,7,10-tris(carboxymethyl) -1,4,7,10- tetraazacyclododecan-1-yl]butanoic acid (Compound C) [0223] A bifunctional chelate, 4-{[2-(2-{2-[3-oxo-3-(2,3,5,6- tetrafluorophenoxy)propoxy] ethoxy}ethoxy)ethyl]carbamoyl}-2-[4,7,10- tris(carboxymethyl)-1,4,7,10-tetraazacyclododecan-1-yl]butan oic acid (Compound C), was synthesized according to the scheme provided in FIG.3. [0224] To a solution of 5-(tert-butoxy)-5-oxo-4-(4,7,10-tris(2-(tert-butoxy)-2-oxoet hyl)- 1,4,7,10-tetraazacyclododecan-1-yl)pentanoic acid (DOTA-GA(tBu) ₄ , 100 mg, 0.143 mmol) in ACN (8.0 mL) was added DSC (73 mg, 0.285 mmol) and pyridine (0.80 mL, 9.89 mmol). The reaction mixture was stirred for 90 min at ambient temperature. This solution was added to a semi-solution of amino-PEG3-acid (63 mg, 0.285 mmol in 1.2 mL of DMF) in a 100 mL round bottom flask. After 4 hours at ambient temperature, the reaction was worked up by concentrating to dryness under a stream of air. The crude material was purified by HPLC elution method 2 (dissolved the crude in 6 mL of 20% ACN/H ₂ O). The fractions containing product were pooled and concentrated under vacuum and then co-evaporated with ACN (3 x 2 mL). [0225] To a vial containing Intermediate 1-A (82 mg, 60 μmol) was added ACN (2 mL), NEt ₃ (50 μL, 360 μmol, 6 equiv.), HBTU (23 mg, 60 μmol, 1 equiv) and a TFP solution (50 mg, 300 μmol, 5 equiv., dissolved in 250 μL of ACN). The resulting clear solution was stirred at ambient temperature for 3 hours. The reaction was worked up by concentrating the solution to dryness under an air stream and was then diluted with ACN/H ₂ O (1:1, 3 mL total) and purified on preparative HPLC using elution method 4. Fractions containing product were pooled and concentrated under vacuum and then co-evaporated with ACN (3 x 2 mL). Intermediate 1-B was obtained as a clear residue. [0226] To a vial containing Intermediate 1-B (67 mg, 64 μmol) was added DCM (2 mL) and TFA (2 mL). The resulting solution was stirred at ambient temperature for 16 hour. Additional, TFA (2 mL) was added, and the reaction was stirred at ambient temperature for 6 hours. The reaction was concentrated to dryness under an air stream, with the crude product being finally dissolved in ACN/H ₂ O (1 mL of 10% ACN/H ₂ O). The crude reaction solution was then purified by preparative HPLC using elution method 5. The fractions containing product are pooled, frozen and lyophilized. Compound C was obtained as a white solid. Example 5. Synthesis of [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 and [ ²²⁵ Ac]-Compound C-hMP-E- 8.3 [0227] Compound C was dissolved in a hydrochloric acid solution (0.001 M). An aliquot of Compound C solution was added to a solution containing hMP-E-8.3 in a phosphate buffer (pH 9). After 1 hour at ambient temperature, the resulting immunoconjugate was purified via a Sephadex G-50 resin packed column. The immunoconjugate Compound C-hMP-E-8.3 was eluted from the column with acetate buffer (pH 6.5). Identities of eluates were confirmed by MALDI-TOF. (Throughout, the name “Compound C-hMP-E-8.3” refers to the conjugate formed after reacting Compound C, which contains a crosslinking moiety, with hMP-E-8.3. The conjugate does not contain the cross-linking moiety.) [0228] To make [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3, Lu-177 (0.98 mCi) was added to a solution of Compound C-hMP-E-8.3 (100 μg in SABST (pH 6.5)). The radiolabeling reaction was incubated at 37° C for 30 minutes. The crude product was purified via a Sephadex G-50 resin packed column eluted with acetate buffer. The chelate-antibody-ratio of [ ¹⁷⁷ Lu]- Compound C-hMP-E-8.3 was approximately 4.9. [0229] To make [ ²²⁵ Ac]-Compound C-hMP-E-8.3, Ac-225 (20 μCi, 10 μL) was added to a solution of Compound C-hMP-E-8.3 (400 μg in SABST (pH 6.5)). The radiolabeling reaction was incubated at 37° C for 1 hour. The crude product was purified via a Sephadex G-50 resin packed column eluted with acetate buffer. The chelate-antibody-ratio of [ ²²⁵ Ac]- Compound C-hMP-E-8.3 was approximately 4.9. [0230] [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 and [ ²²⁵ Ac]-Compound C-hMP-E-8.3 were formulated in SABST (pH 6.5) with 10 mM ascorbate and 1 mM DTPA, and product purity was analyzed by size exclusion chromatography and radio thin layer chromatography. [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 exhibited a radiochemical purity (RCP) of > 99% and [ ²²⁵ Ac]-Compound C-hMP-E-8.3 exhibited a radiochemical purity of > 98%. Radiochemical yield for both products was > 75%. Example 6. In vitro binding of hMP-E-8.3 and immunoconjugates to osteosarcoma cells [0231] Expression of TEM-1 in a SK-N-AS (a neuroblastoma cell line) and SJSA-1 (an osteosarcoma cell line) was assessed by flow cytometry using anti-human TEM-1 (CD248) (Clone B1/35; BD PHARMINGEN ^TM ) labeled with ALEXA FLUOR® 647. FIG.4A shows results for SK-N-AS cells, and FIG.4B shows results for SJSA-1 cells. TEM-1 was expressed at high levels in SJSA-1 cells (FIG.4A) and at intermediate levels in SK-N-AS cells (FIG.4B). [0232] To assess whether hMP-E-8.3 and Compound C-hMP-E-8.3 conjugate (see Example 5) could also bind to TEM-1, SJSA-1 cells were stained with 1) hMP-E-8.3 from an original stock solution; 2) hMP-E-8.3 from a re-purified stock solution; 3) Compound C- hMP-E-8.3 conjugate; or 4) an isotype-matched control antibody, then stained with a FITC- labeled secondary antibody. FIG.5 shows flow cytometry results from this experiment. As shown in FIG.5, Compound C-hMP-E-8.3 conjugate bound TEM-1 in SJSA-1 cells as well as unmodified hMP-E-8.3, confirming that conjugation of hMP-E-8.3 as described in Example 5 did not result in loss of target binding. [0233] The binding affinity of [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 to TEM-1 was assessed in SJSA-1 cells using a saturation binding study. As shown in FIG.6, [ ¹⁷⁷ Lu]-Compound C- hMP-E-8.3 demonstrated high affinity binding to SJSA-1 cells, with a low level of non- specific binding. The K _d for [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 was 4.7 nM. (Compare with a K _d of 5.0 nM for hMP-E-8.3.) Example 7. Biodistribution of [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 in an osteosarcoma xenograft model [0234] Biodistribution of [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 was assessed in an osteosarcoma xenograft model. Tumors were established by injecting SJSA-1 cells into Balb/c nude mice. Mice (3 animals per group) were dosed with [ ¹⁷⁷ Lu]-Compound C-hMP-E- 8.3 (10 µCi of radioactivity; 1 µg of antibody) and then sacrificed at 4 h, 24 h, 48 h, 96 h, or 168 h depending on their group. Uptake was assessed in tumors and tissues from each group. [0235] FIG.7 shows the percentage injected dose per gram (% ID/g) in the blood, bone, heart, intestines, kidneys and adrenals, liver and gallbladder, lungs, muscle, pancreas, spleen, stomach, and tumor at each timepoint. As shown in FIG.7, [ ¹⁷⁷ Lu]-Compound C-hMP-E-8.3 demonstrated high uptake in SJSA-1 tumors but low tissue uptake. At 168 h (7 days), [ ¹⁷⁷ Lu]- Compound C-hMP-E-8.3 had a high tumor accumulation of approximately 85% ID/g. This level corresponds to an accumulation of ~20% of the total dose (%ID). [0236] FIG.7 also shows rapid blood clearance for a radioimmunoconjugate, in this example, dropping from ~44% ID/g at 4 h to ~9% ID/g at 7 days. The distribution in off- target tissues was low, <5% ID/g after 7 days. (hMP-E-8.3 does not cross react with mouse TEM-1.) Example 8. Efficacy of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 in an osteosarcoma xenograft model [0237] [ ²²⁵ Ac]-Compound C-hMP-E-8.3 was tested in a human osteosarcoma cancer xenograft model. Female Balb/c mice (5 per group) were injected with SJSA-1 cells to induce subcutaneous tumor xenografts. Once tumors reached a volume of ~200 mm ³ , mice were dosed with single doses of 10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi [ ²²⁵ Ac]-Compound C-hMP-E-8.3. Vehicle and antibody only controls were also included. Tumor volumes were monitored and assessed for 28 days after dosing. [0238] FIG.8 shows relative tumor volumes over time. [ ²²⁵ Ac]-Compound C-hMP-E-8.3 was highly effective in reducing tumor growth, with tumors appearing to regress at higher doses. Example 9. Efficacy of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 in a neuroblastoma xenograft model [0239] [ ²²⁵ Ac]-Compound C-hMP-E-8.3 was tested in a human neuroblastoma cancer xenograft model. Female Balb/c mice (5 per group) were injected with SK-N-AS cells to induce subcutaneous tumor xenografts. Once tumors reached a volume of ~200 mm ³ , mice were dosed with single doses of 10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi [ ²²⁵ Ac]- Compound C-hMP-E-8.3. Vehicle and antibody only controls were also included. Tumor volumes were monitored and assessed for 28 days after dosing. [0240] FIG.9 shows relative tumor volumes over time. [ ²²⁵ Ac]-Compound C-hMP-E-8.3 was highly effective in reducing tumor growth, with tumors appearing to regress at higher doses. Example 10. Efficacy of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 in an Ewing’s sarcoma xenograft model [0241] [ ²²⁵ Ac]-Compound C-hMP-E-8.3 was tested in a human Ewing’s sarcoma cancer xenograft model. Female Balb/c mice (5 per group) were injected with A673 cells to induce subcutaneous tumor xenografts. Once tumors reached a volume of ~200 mm ³ , mice were dosed with single doses of 10 nCi, 50 nCi, 100 nCi, 200 nCi, or 400 nCi [ ²²⁵ Ac]-Compound C-hMP-E-8.3. Vehicle and antibody only controls were also included. Tumor volumes were monitored and assessed for 28 days after dosing. [0242] FIG.10 shows relative tumor volumes over time. [ ²²⁵ Ac]-Compound C-hMP-E- 8.3 reduced tumor growth at the high dose. The Ewing’s sarcoma cells line used in this Example is known to express lower levels of TEM-1 than the osteosarcoma and neuroblastoma cell lines used in Examples 7-9 and therefore demonstrates the ability of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 to be effective against tumors that express low levels of TEM-1. Example 11. Effects of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 on tumor stroma [0243] In human cancers, TEM-1 is often expressed in stromal cells associated with tumors. In some cases, including, but not limited to, breast, lung, colon, ovarian cancers or others, TEM-1 may not be expressed (or only expressed at low levels) in the cancerous cells themselves but remains expressed in the stromal compartment. hMP-E-8.3 binds to human TEM-1 but shows little to no cross-reactivity to mouse TEM-1 and is therefore unable to bind to mouse derived stromal cells in a conventional tumor xenograft model where human TEM- 1 is expressed in human cancer cells supported by mouse derived stromal cells. [0244] To test the therapeutic effects of [ ²²⁵ Ac]-Compound C-hMP-E-8.3 in a model where the TEM-1 targeting moiety (hMP-E-8.3) is capable of binding only to stromal cells associated with tumors, [ ²²⁵ Ac]-Compound C-hMP-E-8.3 is tested using tumors implanted in humanized TEM-1-transgenic mouse model. The mice in this model are genetically engineered to express human TEM-1, instead of mouse TEM-1, in cells including the stromal cells. To form tumors, cells of a cancer cell line that do not express endogenous human TEM- 1 are implanted into the transgenic mice. In this way the only human TEM-1 target expressed in the resulting tumor is derived from the humanized mouse stromal cells and the therapeutic effect of targeting human TEM-1 in those stromal cells with [ ²²⁵ Ac]-Compound C-hMP-E-8.3 may be determined. [0245] To determine the effect of targeting human TEM-1 in the stromal compartment of tumors formed in the hTEM-1 transgenic mice, [ ²²⁵ Ac]-Compound C-hMP-E-8.3 is administered similarly as described in Examples 7-10, and tumor volume is assessed relative to controls. Survival may also be assessed. OTHER EMBODIMENTS [0246] While the invention has been described in connection with specific embodiments thereof, it will be understood that it is capable of further modifications and this application is intended to cover any variations, uses, or adaptations of the invention following, in general, the principles of the invention and including such departures from the present disclosure that come within known or customary practice within the art to which the invention pertains and may be applied to the essential features herein before set forth.