Attorney Docket No.51624-0017WO1 ANTI-KRAS T CELL RECEPTORS AND ENGINEERED CELLS CROSS REFERENCE TO RELATED APPLICATION This application claims benefit of priority of United States provisional application No. 63/421,030 filed on October 31, 2022, the content of which is incorporated herein by reference in its entirety. SEQUENCE STATEMENT This application contains a Sequence Listing that has been submitted electronically as an XML file named “51624-0017WO1_SL_ST26.XML.” The XML file, created on October 27, 2023, is 44,134 bytes in size. The material in the XML file is hereby incorporated by reference in its entirety. TECHNICAL FIELD The present disclosure relates to T cells receptors that recognize or bind to Kras G12V mutant proteins or peptides thereof, engineered cells comprising such T cell receptors, and cell- based therapies. BACKGROUND Kras has long been considered to be “undruggable” until 2013 when covalent drugs targeting Kras (G12C) were identified, a common mutant in which a glycine amino acid is mutated to a cysteine. That discovery led to increased drug discovery research, and eventually the first inhibitors targeting Kras (G12C). Unfortunately, other mutants of Kras presented different challenges. All of the known inhibitors of Kras (G12C) relied on an inactive state of the protein that other mutants do not frequently exhibit. Thus, there exists an unmet need for effective therapies for cancers carrying other Kras mutants (e.g., Kras G12V mutant). SUMMARY The present disclosure is related to T cells receptors that recognize or bind to Kras G12V mutant proteins or peptides thereof, genetically engineered cells, and cell therapies for treating cancers carrying Kras G12V mutant. Attorney Docket No.51624-0017WO1 In one aspect, the disclosure is related to a T cell receptor (TCR) or antigen-binding fragment thereof, comprising an alpha chain variable region (Va) and a beta chain variable region (Vb), in some embodiments, the Va region comprises a complementarity determining region 1 (CDR1), a complementarity determining region 2 (CDR2), and a complementarity determining region 3 (CDR3), in some embodiments, the Va region CDR1 comprises an amino acid sequence that is at least 80% identical to a selected Va region CDR1 amino acid sequence, the Va region CDR2 comprises an amino acid sequence that is at least 80% identical to a selected Va region CDR2 amino acid sequence, and the Va region CDR3 comprises an amino acid sequence that is at least 80% identical to a selected Va region CDR3 amino acid sequence; and the Vb region comprises a complementarity determining region 1 (CDR1), a complementarity determining region 2 (CDR2), and a complementarity determining region 3 (CDR3), in some embodiments, the Vb region CDR1 comprises an amino acid sequence that is at least 80% identical to a selected Vb region CDR1 amino acid sequence, the Vb region CDR2 comprises an amino acid sequence that is at least 80% identical to a selected Vb region CDR2 amino acid sequence, and the Vb region CDR3 comprises an amino acid sequence that is at least 80% identical to a selected Vb region CDR3 amino acid sequence; in some embodiments, the selected Va region CDR1, CDR2, and CDR3 amino acid sequences and the selected Vb region CDR1, CDR2, and CDR3 amino acid sequences are one of the following: (1) the selected Va region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 10, 11, and 12, respectively, and the selected Vb region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 13, 14, and 15, respectively; (2) the selected Va region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 16, 17, and 18, respectively, and the selected Vb region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 19, 20, and 21, respectively; and (3) the selected Va region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 22, 23, and 24, respectively, and the selected Vb region CDR1, CDR2, and CDR3 amino acid sequences are set forth in SEQ ID NOs: 25, 26, and 27, respectively. In some embodiments, the Va region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 10, 11, and 12, respectively; and the Vb region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 13, 14, and 15, respectively. In some embodiments, the Va region comprises the amino acid Attorney Docket No.51624-0017WO1 sequence set forth in any of SEQ ID NO: 4, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto; and the Vb region comprises the amino acid sequence set forth in any of SEQ ID NO: 5, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. In some embodiments, the Va region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 16, 17, and 18, respectively; and the Vb region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 19, 20, and 21, respectively. In some embodiments, the Va region comprises the amino acid sequence set forth in any of SEQ ID NO: 6, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto; and the Vb region comprises the amino acid sequence set forth in any of SEQ ID NO: 7, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. In some embodiments, the TCR or antigen-binding fragment thereof binds to or recognizes a peptide epitope of Kras G12V mutant protein (SEQ ID NO: 1) that is presented by a major histocompatibility complex (MHC) molecule. In some embodiments, the MHC molecule is an HLA-A molecule (e.g., HLA-A*11:01). In some embodiments, the Va region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 22, 23, and 24, respectively; and the Vb region comprises CDR1, CDR2, and CDR3 with the amino acid sequences set forth in SEQ ID NOs: 25, 26, and 27, respectively. In some embodiments, the Va region comprises the amino acid sequence set forth in any of SEQ ID NO: 8, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto; and the Vb region comprises the amino acid sequence set forth in any of SEQ ID NO: 9, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. In some embodiments, the TCR or antigen-binding fragment thereof binds to or recognizes a peptide epitope of Kras G12V mutant protein (SEQ ID NO: 2) that is presented by a major histocompatibility complex (MHC) molecule. In some embodiments, the MHC molecule is an HLA-A molecule (e.g., HLA-A*11:01). In some embodiments, the TCR or antigen-binding fragment thereof comprises an alpha chain and a beta chain, in some embodiments, the alpha chain comprises a mouse alpha chain constant region, and the beta chain comprises a mouse beta chain constant region. In some Attorney Docket No.51624-0017WO1 embodiments, the TCR or antigen-binding fragment thereof comprises an alpha chain and a beta chain, in some embodiments, the alpha chain comprises a human alpha chain constant region, and the beta chain comprises a human beta chain constant region. In some embodiments, the TCR or antigen-binding fragment thereof, when expressed on the surface of a T cell, stimulates cytotoxic activity against a target cancer cell. In some embodiments, the target cancer cell comprises a nucleic acid sequence encoding a Kras G12V mutant protein and/or expresses a Kras G12V mutant protein. In one aspect, the disclosure is related to a T cell receptor (TCR) or antigen-binding fragment thereof, comprising an alpha chain variable region (Va) and a beta chain variable region (Vb), in some embodiments, the Va region comprises a complementarity determining region 1 (CDR1), a complementarity determining region 2 (CDR2), and a complementarity determining region 3 (CDR3), and the Vb region comprises a CDR1, a CDR2, and a CDR3, in some embodiments, (1) the Va region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 4, respectively, and the Vb region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 5, respectively; (2) the Va region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 6, respectively, and the Vb region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 7, respectively; or (3) the Va region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 8, respectively, and the Vb region CDR1, CDR2, and CDR3 are identical to complementarity determining regions 1, 2, and 3 in SEQ ID NO: 9, respectively. In one aspect, the disclosure is related to an isolated nucleic acid comprising a nucleotide sequence encoding the TCR or antigen-binding fragment thereof as described herein. In one aspect, the disclosure is related to a vector comprising the nucleic acid as described herein. In one aspect, the disclosure is related to a vector comprising: a) a first nucleic acid sequence encoding a TCR alpha chain comprising an alpha chain variable region and an alpha chain constant region; and b) a second nucleic acid sequence encoding a TCR beta chain comprising a beta chain variable region and a beta chain constant region; in some embodiments, the alpha chain variable region and the beta chain variable region associate with each other, forming an antigen-binding site that binds to a Kras G12V mutant peptide that is presented by a Attorney Docket No.51624-0017WO1 major histocompatibility complex (MHC) molecule. In some embodiments, the alpha chain constant region is a mouse TCR alpha chain constant region and the beta chain constant region is a mouse TCR beta chain constant region. In some embodiments, the alpha chain constant region is a human TCR alpha chain constant region and the beta chain constant region is a human TCR beta chain constant region. In some embodiments, the first nucleic acid sequence and the second nucleic acid sequence are linked by a linker sequence. In some embodiments, the linker sequence encodes a P2A sequence. In some embodiments, the vector is an expression vector or a viral vector (e.g., a retroviral vector or a lentiviral vector). In one aspect, the disclosure is related to an engineered cell, comprising the TCR or antigen-binding fragment thereof, the nucleic acid, or the vector as described herein. In some embodiments, the TCR or antigen binding fragment thereof is heterologous to the cell. In some embodiments, the engineered cell is a cell line. In some embodiments, the engineered cell is a primary cell obtained from a subject (e.g., a human subject). In some embodiments, the engineered cell is a T cell. In some embodiments, the T cell is isolated from a human subject. In some embodiments, the T cell is CD8+ T cell. In some embodiments, the T cell is CD4+ T cell. In one aspect, the disclosure is related to a pharmaceutical composition comprising the TCR or antigen-binding fragment thereof or the engineered cell as described herein, and a pharmaceutically acceptable carrier. In one aspect, the disclosure is related to a method for producing the engineered cell, comprising introducing the vector as described herein into a cell in vitro or ex vivo. In some embodiments, the vector is a viral vector (e.g., a lentiviral vector) and the introducing is carried out by transduction. In one aspect, the disclosure is related to a method of treating cancer in a subject in need thereof, the method comprising administering the engineered cell or pharmaceutical composition as described herein to the subject. In some embodiments, the subject is a cancer patient having a mutated Kras gene that encodes a Kras G12V mutant protein. In some embodiments, the cancer is non-small cell lung cancer, colorectal cancer, ovarian cancer, pancreatic cancer or any other types of cancers carrying Kras G12V mutation. In one aspect, the disclosure is related to a TCR or antigen-binding fragment thereof that cross competes with the TCR or antigen-binding fragment thereof as described herein. In one aspect, the disclosure further provides an engineered cell receptor or antigen- Attorney Docket No.51624-0017WO1 binding fragment thereof, comprising an alpha chain variable region (Va) and a beta chain variable region (Vb) as described herein. In some embodiments, the engineered cell receptor is a TCR. In some embodiments, the engineered cell receptor is a chimeric antigen receptor. In one aspect, the disclosure further provides a method for patient-specific T-cell therapy, wherein a gene is engineered into patient-specific T cells and delivered back into the patient as a therapeutic agent. The present disclosure further provides a method of diagnosing a disease/condition, wherein the condition can include cancer, and wherein the disease can be diagnosed by analyzing the complex formed as a result of the contact between the T-cell receptors with the sample from the patient/mammal to be diagnosed, and wherein the complex can be detected by any of the means well-known in the art. In some embodiments, the results can be used to determine whether the cell therapy will be effective. The present disclosure further provides a pharmaceutical composition comprising an engineered T cell receptor (TCR) or an antigen-binding fragment thereof having antigenic specificity for human Kras G12V mutant and a pharmaceutically acceptable carrier. The present disclosure also provides a vector system for transfecting cells with a chimeric gene, wherein the vector system includes nucleic acid sequences encoding the variable region of the alpha chain of a humanized anti-Kras G12V TCR, nucleic acid sequences encoding the variable region of the beta chain of the same humanized anti-Kras G12V TCR. As used herein, the term “genetically engineered cell” or “genetically modified cell” refers to a cell with a modification of a nucleic acid sequence in the cell, including, but not limited to, a cell having a insertion, deletion, substitution, or modification of one or more nucleotides in its genome, and a cell with an exogenous nucleic acid sequence (e.g., a vector), wherein the exogenous nucleic acid sequence is not necessarily integrated into the genome. As used herein, the term “cancer” or “cancer cell” refers to the cells dividing in an uncontrolled manner. Examples of such cells include cells having an abnormal state or condition characterized by rapidly proliferating cell growth. The term is meant to include cancerous growths, e.g., tumors; oncogenic processes, metastatic tissues, and malignantly transformed cells, tissues, or organs, irrespective of histopathologic type or stage of invasiveness. The cancer cells can form the solid tumors or the excessive tumor cells in blood (e.g., hematologic cancer). Alternatively or additionally it can include all types of cancerous growths or oncogenic Attorney Docket No.51624-0017WO1 processes, metastatic tissues or malignantly transformed cells, tissues, or organs, irrespective of histopathologic type or stage of invasiveness. Examples of solid tumors include malignancies, e.g., sarcomas, adenocarcinomas, and carcinomas, of the various organ systems, such as those affecting liver, lung, breast, lymphoid, gastrointestinal (e.g., colon), genitourinary tract (e.g., renal, urothelial cells), prostate and pharynx. Adenocarcinomas include malignancies such as most colon cancers, rectal cancer, renal-cell carcinoma, liver cancer, non-small cell carcinoma of the lung, cancer of the small intestine and cancer of the esophagus. Examples of cancers that can be treated by the methods described herein include e.g., bone cancer, pancreatic cancer, skin cancer (e.g., melanoma), cancer of the head or neck, cutaneous or intraocular malignant melanoma, uterine cancer, ovarian cancer, rectal cancer, cancer of the anal region, stomach cancer, testicular cancer, uterine cancer, carcinoma of the fallopian tubes, carcinoma of the endometrium, carcinoma of the cervix, carcinoma of the vagina, carcinoma of the vulva, Hodgkin Disease, non-Hodgkin lymphoma, cancer of the esophagus, cancer of the small intestine, cancer of the endocrine system, cancer of the thyroid gland, cancer of the parathyroid gland, cancer of the adrenal gland, sarcoma of soft tissue, cancer of the urethra, cancer of the penis, chronic or acute leukemias including acute myeloid leukemia, chronic myeloid leukemia, acute lymphoblastic leukemia, chronic lymphocytic leukemia, lymphocytic lymphoma, cancer of the bladder, cancer of the kidney or ureter, carcinoma of the renal pelvis, neoplasm of the central nervous system (CNS), primary CNS lymphoma, tumor angiogenesis, spinal axis tumor, brain stem glioma, pituitary adenoma, Kaposi's sarcoma, epidermoid cancer, squamous cell cancer, and/or T-cell lymphoma. As used herein, the term “vector” refers to a vehicle by which a polynucleotide sequence (e.g., a foreign gene) can be introduced into a host cell, in order to obtain the desired gene expression of the introduced nucleotide sequence. Cloning vectors can include e.g., plasmids, phages, viruses, etc. Most popular type of vector is a "plasmid", which refers to a closed circular double stranded DNA loop into which additional DNA segments comprising gene of interest can be ligated. Another type of vector is a viral vector, in which a nucleic acid construct to be transported is ligated into the viral genome. Viral vectors are capable of autonomous replication in a host cell into which they are introduced or may integrate themselves into the genome of a host cell and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. In some Attorney Docket No.51624-0017WO1 embodiments, the vectors are viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses). As used herein, a "subject" is a mammal, such as a human or a non-human animal. In some embodiments, the subject, e.g., patient, to whom the cells, cell populations, or compositions are administered is a mammal, typically a primate, such as a human. In some embodiments, the primate is a monkey or an ape. The subject can be male or female and can be any suitable age, including infant, juvenile, adolescent, adult, and geriatric subjects. In some embodiments, the subject is a non-primate mammal, such as a dog, a cat, a horse, a rodent, a rat, or a mouse. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. Methods and materials are described herein for use in the present disclosure; other, suitable methods and materials known in the art can also be used. The materials, methods, and examples are illustrative only and not intended to be limiting. All publications, patent applications, patents, sequences, database entries, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, the present specification, including definitions, will control. Other features and advantages of the disclosure will be apparent from the following detailed description and figures, and from the claims. DESCRIPTION OF DRAWINGS Exemplary embodiments are illustrated in referenced figures. It is intended that the embodiments and figures disclosed herein are to be considered illustrative rather than restrictive. FIG.1 shows a set of flow cytometry results of activated human T cells transduced with lentivirus encoding Kras G12V specific TCR 9mV11, 9mV15, or 10mV11. The cells were stained with an antibody specific for mouse TCR β chain constant region (mTCR) and HLA- A*11:1-Kras G12V tetramer (Tetramer) before flow cytometry analysis. Untransduced (UTD) cells were used as negative control cells. FIG.2 shows a set of flow cytometry results of TCR-T cells expressing 9mV11, 9mV15, or 10mV11 TCR when cocultured with SW480 parental cells or SW480-HLA-A*11:01 cells. The T cells were stained with an antibody specific for mouse TCR β chain constant region Attorney Docket No.51624-0017WO1 (mTCR), and an anti-human CD137 antibody (CD137). Untransduced (UTD) cells were used as negative control cells. FIG.3 shows concentrations of secreted IFN-γ by TCR-T cells expressing 9mV11, 9mV15, or 10mV11 TCR when cocultured with SW480 parental cells or SW480-HLA-A*11:01 cells. Untransduced (UTD) cells were used as negative control cells. FIG.4A shows a set of flow cytometry results of TCR-T cells expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA-A*11:01 cells. The T cells were stained with an anti-TNF-α antibody (TNF-α) and an anti-CD8 antibody (CD8). Untransduced (UTD) cells were used as negative control cells. FIG.4B shows the percentage of TNF-α positive cells in CD8+ TCR-T cells (left) and CD4+ TCR-T cells (right) expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA-A*11:01 cells. Untransduced (UTD) cells were used as negative control cells. FIG.4C shows the percentage of IFN-γ positive cells in CD8+ TCR-T cells (left) and CD4+ TCR-T cells (right) expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA-A*11:01 cells. Untransduced (UTD) cells were used as negative control cells. FIG.4D shows the percentage of IL-2 positive cells in CD8+ TCR-T cells (left) and CD4+ TCR-T cells (right) expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA-A*11:01 cells. Untransduced (UTD) cells were used as negative control cells. FIGS.5A-5C show cytolytic assay results of CD8+ TCR-T cells expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA- A*11:01 cells at different ratios of effector to tumor cells (or E:T ratio). Tumor cell stands for tumor cell only culture (without TCR-T cells). Untransduced (UTD) cells were used as negative control cells. FIGS.5D-5F show cytolytic assay results of CD4+ TCR-T cells expressing 9mV1, 9mV2, 9mV9, 9mV10, 9mV11, 9mV15, or 10mV11 TCR, when cocultured with SW480-HLA- A*11:01 cells at different ratios of effector to tumor cells (or E:T ratio). Tumor cell stands for tumor cell only culture (without TCR-T cells). Untransduced (UTD) cells were used as negative control cells. Attorney Docket No.51624-0017WO1 FIG.6A shows the concentration of secreted IFN-γ by 9mV11 TCR-T cells cocultured with T2-HLA-A*11:01 cells that were loaded with selected artificially generated peptides at diluted concentrations (0, 1, 10, and 100 nM). FIG.6B shows the concentration of secreted IFN-γ by 9mV15 TCR-T cells cocultured with T2-HLA-A*11:01 cells that were loaded with selected artificially generated peptides at diluted concentrations (0, 1, 10, and 100 nM). FIG.6C shows the concentration of secreted IFN-γ by 10mV11 TCR-T cells cocultured with T2-HLA-A*11:01 cells that were loaded with selected artificially generated peptides at diluted concentrations (0, 1, 10, and 100 nM). FIG.6D shows sequences of the artificially generated peptides used in FIGS.6A-6C. FIG.7 shows the concentration of secreted IFN-γ by T cells expressing 9mV11, 9mV15, or 10mV11 TCR that were cocultured for 24 hours with human primary cells engineered to express HLA-A*11:01, in the presence or absence of Kras G12V mutant peptides. SW480-HLA- A*11:01 cells (SW480-A11) were used as positive control cells. Untransduced (UTD) cells were used as negative control cells. FIG.8 lists alpha chain and beta chain CDR sequences of 9mV11, 9mV15, or 10mV11 TCRs. FIG.9 lists additional sequences discussed in the disclosure. DETAILED DESCRIPTION Ras is a kind of GTPase that involves the signal transmission within cells and control cell growth, differentiation and survival. Mutations in Ras genes can lead to the production of permanently activated Ras proteins, which can cause unintended and overactive signaling inside the cell, even in the absence of incoming signals, and cause uncontrolled cell proliferation and growth (e.g., cancers). The three Ras genes in human (Hras, Kras and Nras) are the most common oncogenes in human cancer. Ras mutation are found in 20-25% of all human tumors and up to 90% in certain types of cancer (e.g., 40% in non-small cell lung cancer, 30% in colorectal cancer and 90% in pancreatic cancer). Among all the Ras mutations, Kras mutations account for about 85% and there is a hot-spot mutation at the 12 ^th amino acid. The amino acid glycine (G) at position 12 can mutate into alanine (A), cysteine (C), aspartic acid (D), arginine (R), serine (S) and valine (V). The G12V mutation is one of the most common G12 mutations Attorney Docket No.51624-0017WO1 among all Kras mutations. For this reason, Ras inhibitors are being widely studied as a treatment for cancer and other diseases with Ras overexpression and mutations. So far, only G12C-specific inhibitors have been developed and approved by FDA for the treatment of NSCLC; and the clinical efficacy is limited. There is no FDA-approved therapies for other G12 mutations, e.g., G12V. Gene mutations often result in the change of immunogenicity of peptide/proteins encoded by the gene, further leading to the generation of mutation-specific T cell and/or B cell response. T cells specific for Kras G12V mutations have been identified and isolated from cancer patients carrying these Kras mutations. Adaptive cell therapies (ACT) with T cells engineered with Chimeric Antigen Receptor (CAR) have been made great success in some types of hematological cancers (e.g., acute lymphocytic leukemia or multiple myeloma), but have not made progression in solid cancers (e.g., prostate cancer or pancreatic cancers). Many reasons can cause the failure in CAR-based ACT. One of the reasons is that CAR-T cells can only target tumor-associated antigens, which are expressed by cancer cells at relatively high levels but also are expressed by some types of normal cells at lower levels, resulting in the on-target, off-tumor toxicity of CAR-T cells. In addition, there are several other disadvantages of CAR-T cell-based therapies, e.g., higher degree/frequency of cytokines release syndrome (CRS) and tonic-signaling, which can cause exhaustion of CAR-T cells. T cell receptor (TCR), unlike the artificially synthesized CAR, is the natural receptor of T cell for antigen recognition. TCR-T cells have shown efficacy in controlling some types of solid caners, e.g., melanoma and cervical cancers. The present disclosure provided TCRs specific for Kras G12V mutant and tested T cells engineered with such TCRs to recognize and kill cancer cells expressing Kras G12V mutation. The present disclosure also provides T-cell receptor (TCR)-engineered T cells, which can be used in cell therapy. The engineered T-cell receptors are capable of recognizing the surface antigen on the cell receptor which are otherwise not recognized by normal T-cells. The engineered T cells can be employed against multiple targets such as cancer cells expressing appropriate antigens. T CELL RECEPTORS AND BINDING MOLECULES T cells are a type of lymphocyte which typically develops in the thymus gland and plays Attorney Docket No.51624-0017WO1 a central role in the immune response. It plays an important role in the "adaptive immune response." T cells can be distinguished from other lymphocytes by the presence of a T-cell receptor on the cell surface. Differentiated T cells have an important role in controlling the immune response. CD8+ T cells, also known as "killer cells", are cytotoxic. Once they recognize a target cell, they are able to directly kill the target cell (e.g., virus-infected cells or cancer cells). CD8+ T cells can also produce cytokines and recruit other cells (e.g., macrophages and natural killer (NK) cells) to mount an immune response. CD4+ T cells, also known as "helper cells", can indirectly kill target cells, e.g., by facilitating maturation of B cells into plasma cells and memory B cells, and activation of cytotoxic T cells and macrophages. Helper T cells become activated when they are presented with peptide antigens by MHC class II molecules, which are expressed on the surface of antigen-presenting cells (APCs). Once activated, they divide rapidly and secrete cytokines that regulate or assist the immune response. Regulatory T cells are important for tolerance, thereby preventing or inhibiting autoimmune response. The major role of regulatory T cells is to shut down T cell-mediated immunity toward the end of an immune reaction and to suppress autoreactive T cells that escaped the process of negative selection in the thymus. T cells play an important role in cancer immunity where antigens from the cancer cells are taken up and presented on the cell surface of special immune cells called antigen-presenting cells (APCs) so that other immune cells can recognize the antigens of interest. In the lymph nodes, the APCs activate the T-cells and activate them to recognize the tumor cells. The activated T-cells can then travel via the blood vessels to reach the tumor, infiltrate it, recognize the cancer cells and kill them. The activation of T cells requires T cell receptors. A “T cell receptor” or “TCR” is a molecule that contains a variable α (or alpha) and β (or beta) chains (also known as TCR ^ and TCR ^, respectively) or a variable ^ (or gamma) and ^ (or delta) chains (also known as TCR ^ and TCR ^, respectively), or antigen-binding portions thereof, and which is capable of specifically binding to an antigen, e.g., a peptide antigen or peptide epitope bound to an major histocompatibility complex (MHC) molecule. The present disclosure provides a T cell receptor (TCR) or antigen-binding fragment thereof, and binding molecules derived from TCR. In some embodiments, the TCR is in the αβ form. TCRs that exist in αβ and ^ ^ forms are generally structurally similar, but T cells expressing them may have distinct anatomical locations or functions. Generally, a TCR is found on the Attorney Docket No.51624-0017WO1 surface of T cells (or T lymphocytes) where it is generally responsible for recognizing antigens, such as peptides bound to major histocompatibility complex (MHC) molecules. In some embodiments, the TCR is an intact or full-length TCR, such as a TCR containing the α chain and β chain. In some embodiments, the TCR is an antigen-binding portion that is less than a full-length TCR but that binds to a specific peptide bound in an MHC molecule, such as binds to an MHC-peptide complex. In some cases, an antigen-binding portion or fragment of a TCR can contain only a portion of the structural domains of a full-length or intact TCR, but yet is able to bind the peptide epitope, such as MHC-peptide complex, to which the full TCR binds. In some cases, an antigen-binding portion contains the variable domains of a TCR, such as variable α (Va or Vα) chain and variable β (Vb or Vβ) chain of a TCR, or antigen -binding fragments thereof sufficient to form a binding site for binding to a specific MHC-peptide complex. The variable domains of the TCR contain complementarity determining regions (CDRs), which generally are the primary contributors to antigen recognition and binding capabilities and specificity of the peptide, MHC and/or MHC-peptide complex. In some embodiments, a CDR of a TCR or combination thereof forms all or substantially all of the antigen-binding site of a given TCR molecule. The various CDRs within a variable region of a TCR chain generally are separated by framework regions (FRs), which generally display less variability among TCR molecules as compared to the CDRs. In some embodiments, CDR3 is the main CDR responsible for antigen binding or specificity, or is the most important among the three CDRs on a given TCR variable region for antigen recognition, and/or for interaction with the processed peptide portion of the peptide-MHC complex. In some contexts, the CDR1 of the alpha chain can interact with the N-terminal part of certain antigenic peptides. In some cases, CDR1 of the beta chain can interact with the C-terminal part of the peptide. In some contexts, CDR2 contributes most strongly to or is the primary CDR responsible for the interaction with or recognition of the MHC portion of the MHC-peptide complex. The α-chain and/or β-chain of a TCR also can contain a constant domain, a transmembrane domain and/or a short cytoplasmic tail. In some aspects, each chain (e.g., alpha or beta) of the TCR can possess one N-terminal immunoglobulin variable domain, one immunoglobulin constant domain, a transmembrane region, and a short cytoplasmic tail at the C- terminal end. In some embodiments, a TCR, for example via the cytoplasmic tail, is associated Attorney Docket No.51624-0017WO1 with invariant proteins of the CD3 complex involved in mediating signal transduction. In some cases, the structure allows the TCR to associate with other molecules like CD3 and subunits thereof. For example, a TCR containing constant domains with a transmembrane region may anchor the protein in the cell membrane and associate with invariant subunits of the CD3 signaling apparatus or complex. The intracellular tails of CD3 signaling subunits (e.g., CD3γ, CD3δ, CD3ε and CD3ζ chains) contain one or more immunoreceptor tyrosine-based activation motif or ITAM and generally are involved in the signaling capacity of the TCR complex. The exact locus of a domain or region can vary depending on the particular structural or homology modeling or other features used to describe a particular domain. It is understood that reference to amino acids, including to a specific sequence set forth as a SEQ ID NO used to describe domain organization of a TCR are for illustrative purposes and are not meant to limit the scope of the embodiments provided. In some cases, the specific domain (e.g., variable or constant) can be several amino acids (such as one, two, three or four) longer or shorter. In some aspects, residues of a TCR are known or can be identified according to the International Immunogenetics Information System (IMGT) numbering system (see e.g., www.imgt.org; Lefranc et al. "IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains." Developmental & Comparative Immunology 27.1 (2003): 55-77.). The structures and variations of TCR are known in the art, and are described, e.g., in WO 2019 /195486, which is incorporated herein by reference in its entirety. In some embodiments, the α chain and β chain of a TCR each further contain a constant domain. In some embodiments, the α chain constant domain (Cα) and β chain constant domain (Cβ) individually are mammalian, such as is a human or a non-human constant domain (e.g., a mouse constant domain). In some embodiments, the constant domain is adjacent to the cell membrane. For example, in some cases, the extracellular portion of the TCR formed by the two chains contains two membrane-proximal constant domains, and two membrane-distal variable domains, which variable domains each contain CDRs. In some aspects, TCRs as descried herein can contain a human constant region, such as an alpha chain containing a human Cα region and a beta chain containing a human Cβ region. In some embodiments, the TCRs are fully human or humanized. In some embodiments, the expression and/or activity of TCRs, such as when expressed in human cells, e.g., human T cells, such as primary human T cells, are not impacted by or are not substantially impacted by the Attorney Docket No.51624-0017WO1 presence of an endogenous human TCR. In some embodiments, the engineered TCRs are expressed at similar or improved levels on the cell surface, exhibit the similar or greater functional activity (e.g., cytolytic activity) and/or exhibit similar or greater anti-tumor activity, when expressed by human cells that contain or express an endogenous human TCR, such as human T cells, as compared to the level of expression, function activity and/or anti-tumor activity of the same TCR in similar human cells but in which expression of the endogenous TCR has been reduced or eliminated. In some examples an engineered TCR as described herein, when expressed in human T cells, is expressed on the cell surface at a level that is at least or at least about 80%, 85%, 90%, 95%, 100%, 105%, 110%, 115% or 120% of the level of expression of the same TCR when expressed in similar human T cells but in which expression of the endogenous TCR has been reduced or eliminated. In some embodiments, each of the Cα and Cβ domains is human. In some embodiments, each of the Cα and Cβ domains is derived from a rodent (e.g., a mouse). In some embodiments, the TCR can be a heterodimer of two chains α and β that are linked, such as by a disulfide bond or disulfide bonds. In some embodiments, the constant domain of the TCR can contain short connecting sequences in which a cysteine residue forms a disulfide bond, thereby linking the two chains of the TCR. In some embodiments, a TCR can have an additional cysteine residue in each of the α and β chains, such that the TCR contains two disulfide bonds in the constant domains. In some embodiments, each of the constant and variable domains contains disulfide bonds formed by cysteine residues. In some embodiments, the TCR comprises CDRs, Va and/or Vb and constant region sequences as described herein. In some embodiments, the TCR is a dimeric TCR (dTCR). In some embodiments a dTCR contains a first polypeptide wherein a sequence corresponding to a provided TCR α chain variable region sequence is fused to the N terminus of a sequence corresponding to a TCR α chain constant region extracellular sequence, and a second polypeptide wherein a sequence corresponding to a provided TCR β chain variable region sequence is fused to the N terminus a sequence corresponding to a TCR β chain constant region extracellular sequence, the first and second polypeptides being linked by a disulfide bond. In some embodiments, a TCR can be cell-bound or in soluble form. In some embodiments, the TCR is in cell-bound form expressed on the surface of a cell. Attorney Docket No.51624-0017WO1 In some embodiments, the TCR is a single chain TCR (scTCR). The scTCR is a single amino acid strand containing an α chain and a β chain that is able to bind to MHC-peptide complexes. Typically, a scTCR can be generated using methods known to those of skill in the art. These methods are described e.g., in WO96/13593, WO96/18105, WO99/18129, WO 04/033685, WO2006/037960, WO2011/044186; WO 2019/195486; U.S. Patent No.7,569,664; each of which is incorporated herein by reference in its entirety. The TCR, antigen binding fragments thereof, and TCR-derived binding molecules can bind to or recognize a peptide epitope associated with an antigen of interest (e.g., a cancer antigen). In some embodiments, the peptide epitope is a Kras G12V mutant peptide or fragment thereof, e.g., SEQ ID NO: 1 or SEQ ID NO: 2. In some embodiments, the antigen is presented in the context of an MHC molecule. Such binding molecules include e.g., T cell receptors (TCRs) and antigen-binding fragments thereof, antibodies and antigen binding fragments thereof, and TCR-like CAR. They exhibit antigenic specificity for binding or recognizing such peptide epitopes. In some aspects, engineered cells that express a provided binding molecule, e.g., a TCR or antigen-binding fragment, exhibit cytotoxic activity against target cells expressing the peptide epitope, such as cancer cells or cells that include a nucleic acid encoding a Kras G12V mutant protein or carry a Kras G12V mutant protein. In some embodiments, the TCR, antigen binding fragments thereof, and TCR-derived binding molecules cannot bind to a wildtype Kras peptide presented by a MHC molecule (e.g., SEQ ID NO: 3 presented by HLA-A*11:01). In some embodiments, the TCR, antigen binding fragments thereof, and TCR-derived binding molecules cannot bind to SEQ ID NO: 28-49, or such peptide presented by an MHC molecule. In some aspects, the TCR, antigen binding fragments thereof, and TCR-derived binding molecules recognize or bind to epitopes in the context of an MHC molecule, such as an MHC Class I molecule or an MHC class II molecule. Both MHC Class I molecules or MHC class II molecules are human leukocyte antigens (HLA). They play an important component of adaptive immune system. The HLA expression is controlled by genes located on chromosome 6. It encodes cell surface molecules specialized to present antigenic peptides to the T-cell receptor on T cells. In some embodiments, the MHC molecule is an HLA-A molecule, e.g., HLA-A*11:01. In some embodiments, the TCR, antigen binding fragments thereof, and TCR-derived binding molecules recognize or bind to epitopes in the context of an MHC Class I molecule. The MHC Class I molecule can be a human leukocyte antigen (HLA)-A11 molecule, including any Attorney Docket No.51624-0017WO1 one or more subtypes thereof, e.g., HLA-A*11:01. The human leukocyte antigen A11 (HLA- A11) is among the most common human serotypes. In some cases, there can be differences in the frequency of subtypes between different populations. For example, HLA-A11 is more common in East Asia than elsewhere, and it is part of several long haplotypes that appear to have been frequent in the ancient peoples of Asia. In some embodiments, the MHC molecule is HLA- A*11:01. In some embodiments, the present disclosure provides TCR or antigen-binding fragment thereof that bind a Kras G12V peptide/HLA-A*11:01 complex. In some embodiments, the binding molecule, e.g., TCR or antigen-binding fragment thereof or TCR-derived binding molecule, is isolated or purified, or is recombinant. In some aspects, the binding molecule, e.g., TCR or antigen-binding fragment thereof or TCR-derived binding molecule, is fully human or humanized. In some embodiments, the binding molecule is monoclonal. In some aspects, the binding molecule is a single chain. In other embodiments, the binding molecule contains two chains. In some embodiments, the binding molecule, e.g., TCR, antigen-binding fragment thereof or TCR-derived binding molecule, is expressed on the surface of a cell. The TCR, antigen-binding fragment thereof, or TCR-derived binding molecules can have a Va and a Vb, or a region that is similar to Va and a region that is similar to Vb. In some embodiments, the Va region comprises the amino acid sequence set forth in any of SEQ ID NO: 4, 6, 8, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. In some embodiments, the Vb region comprises the amino acid sequence set forth in any of SEQ ID NO: 5, 7, 9, or an amino acid sequence that has at least 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. In some embodiments, the Va region comprises one or more Va CDR sequences as described herein. In some embodiments, the Vb region comprises one or more Vb CDR sequences as described herein. In some embodiments, the TCR, TCR-derived binding molecules, or antigen-binding fragment thereof, comprising an alpha chain comprising a variable alpha (Va) region and a beta chain comprising a variable beta (Vb) region, wherein the Va region can have complementarity determining regions (CDRs) 1, 2, 3, wherein the CDR1 region comprises or consists of an amino acid sequence that is at least 80%, 85%, 90%, or 95% identical to a selected Va CDR1 amino acid sequence, the CDR2 region comprises or consists of an amino acid sequence that is at least Attorney Docket No.51624-0017WO1 80%, 85%, 90%, or 95% identical to a selected Va CDR2 amino acid sequence, and the CDR3 region comprises or consists of an amino acid sequence that is at least 80%, 85%, 90%, or 95% identical to a selected Va CDR3 amino acid sequence, and a variable beta (Vb) region comprising CDRs 1, 2, 3, wherein the CDR1 region comprises or consists of an amino acid sequence that is at least 80%, 85%, 90%, or 95% identical to a selected Vb CDR1 amino acid sequence, the CDR2 region comprises or consists of an amino acid sequence that is at least 80%, 85%, 90%, or 95% identical to a selected Vb CDR2 amino acid sequence, and the CDR3 region comprises or consists of an amino acid sequence that is at least 80%, 85%, 90%, or 95% identical to a selected Vb CDR3 amino acid sequence. The selected Va CDRs 1, 2, 3 amino acid sequences and the selected Vb CDRs, 1, 2, 3 amino acid sequences are shown in FIG.8. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Va) containing one, two, or three of the CDRs of SEQ ID NO: 10 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 11 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 12 with zero, one or two amino acid insertions, deletions, or substitutions. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Vb) containing one, two, or three of the CDRs of SEQ ID NO: 13 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 14 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 15 with zero, one or two amino acid insertions, deletions, or substitutions. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Va) containing one, two, or three of the CDRs of SEQ ID NO: 16 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 17 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 18 with zero, one or two amino acid insertions, deletions, or substitutions. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Vb) containing one, two, or three of the CDRs of SEQ ID NO: 19 with zero, one or two amino acid insertions, deletions, Attorney Docket No.51624-0017WO1 or substitutions; SEQ ID NO: 20 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 21 with zero, one or two amino acid insertions, deletions, or substitutions. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Va) containing one, two, or three of the CDRs of SEQ ID NO: 22 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 23 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 24 with zero, one or two amino acid insertions, deletions, or substitutions. In some embodiments, the TCR, antigen-binding fragment thereof, or TCR derived binding molecules described herein can contain a variable region (e.g., Vb) containing one, two, or three of the CDRs of SEQ ID NO: 25 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 26 with zero, one or two amino acid insertions, deletions, or substitutions; SEQ ID NO: 27 with zero, one or two amino acid insertions, deletions, or substitutions. The present disclosure also provides TCR α (alpha) and/or β (beta) chain. In some embodiments, the α chain comprises one or more Va CDR sequences as described herein. In some embodiments, the β chain comprises one or more Vb CDR sequences as described herein. In some embodiments, the TCR may be a heterodimer of two chains α and β that are linked, such as by a disulfide bond or disulfide bonds. In some embodiments, the constant domain of the TCR may contain short connecting sequences in which a cysteine residue forms a disulfide bond, thereby linking the two chains of the TCR. In some embodiments, a TCR may have an additional cysteine residue in each of the α and β chains, such that the TCR contains two disulfide bonds in the constant domains. In some embodiments, each of the constant and variable domains contains disulfide bonds formed by cysteine residues. In some embodiments, the native disulfide bonds are not present. In some embodiments, the one or more of the native cysteines (e.g., in the constant domain of the α chain and β chain) that form a native interchain disulfide bond are substituted to another residue, such as to a serine or alanine. In some embodiments, an introduced disulfide bond can be formed by mutating non- cysteine residues on the alpha and beta chains, such as in the constant domain of the α chain and β chain, to cysteine. Opposing cysteines in the TCR α and β chains provide a disulfide bond that Attorney Docket No.51624-0017WO1 links the constant regions of TCR α and β chains of the substituted TCR to one another and which is not present in a TCR comprising the unsubstituted constant region in which the native disulfide bonds are present, such as unsubstituted native human constant region or the unsubstituted native mouse constant region. In some embodiments, the presence of non-native cysteine residues (e.g., resulting in one or more non-native disulfide bonds) in a recombinant TCR can favor production of the desired recombinant TCR in a cell in which it is introduced over expression of a mismatched TCR pair containing a native TCR chain. In some embodiments, the nucleic acid encoding the alpha chain and the nucleic acid encoding the beta chain can be connected via a linker, such as any described elsewhere herein. The disclosure also provides nucleic acid comprising a polynucleotide encoding a polypeptide comprising a TCR α chain variable region, and/or a TCR β chain variable region. The variable region comprises CDRs as shown in FIG.8. When the polypeptides are paired with corresponding polypeptide (e.g., a corresponding α chain variable region or a corresponding β chain variable region), the paired polypeptides bind to the target of interest (e.g., a Kras G12V mutant protein, peptide, or fragment thereof). In some embodiments, by binding to the target of interest, the TCR or antigen-binding fragment thereof, or TCR-derived binding molecules, can activate T cells (e.g., by activating TCR signaling pathway). In some embodiments, the activation can upregulate immune response, increase expression of cytokines (e.g., IFN-γ, TNF-α, and/or IL2), promote T-cell proliferation, and/or T cell-mediated killing. In some embodiments, the TCR or antigen-binding fragment thereof, or TCR-derived binding molecules as described herein can increase immune response, activity or number of T cells by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 2 folds, 3 folds, 5 folds, 10 folds, 20 folds, 50 folds, or 100 folds. In some embodiments, the TCR or antigen- binding fragment thereof, or TCR-derived binding molecules, when the antigen of interest is present, can increase production of cytokines (e.g., IFN-γ, TNF-α, and/or IL2). In some embodiments, the activation can induce at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 1 fold, 2 folds, 5 folds, 10 folds, 100 folds, 200 folds, 500 folds, or 1000 folds increase of production of cytokines (e.g., IFN-γ, TNF-α, and/or IL2). In some embodiments, the activation can induce at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 1 fold, 2 folds, 3 folds, 4 folds, 5 folds, 10 folds, 20 folds, 50 folds, 100 folds, 200 folds, 500 folds, or 1000 folds increase Attorney Docket No.51624-0017WO1 of specific killing of target cells. In some embodiments, the specific killing of target cells is determined by in vitro cytolytic assays (e.g., coculturing any of the anti-Kras G12V TCR-T cells with cancer cells carrying the Kras G12V mutation) using any of the methods described herein. In some aspects, the provided recombinant TCR-T cells are CD8+ TCR-T cells. In some aspects, the provided recombinant TCR-T cells are CD4+ TCR-T cells. In some embodiments, the TCR or antigen-binding fragment thereof, or TCR-derived binding molecules as described herein specifically binds to Kras G12V peptide epitopes. In some embodiments, the epitope has a sequence of SEQ ID NO: 1 or SEQ ID NO: 2. Binding affinities can be deduced from the quotient of the kinetic rate constants (KD=k _off /k _on ). In some embodiments, KD is less than 1 × 10 ^-6 M, less than 1 × 10 ^-7 M, less than 1 × 10 ^-8 M, less than 1 × 10 ^-9 M, less than 1 × 10 ^-10 M, or less than 1 × 10 ^-11 M. In some embodiments, the KD is less than 50 nM, 30 nM, 20 nM, 15 nM, 10 nM, 9 nM, 8 nM, 7 nM, 6 nM, 5 nM, 4 nM, 3 nM, 2 nM, or 1 nM. In some embodiments, KD is greater than 1 × 10 ^-7 M, greater than 1 × 10 ^-8 M, greater than 1 × 10 ^-9 M, greater than 1 × 10 ^-10 M, greater than 1 × 10 ^-11 M, or greater than 1 × 10 ^-12 M. General techniques for measuring the affinity of a binding molecule for an antigen include, e.g., ELISA, RIA, and surface plasmon resonance (SPR). In some embodiments, the T cells expressing the TCR, antigen-binding fragment thereof, or TCR-derived binding molecules as described herein specifically binds to target cells or APCs carrying the Kras G12V mutation. In some embodiments, the T cells and the target cells are co- cultured at a 1: 1 effector-to-target cell ratio. In some embodiments, the TCR or antigen-binding fragment thereof, or TCR-derived binding molecules have a relatively high expression efficiency. For example, the expression efficiency for the TCR or antigen-binding fragment thereof, or TCR-derived binding molecules described herein can be at least 10%, 20%, 30%, 40%, 50%, or 100% higher than an reference molecule (e.g., an endogenous TCR) under the same conditions. In some embodiments, the binding molecule, e.g., TCR, does not exhibit cross-reactive or off-target binding, such as undesirable off-target binding, e.g., off-target binding to antigens present in healthy or normal tissues or cells. In some embodiments, the TCRs described herein do not cross-react with other human protein peptides originated from normal tissues or cells. KRAS AND CANCER Attorney Docket No.51624-0017WO1 GTPase KRas (Kras) is a signal transducer protein, which plays an important role in various cellular signaling events such as in regulation of cell proliferation. It is a critical hub in the cell circuitry, as upon an upstream stimulus it transduces activating signals to several cellular signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway. Kras cycles between inactive guanosine diphosphate (GDP)-bound and active guanosine triphosphate (GTP)-bound states. Only in the GTP-bound state, Kras is able to bind and activate its effector proteins, such as RAF-kinases, PI3K and RalGDS. Kras itself becomes activated when a guanosine exchange factor (GEF) protein displaces GDP from the nucleotide binding site, resulting eventually in GTP binding, as there is a higher intracellular concentration of GTP than GDP. Inactivation of the active Kras occurs upon GTP hydrolysis to GDP. On its own Kras has low intrinsic GTPase activity, which is greatly enhanced by GTPase activating proteins (GAP) that catalyse the hydrolysis reaction. Hyperactivation of RAS signaling, which may occur via a direct mutation of RAS or indirectly via other proteins in RAS pathways, plays a significant role in cancer and in particular rare diseases such as RASopathies. There are three closely related RAS isoforms: HRAS, Kras and NRAS. From all of the RAS isoforms, Kras is the most oncogenic with its 85% share of all mutated RAS proteins observed in cancer. Kras missense mutations are particularly frequent in the pancreatic, colorectal and lung cancers (COSMIC v.90). In cancer, three mutation hotspots: G12, G13 and Q61 are observed in RAS genes. In this regard, Kras differs from the NRAS and HRAS, as it is the only RAS isoform where the position 12 mutations are predominant. Details of Kras and its functions can be found, e.g., in Pantsar, T. "The current understanding of Kras protein structure and dynamics." Computational and Structural Biotechnology Journal 18 (2020): 189-198; Mustachio, L.M., et al. "Targeting KRAS in cancer: promising therapeutic strategies." Cancers 13.6 (2021): 1204; and Zhu, C., et al. "Targeting KRAS mutant cancers: from druggable therapy to drug resistance." Molecular Cancer 21.1 (2022): 1-19; each of which is incorporated herein by reference in its entirety. ENGINEERED CELLS The present disclosure provides engineered cells (e.g., T cells) that comprise TCR or antigen-binding fragment thereof, or other similar antigen-binding molecules as described herein. These engineered cells can be used to treat various disorders or disease as described herein (e.g., Attorney Docket No.51624-0017WO1 cancers). In various embodiments, the cell that is engineered can be obtained from e.g., humans and non-human animals. In various embodiments, the cell that is engineered can be obtained from humans, rats, mice, rabbits, monkeys, pig or any other species. Preferably, the cell is from humans, rats or mice. More preferably, the cell is obtained from humans. In various embodiments, the cell that is engineered is a blood cell. Preferably, the cell is a leukocyte (e.g., a T cell), lymphocyte or any other suitable blood cell type. In some embodiments, the cell is a peripheral blood cell. In some embodiments, the cell is a T cell, B cell or NK cell. In some embodiments, the cell is a T cell. In some embodiments, the T cells can express a cell surface receptor that recognizes a Kras G12V peptide (e.g., SEQ ID NO: 1 or SEQ ID NO: 2) that is presented by a MHC molecule (e.g., HLA-A*11:01) on the surface of a target cell. The cell surface receptor can be a wild type or recombinant T cell receptor (TCR), a chimeric antigen receptor (CAR), or any other surface receptor capable of recognizing the Kras G12V peptide that is associated with the target cell. T cells can be obtained by various methods known in the art, e.g., in vitro culture of T cells (e.g., tumor infiltrating lymphocytes) isolated from patients. TCR gene-modified T cells can be obtained by transducing T cells (e.g., isolated from the peripheral blood of patients), with a viral vector (e.g., a vector encoding a lentivirus). In some embodiments, the T cell is a TCR gene-modified T cell. In some embodiments, the T cells are CD4+ T cells, CD8+ T cells, or regulatory T cells. In some embodiments, the T cells are T helper type 1 T cells and T helper type 2 T cells. In some embodiments, the T cell expressing this receptor is an αβ-T cell. In alternate embodiments, the T cell expressing this receptor is a γδ-T cell. In some embodiments, the cell is an NK cell. In some embodiments, preparation of the engineered cells includes one or more culture and/or preparation steps. The cells for introduction of the binding molecule, e.g., TCR, can be isolated from a sample, such as a biological sample, e.g., one obtained from or derived from a subject. In some embodiments, the subject from which the cell is isolated is one having the disease or condition or in need of a cell therapy or to which cell therapy will be administered. The subject in some embodiments is a human in need of a particular therapeutic intervention, such as the adoptive cell therapy for which cells are being isolated, processed, and/or engineered. In some embodiments, the cells are stem cells, such as multipotent and pluripotent stem Attorney Docket No.51624-0017WO1 cells, including induced pluripotent stem cells (iPSCs). The cells can be primary cells, such as those isolated directly from a subject and/or isolated from a subject and frozen. In some embodiments, the stem cells are cultured with additional differentiation factors to obtain desired cell types (e.g., T cells). Different cell types can be obtained from appropriate isolation methods. The isolation methods include the separation of different cell types based on the expression or presence in the cell of one or more specific molecules, such as surface markers, e.g., surface proteins, intracellular markers, or nucleic acid. In some embodiments, any known method for separation based on such markers can be used. In some embodiments, the separation is affinity- or immunoaffinity-based separation. For example, the isolation in some aspects includes separation of cells and cell populations based on the cells’ expression or expression level of one or more markers, typically cell surface markers, for example, by incubation with an antibody or binding partner that specifically binds to such markers, followed generally by washing steps and separation of cells having bound the antibody or binding partner, from those cells having not bound to the antibody or binding partner. Such separation steps can be based on positive selection, in which the cells having bound the reagents are retained for further use, and/or negative selection, in which the cells having not bound to the antibody or binding partner are retained. In some examples, both fractions are retained for further use. In some aspects, negative selection can be particularly useful where no antibody is available that specifically identifies a cell type in a heterogeneous population, such that separation is best carried out based on markers expressed by cells other than the desired population. Also provided are methods, nucleic acids, compositions, and kits, for expressing the binding molecules, and for producing the genetically engineered cells expressing such binding molecules. The genetic engineering generally involves introduction of a nucleic acid encoding the therapeutic molecule, e.g., TCR, CAR, TCR-like CAR, polypeptides, fusion proteins, into the cell, such as by retroviral or lentiviral transduction, transfection, or transformation. In some embodiments, gene transfer is accomplished by first stimulating the cell, such as by combining it with a stimulus that induces a response such as proliferation, survival, and/or activation, e.g., as measured by expression of a cytokine or activation marker, followed by transduction of the activated cells, and expansion in culture to numbers sufficient for clinical application. In some embodiments, recombinant nucleic acids are transferred into cells using Attorney Docket No.51624-0017WO1 recombinant infectious virus particles, such as, e.g., vectors derived from simian virus 40 (SV40), adenoviruses, adeno-associated virus (AAV). In some embodiments, recombinant nucleic acids are transferred into T cells using recombinant lentiviral vectors or retroviral vectors, such as gamma-retroviral vectors. In some embodiments, the retroviral vector has a long terminal repeat sequence (LTR), e.g., a retroviral vector derived from the Moloney murine leukemia virus (MoMLV), myeloproliferative sarcoma virus (MPSV), murine embryonic stem cell virus (MESV), murine stem cell virus (MSCV), or spleen focus forming virus (SFFV). In some embodiments, the retroviruses include those derived from any avian or mammalian cell source. The retroviruses typically are amphotropic, meaning that they are capable of infecting host cells of several species, including humans. In some embodiments, the vector is a lentivirus vector. In some embodiments, recombinant nucleic acids are transferred into T cells via electroporation. In some embodiments, recombinant nucleic acids are transferred into T cells via transposition. Other methods of introducing and expressing genetic material in immune cells include calcium phosphate transfection, protoplast fusion, cationic liposome-mediated transfection; tungsten particle-facilitated microparticle bombardment and strontium phosphate DNA co-precipitation. Many of these methods are descried e.g., in WO2019/195486, which is incorporated herein by reference in its entirety. In some aspects, development of a humanized and/or fully human recombinant TCR presents technical challenges. For example, in some aspects, a humanized and/or a fully human recombinant TCR receptor, when engineered into a human T cell, may compete with endogenous TCR complexes and/or can form mispairings with endogenous TCRa and/or TCRb chains, which may, in certain aspects, reduce recombinant TCR signaling, activity, and/or expression, and ultimately result in reduced activity of the engineered cells. The engineered cell can be genetically modified. In some embodiments, the engineered cells can comprise a genetic disruption of a T cell receptor alpha constant (TRAC) gene and/or a T cell receptor beta constant (TRBC) gene. In some embodiments, the TRBC gene is one or both of a T cell receptor beta constant 1 (TRBC1) or T cell receptor beta constant 2 (TRBC2) gene. In some embodiments, the engineered cells do not express endogenous TCR α chain and/or TCR β chain. In some other aspects, non-human constant domains are used, e.g., rodent (e.g., mouse) constant domains. The use of non-human constant domains can effectively reduce the likelihood of mispairing. Also provided are populations of engineered cells, compositions containing such cells Attorney Docket No.51624-0017WO1 and/or enriched for such cells, such as in which cells expressing the binding molecule make up at least 15%, 20%, 25%, 30%, 35%, 40%, 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more percent of the total cells in the composition or cells of a certain type such as T cells, CD8+ T cells or CD4+ T cells. RECOMBINANT VECTORS The present disclosure also provides recombinant vectors (e.g., an expression vectors) that include an isolated polynucleotide disclosed herein (e.g., a polynucleotide that encodes a polypeptide disclosed herein), host cells into which are introduced the recombinant vectors (i.e., such that the host cells contain the polynucleotide and/or a vector comprising the polynucleotide), and the production of recombinant polypeptides or fragments thereof by recombinant techniques. A vector is a construct capable of delivering one or more polynucleotide(s) of interest to a host cell when the vector is introduced to the host cell. An “expression vector” is capable of delivering and expressing the one or more polynucleotide(s) of interest as an encoded polypeptide in a host cell into which the expression vector has been introduced. Thus, in an expression vector, the polynucleotide of interest is positioned for expression in the vector by being operably linked with regulatory elements such as a promoter, enhancer, and/or a poly-A tail, either within the vector or in the genome of the host cell at or near or flanking the integration site of the polynucleotide of interest such that the polynucleotide of interest will be translated in the host cell introduced with the expression vector. A vector can be introduced into the host cell by methods known in the art, e.g., electroporation, chemical transfection (e.g., DEAE-dextran), transformation, transfection, and infection and/or transduction (e.g., with recombinant virus). Thus, non-limiting examples of vectors include viral vectors (which can be used to generate recombinant virus), naked DNA or RNA, plasmids, cosmids, phage vectors, and DNA or RNA expression vectors associated with cationic condensing agents. The present disclosure provides a recombinant vector comprising a nucleic acid construct suitable for genetically modifying a cell, which can be used for treatment of pathological disease or condition. Any vector or vector type can be used to deliver genetic material to the cell. These Attorney Docket No.51624-0017WO1 vectors include but are not limited to plasmid vectors, viral vectors, bacterial artificial chromosomes (BACs), yeast artificial chromosomes (YACs), and human artificial chromosomes (HACs). Viral vectors can include but are not limited to recombinant retroviral vectors, recombinant lentiviral vectors, recombinant adenoviral vectors, foamy virus vectors, recombinant adeno-associated viral (AAV) vectors, hybrid vectors, and plasmid transposons (e.g., sleeping beauty transposon system, and PiggyBac transposon system) or integrase based vector systems. Other vectors that are known in the art can also be used in connection with the methods described herein. In some embodiments, the vector is a viral vector. The viral vector can be grown in a culture medium specific for viral vector manufacturing. Any suitable growth media and/or supplements for growing viral vectors can be used in accordance with the embodiments described herein. In some embodiments, the vector used is a recombinant retroviral vector. A retroviral vector is capable of directing the expression of a nucleic acid molecule of interest. A retrovirus is present in the RNA form in its viral capsule and forms a double-stranded DNA intermediate when it replicates in the host cell. Similarly, retroviral vectors are present in both RNA and double-stranded DNA forms. The retroviral vector also includes the DNA form which contains a recombinant DNA fragment and the RNA form containing a recombinant RNA fragment. The vectors can include at least one transcriptional promoter/enhancer, or other elements which control gene expression. Such vectors can also include a packaging signal, long terminal repeats (LTRs) or portion thereof, and positive and negative strand primer binding sites appropriate to the retrovirus used. Long terminal repeats (LTRs) are identical sequences of DNA that repeat many times (e.g., hundreds or thousands of times) found at either end of retrotransposons or proviral DNA formed by reverse transcription of retroviral RNA. They are used by viruses to insert their genetic material into the host genomes. Optionally, the vectors can also include a signal which directs polyadenylation, selectable markers such as Ampicillin resistance, Neomycin resistance, TK, hygromycin resistance, phleomycin resistance histidinol resistance, or DHFR, as well as one or more restriction sites and a translation termination sequence. For example, such vectors can include a 5' LTR, a leading sequence, a tRNA binding site, a packaging signal, an origin of second strand DNA synthesis, and a 3' LTR or a portion thereof. Additionally, retroviral vector used herein can also refers to the recombinant vectors created by Attorney Docket No.51624-0017WO1 removal of the retroviral gag, pol, and env genes and replaced with the gene of interest. In some embodiments, the vector or construct can contain a single promoter that drives the expression of one or more nucleic acid molecules. In some embodiments, such promoters can be multicistronic (bicistronic or tricistronic). For example, in some embodiments, transcription units can be engineered as a bicistronic unit containing an IRES (internal ribosome entry site), which allows coexpression of gene products (e.g., encoding an alpha chain and/or beta chain of a TCR) by a message from a single promoter. Alternatively, in some cases, a single promoter may direct expression of an RNA that contains, in a single open reading frame (ORF), two or three genes (e.g., encoding an alpha chain and/or beta chain of a TCR) separated from one another by sequences encoding a self-cleavage peptide (e.g., P2A or T2A) or a protease recognition site (e.g., furin). The ORF thus encodes a single polyprotein, which, either during (in the case of 2A e.g., T2A) or after translation, is cleaved into the individual proteins. In some cases, the peptide, such as T2A, can cause the ribosome to skip (ribosome skipping) synthesis of a peptide bond at the C-terminus of a 2A element, leading to separation between the end of the 2A sequence and the next peptide downstream. Various cell lines can be used in connection with the vectors as described herein. Exemplary eukaryotic cells that may be used to express polypeptides include, but are not limited to, COS cells, including COS 7 cells; 293 cells, including 293-6E cells; CHO cells, including CHO-S, DG44. Lec13 CHO cells, and FUT8 CHO cells; PER.C6 ^® cells; and NSO cells. In one aspect, the disclosure also relates to a nucleic acid comprising a polynucleotide encoding a polypeptide comprising: (1) a TCR α chain or a fragment thereof comprising an α chain variable region (Va) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 10, 11, and 12, respectively, and wherein the Va, when paired with a β chain variable region (Vb) comprising the amino acid sequence set forth in SEQ ID NO: 5 binds to human Kras G12V mutant protein; (2) a TCR β chain or a fragment thereof comprising a β chain variable region (Vb) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 13, 14, and 15, respectively, and wherein the Vb, when paired with an α chain variable region (Va) comprising the amino acid sequence set forth in SEQ ID NO: 4 binds to human Kras G12V mutant protein; Attorney Docket No.51624-0017WO1 (3) a TCR α chain or a fragment thereof comprising an α chain variable region (Va) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 16, 17, and 18, respectively, and wherein the Va, when paired with a β chain variable region (Vb) comprising the amino acid sequence set forth in SEQ ID NO: 7 binds to human Kras G12V mutant protein; (4) a TCR β chain or a fragment thereof comprising a β chain variable region (Vb) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 19, 20, and 21, respectively, and wherein the Vb, when paired with an α chain variable region (Va) comprising the amino acid sequence set forth in SEQ ID NO: 6 binds to human Kras G12V mutant protein; (5) a TCR α chain or a fragment thereof comprising an α chain variable region (Va) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 22, 23, and 24, respectively, and wherein the Va, when paired with a β chain variable region (Vb) comprising the amino acid sequence set forth in SEQ ID NO: 9 binds to human Kras G12V mutant protein; or (6) a TCR β chain or a fragment thereof comprising a β chain variable region (Vb) comprising complementarity determining regions (CDRs) 1, 2, and 3 comprising the amino acid sequences set forth in SEQ ID NOs: 25, 26, and 27, respectively, and wherein the Vb, when paired with an α chain variable region (Va) comprising the amino acid sequence set forth in SEQ ID NO: 8 binds to human Kras G12V mutant protein. In some embodiments, the Va when paired with a Vb specifically binds to human Kras G12V mutant protein, or the Vb when paired with a Va specifically binds to human Kras G12V mutant protein. In some embodiments, the nucleic acid is cDNA. In one aspect, the disclosure relates to a vector comprising one or more of the nucleic acids as described herein. In one aspect, the disclosure also relates to a vector comprising two of the nucleic acids as described herein. In some embodiments, the vector encodes the Va region and the Vb region that together bind to human Kras G12V protein peptide (e.g., presented by a MHC molecule). In one aspect, the disclosure relates to a pair of vectors, wherein each vector comprises one of the nucleic acids as described herein, wherein together the pair of vectors encodes the Va region and the Vb region that together bind to human Kras G12V protein peptide (e.g., presented Attorney Docket No.51624-0017WO1 by a MHC molecule). In one aspect, the disclosure relates to a cell comprising the vector or the pair of vectors as described herein. In some embodiments, the cell is a T cell. In some cases, certain TCRs, may exhibit poor expression or activity in part due to mispairing and/or competition with endogenous TCR chains and/or other factors. One method to address these challenges has been to design recombinant TCRs with mouse constant domains to prevent mispairings with endogenous human TCR α or β chains. However, the use of recombinant TCRs with mouse sequences may present a risk for immune response. In some embodiments, a genetic disruption is introduced, e.g., by gene editing, at an endogenous gene encoding one or more TCR chains. The present disclosure also provides nucleic acids that encode TCR α and/or β chain. In some embodiments, the α chain comprises one or more Va CDR sequences as described herein. In some embodiments, the β chain comprises one or more Vb CDR sequences as described herein. The term “Linker” (L) or “linker domain” or “linker region” as used herein refer to an oligo- or polypeptide region from about 1 to 100 amino acids in length, which links together any of the domains/regions. Linkers can be composed of flexible residues like glycine and serine so that the adjacent protein domains are free to move relative to one another. Longer linkers can be used when it is desirable to ensure that two adjacent domains do not sterically interfere with one another. Linkers can be cleavable or non-cleavable. Examples of cleavable linkers include 2A linkers (for example P2A, T2A), 2A-like linkers or functional equivalents thereof and combinations thereof. In some embodiments, the linkers include the picornaviral 2A-like linker, CHYSEL sequences of porcine teschovirus (P2A), Thosea asigna virus (T2A) or combinations, variants and functional equivalents thereof. Other linkers will be apparent to those of skill in the art and can be used in the methods described herein. The present disclosure also provides a nucleic acid sequence comprising a nucleotide sequence encoding any of the TCRs, antigen binding fragments thereof, and/or TCR-derived binding molecules (including e.g., functional portions and functional variants thereof, polypeptides, or proteins described herein). “Nucleic acid” as used herein can include “polynucleotide,” “oligonucleotide,” and “nucleic acid molecule,” and generally means a polymer of DNA or RNA, which can be single-stranded or double-stranded, synthesized or Attorney Docket No.51624-0017WO1 obtained from natural sources, which can contain natural, non-natural or altered nucleotides. Furthermore, the nucleic acid comprises complementary DNA (cDNA). It is generally preferred that the nucleic acid does not comprise any insertions, deletions, inversions, and/or substitutions. However, it can be suitable in some instances, as discussed herein, for the nucleic acid to comprise one or more insertions, deletions, inversions, and/or substitutions. The nucleic acids as described herein can be constructed based on chemical synthesis and/or enzymatic ligation reactions using procedures known in the art. For example, a nucleic acid can be chemically synthesized using naturally occurring nucleotides or variously modified nucleotides. In some of any such embodiments, the nucleotide sequence is codon-optimized. The present disclosure also provides the nucleic acids comprising a nucleotide sequence complementary to the nucleotide sequence of any of the nucleic acids described herein or a nucleotide sequence which hybridizes under stringent conditions to the nucleotide sequence of any of the nucleic acids described herein. In some embodiments, the nucleotide sequence encoding the alpha chain and the nucleotide sequence encoding the beta chain are separated by a peptide sequence that causes ribosome skipping. In some embodiments, the peptide that causes ribosome skipping is a P2A or T2A peptide. In some embodiments, the nucleic acid is synthetic. In some embodiments, the nucleic acid is cDNA. In some of any such embodiments, the TCR or antigen-binding fragment thereof is encoded by a nucleotide sequence that has been codon-optimized. In certain embodiments, the alpha and/or beta chain further comprises a signal peptide. In particular embodiments, the TCR or antigen-binding fragment thereof is isolated or purified or is recombinant. In some of any such embodiments, the TCR or antigen-binding fragment is recombinant. In some of any such embodiments, the TCR or antigen-binding fragment thereof is humanized. The disclosure also provides a nucleic acid sequence that is at least 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% identical to any nucleotide sequence as described herein, and an amino acid sequence that is at least 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% identical to any amino acid sequence as described herein. In some embodiments, the disclosure relates to Attorney Docket No.51624-0017WO1 nucleotide sequences encoding any peptides that are described herein, or any amino acid sequences that are encoded by any nucleotide sequences as described herein. In some embodiments, the nucleic acid sequence is at least or about 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 150, 200, 250, 300, 350, 400, 500, or 600 nucleotides. In some embodiments, the amino acid sequence is at least or about 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, or 200 amino acid residues. In some embodiments, the nucleic acid sequence is less than 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 150, 200, 250, 300, 350, 400, 500, or 600 nucleotides. In some embodiments, the amino acid sequence is less than 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, or 200 amino acid residues. To determine the percent identity of two amino acid sequences, or of two nucleic acid sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second amino acid or nucleic acid sequence for optimal alignment and non-homologous sequences can be disregarded for comparison purposes. The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences. METHODS OF GENERATING T CELL RECEPTORS AND TCR-LIKE MOLECULES The present disclosure also provides methods for identifying and generating T cell receptors that can recognize a target antigen. In some aspects, the methods involve subjecting biological samples containing T cells, such as primary T cells, including those derived from normal donors or patients having a disease or condition of interest, to multiple rounds of antigen exposure and assessment. In some aspects, the rounds involve the use of artificial or engineered antigen presenting cells, such as autologous dendritic cells or other APCs pulsed with a desired peptide antigen, to promote presentation on an MHC, such as a class I or II MHC. In some aspects, multiple rounds of antigen exposure are carried out and in some aspects Attorney Docket No.51624-0017WO1 T cells are sorted following one or more of the rounds, e.g., based on ability to bind to the desired antigen (e.g., peptide-MHC tetramers). Sorting can be carried out by methods known in the art, e.g., flow cytometry. Cells that can bind to the desired antigen (positive fraction) and cells that cannot effectively bind to the desired antigen (negative fraction) are analyzed, e.g., by single-cell sequencing methods. In some embodiments, sequencing is performed to identify, at a single-cell level, TCR pairs present in each sample. In some aspects, the methods can quantify the number of copies of a given TCR pair present in a sample, and as such can assess the abundance of a given TCR in a given sample, and/or enrichment thereof over another sample, such as enrichment or abundance in the positive (antigen-binding) fraction, e.g., over one or more rounds, for example, as compared to the negative fraction. Such assays can be performed to generate antigen-specific T cell receptors (TCRs). In some aspects, clonal T cell lines are generated and the sequences of individual paired TCR alpha and beta chains and abundance thereof in various populations are determined on a single-cell basis, using high-throughput paired TCR sequencing. The TCR or antigen-binding fragment thereof can be further modified. In some embodiments, the binding molecules, e.g., TCRs or antigen-binding fragments thereof, include one or more amino acid variations, e.g., substitutions, deletions, insertions, and/or mutations, compared to the sequence of a binding molecule, e.g., any TCR described herein. Exemplary variants include those designed to improve the binding affinity and/or other biological properties of the binding molecule. Amino acid sequence variants of a binding molecule can be prepared by introducing appropriate modifications into the nucleotide sequence encoding the binding molecule, 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 binding molecule. Any combination of deletion, insertion, and substitution can be made to arrive at the final construct, provided that the final construct possesses the desired characteristics, e.g., specifically bind to the antigen. Various binding molecules can be made from TCR. The binding molecules, e.g., TCRs or antigen-binding fragments thereof, can include one or more amino acid substitutions, e.g., as compared to a binding molecule, e.g., TCR, sequence described herein and/or compared to a sequence of a natural repertoire, e.g., human repertoire. Sites of interest for substitutional mutagenesis include the CDRs, FRs and /or constant regions. Amino acid substitutions can be Attorney Docket No.51624-0017WO1 introduced into a binding molecule of interest and the products screened for a desired activity, e.g., retained/improved antigen affinity or avidity, decreased immunogenicity, improved half- life, CD8-independent binding or activity, surface expression, promotion of TCR chain pairing and/or other improved properties or functions. In some embodiments, one or more residues within a CDR of a parent binding molecule, e.g., TCR, is/are substituted. In some embodiments, the substitution is made to revert a sequence or position in the sequence to a germline sequence, such as a binding molecule sequence found in the germline (e.g., human germline), for example, to reduce the likelihood of immunogenicity, e.g., upon administration to a human subject. In some embodiments, a functional variant is made from a TCR or a TCR-derived binding molecule. The term "functional variant," as used herein, refers to a binding molecule having an adequate or significant sequence identity to a parent molecule. Further, the functional variant retains the same biological activity as of the parent protein. The functional variant encompasses those variants of the TCR protein described herein (the parent TCR, polypeptide, or protein) that retain the ability to specifically bind to Kras G12V epitope for which the parent TCR has antigenic specificity or to which the parent polypeptide or protein specifically binds. Furthermore the binding region (e.g., variable domain) of the functional variant can be to a similar extent, the same extent, or to a higher extent, as the parent TCR protein. In reference to the parent TCR, polypeptide, or protein, the functional variant can, for instance, be at least about 30%, 50%, 75%, 80%, 90%, 95%, 96%, 97%, 98%, 99% or more identical in amino acid sequence to the parent TCR, polypeptide, or protein. Substitutions, insertions, or deletions can be made to one or more CDRs so long as such alterations do not substantially reduce the ability of the binding molecule, e.g., TCR or antigen- binding fragment thereof, to bind antigen. For example, conservative alterations (e.g., conservative substitutions as provided herein) that do not substantially reduce binding affinity can be made in CDRs. Such alterations can, for example, be outside of antigen contacting residues in the CDRs. In certain embodiments of the variable sequences provided herein, each CDR either is unaltered, or contains no more than one, two or three amino acid substitutions. TCR-derived antibodies The present disclosure also provides an antibody or antigen-binding fragment thereof that Attorney Docket No.51624-0017WO1 contains any one or more of the CDRs as described above. In some embodiments, the antibody or antigen-binding fragment contains variable heavy and light chain containing a CDR1, a CDR2 and/or a CDR3 contained in the alpha chain and a CDR1, a CDR2 and/or a CDR3 contained in the beta chain. In some embodiments, the antibody or antigen-binding fragment contains one or more CDRs that are at least at or about 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to CDR sequences in FIG.8. In some embodiments, the antibodies and antigen binding fragments thereof, e.g., TCR- like antibodies, specifically recognize a peptide epitope (e.g., Kras G12V mutant) in the context of an MHC molecule, such as an MHC class I. In some cases, the MHC class I molecule is an HLA-A11 molecule, e.g., HLA-A11*11:01. In some embodiments, the antibodies and antigen binding fragments thereof can specifically recognize a peptide epitope (e.g., Kras G12V mutant) in an MHC molecule independent manner. In general, antibodies (also called immunoglobulins) are made up of two classes of polypeptide chains, light chains and heavy chains. A non-limiting antibody of the present disclosure can be an intact, four immunoglobulin chain antibody comprising two heavy chains and two light chains. The heavy chain of the antibody can be of any isotype including IgM, IgG, IgE, IgA, or IgD or sub-isotype including IgG1, IgG2, IgG2a, IgG2b, IgG3, IgG4, IgE1, IgE2, etc. The light chain can be a kappa light chain or a lambda light chain. An antibody can comprise two identical copies of a light chain and two identical copies of a heavy chain. The heavy chains, which each contain one variable domain (or variable region, VH) and multiple constant domains (or constant regions), bind to one another via disulfide bonding within their constant domains to form the “stem” of the antibody. The light chains, which each contain one variable domain (or variable region, VL) and one constant domain (or constant region), each bind to one heavy chain via disulfide binding. The variable region of each light chain is aligned with the variable region of the heavy chain to which it is bound. The variable regions of both the light chains and heavy chains contain three hypervariable regions sandwiched between more conserved framework regions (FR). In some embodiments, the antibody is an intact immunoglobulin molecule (e.g., IgG1, IgG2a, IgG2b, IgG3, IgM, IgD, IgE, IgA). The IgG subclasses (IgG1, IgG2, IgG3, and IgG4) are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 Attorney Docket No.51624-0017WO1 domains. The sequences and differences of the IgG subclasses are known in the art, and are described, e.g., in Vidarsson, et al, "IgG subclasses and allotypes: from structure to effector functions." Frontiers in immunology 5 (2014); Irani, et al. "Molecular properties of human IgG subclasses and their implications for designing therapeutic monoclonal antibodies against infectious diseases." Molecular immunology 67.2 (2015): 171-182; Shakib, Farouk, ed. The human IgG subclasses: molecular analysis of structure, function and regulation. Elsevier, 2016; each of which is incorporated herein by reference in its entirety. The antibody can also be an immunoglobulin molecule that is derived from any species (e.g., human, rodent, mouse, or camelid). Antibodies disclosed herein also include, but are not limited to, polyclonal, monoclonal, monospecific, polyspecific antibodies, and chimeric antibodies that include an immunoglobulin binding domain fused to another polypeptide. The term “antigen binding domain” or “antigen binding fragment” is a portion of an antibody that retains specific binding activity of the intact antibody, i.e., any portion of an antibody that is capable of specific binding to an epitope on the intact antibody’s target molecule. It includes, e.g., Fab, Fab', F(ab')2, and variants of these fragments. Thus, in some embodiments, an antibody or an antigen binding fragment thereof can be, e.g., a scFv, a Fv, a Fd, a dAb, a bispecific antibody, a bispecific scFv, a diabody, a linear antibody, a single-chain antibody molecule, a multi-specific antibody formed from antibody fragments, and any polypeptide that includes a binding domain which is, or is homologous to, an antibody binding domain. Non-limiting examples of antigen binding domains include, e.g., the heavy chain and/or light chain CDRs of an intact antibody, the heavy and/or light chain variable regions of an intact antibody, full length heavy or light chains of an intact antibody, or an individual CDR from either the heavy chain or the light chain of an intact antibody. In some embodiments, the antigen binding fragment can form a part of a chimeric antigen receptor (CAR). In some embodiments, the chimeric antigen receptor are fusions of single-chain variable fragments (scFv) as described herein, fused to CD3-zeta transmembrane- and endodomain. In some embodiments, the chimeric antigen receptor also comprises intracellular signaling domains from various costimulatory protein receptors (e.g., CD28, 41BB, ICOS). In some embodiments, the chimeric antigen receptor comprises multiple signaling domains, e.g., CD3z-CD28-41BB or CD3z-CD28-OX40, to increase potency. Thus, in one aspect, the disclosure further provides cells (e.g., T cells) that express the chimeric antigen receptors as Attorney Docket No.51624-0017WO1 described herein. In some embodiments, the scFv comprises one heavy chain variable domain, and one light chain variable domain. In some embodiments, the scFv comprises two heavy chain variable domains, and two light chain variable domains. TCR-derived CAR The antibody or antigen-binding portion thereof can be expressed on cells as part of a recombinant receptor, such as an antigen receptor. Among the antigen receptors are functional non-TCR antigen receptors, such as chimeric antigen receptors (CARs). Generally, a CAR containing an antibody or antigen-binding fragment that exhibits TCR-like specificity directed against a peptide in the context of an MHC molecule can also be referred to as a TCR-like CAR. Thus, among the provided binding molecules, e.g., Kras G12V mutant binding molecules, are antigen receptors, such as those that include one of the provided antibodies, e.g., TCR-like antibodies. In some embodiments, the antigen receptors and other chimeric receptors specifically bind to a region or epitope of an antigen, e.g., TCR-like antibodies. Among the antigen receptors are functional non-TCR antigen receptors, such as chimeric antigen receptors (CARs). Also provided are cells expressing the CARs and uses thereof in adoptive cell therapy, such as treatment of diseases and disorders associated with Kras G12V mutation. TCR-like CARs that contain a non-TCR molecule that exhibits T cell receptor specificity, such as for a T cell epitope or peptide epitope when displayed or presented in the context of an MHC molecule. In some embodiments, a TCR-like CAR can contain an antibody or antigen- binding portion thereof, e.g., TCR-like antibody, such as described herein. In some embodiments, the antibody or antibody-binding portion thereof is reactive against specific peptide epitope in the context of an MHC molecule, wherein the antibody or antibody fragment can differentiate the specific peptide in the context of the MHC molecule from the MHC molecule alone, the specific peptide alone, and, in some cases, an irrelevant peptide in the context of an MHC molecule. In some embodiments, an antibody or antigen-binding portion thereof can exhibit a higher binding affinity than a T cell receptor. Exemplary antigen receptors, including CARs, and methods for engineering and introducing such receptors into cells, include those described, for example, in US2002/131960, US2013/287748, US2013/0149337, U.S. Patent No.6,451,995, U.S. Patent No.7,446,190, and Attorney Docket No.51624-0017WO1 U.S. Patent No.8,252,592; each of which is incorporated herein by reference in its entirety. In some embodiments, the CARs generally include an extracellular antigen (or ligand) binding domain, including e.g., an antibody or antigen-binding fragment thereof specific for a peptide, linked to one or more intracellular signaling components, in some aspects via linkers and/or transmembrane domain(s). In some embodiments, such molecules can typically mimic or approximate a signal through a natural antigen receptor, such as a TCR, and, optionally, a signal through such a receptor in combination with a co-stimulatory receptor. In some embodiments, the CAR typically includes in its extracellular portion one or more antigen binding molecules, such as one or more antigen-binding fragment, domain, or portion, or one or more antibody variable domains, and/or antibody molecules. In some embodiments, the CAR includes an antigen-binding portion or portions of an antibody molecule, such as a single- chain antibody fragment (scFv) derived from the variable heavy (VH) and variable light (VL) chains of a monoclonal antibody (mAb). In some embodiments, the CAR contains a TCR-like antibody, such as an antibody or an antigen-binding fragment (e.g., scFv) that specifically recognizes a peptide epitope presented on the cell surface in the context of an MHC molecule. In certain embodiments, the intracellular signaling domain comprises a CD28 transmembrane and signaling domain linked to a CD3 (e.g., CD3-zeta) intracellular domain. In some embodiments, the intracellular signaling domain comprises a chimeric CD28 and CD137 (4-1BB, TNFRSF9) co-stimulatory domains, linked to a CD3-zeta intracellular domain. In some embodiments, the binding molecule can also be a genetically engineered T cell receptor (TCR), killer-cell immunoglobulin-like receptor (KIR), C-type lectin receptor, leukocyte immunoglobulin-like receptor (LILR), Type 1 cytokine receptor, Type 2 cytokine receptor, tumor necrosis factor family, TGFβ receptor, chemokine receptor, or a member of immunoglobulins superfamily (IgSF). In some embodiments, the engineered cells are further modified in any number of ways, such that their therapeutic or prophylactic efficacy is increased. For example, the engineered TCR or other binding molecules expressed by the population can be conjugated either directly or indirectly through a linker to a targeting moiety. The practice of conjugating binding molecules, e.g., the CAR or TCR, to targeting moieties is known in the art, and are described e.g., in Wadhwa et al. "Receptor mediated glycotargeting." Journal of Drug Targeting 3.2 (1995): 111- 127., and U.S. Patent No.5,087,616; which are incorporated herein by reference in the entirety. Attorney Docket No.51624-0017WO1 METHOD FOR PREPARATION OF ENGINEERED CELLS The present disclosure provides a method or process for preparing, manufacturing and/or using the engineered cells for treatment of pathological diseases or conditions. The cells for introduction of the binding molecule, e.g., TCR, can be isolated from a sample, such as a biological sample, e.g., one obtained from or derived from a subject. In some embodiments, the subject from which the cell is isolated is one having the disease or condition or in need of a cell therapy or to which cell therapy will be administered. The subject in some embodiments is a human in need of a particular therapeutic intervention, such as the adoptive cell therapy for which cells are being isolated, processed, and/or engineered. Accordingly, the cells in some embodiments are primary cells, e.g., primary human cells. The samples include tissue, fluid, and other samples taken directly from the subject, as well as samples resulting from one or more processing steps, such as separation, centrifugation, genetic engineering (e.g., transduction with viral vector), washing, and/or incubation. The biological sample can be a sample obtained directly from a biological source or a sample that is processed. Biological samples include, but are not limited to, body fluids, such as blood, plasma, serum, cerebrospinal fluid, synovial fluid, urine and sweat, tissue and organ samples, including processed samples derived therefrom. In some aspects, the sample from which the cells are derived or isolated is blood or a blood-derived sample, or is derived from an apheresis or leukapheresis product. Exemplary samples include whole blood, peripheral blood mononuclear cells (PBMCs), leukocytes, bone marrow, thymus, tissue biopsy, tumor, leukemia, lymphoma, lymph node, gut associated lymphoid tissue, mucosa associated lymphoid tissue, spleen, other lymphoid tissues, liver, lung, stomach, intestine, colon, kidney, pancreas, breast, bone, prostate, cervix, testes, ovaries, tonsil, or other organ, and/or cells derived therefrom. Samples include, in the context of cell therapy, e.g., adoptive cell therapy, samples from autologous and allogeneic sources. In some embodiments, the cells are derived from cell lines, e.g., T cell lines. The cells in some embodiments are obtained from a xenogeneic source, for example, from mouse, rat, or non-human primate. In some embodiments, the blood cells collected from the subject are washed, e.g., to remove the plasma fraction and to place the cells in an appropriate buffer or media for Attorney Docket No.51624-0017WO1 subsequent processing steps. In some embodiments, the cells are washed with phosphate buffered saline (PBS). In some embodiments, the wash solution lacks calcium and/or magnesium and/or many or all divalent cations. In some aspects, a washing step is accomplished a semi- automated "flow-through" centrifuge. In some aspects, a washing step is accomplished by tangential flow filtration (TFF). In some embodiments, the cells are resuspended in a variety of biocompatible buffers after washing, such as, for example, Ca ²⁺ /Mg ²⁺ free PBS. In certain embodiments, components of a blood cell sample are removed and the cells directly resuspended in culture media. In some embodiments, the methods include density-based cell separation methods, such as the preparation of white blood cells from peripheral blood by lysing the red blood cells and centrifugation through a Percoll or Ficoll gradient. In some embodiments, the method comprises one or more steps of: e.g., isolating the T cells from a patient’s blood; transducing the population T cells with a viral vector including the nucleic acid construct encoding a genetically engineered antigen receptor; expanding the transduced cells in vitro; and/or infusing the expanded cells into the patient, where the engineered T cells will seek and destroy antigen positive tumor cells. In some embodiments, the methods involve introducing any vectors described herein into a cell in vitro or ex vivo. In some embodiments, the vector is a viral vector and the introducing is carried out by transduction. In some embodiments, the methods further involve introducing into the cell one or more agent, wherein each of the one or more agent is independently capable of inducing a genetic disruption of a T cell receptor alpha constant (TRAC) gene and/or a T cell receptor beta constant (TRBC) gene. In some embodiments, the one or more agent is an inhibitory nucleic acid (e.g., siRNA). In some embodiments, the one or more agent is a fusion protein comprising a DNA-targeting protein and a nuclease or an RNA-guided nuclease (e.g., a clustered regularly interspaced short palindromic nucleic acid (CRISPR)-associated nuclease). The transfection of T cells can be achieved by using any standard method such as calcium phosphate, electroporation, liposomal mediated transfer, microinjection, biolistic particle delivery system, or any other known methods by skilled artisan. In some embodiments, transfection of T cells is performed using the calcium phosphate method. The present disclosure provides a method to create a personalized anti-tumor immunotherapy. Genetically engineered T cells can be produced from a patient’s blood cells. These engineered T cells are then reinfused into the patient as a cellular therapy product. This Attorney Docket No.51624-0017WO1 product can be applied to any patient who has a Kras-associated cancer, including, but are not limited to non-small cell lung cancer, colorectal cancer, ovarian cancer, and pancreatic cancer. In some embodiments, the Kras-associated cancer is pancreatic carcinoma, pancreatic ductal adenocarcinoma, colorectal carcinoma, non-small cell lung carcinoma, pancreatic adenocarcinoma, malignant colorectal neoplasm, or malignant solid tumor. In some embodiments, the Kras-associated cancer is blood cancer, breast cancer, colorectal cancer, gynecological cancer, lung cancer, pancreatic cancer, prostate cancer, or skin cancer. Methods of preparing engineered cells and administering these engineered cells to a subject are known in the art, and are described e.g., in US Pat. No.10,174,098 and Draper et al. "Targeting Of HPV-16+ Epithelial Cancer Cells By Tcr Gene Engineered t Cells Directed Against e6." Clinical Cancer Research 21.19 (2015): 4431-4439, both of which are incorporated by reference in their entirety. METHODS OF TREATMENT Adoptive cell transfer (ACT) is a modality of cancer immunotherapy which has demonstrated remarkable success in treating hematologic malignancies and malignant melanoma. The methods disclosed herein can be used for various therapeutic purposes. In one aspect, the disclosure provides methods for treating a cancer in a subject, methods of reducing the rate of the increase of volume of a tumor in a subject over time, methods of reducing the risk of developing a metastasis, or methods of reducing the risk of developing an additional metastasis in a subject. In some embodiments, the treatment can halt, slow, retard, or inhibit progression of a cancer. In some embodiments, the treatment can result in the reduction of in the number, severity, and/or duration of one or more symptoms of the cancer in a subject. In one aspect, the disclosure features methods that include administering a therapeutically effective amount of engineered cells expressing TCR, antigen binding fragments thereof, and TCR-derived binding molecules to a subject in need thereof (e.g., a subject having, or identified or diagnosed as having, a cancer), e.g., an Kras-associated cancer. In some embodiments, the Kras-associated cancer is non-small cell lung cancer, colorectal cancer, ovarian cancer, and pancreatic cancer. In some embodiments, the subject has a solid tumor. In some embodiments, the subject Attorney Docket No.51624-0017WO1 has breast cancer (e.g., triple-negative breast cancer), carcinoid cancer, cervical cancer, endometrial cancer, glioma, head and neck cancer, liver cancer, lung cancer, small cell lung cancer, lymphoma, melanoma, ovarian cancer, pancreatic cancer, prostate cancer, renal cancer, colorectal cancer, gastric cancer, testicular cancer, thyroid cancer, bladder cancer, urethral cancer, or hematologic malignancy. In some embodiments, the cancer is unresectable melanoma or metastatic melanoma, non-small cell lung carcinoma (NSCLC), small cell lung cancer (SCLC), bladder cancer, or metastatic hormone-refractory prostate cancer. In some embodiments, the compositions and methods disclosed herein can be used for treatment of patients at risk for a cancer. Patients with cancer can be identified with various methods known in the art. As used herein, by an “effective amount” is meant an amount or dosage sufficient to effect beneficial or desired results including halting, slowing, retarding, or inhibiting progression of a disease, e.g., a cancer. An effective amount will vary depending upon, e.g., an age and a body weight of a subject to which the therapeutic agent and/or therapeutic compositions is to be administered, a severity of symptoms and a route of administration, and thus administration can be determined on an individual basis. As used herein, the term "delaying development of a disease" refers to defer, hinder, slow, retard, stabilize, suppress and/or postpone development of the disease (such as cancer). This delay can be of varying lengths of time, depending on the history of the disease and/or individual being treated. As is evident to one skilled in the art, a sufficient or significant delay can, in effect, encompass prevention, in that the individual does not develop the disease. For example, a late stage cancer, such as development of metastasis, can be delayed. An effective amount can be administered in one or more administrations. By way of example, an effective amount of a composition is an amount sufficient to ameliorate, stop, stabilize, reverse, inhibit, slow and/or delay progression of a cancer in a patient or is an amount sufficient to ameliorate, stop, stabilize, reverse, slow and/or delay proliferation of a cell (e.g., a biopsied cell, any of the cancer cells described herein, or cell line (e.g., a cancer cell line)) in vitro. As is understood in the art, an effective may vary, depending on, inter alia, patient history as well as other factors such as the type (and/or dosage) of compositions used. Effective amounts and schedules for administrations may be determined empirically, and making such determinations is within the skill in the art. Those skilled in the art will understand Attorney Docket No.51624-0017WO1 that the dosage that must be administered will vary depending on, for example, the mammal that will receive the treatment, the route of administration, the particular type of therapeutic agents and other drugs being administered to the mammal. Guidance in selecting appropriate doses can be found in the literature. In addition, a treatment does not necessarily result in the 100% or complete treatment or prevention of a disease or a condition. There are multiple treatment/prevention methods available with a varying degree of therapeutic effect which one of ordinary skill in the art recognizes as a potentially advantageous therapeutic mean. In some aspects, the present disclosure also provides methods of diagnosing a disease/condition in a mammal, wherein the TCRs, antigen binding fragments, TCR-derived binding molecules interact with the sample(s) obtained from a subject to form a complex, wherein the sample can comprise one more cells, polypeptides, proteins, nucleic acids, antibodies, or antigen binding portions, blood, whole cells, lysates thereof, or a fraction of the whole cell lysates, e.g., a nuclear or cytoplasmic fraction, a whole protein fraction, or a nucleic acid fraction thereof, wherein the detection of the complex is the indicative of presence of a condition in the mammal, wherein the condition is cancer, e.g., those carrying the Kras G12V mutation. Further, the detection of the complex can be in any number of way known in the art but not limited to, ELISA, Flow cytometery, Fluorescence in situ hybridization (FISH), Polymerase chain reaction (PCR), microarray, southern blotting, electrophoresis, phage analysis, chromatography and more. Thus, the treatment methods described herein can further include determining whether a subject can benefit from a treatment as disclosed herein, e.g., by determining whether the subject has cancer cells carrying the Kras G12V mutation. In any of the methods described herein, the engineered cells, and/or at least one additional therapeutic agent can be administered to the subject at least once a week (e.g., once a week, twice a week, three times a week, four times a week, once a day, twice a day, or three times a day). In some embodiments, at least two different engineered cells (e.g., cells express different binding molecules) are administered in the same composition (e.g., a liquid composition). In some embodiments, engineered cells and at least one additional therapeutic agent are administered in the same composition (e.g., a liquid composition). In some embodiments, engineered cells and the at least one additional therapeutic agent are administered in two different compositions. In some embodiments, the at least one additional therapeutic agent is administered as a pill, tablet, or capsule. In some embodiments, the at least one additional Attorney Docket No.51624-0017WO1 therapeutic agent is administered in a sustained-release oral formulation. In some embodiments, the one or more additional therapeutic agents can be administered to the subject prior to, concurrently with, or after administering the engineered cells to the subject. In some embodiments, one or more additional therapeutic agents can be administered to the subject. In some embodiments, the additional therapeutic agent is an anti-OX40 antibody, an anti-PD-L1 antibody, an anti-PD-L2 antibody, an anti-LAG-3 antibody, an anti-TIGIT antibody, an anti-BTLA antibody, an anti-CTLA-4 antibody, or an anti-GITR antibody. In some embodiments, the additional therapeutic agent is an anti-CTLA4 antibody (e.g., ipilimumab), an anti-CD20 antibody (e.g., rituximab), an anti-EGFR antibody (e.g., cetuximab), an anti-CD319 antibody (e.g., elotuzumab), or an anti-PD1 antibody (e.g., nivolumab). In one some embodiments, the additional therapeutic agent can comprise one or more inhibitors selected from the group consisting of an inhibitor of B-Raf, an EGFR inhibitor, an inhibitor of a MEK, an inhibitor of ERK, an inhibitor of K-Ras, an inhibitor of c-Met, an inhibitor of anaplastic lymphoma kinase (ALK), an inhibitor of a phosphatidylinositol 3-kinase (PI3K), an inhibitor of an Akt, an inhibitor of mTOR, a dual PI3K/mTOR inhibitor, an inhibitor of Bruton's tyrosine kinase (BTK), and an inhibitor of Isocitrate dehydrogenase 1 (IDH1) and/or Isocitrate dehydrogenase 2 (IDH2). In some embodiments, the additional therapeutic agent is an inhibitor of indoleamine 2,3-dioxygenase-1) (IDO1) (e.g., epacadostat). In some embodiments, the additional therapeutic agent can comprise one or more inhibitors selected from the group consisting of an inhibitor of HER3, an inhibitor of LSD1, an inhibitor of MDM2, an inhibitor of BCL2, an inhibitor of CHK1, an inhibitor of activated hedgehog signaling pathway, and an agent that selectively degrades the estrogen receptor. In some embodiments, the additional therapeutic agent can comprise one or more therapeutic agents selected from the group consisting of Trabectedin, nab-paclitaxel, Trebananib, Pazopanib, Cediranib, Palbociclib, everolimus, fluoropyrimidine, IFL, regorafenib, Reolysin, Alimta, Zykadia, Sutent, temsirolimus, axitinib, everolimus, sorafenib, Votrient, Pazopanib, IMA- 901, AGS-003, cabozantinib, Vinflunine, an Hsp90 inhibitor, Ad-GM-CSF, Temazolomide, IL-2, IFNa, vinblastine, Thalomid, dacarbazine, cyclophosphamide, lenalidomide, azacytidine, lenalidomide, bortezomid, amrubicine, carfilzomib, pralatrexate, and enzastaurin. In some embodiments, the additional therapeutic agent can comprise one or more therapeutic agents selected from the group consisting of an adjuvant, a TLR agonist, tumor necrosis Attorney Docket No.51624-0017WO1 factor (TNF) alpha, IL-1, HMGB1, an IL-10 antagonist, an IL-4 antagonist, an IL-13 antagonist, an IL-17 antagonist, an HVEM antagonist, an ICOS agonist, a treatment targeting CX3CL1, a treatment targeting CXCL9, a treatment targeting CXCL10, a treatment targeting CCL5, an LFA- 1 agonist, an ICAM1 agonist, and a Selectin agonist. In some embodiments, carboplatin, nab-paclitaxel, paclitaxel, cisplatin, pemetrexed, gemcitabine, FOLFOX, and/or FOLFIRI are administered to the subject. In some embodiments, the additional therapeutic agent is selected from asparaginase, busulfan, carboplatin, cisplatin, daunorubicin, doxorubicin, fluorouracil, gemcitabine, hydroxyurea, methotrexate, paclitaxel, rituximab, vinblastine, vincristine and/or combinations thereof. COMPOSITIONS AND FORMULATIONS The present disclosure provides compositions (including pharmaceutical and therapeutic compositions) containing the engineered cells and populations thereof, produced by the methods disclosed herein. Also provided are methods, e.g., therapeutic methods for administrating the engineered T cells and compositions thereof to subjects, e.g., patients. Compositions including the engineered T cells for administration, including pharmaceutical compositions and formulations, such as unit dose form compositions including the number of cells for administration in a given dose or fraction thereof are provided. The pharmaceutical compositions and formulations can include one or more optional pharmaceutically acceptable carrier or excipient. In some embodiments, the composition includes at least one additional therapeutic agent. A pharmaceutically acceptable carrier refers to an ingredient in a pharmaceutical composition, other than an active ingredient. The pharmaceutically acceptable carrier does not interfere with the active ingredient and is nontoxic to a subject. A pharmaceutically acceptable carrier can include, but is not limited to, a buffer, excipient, stabilizer, or preservative. The pharmaceutical formulation refers to process in which different substances and/or agents are combined to produce a final medicinal product. The formulation studies involve developing a preparation of drug acceptable for patient. Additionally, a preparation which is in such form as to permit the biological activity of an active ingredient contained therein to be effective, and which contains no additional components which are unacceptably toxic to a subject to which the formulation would be administered. Attorney Docket No.51624-0017WO1 In some embodiments, the choice of carrier is determined in part by the particular cell (e.g., T cell or NK cell) and/or by the method of administration. A variety of suitable formulations are available. For example, the pharmaceutical composition can contain preservatives. Suitable preservatives can include, for example, methylparaben, propylparaben, sodium benzoate, and benzalkonium chloride. In some embodiments, a mixture of two or more preservatives is used. The preservative or mixtures thereof are typically present in an amount of about 0.0001% to about 2% by weight of the total composition. Carriers are described, e.g., by Remington's Pharmaceutical Sciences 16th edition, Osol, A. Ed. (1980). Pharmaceutically acceptable carriers are generally nontoxic to recipients at the dosages and concentrations employed, and include, but are not limited to: buffers such as phosphate, citrate, and other organic acids; antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride; benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt-forming counter-ions such as sodium; metal complexes (e.g., Zn-protein complexes); and/or non-ionic surfactants such as polyethylene glycol (PEG). Suitable buffering agents include, for example, citric acid, sodium citrate, phosphoric acid, potassium phosphate, and various other acids and salts. In some embodiments, a mixture of two or more buffering agents is used. The buffering agent or mixtures thereof are typically present in an amount of about 0.001% to about 4% by weight of the total composition. Methods for preparing administrable pharmaceutical compositions are known. Exemplary methods are described in more detail in, for example, Remington: The Science and Practice of Pharmacy, Lippincott Williams & Wilkins; 21st ed. (May 1, 2005). The formulations can include aqueous solutions. The formulation or composition can also contain more than one active ingredient useful for a particular indication, disease, or condition being treated with the engineered cells, preferably those with activities complementary to the Attorney Docket No.51624-0017WO1 cells, where the respective activities do not adversely affect one another. Such active ingredients are suitably present in combination in amounts that are effective for the purpose intended. Thus, in some embodiments, the pharmaceutical composition can further include other pharmaceutically active agents or drugs, such as checkpoint inhibitors, fusion proteins, chemotherapeutic agents, e.g., asparaginase, busulfan, carboplatin, cisplatin, daunorubicin, doxorubicin, fluorouracil, gemcitabine, hydroxyurea, methotrexate, paclitaxel, rituximab, vinblastine, and/or vincristine. The pharmaceutical composition in some embodiments contains the cells in amounts effective to treat or prevent the disease or condition, such as a therapeutically effective or prophylactically effective amount. Therapeutic or prophylactic efficacy in some embodiments is monitored by periodic assessment of treated subjects. The desired dosage can be delivered by a single bolus administration of the cells, by multiple bolus administrations of the cells, or by continuous infusion administration of the cells. The cells and compositions can be administered using standard administration techniques, formulations, and/or devices. Administration of the cells can be autologous or heterologous. For example, immunoresponsive T cells or progenitors can be obtained from one subject, and administered to the same subject or a different, compatible subject after genetically modifying them in accordance with various embodiments described herein. Peripheral blood derived immunoresponsive T cells or their progeny (e.g., in vivo, ex vivo or in vitro derived) can be administered via localized injection, including catheter administration, systemic injection, localized injection, intravenous injection, or parenteral administration. Usually, when administering a therapeutic composition (e.g., a pharmaceutical composition containing a genetically modified immunoresponsive cell), it is generally formulated in a unit dosage injectable form (solution, suspension, emulsion). Formulations disclosed herein include those for oral, intravenous, intraperitoneal, subcutaneous, pulmonary, transdermal, intramuscular, intranasal, buccal, sublingual, or suppository administration. In some embodiments, the cell populations are administered parenterally. The term “parenteral,” as used herein, includes intravenous, intramuscular, subcutaneous, rectal, vaginal, and intraperitoneal administration. In some embodiments, the cells are administered to the subject using peripheral systemic delivery by intravenous, intraperitoneal, or subcutaneous injection. Attorney Docket No.51624-0017WO1 The compositions in some embodiments are provided as sterile liquid preparations, e.g., isotonic aqueous solutions, suspensions, emulsions, dispersions, or viscous compositions, which can in some aspects be buffered to a selected pH. Liquid preparations are normally easier to prepare than gels, other viscous compositions, and solid compositions. Additionally, liquid compositions are somewhat more convenient to administer, especially by injection. Viscous compositions, on the other hand, can be formulated within the appropriate viscosity range to provide longer contact periods with specific tissues. Liquid or viscous compositions can comprise carriers, which can be a solvent or dispersing medium containing, for example, water, saline, phosphate buffered saline, polyol (for example, glycerol, propylene glycol, liquid polyethylene glycol) and suitable mixtures thereof. Sterile injectable solutions can be prepared by incorporating the cells in a solvent, such as in admixture with a suitable carrier, diluent, or excipient such as sterile water, physiological saline, glucose, dextrose, or the like. The compositions can contain auxiliary substances such as wetting, dispersing, or emulsifying agents (e.g., methylcellulose), pH buffering agents, gelling or viscosity enhancing additives, preservatives, flavoring agents, and/or colors, depending upon the route of administration and the preparation desired. Standard texts can in some aspects be consulted to prepare suitable preparations. Various additives which enhance the stability and sterility of the compositions, including antimicrobial preservatives, antioxidants, chelating agents, and buffers, can be added. Prevention of the action of microorganisms can be ensured by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, and sorbic acid. Prolonged absorption of the injectable pharmaceutical form can be brought about by the use of agents delaying absorption, for example, aluminum monostearate and gelatin. The formulations to be used for in vivo administration are generally sterile. Sterility can be readily accomplished, e.g., by filtration through sterile filtration membranes. The compositions or pharmaceutical compositions as described herein can be included in a container, pack, or dispenser together with instructions for administration. METHODS OF ADMINISTRATION Provided are also methods of administering the cells, populations, and compositions, and uses of such cells, populations, and compositions to treat or prevent diseases, conditions, and Attorney Docket No.51624-0017WO1 disorders, including cancers. In some embodiments, the methods described herein can reduce the risk of the developing diseases, conditions, and disorders as described herein. In some embodiments, the cells, populations, and compositions, described herein are administered to a subject or patient having a particular disease or condition to be treated, e.g., via adoptive cell therapy, such as adoptive T cell therapy. In some embodiments, cells and compositions prepared by the provided methods, such as engineered compositions and end-of- production compositions following incubation and/or other processing steps, are administered to a subject, such as a subject having or at risk for the disease or condition. In some aspects, the methods thereby treat, e.g., ameliorate one or more symptom of, the disease or condition, such as by lessening tumor burden in cancer expressing an antigen recognized by the engineered T cells. Methods for administration of cells for adoptive cell therapy are known and can be used in connection with the provided methods and compositions. For example, adoptive T cell therapy methods are described, e.g., in U.S.2003/0170238; U.S. Pat. No.4,690,915; Rosenberg, "Cell transfer immunotherapy for metastatic solid cancer—what clinicians need to know." Nature reviews Clinical oncology 8.10 (2011): 577; Themeli et al. "Generation of tumor-targeted human T lymphocytes from induced pluripotent stem cells for cancer therapy." Nature biotechnology 31.10 (2013): 928; Tsukahara et al. "CD19 target-engineered T-cells accumulate at tumor lesions in human B-cell lymphoma xenograft mouse models." Biochemical and biophysical research communications 438.1 (2013): 84-89; Davila et al. "CD19 CAR-targeted T cells induce long- term remission and B Cell Aplasia in an immunocompetent mouse model of B cell acute lymphoblastic leukemia." PloS One 8.4 (2013); each of which is incorporated herein by reference in its entirety. In some embodiments, the cell therapy, e.g., adoptive T cell therapy, is carried out by autologous transfer, in which the T cells are isolated and/or otherwise prepared from the subject who is to receive the cell therapy, or from a sample derived from such a subject. Thus, in some aspects, the cells are derived from a subject, e.g., patient, in need of a treatment and the cells, following isolation and processing are administered to the same subject. In some embodiments, the cell therapy, e.g., adoptive T cell therapy, is carried out by allogeneic transfer, in which the T cells are isolated and/or otherwise prepared from a subject other than a subject who is to receive or who ultimately receives the cell therapy, e.g., a first subject. In such embodiments, the cells then are administered to a different subject, e.g., a second Attorney Docket No.51624-0017WO1 subject, of the same species. In some embodiments, the first and second subjects are genetically identical. In some embodiments, the first and second subjects are genetically similar. In some embodiments, the second subject expresses the same HLA class or supertype as the first subject. In some embodiments, the subject has been treated with a therapeutic agent targeting the disease or condition, e.g., the tumor, prior to administration of the cells or composition containing the cells. In some aspects, the subject is refractory or non-responsive to the other therapeutic agent. In some embodiments, the subject has persistent or relapsed disease, e.g., following treatment with another therapeutic intervention, including chemotherapy, radiation, and/or hematopoietic stem cell transplantation (HSCT), e.g., allogenic HSCT. In some embodiments, the administration effectively treats the subject despite the subject having become resistant to another therapy. In some embodiments, the subject is responsive to the other therapeutic agent, and treatment with the therapeutic agent reduces disease burden. In some aspects, the subject is initially responsive to the therapeutic agent, but exhibits a relapse of the disease or condition over time. In some embodiments, the subject has not relapsed. In some such embodiments, the subject is determined to be at risk for relapse, such as at high risk of relapse, and thus the cells are administered prophylactically, e.g., to reduce the likelihood of or prevent relapse. In some embodiments, the subject has not received prior treatment with another therapeutic agent. In some embodiments, the cells are administered at a desired dosage, which in some aspects includes a desired dose or number of cells or cell type(s) and/or a desired ratio of cell types. Thus, the dosage of cells in some embodiments is based on a total number of cells (or number per kg body weight) and a desired ratio of the individual populations or sub-types, such as the CD4+ T cell to CD8+ T cell ratio. In some embodiments, the dosage of cells is based on a desired total number (or number per kg of body weight) of cells in the individual populations or of individual cell types. In some embodiments, the dosage is based on a combination of such features, such as a desired number of total cells, desired ratio, and desired total number of cells in the individual populations. In some embodiments, the populations or sub-types of cells, such as CD8+ T cells and CD4+ T cells, are administered at or within a tolerated difference of a desired dose of total cells, such as a desired dose of T cells. In some embodiments, the desired dose is a desired number of cells or a desired number of cells per unit of body weight of the subject to whom the Attorney Docket No.51624-0017WO1 cells are administered, e.g., cells/kg. In some embodiments, the desired dose is at or above a minimum number of cells or minimum number of cells per unit of body weight. In some embodiments, among the total cells, administered at the desired dose, the individual populations or subtypes are present at or near a desired output ratio (such as CD4+ T cell to CD8+ T cell ratio), e.g., within a certain tolerated difference or error of such a ratio. In some embodiments, the cells are administered at or within a tolerated difference of a desired dose of one or more of the individual populations or sub-types of cells, such as a desired dose of CD4+ T cells and/or a desired dose of CD8+ T cells. In some embodiments, the desired dose is a desired number of cells of the sub-type or population, or a desired number of such cells per unit of body weight of the subject to whom the cells are administered, e.g., cells/kg. In some embodiments, the desired dose is at or above a minimum number of cells of the population or subtype, or minimum number of cells of the population or subtype per unit of body weight. Thus, in some embodiments, the dosage is based on a desired fixed dose of total cells and a desired ratio, and/or based on a desired fixed dose of one or more, e.g., each, of the individual sub-types or sub-populations. Thus, in some embodiments, the dosage is based on a desired fixed or minimum dose of T cells and a desired ratio of CD4+ T cells to CD8+ T cells, and/or is based on a desired fixed or minimum dose of CD4+ T cells and/or CD8+ T cells. In certain embodiments, the cells or individual populations of sub-types of cells, are administered to the subject at a range of about one million to about 100 billion cells, such as, e.g., 1 million to about 50 billion cells (e.g., about 5 million cells, about 25 million cells, about 500 million cells, about 1 billion cells, about 5 billion cells, about 20 billion cells, about 30 billion cells, about 40 billion cells, or a range defined by any two of the foregoing values), such as about 10 million to about 100 billion cells (e.g., about 20 million cells, about 30 million cells, about 40 million cells, about 60 million cells, about 70 million cells, about 80 million cells, about 90 million cells, about 10 billion cells, about 25 billion cells, about 50 billion cells, about 75 billion cells, about 90 billion cells, or a range defined by any two of the foregoing values), and in some cases about 100 million cells to about 50 billion cells (e.g., about 120 million cells, about 250 million cells, about 350 million cells, about 450 million cells, about 650 million cells, about 800 million cells, about 900 million cells, about 3 billion cells, about 30 billion cells, about 45 billion cells) or any value in between these ranges. In some embodiments, the dose of total cells and/or dose of individual sub-populations Attorney Docket No.51624-0017WO1 of cells is within a range of between at or about 10 ⁴ and at or about 10 ⁹ cells/kilograms (kg) body weight, such as between 10 ⁵ and 10 ⁶ cells/kg body weight, for example, at least or at least about or at or about 1×10 ⁵ cells/kg, 1.5×10 ⁵ cells/kg, 2×10 ⁵ cells/kg, or 1×10 ⁶ cells/kg body weight. For example, in some embodiments, the cells are administered at, or within a certain range of error of, between at or about 10 ⁴ and at or about 10 ⁹ T cells/kilograms (kg) body weight, such as between 10 ⁵ and 10 ⁶ T cells/kg body weight, for example, at least or at least about or at or about 1×10 ⁵ T cells/kg, 1.5×10 ⁵ T cells/kg, 2×10 ⁵ T cells/kg, or 1×10 ⁶ T cells/kg body weight. In some embodiments, the cells are administered at or within a certain range of error _{of between at or about 10} ⁴ _{and at or about 10} ⁹ _{CD4+ T cells and/or CD8+ T cells/kilograms (kg) body weight, such as between 10} ⁵ _{and 10} ⁶ _{CD4+ T cells and/or CD8+ T cells/kg body weight, for example, at least or at least about or at or about 1×10} ⁵ _{CD4+ T cells and/or CD8+ T cells/kg, 1.5×10} ⁵ _{CD4+ T cells and/or CD8+ T cells/kg, 2×10} ⁵ _{CD4+ T cells and/or CD8+ T cells/kg, or 1×10} ⁶ _{CD4+ T cells and/or CD8+ T cells/kg body weight.} In some embodiments, the cells are administered at or within a certain range of error of, greater than, and/or at least about 1×10 ⁶ , about 2.5×10 ⁶ , about 5×10 ⁶ , about 7.5×10 ⁶ , or about _9×10 ⁶ _{CD4+ T cells, and/or at least about 1×10} ⁶ _{, about 2.5×10} ⁶ _{, about 5×10} ⁶ _{, about 7.5×10} ⁶ _{, or about 9×10} ⁶ _{CD8+ T cells, and/or at least about 1×10} ⁶ _{, about 2.5×10} ⁶ _{, about 5×10} ⁶ _{, about 7.5×10} ⁶ _{, or about 9×10} ⁶ _{T cells. In some embodiments, the cells are administered at or within a certain range of error of between about 10} ⁸ _{and 10} ¹² _{or between about 10} ¹⁰ _{and 10} ¹¹ _{T cells, between about 10} ⁸ _{and 10} ¹² _{or between about 10} ¹⁰ _{and 10} ¹¹ _{CD4+ T cells, and/or between about 10} ⁸ _{and 10} ¹² _{or between about 10} ¹⁰ _{and 10} ¹¹ _{CD8+ T cells.} In some embodiments, the cells are administered at or within a tolerated range of a desired output ratio of multiple cell populations or sub-types, such as CD4+ T cells and CD8+ T cells or subtypes. In some aspects, the desired ratio can be a specific ratio or can be a range of ratios. for example, in some embodiments, the desired ratio (e.g., ratio of CD4+ T cells to CD8+ T cells) is between at or about 1:5 and at or about 5:1 (or greater than about 1:5 and less than about 5:1), or between at or about 1:3 and at or about 3:1 (or greater than about 1:3 and less than about 3:1), such as between at or about 2:1 and at or about 1:5 (or greater than about 1:5 and less than about 2:1, such as at or about 5:1, 4.5:1, 4:1, 3.5:1, 3:1, 2.5:1, 2:1, 1.9:1, 1.8:1, 1.7:1, 1.6:1, 1.5:1, 1.4:1, 1.3:1, 1.2:1, 1.1:1, 1:1, 1:1.1, 1:1.2, 1:1.3, 1:1.4, 1:1.5, 1:1.6, 1:1.7, 1:1.8, 1:1.9: 1:2, 1:2.5, 1:3, 1:3.5, 1:4, 1:4.5, or 1:5. In some aspects, the tolerated difference is within about 1%, Attorney Docket No.51624-0017WO1 about 2%, about 3%, about 4% about 5%, about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50% of the desired ratio, including any value in between these ranges. In some aspects, the TCR described here provides improved expression and activity, thereby providing therapeutic effects even at a low effector to target (E:T) ratio. Optimal response to therapy can depend on the ability of the engineered recombinant receptors such as TCRs, to be consistently and reliably expressed on the surface of the cells and/or bind the target antigen. For example, in some cases, properties of certain recombinant receptors, e.g., TCRs, can affect the expression and/or activity of the recombinant receptor, in some cases when expressed in a cell, such as a human T cell, used in cell therapy. In some contexts, the level of expression of particular recombinant receptors, e.g., TCRs, can be low, and activity of the engineered cells, such as human T cells, expressing such recombinant receptors, may be limited due to poor expression or poor signaling activity. In some cases, consistency and/or efficiency of expression of the recombinant receptor, and activity of the receptor is limited in certain cells or certain cell populations of available therapeutic approaches. In some cases, a large number of engineered T cells (a high effector to target (E:T) ratio) is required to exhibit functional activity. In some embodiments, the desired ratio (E:T ratio) is between at or about 1:20 and at or about 20:1 (or greater than about 1:20 and less than about 20:1), or between at or about 1:1 and at or about 10:1 (or greater than about 1:1 and less than about 10:1), such as between at or about 2:1 and at or about 5:1. In some embodiments, the E:T ratio is greater than or about 1:1, 2:1, 3:1, 4:1, 5:1, 6:1, 7:1, 8:1, 9:1, or 10:1. In some embodiments, the E:T ratio described herein is about 1:5, 1:10, or 1:20, when CD8+ TCR-T cells are co-cultured with target cells. In some embodiments, the E:T ratio described herein is about 2:1, 1:1, or 1:2, when CD4+ TCR-T cells are co-cultured with target cells. For the prevention or treatment of disease, the appropriate dosage may depend on the type of disease to be treated, the type of cells or recombinant receptors, the severity and course of the disease, whether the cells are administered for preventive or therapeutic purposes, previous therapy, the subject's clinical history and response to the cells, and the discretion of the attending physician. The compositions and cells are in some embodiments suitably administered to the subject at one time or over a series of treatments. The cells described herein can be administered by any suitable means, for example, by bolus infusion, by injection, e.g., intravenous or subcutaneous injections, intraocular injection, Attorney Docket No.51624-0017WO1 periocular injection, subretinal injection, intravitreal injection, trans-septal injection, subscleral injection, intrachoroidal injection, intracameral injection, subconjectval injection, subconjuntival injection, sub-Tenon's injection, retrobulbar injection, peribulbar injection, or posterior juxtascleral delivery. In some embodiments, they are administered by parenteral, intrapulmonary, and intranasal, and, if desired for local treatment, intralesional administration. Parenteral infusions include intramuscular, intravenous, intraarterial, intraperitoneal, or subcutaneous administration. In some embodiments, a given dose is administered by a single bolus administration of the cells. In some embodiments, it is administered by multiple bolus administrations of the cells, for example, over a period of no more than 3 days, or by continuous infusion administration of the cells. In some embodiments, the cells are administered as part of a combination treatment, such as simultaneously with or sequentially with, in any order, another therapeutic intervention, such as an antibody or engineered cell or receptor or agent, such as a cytotoxic or therapeutic agent. The cells in some embodiments are co-administered with one or more additional therapeutic agents or in connection with another therapeutic intervention, either simultaneously or sequentially in any order. In some contexts, the cells are co- administered with another therapy sufficiently close in time such that the cell populations enhance the effect of one or more additional therapeutic agents, or vice versa. In some embodiments, the cells are administered prior to the one or more additional therapeutic agents. In some embodiments, the cells are administered after the one or more additional therapeutic agents. In some embodiments, the one or more additional agents includes a cytokine, such as IL-2, for example, to enhance persistence. In some embodiments, the methods comprise administration of a chemotherapeutic agent. Repeated dosing methods are provided in which a first dose of cells is given followed by one or more second consecutive doses. In some embodiments, multiple doses can be administered to a subject over an extended period of time (e.g., over a period of at least 1 week, 2 weeks, 3 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, 1 year, 2 years, 3 years, 4 years, or 5 years). A skilled medical professional may determine the length of the treatment period using any of the methods described herein for diagnosing or following the effectiveness of treatment (e.g., the observation of at least one symptom of cancer). Following administration of the cells, the biological activity of the engineered cell Attorney Docket No.51624-0017WO1 populations in some embodiments is measured, e.g., by any of a number of known methods. Parameters to assess include specific binding of engineered T cells to the antigen, in vivo, e.g., by imaging, or ex vivo, e.g., by ELISA or flow cytometry. In certain embodiments, the ability of the engineered cells to destroy target cells can be measured using any suitable method known in the art, such as cytotoxicity assays described in, for example, Kochenderfer et al. "Construction and pre-clinical evaluation of an anti-CD19 chimeric antigen receptor." Journal of Immunotherapy (Hagerstown, Md.: 1997) 32.7 (2009): 689 and Hermans et al. "The VITAL assay: a versatile fluorometric technique for assessing CTL-and NKT-mediated cytotoxicity against multiple targets in vitro and in vivo." Journal of Immunological Methods 285.1 (2004): 25-40. In certain embodiments, the biological activity of the cells is measured by assaying expression and/or secretion of one or more cytokines, such as CD107a, IFNγ, IL-2, and TNFα. In some aspects the biological activity is measured by assessing clinical outcome, such as reduction in tumor burden or load. EXAMPLES The disclosure is further described in the following examples, which do not limit the scope of the disclosure described in the claims. EXAMPLE 1:^Transduction of T cells with lentivirus to prepare TCR-T cells In order to obtain Kras-specific TCRs with a high affinity to HLA-A*11:01-Kras G12V complex, transgenic mice expressing HLA-A*11:01 were immunized with Kras G12V mutant peptides (VVGAVGVGK (SEQ ID NO: 1) and VVVGAVGVGK (SEQ ID NO: 2)) in the presence of immune adjuvants. Mouse spleens and lymph nodes were harvested after immunization. Lymphocytes from the spleens and lymph nodes were stimulated with 1 µM each of the Kras G12V peptides for 7 days in the presence of 100 IU/mL human recombinant IL-2. At the end of the culture, cells were stained with HLA-A*11:01-Kras G12V tetramer (MBL, Cat.#: TBCM3-A111I-1), an anti-human CD3 antibody (BioLegend, Cat.#: 344828), and an anti-CD8 antibody (BioLegend Cat.#: 344718). The triple positive cells for CD3, CD8 and the HLA- A*11:01-Kras G12V tetramer were sorted out and the TCR sequences of TCR α chain and β chain were obtained by single cell sequencing. Attorney Docket No.51624-0017WO1 Paired TCR α chain and β chain cDNA sequences were inserted into a third generation lentiviral vector, in which sequences encoding the TCR α chain and β chain were separated with a self-cleavage P2A sequence. Human T cells from healthy donors (HLA-A*11:01 negative; ratio of CD4 ⁺ to CD8 ⁺ cells of about 1:1) were activated by CD3/CD28 Dynabeads ^® (ThermoFisher, Cat.#: 40203D) at a ratio of 1 cell to 3 beads. Lentivirus transduction of T cells was performed 20 hours after the activation with a multiplicity of infection of 5. Transduced and untransduced control T cells were cultured for 10 days in the presence of 100 IU/mL human IL-2 (PeproTech, Cat.# 200-02-1MG). The transduction efficacy was determined by flow cytometry after staining the cells with an antibody specific for mouse TCR β chain constant region (Clone H57-597; or anti-mTCR antibody) and HLA-A*11:1-Kras G12V tetramer (9mer and 10mer peptide, respectively). As shown in FIG.1, T cells transduced with lentivirus encoding Kras G12V specific TCR 9mV11, 9mV15, or 10mV11 showed high transduction efficacy. For example, over 70% of the transduced T cells were stained by both of the anti-mTCR antibody and HLA-A*11:01-Kras G12V tetramer. EXAMPLE 2:^CD137 expression and IFN-γ production in TCR-T cells co-cultured with SW480 cells expressing Kras G12V mutation For functional screening of TCR-T cells, human colorectal cancer cells SW480 carrying Kras G12V mutation were engineered to stably express human HLA-A*11:01 molecules (SW480-HLA-A*11:01 cells) and these cell lines were used as target cells of the TCR-T cells. To test the anti-tumor function of TCR-T cells, 1 × 10 ⁵ T cells and 1 × 10 ⁵ tumor cells were co- cultured in wells of a 96-well U bottom plate overnight. As shown in FIG.2, the expression of T cell surface marker CD137 (4-1BB) was measured by flow cytometry. Specifically, TCR-T cells were co-cultured with SW480 parental cells (HLA-A*11:01 negative) or SW480-HLA-A*11:01 cells overnight. The expression of CD137 on T cells was determined by flow cytometry after staining the cells with an anti-human CD8 antibody (Biolegend, Cat.# 300928), an anti-mouse TCR-V ^ constant region antibody (Biolegend, Cat.# 109208) , and an anti-human CD137 antibody (BD, Cat.# 564091). The results show that CD137 was upregulated in transduced T cells. Untransduced (UTD) T cells were used as negative control cells. Attorney Docket No.51624-0017WO1 As shown in FIG.3, the secretion of soluble cytokine IFN-γ in the supernatant was measured by ELISA (Biolegend, Cat.# 430116). Specifically, TCR-T cells were cocultured with SW480 parental cells (HLA-A*11:01 negative) or SW480-HLA-A*11:01 cells overnight. The production of IFN- ^ by T cells was determined by ELISA. The results show that IFN-γ production was detected only when the TCR-T cells were co-cultured with SW480-HLA- A*11:01 cells, but not SW480 parental cells. The above results indicate that the TCR-T cells expressing 9mV11, 9mV15, and 10mV11 TCRs can be specifically activated when co-cultured with tumor cells carrying Kras G12V mutation and expressing HLA-A*11:01 molecules. EXAMPLE 3:^Intracellular cytokine staining of TCR-T cells after co-culture with SW480- HLA*11:01 cells CD4+ T cells engineered to express a TCR recognizing a complex of peptide-HLA-I molecule usually do not respond or respond weakly to antigens, comparing to their CD8+ counterparts, due to the lack of CD8 coreceptor expression on CD4+ cells. However, when TCR’s affinity is high enough, CD4+ TCR-T cells can respond well to antigens even in the absence of CD8 coreceptor. To screen the TCR candidates and identify the TCR candidates with a higher affinity to HLA-A*11:01-Kras G12V complex, TCR-T cells were cocultured with SW480 cells for 5 hours and intracellular cytokine staining was performed to determine the production of cytokines (IL-2 antibody: BD, Cat.# 563467; IFN- ^: BD, Cat.# 557643; TNF- ^, BD, Cat.# 566369). Results in FIGS.4B-4D show that CD8+ TCR-T cells, when transduced to express the selected TCR candidates in FIG.4A, produced comparable levels of TNF-α, IFN-γ, and IL-2. However, CD4+ TCR-T cells produced cytokines only when transduced to express TCR candidate 9mV11, 9mV15, or 10mV11. The results indicate that TCR candidate 9mV11, 9mV15, and 10mV11 have a relatively high affinity to the HLA-A*11:01-Kras G12V complex. EXAMPLE 4:^Cytolytic assays of TCR-T cells against SW480-HLA*A11:01 cells The anti-tumor function of those TCR-T cells was also tested for their in vitro cytotoxicity with the xCELLigence real-time cell analysis instruments (Agilent), in which TCR- T cells and SW480-HLA-A*11:01 cells were continuously co-cultured at different ratios for Attorney Docket No.51624-0017WO1 three days. The cytolytic assay results are shown in FIGS.5A-5F. When CD4+ T cells were used (FIGS.5D-5F), only those transduced to express TCR candidate 9mV11, 9mV15, or 10mV11 exhibited inhibitive tumor growth. The results indicate that TCR candidate 9mV11, 9mV15, and 10mV11 have a stronger affinity to the HLA-A*11:01-Kras G12V complex than other tested TCR candidates. EXAMPLE 5:^IFN-γ secretion by TCR-T cells stimulated with diluted peptides (ELISA) TCR candidates 9mV11, 9mV15, and 10mV11 were further characterized for their potential applications for cancer therapy. Because sequences of the TCR candidates were obtained from mice, these TCRs may cross-react with human peptides from normal tissues expressing HLA-A*11:01 or other HLA-I molecules. To test this possibility, several strategies were used. The first study was to test if these TCR candidates can respond to stimulations from peptides having similar amino acid sequences with the Kras G12V peptides that can be presented by HLA-A*11:01 molecules. The online tool Expitope 2.0 (Technical University Munich) was used to define peptides and NetMHCpan 4.1 (DTU Health Tech) was used to predict the HLA- A*11:01 presentation (cutoff is Ranking of 2).67 peptides (9 amino acids in length) with up to 3 amino acids mismatch relative to Kras peptide of VVGAVGVGK (SEQ ID NO: 1); and 95 peptides (10 amino acids in length) with up to 4 amino acids mismatch relative to Kras peptide of VVVGAVGVGK (SEQ ID NO: 2) were defined. IFN-γ ELISPOT test was used to test the potential cross-reaction of TCR to these peptides. Each of these peptides were directly added into cocultures of TCR-T cells and T2 cells transduced to express HLA-A*11:01 molecules. Specifically, peptides selected based on ELISPOT screening results were loaded onto T2-HLA-A*11:01 cells with different concentrations. Such T2 cells were then co-cultured with TCR-T cells of 9mV11, 9mV15 and 10mV11 for 24 hours. IFN- ^ secretion was measured with ELISA. The Kras G12V 9mer peptide (VVGAVGVGK; SEQ ID NO: 1) and 10mer peptide (VVVGAVGVGK; SEQ ID NO: 2) were used as positive controls; and Kras wild-type peptide (G12) (VVGAGGVGK; SEQ ID NO: 3) was used as a negative control. The ELISPOT test results show that TCR clones 9mV11 and 9mV15 responded to 9mer Kras peptide (VVGAVGVGK; SEQ ID NO: 1) but not to 10mer peptide (VVVGAVGVGK; SEQ ID NO: 2) stimulation; and TCR clone 10mV11 responded to Attorney Docket No.51624-0017WO1 10mer but not to 9mer Kras G12V peptide stimulation. When stimulated with a high concentration of peptides (e.g., a final concentration of 1 µM), T cells transduced to express each of the 3 TCR candidates (9mV11, 9mV15, and 10mV11) responded to a few peptides (See FIG. 6D) besides the positive control peptide, indicating potential cross-reaction to proteins containing these peptides. As at physiological conditions, the intracellular concentration of these peptides is unlikely to reach 1 μM. Nevertheless, these response-positive peptides were selected for further analysis. Specifically, TCR-T cells were stimulated with diluted concentrations of these peptides and the T cell response was determined by measuring IFN-γ secretion using ELISA. Results in FIGS.6A-6D show that T cells transduced to express TCR clone 9mV11 or 10mV11 lost their response to all selected peptides (except the positive control peptides), when peptide concentration was diluted to 1 nM; and T cells transduced to express TCR clone 9mV15 lost their response to all selected peptides except the positive control peptide and peptide 385 (IVGAIGVGK (SEQ ID NO: 4), originated from protein RAB7B), when peptide concentration were diluted to 1 nM. As the peptide pool generated in this experiment was based on the artificial algorism of Expitope 2.0, the peptide IVGAIGVGK (SEQ ID NO: 4) may not be produced or produced at a very low concentration at physiology conditions. This can be further verified by engineering HLA-A*11:01 positive cells to overexpress protein RAB7B and coculturing such cells with 9mV15 TCR-T cells. EXAMPLE 6:^IFN- ^ secretion by TCR-T cells cocultured with primary cells engineered to express HLA-A*11:01 As the peptide pool was artificially generated, it may not include all physiologically generated peptides that can be presented by HLA-A*11:01 to stimulate TCR-T cells of 9mV11, 9mV15 and 10mV11. To further test the potential cross-reaction of the 3 TCR candidates to normal human proteins, TCR-T cells were cocultured with a panel of primary cells isolated from different vital organs or tissues from healthy donors. These primary cells were engineered to transiently express HLA-A*11:01 by mRNA electroporation. Twenty hours after electroporation, the expression of HLA-A*11:01 was determined by flow cytometry. A coculture system including 1 × 10 ⁵ TCR-T cells and 1 × 10 ⁵ HLA-A*11:01 mRNA electroporated primary cells was prepared. A coculture system including TCR-T cells and SW480-HLA-A*11:01 cells was used as a positive control. To verify the antigen-presenting function of transiently expressed Attorney Docket No.51624-0017WO1 HLA-A*11:01 molecules on primary cells, Kras G12V 9mer (for TCR 9mV11 and 9mV15) or 10mer (for TCR 10mV11) peptide was directly added to some coculture wells. The supernatant of 24-hour coculture was harvested and the secretion of IFN-γ in the supernatant was determined by ELISA. Results in FIG.7 show that TCR-T cells produced a large amount of IFN-γ when cocultured with SW480 cells (carrying Kras G12V mutation) and with primary cells in the presence of Kras G12V peptide, but only produced minimal IFN-γ when cocultured with primary cells alone. All these results demonstrate that the TCR candidates 9mV11, 9mV15, and 10mV11 do not cross-react with the selected primary cells. In summary, 3 TCRs specific for human Kras G12V-HLA*A11:01 were identified (9mV11, 9mV15, and 10mV11). These TCRs did not cross react with other human protein peptides originated from normal tissues. In addition, T cells transduced to express the three TCR inhibited tumor growth in vitro, indicating that these TCRs can be used to develop TCR-T cell based therapy for cancers expressing HLA-A*11:01 and Kras G12V mutant. OTHER EMBODIMENTS It is to be understood that while the disclosure has been described in conjunction with the detailed description thereof, the foregoing description is intended to illustrate and not limit the scope of the invention, which is defined by the scope of the appended claims. Other aspects, advantages, and modifications are within the scope of the following claims.