Methods and compositions related to antibody drug conjugates (ADCS) that bind steap-1 proteins

Abstract

Antibody drug conjugates (ADCs) that bind to STEAP-1 protein(s) and variants thereof are described herein. STEAP-1 exhibits tissue specific expression in normal adult tissue, and is aberrantly expressed in the cancers listed in Table I. Consequently, the ADCs of the invention provide a therapeutic composition for the treatment of cancer.

Description

[0001] Methods and Compositions Related to Antibody Drug Conjugates (ADCs) That Bind STEAP-1 Proteins CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to International Patent Application number PCT / CN2024 / 099593 filed 17-Jun-2024, and United States Provisional Patent Application number 63 / 791,953 filed 21-April- 2025, the contents of which are fully incorporated by reference herein. SUBMISSION OF SEQUENCE LISTING XML FILE (“SEQUENCE LISTING XML”) The content(s) of the following submissions are fully incorporated by reference herein in their entirety: the content of a computer readable form (CRF) of the Sequence Listing entitled SEQ LIST XML (file name: 9300-20002.40 – SEQ LIST XML – 16-Jun-2025.xml), date recorded June 14, 2025 (file size 26.7 KB). STATEMENT OF RIGHTS TO INVENTIONS MADE UNDER FEDERALLY SPONSORED RESEARCH Not applicable. FIELD OF THE INVENTION The invention described herein relates to antibodies, antigen-binding fragments, and antibody drug conjugates (ADCs) thereof that bind STEAP-1 proteins. The invention further relates to the prognostic, prophylactic, and therapeutic methods, and compositions useful in the treatment of cancers and other immunological and neurological disorders. BACKGROUND OF THE INVENTION Cancer is the second leading cause of death next to coronary disease worldwide. Although cancer therapy has improved over the past decades and survival rates have increased, the heterogeneity of cancer still demands new therapeutic strategies utilizing a plurality of treatment modalities. This is especially true in treating solid tumors at anatomical crucial sites (e.g., glioblastoma, squamous carcinoma of the head and neck and lung adenocarcinoma) which are sometimes limited to standard radiotherapy and / or chemotherapy. Nonetheless, detrimental effects of these therapies are chemo- and radio resistance, which promote loco-regional recurrences, distant metastases and second primary tumors, in addition to severe side-effects that reduce the patients’ quality of life. In fighting cancer and other medical conditions, the therapeutic utility of monoclonal antibodies (mAbs) (G. KOHLER and C. MILSTEIN, Nature 256:495-497 (1975)) is being realized. In general, antibodies act by a number of mechanisms, most of which engage other arms of the immune system. Accordingly, Antibody-drug conjugates (ADCs) are an emerging class of targeted therapeutics having an improved therapeutic index over traditional chemotherapy. Drugs and linkers have been the focus of ADC development, in addition to (monoclonal) antibody (mAb) and target selection. Recently, however, the importance of conjugate homogeneity has been explored. It has been reported that the pharmacological profile of ADCs may be improved by applying site-specific conjugation technologies that make use of surface-exposed cysteine residues engineered into antibodies that are then conjugated to a linker drug, resulting in site-specifically conjugated ADCs with defined drug-to-antibody ratios (DARs). The prior art discloses several approaches to obtaining ADCs. See, for example, WO2006 / 034488 (Genentech), SUTHERLAND, et. al., Blood 122(8):1455-1463 (2013), WO2014 / 124316 (Novartis), US2017 / 0080103 (Synthon Biopharmaceuticals), US11,559,582 (Agensys, Inc.) and WO2019 / 183438 (Seattle Genetics, Inc.), etc. In all of the prior art methods disclosed thus far, the emphasis was put on site conjugating linker drugs at surface / solvent-exposed positions, at positions showing high thiol reactivity, and at positions in specifically the constant regions of monoclonal antibodies, with the aim of improving homogeneity and pharmacokinetic properties. Even though the above-described conventional lysine and cysteine conjugation methods have led to FDA-approved antibody-drug conjugates and they are being used for constructing most of a large number of ADCs currently in preclinical and clinical trials, there is still a need for new conjugation strategies with the aim to (further) improve the physicochemical, pharmacokinetic, pharmacological, and / or toxicological properties of ADCs to obtain ADCs having acceptable antigen binding properties, in vivo efficacy, therapeutic index, and / or stability. From the aforementioned, it will be readily apparent to those skilled in the art that a new treatment paradigm is needed in the treatment of cancers and immunological diseases. By using modern antibody engineering techniques as well as new conjugation methodologies, a new class of antibodies can be achieved with the overall goal of more effective treatment, reduced side effects, and lower production costs. Given the current deficiencies known in the art, it is an object of the present invention to provide new and improved antibodies and binding ligands and methods of treating cancer(s), immunological disorders, and other diseases utilizing antibodies and ADCs. SUMMARY OF THE INVENTION The invention provides antibodies, antigen-binding fragments, antibody drug conjugates (ADCs), antibody immune modifying conjugates, antibody fusion proteins, and antibody fragment fusion proteins that bind to STEAP-1 proteins and polypeptide fragments of STEAP-1 proteins. Briefly, STEAP proteins describe a family of cell surface serpentine transmembrane antigens. Two (2) of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (Six Transmembrane Epithelial Antigen of the Prostate). Four (4) particular human STEAPs are described and characterized in the art (See, U.S. 7,947,459, Agensys, Inc., Santa Monica, CA). The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any other known human proteins. The prototype member of the STEAP family, STEAP-1, has been characterized as a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N- and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops. STEAP-1 protein expression is known to be maintained at elevated levels across various stages of prostate cancer. Moreover, STEAP-1 is highly over-expressed in certain other human cancers. In particular, the cell surface expression of STEAP-1 has been definitively confirmed in a variety of prostate and prostate cancer cells, lung cancer, bladder cancer cells, and colon cancer cells. A second member of the family, STEAP-2, is a 454 amino acid protein with a predicted molecular topology similar to that of STEAP-1. STEAP-2, like STEAP-1, is prostate-specific in normal human tissues and is also expressed in prostate cancer. Alignment of the STEAP-2 and STEAP-1 ORFs shows 54.9% identity over a 237 amino acid residue overlap, and the locations of the six putative transmembrane domains in STEAP-2 coincide with the locations of the transmembrane domains in STEAP-1. STEAP-3 and STEAP-4 are also known family members. These are also structurally related and show unique expression profiles. Notably, STEAP-3 and STEAP-4 appear to show different tissue restriction patterns. In some embodiments, the invention comprises fully human antibodies that bind STEAP proteins. In some embodiments, the invention comprises fully human antibodies that bind STEAP-1. In some embodiments, the invention comprises fully human antibodies conjugated with a therapeutic agent. In certain embodiments, there is a proviso that the entire nucleic acid sequence of Table IV is not encoded and / or the entire amino acid sequence of Table V is not prepared. In certain embodiments, the entire nucleic acid sequence of Table IV is encoded and / or the entire amino acid sequence of Table V is prepared, either of which are in respective human unit dose forms. The invention further provides various immunogenic or therapeutic compositions, such as antibodies, antibody drug conjugates, and strategies for treating cancers that express STEAP-1 such as those cancers listed in Table I. In another embodiment, the present disclosure teaches an antibody composition denoted STP1-Ab. In another embodiment, the present disclosure teaches methods of synthesizing antibodies. In another embodiment, the present disclosure teaches methods of synthesizing antibodies and conjugating a drug moiety to the antibody to form an ADC. In another embodiment, the present disclosure teaches methods of treating cancer(s) in humans. In another embodiment, the present disclosure teaches methods of treating immunological or neurological disorder(s) in humans. In another embodiment, the present disclosure teaches uses of one or more compositions herein in the manufacture of a medicament for treating cancer(s), immunological and / or neurological disorder(s) in humans. BRIEF DESCRIPTION OF THE FIGURES Figure 1. Binding of STEAP-1 Antibody (STP1-Ab) to STEAP-1 Target Expressed on the Cell Surface of Cancer Cell Lines by Flow Cytometry. Figure 2. Histograms showing binding by flow cytometry of STP1-Ab (open histogram) compared to isotype control antibody (grey histogram) to STEAP1 on the cell-surface of human cancer cell lines 22RV1 (Figure 2(A)), LNCaP (Figure 2(B)), EBC-1 (Figure 2(C)), SU-DHL-1 (Figure 2(D)), as well as recombinantly expressed STEAP1 in CHO-K1 (Figure 2(E)), 293T (Figure 2(F)) and PC-3 (Figure 2(G)). Figure 3. Antibody Affinity of STP1-Ab to STEAP-1 on Cell Surface of LNCaP by Flow Cytometry. Figure 3(A). Shows binding affinity of STP1-Ab to STEAP1 on the cell-surface of a human prostate cancer cell line LNCaP by flow cytometry compared to isotype control antibody. Figure 3(B). Shows binding affinity of STP1-Ab and STP1-ADC3 to STEAP1 on the cell-surface of a human cancer cell line SU-DHL-1 by flow cytometry. Figure 4. Binding affinity of STP1-Ab (Figure 4(A)) compared to isotype control antibody (Figure 4(B)) to human and cynomolgus monkey STEAP1 recombinantly expressed on the cell-surface of 293T cells by flow cytometry. Figure 5. In Vitro Cytotoxicity of STP1-ADC2, STP1-ADC3, and STP1-GGFG-Dxd on CHO-K1 Cells Expressing STEAP-1. Figure 6. In Vitro Cytotoxicity of STP1-ADC3 compared to unconjugated STP-1 Ab and corresponding isotype controls, as well as free payload on 293T cells expressing human STEAP1 (Figure 6(A)) and monkey STEAP1 (Figure 6(B)). Figure 7. In vivo efficacy of STP1-ADC1 and STP1-ADC2 compared to STP1-GGFG-Dxd in lung squamous carcinoma EBC-1 NSCLC xenograft model. Figure 8. In vivo efficacy of STP1-ADC3 compared to STP1-Ab conjugated to different linker- payload entities, STP1-GGFG-Dxd and STEAP1-vcMMAE in lung squamous carcinoma EBC-1 NSCLC xenograft model. Figure 9. In Vivo efficacy of a STP1-ADC3 compared to vehicle control in 3 different prostate cancer patient-derived xenograft models, PDX82 (Figure 9(A)), PDX87 (Figure 9(B)), and PDX11 (Figure 9(C)). IHC confirming STEAP-1 expression is shown. Figure 10. In Vivo efficacy of a STP1-ADC3 compared to vehicle control in a NSCLC cancer patient-derived xenograft model PDX59. IHC confirming STEAP-1 expression is shown. Figure 11. In Vivo shows in vivo efficacy of a STP1-ADC3 compared to vehicle control in a gastric cancer patient-derived xenograft model PDX10. IHC confirming STEAP-1 expression is shown. Figure 12. Drug-Linker (DL) Payload Structure(s). Figure 12(A). Shows the structure denoted ADL-01. Figure 12(B). Shows the structure denoted ADL-02. Figure 12(C). Shows the structure denoted ADL-03. Figure 12(D). Shows the structure denoted ADL-04. Figure 12(E). Shows the structure denoted ADL-05. Figure 12(F). Shows the structure denoted ADL-06. Figure 12(G). Shows the structure denoted ADL-07. Figure 12(H). Shows the structure denoted ADL-08. Figure 12(I). Shows the structure denoted ADL-09. Figure 12(J). Shows the structure denoted ADL-10. Figure 13. Exemplary Prior Art Drug-Linker (DL) Payload Structure(s). Figure 13(A). Shows the structure denoted MC-GGFG-Dxd. Figure 13(B). Shows the structure denoted MC-vcMMAE. Figure 14. Figure 14(A). Shows STP1-ADC3 has hydrophilic profile by Hydrophobic Interaction Chromatography (HIC) analysis, and the ADC is stable after incubation for 2 weeks at 40°C. Figure 14(B). Shows STP1-ADC3 mediated strong potency and bystander activity. Figure 14(C). Shows STP1-ADC3 synergizes with PARPi, olaparib and saruparib. Figure 14(D). Shows STP1-ADC3 manifests Topo1i and ICD biomarkers in vivo. Figure 14(F). Shows STP1-ADC3 is highly tolerated in monkeys. Figure 14(E). Shows STP1-ADC3 maintains DAR in the blood circulation in monkeys. DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions II.) Antibodies III.) Antibody-Drug-Conjugates IV.) Linker Units V.) The Stretcher Unit VI.) The Amino Acid Unit VII.) The Spacer Unit VIII.) The Drug Unit IX.) Drug Loading X.) Methods of Determining Cytotoxic Effect of ADCs XI.) Treatment of Cancer(s) Expressing STEAP-1 XII.) STEAP-1 ADC Cocktails XIII.) Combination Therapy XIV.) KITS / Articles of Manufacture I.) Definitions: Unless otherwise defined, all terms of art, notations and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains unless the context clearly indicates otherwise. In some cases, terms with commonly understood meanings are defined herein for clarity and / or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer defined protocols and / or parameters unless otherwise noted. When a trade name is used herein, reference to the trade name also refers to the product formulation, the generic drug, and the active pharmaceutical ingredient(s) of the trade name product, unless otherwise indicated by context. The terms “advanced cancer”, “locally advanced cancer”, “advanced disease” and “locally advanced disease” mean cancers that have extended through the relevant tissue capsule and are meant to include stage C disease under the American Urological Association (AUA) system, stage C1- C2 disease under the Whitmore-Jewett system, and stage T3-T4 and N+ disease under the TNM (tumor, node, metastasis) system. In general, surgery is not recommended for patients with locally advanced diseases and these patients have substantially less favorable outcomes compared to patients having clinically localized (organ-confined) cancer. The term “substituted” means that the specified group or moiety bears one or more substituents. The term “unsubstituted” means that the specified group bears no substituents. The term “optionally substituted” means that the specified group is unsubstituted or substituted by one or more substituents. Where the term “substituted” is used to describe a structural system, the substitution is meant to occur at any valency-allowed position on the system. The term “analog” refers to a molecule which is structurally similar or shares similar or corresponding attributes with another molecule (e.g., a STEAP-1 related protein). For example, an analog of a STEAP-1 protein can be specifically bound by an antibody or T cell that specifically binds to STEAP-1. The term “antibody” is used in the broadest sense unless clearly indicated otherwise. Therefore, an “antibody” can be naturally occurring or synthetic such as monoclonal antibodies produced by conventional hybridoma or transgenic mice technology. STEAP-1 antibodies comprise monoclonal and polyclonal antibodies as well as fragments containing the antigen-binding domain and / or one or more complementarity determining regions of these antibodies. As used herein, the term “antibody” refers to any form of antibody or fragment thereof that specifically binds STEAP-1 and / or exhibits the desired biological activity and specifically covers monoclonal antibodies (including full length monoclonal antibodies), polyclonal antibodies, multi-specific antibodies (e.g., bi-specific antibodies), and antibody fragments so long as they specifically bind STEAP-1 and / or exhibit the desired biological activity. Any specific antibody can be used in the methods and compositions provided herein. Thus, in one embodiment the term “antibody” encompasses a molecule comprising at least one variable region from a light chain immunoglobulin molecule and at least one variable region from a heavy chain molecule that in combination form a specific binding site for the target antigen. In one embodiment, the antibody is an IgG antibody. For example, the antibody is an IgG1, IgG2, IgG3, or IgG4 antibody. The antibodies useful in the present methods and compositions can be generated in cell culture, in phage, in yeast or in various animals, including but not limited to cows, rabbits, goats, mice, rats, hamsters, guinea pigs, sheep, dogs, cats, monkeys, chimpanzees, and apes. Therefore, in one embodiment, an antibody of the present invention is a mammalian antibody. Phage techniques can be used to isolate an initial antibody or to generate variants with altered specificity or avidity characteristics. Such techniques are routine and well known in the art. In one embodiment, the antibody is produced by recombinant means known in the art. For example, a recombinant antibody can be produced by transfecting a host cell with a vector comprising a DNA sequence encoding the antibody. One or more vectors can be used to transfect the DNA sequence expressing at least one VL and at least one VH region in the host cell. Exemplary descriptions of recombinant means of antibody generation and production include Delves, ANTIBODY PRODUCTION: ESSENTIAL TECHNIQUES (Wiley, 1997); SHEPARD, et al., MONOCLONAL ANTIBODIES (Oxford University Press, 2000); GODING, MONOCLONAL ANTIBODIES: PRINCIPLES AND PRACTICE (Academic Press, 1993); and CURRENT PROTOCOLS IN IMMUNOLOGY (John Wiley & Sons, most recent edition). An antibody of the present invention can be modified by recombinant means to increase the efficacy of the antibody in mediating the desired function. Thus, it is within the scope of the invention that antibodies can be modified by substitutions using recombinant means. Typically, the substitutions will be conservative substitutions. For example, at least one amino acid in the constant region of the antibody can be replaced with a different residue. See, e.g., U.S. Pat. No.5,624,821, U.S. Pat. No.6,194,551, Application No. WO 9958572; and ANGAL, et al., Mol. Immunol.30: 105-08 (1993). The modification in amino acids includes deletions, additions, and substitutions of amino acids. In some cases, such changes are made to reduce undesired activities, e.g., complement-dependent cytotoxicity. Frequently, the antibodies are labeled by joining, either covalently or non-covalently, a substance which provides for a detectable signal. A wide variety of labels and conjugation techniques are known and are reported extensively in both scientific and patent literature. These antibodies can be screened for binding to normal or defective STEAP-1. See e.g., ANTIBODY ENGINEERING: A PRACTICAL APPROACH (Oxford University Press, 1996). Suitable antibodies with the desired biologic activities can be identified using the following in vitro assays including but not limited to proliferation, migration, adhesion, soft agar growth, angiogenesis, cell-cell communication, apoptosis, transport, signal transduction, and the following in vivo assays such as the inhibition of tumor growth. The antibodies provided herein can also be useful in diagnostic applications. As capture or non-neutralizing antibodies, they can be screened for the ability to bind to the specific antigen without inhibiting the receptor-binding or biological activity of the antigen. As neutralizing antibodies, the antibodies can be useful in competitive binding assays. They can also be used to quantify the STEAP-1 and / or its receptor. The term “antigen-binding fragment” or “antibody fragment” of an antibody (or simply “antibody portion”), as used herein, refers to one or more fragments of a STEAP-1 antibody that retain the ability to specifically bind to an antigen (e.g., STEAP-1 and / or variants thereof). It has been shown that the antigen-binding function of an antibody can be performed by fragments of a full-length antibody. Examples of binding fragments encompassed within the term “antigen-binding fragment” of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CLand CH1domains; (ii) a F(ab′)2fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) a Fd fragment consisting of the VHand CH1domains; (iv) a Fv fragment consisting of the VLand VHdomains of a single arm of an antibody, (v) a dAb fragment (WARD et al., (1989) Nature 341:544-546), which consists of a VHdomain; and (vi) an isolated complementarily determining region (CDR). Furthermore, although the two domains of the Fv fragment, VLand VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VLand VHregions pair to form monovalent molecules (known as single chain Fv (scFv); see e.g., BIRD et. al. (1988) Science 242:423-426; and HUSTON et. al. (1988) Proc. Natl. Acad. Sci. USA 85:5879-5883). Such single chain antibodies are also intended to be encompassed within the term “antigen-binding fragment” of an antibody. These antibody fragments are obtained using conventional techniques known to those with skill in the art, and the fragments are screened for utility in the same manner as are intact antibodies. The term “Fc,” as used herein, refers to a region comprising a hinge region, CH2and / or CH3domains. As used herein, any form of the “antigen” can be used to generate an antibody that is specific for STEAP-1 of the invention. Thus, the eliciting antigen may be a single epitope, multiple epitopes, or the entire protein alone or in combination with one or more immunogenicity enhancing agents known in the art. The eliciting antigen may be an isolated full-length protein, a cell surface protein (e.g., immunizing with cells transfected with at least a portion of the antigen), or a soluble protein (e.g., immunizing with only the extracellular domain portion of the protein). The antigen may be produced in a genetically modified cell. The DNA encoding the antigen may be genomic or non-genomic (e.g., cDNA) and encodes at least a portion of the extracellular domain. As used herein, the term “portion,” in the context of an antigen, refers to the minimal number of amino acids or nucleic acids, as appropriate, to constitute an immunogenic epitope of the antigen of interest. Any genetic vectors suitable for transformation of the cells of interest may be employed, including but not limited to adenoviral vectors, plasmids, and non-viral vectors, such as cationic lipids. In one embodiment, the antibody of the methods and compositions herein specifically bind at least a portion of the extracellular domain of the target of interest. The antibodies or antigen binding fragments thereof provided herein may constitute or be part of a “bioactive agent.” As used herein, the term “bioactive agent” refers to any synthetic or naturally occurring compound that binds the antigen and / or enhances or mediates a desired biological effect to enhance cell-killing toxins. In one embodiment, the binding fragments useful in the present invention are biologically active fragments. As used herein, the term “biologically active” refers to an antibody or antibody fragment that is capable of binding the desired antigenic epitope and directly or indirectly exerting a biologic effect. Direct effects include, but are not limited to the modulation, stimulation, and / or inhibition of a growth signal, the modulation, stimulation, and / or inhibition of an anti-apoptotic signal, the modulation, stimulation, and / or inhibition of an apoptotic or necrotic signal, modulation, stimulation, and / or inhibition the ADCC cascade, and modulation, stimulation, and / or inhibition the CDC cascade and / or Fc silencing. The term “specifically binds,” as used herein in relation to antigen binding, proteins means that the antigen binding protein binds to the target as well as a discrete domain, or discrete amino acid sequence, within the target with no or insignificant binding to other (for example, unrelated) proteins. This term, however, does not exclude the fact that the antibodies or binding fragments thereof may also be cross-reactive with closely related molecules. The antibodies and fragments thereof as well as antibody drug conjugates comprising these described herein may specifically bind to STEAP-1 disclosed herein, with at least 2, 5, 10, 50, 100, or 1000-fold greater affinity than they bind to closely related molecules. “Bispecific” antibodies are also useful in the present methods and compositions. As used herein, the term “bispecific antibody” refers to an antibody, typically a monoclonal antibody, having binding specificities for at least two different antigenic epitopes. In one embodiment, the epitopes are from the same antigen. In another embodiment, the epitopes are from two different antigens. Methods for making bispecific antibodies are known in the art. For example, bispecific antibodies can be produced recombinantly using the co-expression of two immunoglobulin heavy chain / light chain pairs. See, e.g., MILSTEIN et. al., Nature 305:537-39 (1983). Alternatively, bispecific antibodies can be prepared using chemical linkage. See, e.g., BRENNAN, et. al., Science 229:81 (1985). Bispecific antibodies include bispecific antibody fragments. See, e.g., HOLLINGER, et. al., Proc. Natl. Acad. Sci. U.S.A.90:6444-48 (1993), GRUBER, et. al., J. Immunol.152:5368 (1994). The monoclonal antibodies described herein specifically include “chimeric” antibodies in which a portion of the heavy and / or light chain is identical with or homologous to corresponding sequences in antibodies derived from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chain(s) is identical with or homologous to corresponding sequences in antibodies derived from another species or belonging to another antibody class or subclass, as well as fragments of such antibodies, so long as they specifically bind the target antigen and / or exhibit the desired biological activity (U.S. Pat. No.4,816,567; and MORRISON et. al., Proc. Natl. Acad. Sci. USA 81: 6851-6855 (1984)). As used herein, the terms “cancer,” “neoplasm,” and “tumor,” are used interchangeably and in either the singular or plural form, refer to cells that have undergone a malignant transformation that makes them pathological to the host organism. Primary cancer cells (that is, cells obtained from near the site of malignant transformation) can be readily distinguished from non-cancerous cells by well- established techniques, particularly histological examination. The definition of a cancer cell, as used herein, includes not only a primary cancer cell, but any cell derived from a cancer cell ancestor. This includes metastasized cancer cells, and in vitro cultures and cell lines derived from cancer cells. When referring to a type of cancer that normally manifests as a solid tumor, a “clinically detectable” tumor is one that is detectable on the basis of tumor mass; e.g., by procedures such as CAT scan, MR imaging, X-ray, ultrasound, or palpation, and / or which is detectable because of the expression of one or more cancer-specific antigens in a sample obtainable from a patient. Tumors may be hematopoietic tumors, for example, tumors of blood cells or the like, meaning liquid tumors. Specific examples of clinical conditions based on such a tumor include leukemia such as chronic myelocytic leukemia or acute myelocytic leukemia; myeloma such as multiple myeloma; lymphoma and the like. The term “therapeutic agent” refers to all agents that provide a therapeutic benefit and / or are therapeutically effective as defined herein. A therapeutic agent may, for example, reverse, ameliorate, alleviate, inhibit, or limit the progress of, or lessen the severity of, a disease, disorder, or condition, affect, improve, or ameliorate one or more symptoms of disease, such as cancer. Such an agent may be cytotoxic or cytostatic. The term includes, but is not limited to, chemotherapeutic agents, anti- neoplastic agents and “Drug Unit” agents as defined herein. The term “anti-neoplastic agent” refers to all agents that provide a therapeutic benefit and / or are therapeutically effective, as defined herein, in the treatment of a neoplasm or cancer. The term “Chemotherapeutic Agent” refers to all chemical compounds that are effective in inhibiting tumor growth. Non-limiting examples of chemotherapeutic agents include alkylating agents; for example, nitrogen mustards, ethyleneimine compounds and alkyl sulphonates; antimetabolites, for example, folic acid, purine or pyrimidine antagonists; mitotic inhibitors, for example, anti-tubulin agents such as vinca alkaloids, auristatins and derivatives of podophyllotoxin; cytotoxic antibiotics; compounds that damage or interfere with DNA expression or replication, for example, DNA minor groove binders; and growth factor receptor antagonists. In addition, chemotherapeutic agents include cytotoxic agents (as defined herein), antibodies, biological molecules, and small molecules. The terms “complementarity determining region,” and “CDR,” are known in the art to refer to non-contiguous sequences of amino acids within antibody variable regions, which confer antigen specificity and binding affinity. In general, there are three (3) CDRs in each heavy chain variable region (CDR-H1, CDR-H2, CDR-H3) and three (3) CDRs in each light chain variable region (CDR-L1, CDR-L2, CDR-L3). The precise amino acid sequence boundaries of a given CDR can be readily determined using any of a number of well-known schemes, including those described by Kabat et al. (1991), “Sequences of Proteins of Immunological Interest,” 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md. (“Kabat” numbering scheme), AL-LAZIKANI et. al., (1997) JMB 273, 927-948 (“Chothia” numbering scheme), MACCALLUM et. al., J. Mol. Biol.262:732-745 (1996), “Antibody-antigen interactions: Contact analysis and binding site topography,” J. Mol. Biol.262, 732-745.” (Contact” numbering scheme), LEFRANC M. P. et. al., “IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains,” Dev Comp Immunol, 2003 January; 27(1):55-77 (“IMGT” numbering scheme), and HONEGGER A. and PLICKTHUN A., “Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool,” J Mol Biol, 2001 Jun.8; 309(3):657-70, (AHo numbering scheme). The boundaries of a given CDR may vary depending on the scheme used for identification. For example, the Kabat scheme is based structural alignments, while the Chothia scheme is based on structural information. Numbering for both the Kabat and Chothia schemes is based upon the most common antibody region sequence lengths, with insertions accommodated by insertion letters, for example, “30a,” and deletions appearing in some antibodies. The two schemes place certain insertions and deletions (“indels”) at various positions, resulting in differential numbering. The Contact scheme is based on analysis of complex crystal structures and is similar in many respects to the Chothia numbering scheme. Thus, unless otherwise specified, the terms “CDR” and “complementary determining region” of a given antibody or region thereof, such as a variable region, as well as individual CDRs (e.g., “CDR- H1, CDR-H2) of the antibody or region thereof, should be understood to encompass the complementary determining region as defined by any of the known schemes described herein above. In some instances, the scheme for identification of a particular CDR or CDRs is specified, such as the CDR as defined by the Kabat, Chothia, or Contact method. As used herein, the term “conservative substitution” refers to substitutions of amino acids and / or amino acid sequences that are known to those of skill in this art and may be made generally without altering the biological activity of the resulting molecule. Those of skill in this art recognize that, in general, single amino acid substitutions in non-essential regions of a polypeptide do not substantially alter biological activity (see, e.g., WATSON, et. al., MOLECULAR BIOLOGY OF THE GENE, The Benjamin / Cummings Pub. Co., p.224 (4th Ed.1987)). Such exemplary substitutions are preferably made in accordance with those set forth in Table II and Table(s) III. For example, such changes include substituting any of isoleucine (I), valine (V), and leucine (L) for any other of these hydrophobic amino acids; aspartic acid (D) for glutamic acid (E) and vice versa; glutamine (Q) for asparagine (N) and vice versa; and serine (S) for threonine (T) and vice versa. Other substitutions can also be considered conservative, depending on the environment of the particular amino acid and its role in the three- dimensional structure of the protein. For example, glycine (G) and alanine (A) can frequently be interchangeable, as can alanine (A) and valine (V). Methionine (M), which is relatively hydrophobic, can frequently be interchanged with leucine and isoleucine, and sometimes with valine. Lysine (K) and arginine (R) are frequently interchangeable in locations in which the significant feature of the amino acid residue is its charge and the differing pK's of these two amino acid residues are not significant. Still other changes can be considered “conservative” in particular environments (see, e.g., Table III herein; pages 13-15 “Biochemistry” 2nd ED. LUBERT STRYER ed. (Stanford University); HENIKOFF et. al., PNAS 1992 Vol 8910915-10919; LEI et. al., J Biol Chem 1995 May 19; 270(20):11882-6). Other substitutions are also permissible and may be determined empirically or in accord with known conservative substitutions. The term “cytotoxic agent” refers to a substance that inhibits or prevents the expression activity of cells, function of cells and / or causes destruction of cells. The term is intended to include radioactive isotopes, chemotherapeutic agents, and toxins such as small molecule toxins or enzymatically active toxins of bacterial, fungal, plant or animal origin, including fragments and / or variants thereof. Examples of cytotoxic agents include, but are not limited to auristatins, auristatin derivatives, auromycins, camptothecins (Topoisomerase 1 inhibitors), maytansinoids, ricin, ricin A-chain, combrestatin, duocarmycins, dolastatins, doxorubicin, daunorubicin, taxols, cisplatin, cc1065, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE40, abrin, abrin A chain, modeccin A chain, alpha-sarcin, gelonin, mitogellin, retstrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Sapaonaria officinalis inhibitor, and glucocorticoid and other chemotherapeutic agents, as well as radioisotopes such as At , I , I , Y, Re , Re , Sm , Bi or , P, and radioactive isotopes of Lu including Lu177. Antibodies, including antibodies of the invention, may also be conjugated to any of the aforementioned cytotoxic agents and also to an anti-cancer prodrug activating enzyme capable of converting the prodrug to its active form. As used herein, the term “diabodies” refers to small antibody fragments with two antigen- binding sites, which fragments comprise a heavy chain variable domain (VH) connected to a light chain variable domain (VL) in the same polypeptide chain (VH—VL). By using a linker that is too short to allow pairing between the two domains on the same chain, the domains are forced to pair with the complementary domains of another chain and create two antigen-binding sites. Diabodies are described more fully in, e.g., EP 404,097; WO 93 / 11161; and HOLLINGER et. al., Proc. Natl. Acad. Sci. USA 90:6444-48 (1993). The term “homolog” refers to a molecule which exhibits homology to another molecule, by for example, having sequences of chemical residues that are the same or similar at corresponding positions. The term “identical” or “sequence identity” indicates the degree of identity between two nucleic acid or two amino acid sequences when optimally aligned and compared with appropriate insertions or deletions. The “percent identity” between two sequences is a function of the number of identical positions shared by the sequences (i.e., % identity=number of identical positions / total number of positions times 100), considering the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm, as described below. The percent identity between two nucleotide sequences can be determined using the GAP program in the GCG software package, using a NWS gap DNA CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. The percent identity between two nucleotide or amino acid sequences can also be determined using the algorithm of Meyers, et al., Comput. Appi. Biosci., 4:11-17 (1988), which has been incorporated into the ALIGN program (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4. In addition, the percentage identity between two amino acid sequences can be determined using the NEEDLEMAN, et. al., J. Mol. Biol.48:444-453 (1970) algorithm which has been incorporated into the GAP program in the GCG software package, using either a Blossum 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. By way of example, a polynucleotide sequence may be identical to a reference polynucleotide sequence that is 100% identical to the reference sequence, or it may include up to a certain integer number of nucleotide alterations as compared to the reference sequence, such as at least 50, 60, 70, 75, 80, 85, 90, 95, 96, 97, 98, or 99% identical. Such alterations are selected from at least one nucleotide deletion, substitution, including transition and transversion, or insertion, and wherein said alterations may occur at the 5′ or 3′ terminal positions of the reference nucleotide sequence or anywhere between those terminal positions, interspersed either individually among the nucleotides in the reference sequence or in one or more contiguous groups within the reference sequence. The number of nucleotide alterations is determined by multiplying the total number of nucleotides in the reference polynucleotide sequence as described herein by the numerical percent of the respective percent identity (divided by 100) and subtracting that product from said total number of nucleotides in the reference polynucleotide sequence, or: nn≤xn-(xny), wherein nnis the number of nucleotide alterations, xnis the total number of nucleotides in the reference polynucleotide sequence as described herein (see the nucleic acid sequences in the “Sequence Listing” for exemplary reference polynucleotides sequences), and y is 0.50 for 50%, 0.60 for 60%, 0.70 for 70%, 0.75 for 75%, 0.80 for 80%, 0.85 for 85%, 0.90 for 90%, 0.95 for 95%, 0.98 for 98%, 0.99 for 99% or 1.00 for 100%, is the symbol for the multiplication operator, and wherein any non-integer product of xnand y is rounded down to the nearest integer prior to subtracting it from xn. Similarly, a polypeptide sequence may be identical to a polypeptide reference sequence as described herein, that is 100% identical, or it may include up to a certain integer number of amino acid alterations as compared to the reference sequence such that the % identity is less than 100%, such as at least 50, 60, 70, 75, 80, 85, 90, 95, 98, or 99% identical. Such alterations are selected from the group consisting of at least one amino acid deletion, substitution, including conservative and non-conservative substitution, or insertion, and wherein said alterations may occur at the amino- or carboxy-terminal positions of the reference polypeptide sequence or anywhere between those terminal positions, interspersed either individually among the amino acids in the reference sequence or in one or more contiguous groups within the reference sequence. The number of amino acid alterations for a given % identity is determined by multiplying the total number of amino acids in the polypeptide sequence encoded by the polypeptide reference sequence by the numerical percent of the respective percent identity (divided by 100) and then subtracting that product from said total number of amino acids in the polypeptide reference sequence as described herein, or: na≤xa-(xay), wherein nais the number of amino acid alterations, xais the total number of amino acids in the reference polypeptide sequence, and y is, 0.50 for 50%, 0.60 for 60%, 0.70 for 70%, 0.75 for 75%, 0.80 for 80%, 0.85 for 85%, 0.90 for 90%, 0.95 for 95%, 0.98 for 98%, 0.99 for 99%, or 1.00 for 100%, is the symbol for the multiplication operator, and wherein any non-integer product of xaand y is rounded down to the nearest integer prior to subtracting it from xa. The percentage identity may be determined across the length of the sequence. As defined herein the term “over 75% identical” includes over 75%, 80%, 85%, 95% and 99% identity as well as all discrete values, and discrete subranges, within this range. In one embodiment, the antibody provided herein is a “human antibody.” As used herein, the term “human antibody” refers to an antibody in which essentially the entire sequences of the light chain and heavy chain sequences, including the complementary determining regions (CDRs), are from human genes. In one embodiment, human monoclonal antibodies are prepared by the trioma technique, the human B-cell technique (see, e.g., KOZBOR, et. al., Immunol. Today 4: 72 (1983), EBV transformation technique (see, e.g., COLE et. al. MONOCLONAL ANTIBODIES AND CANCER THERAPY 77-96 (1985)), or using yeast or phage display (see, e.g., MARKS et. al., J. Mol. Biol.222:581 (1991)). In a specific embodiment, the human antibody is generated in a transgenic mouse. Techniques for making such partially to fully human antibodies are known in the art and any such techniques can be used. According to one particularly preferred embodiment, fully human antibody sequences are made in a transgenic mouse engineered to express human heavy and light chain antibody genes. An exemplary description of preparing transgenic mice that produce human antibodies found in Application No. WO 02 / 43478 and U.S. Pat. No.6,657,103 (Amgen Fremont, Inc., formerly Abgenix, Inc.) and its progeny. B cells from transgenic mice that produce the desired antibody can then be fused to make hybridoma cell lines for continuous production of the antibody. See, e.g., U.S. Pat. Nos.5,569,825; 5,625,126; 5,633,425; 5,661,016; and 5,545,806; and JAKOBOVITS, Adv. Drug Del. Rev.31:33-42 (1998); GREEN, et. al., J. Exp. Med.188:483-95 (1998). As used herein, the term “humanized antibody” refers to forms of antibodies that contain sequences from non-human (e.g., murine) antibodies as well as human antibodies. Such antibodies are chimeric antibodies which contain minimal sequence derived from non-human immunoglobulin. In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the hypervariable loops correspond to those of a non-human immunoglobulin and all or substantially all of the FR regions are those of a human immunoglobulin sequence. The humanized antibody optionally also will comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin. See, e.g., CABILLY, U.S. Pat. No.4,816,567; QUEEN, et. al. (1989) Proc. Nat'l Acad. Sci. USA 86:10029-10033; and ANTIBODY ENGINEERING: A PRACTICAL APPROACH (Oxford University Press 1996). The terms “inhibit” or “inhibition of” as used herein means to reduce by a measurable amount, or to prevent entirely. The term “mammal” refers to any organism classified as a mammal, including mice, rats, rabbits, dogs, cats, cows, horses, and humans. In one embodiment of the invention, the mammal is a mouse. In another embodiment of the invention, the mammal is a human. The terms “metastatic cancer” and “metastatic disease” mean cancers that have spread to regional lymph nodes or to distant sites and are meant to include stage D disease under the AUA system and stage T×N×M+ under the TNM system. The term “modified,” as used herein refers to the presence of a change to a natural amino acid, a non-natural amino acid, a natural amino acid polypeptide or a non-natural amino acid polypeptide. Such changes, or modifications, may be obtained by post synthesis modifications of natural amino acids, non-natural amino acids, natural amino acid polypeptide or a non-natural amino acid polypeptide, or by co-translation, or by post-translational modifications of a natural amino acid, a non-natural amino acid, a natural amino acid polypeptide or a non-natural amino acid polypeptide. “Molecular recognition” means a chemical event in which a host molecule is able to form a complex with a second molecule (i.e., the guest). This process occurs through non-covalent chemical bonds, including but not limited to hydrogen bonding, hydrophobic interactions, ionic interaction. The term “monoclonal antibody,” as used herein, refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical except for possible naturally occurring mutations that may be present in minor amounts. Monoclonal antibodies are highly specific, being directed against a single antigenic epitope. In contrast, conventional (polyclonal) antibody preparations typically include a multitude of antibodies directed against (or specific for) different epitopes. In one embodiment, the polyclonal antibody contains a plurality of monoclonal antibodies with different epitope specificities, affinities, or avidities within a single antigen that contains multiple antigenic epitopes. The modifier “monoclonal” indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies and is not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies to be used in accordance with the present invention may be made by the hybridoma method first described by KOHLER et. al., Nature 256: 495 (1975), or may be made by recombinant DNA methods (see, e.g., U.S. Pat. No.4,816,567). The “monoclonal antibodies” may also be isolated from phage antibody libraries using the techniques described in CLACKSON et. al., Nature 352: 624-628 (1991) and MARKS et. al., J. Mol. Biol.222: 581-597 (1991), for example. These monoclonal antibodies will usually bind with at least a Kd of about 1 μM, more usually at least about 300 nM, typically at least about 30 nM, preferably at least about 10 nM, more preferably at least about 3 nM or better, usually determined by ELISA. A “non-natural amino acid” or otherwise written as “nnAA” refers to an amino acid that is not one of the twenty (20) common amino acids or pyrolysine or selenocysteine. Other terms that may be used synonymously with the term nnAA is “non-natural encoded amino acid,” “unnatural amino acid,” “non-naturally occurring amino acid.” Additionally, the term nnAA includes, but is not limited to, amino acids which do not occur naturally and may be obtained synthetically or may be obtained by modification of non-natural amino acids. The term “other targeted cancer drug(s)” means a drug or therapy, which includes (i) a drug or therapy targeting one or more different components of a STEAP-1 signaling pathway, (ii) one or more genes related to STEAP-1 expression or function in cancer, and / or (iii) one or more drugs targeting one or more other genes (e.g., PARP, HRAS, KRAS, PI3KA, DIS3) or pathways (e.g., immune checkpoint, etc.) in a cancer. A “pharmaceutical excipient” comprises a material such as an adjuvant, a carrier, pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservative, and the like. “Pharmaceutically acceptable” refers to a non-toxic, inert, and / or composition that is physiologically compatible with humans or other mammals. The term “polypeptide” means a polymer of at least about 4, 5, 6, 7, or 8 amino acids. Throughout the specification, standard three letter (See, Table II) or single letter designations for amino acids are used. In the art, this term is often used interchangeably with “peptide” or “protein.” As used herein, the term “single-chain Fv” or “scFv” or “single chain” antibody refers to antibody fragments comprising the VHand VLdomains of antibody, wherein these domains are present in a single polypeptide chain. Generally, the Fv polypeptide further comprises a polypeptide linker between the VHand VLdomains which enables the sFv to form the desired structure for antigen binding. For a review of sFv, see PLUCKTHUN, THE PHARMACOLOGY OF MONOCLONAL ANTIBODIES, vol.113, Rosenburg and Moore eds. Springer-Verlag, New York, pp.269-315 (1994). As used herein, the terms “specific,” “specifically binds” and “binds specifically” refer to the selective binding of the antibody to the target antigen epitope. Antibodies can be tested for specificity of binding by comparing binding to appropriate antigen to binding to irrelevant antigen or antigen mixture under a given set of conditions. If the antibody binds to the appropriate antigen at least 2, 5, 7, and preferably 10 times more than to an irrelevant antigen or antigen mixture then it is considered to be specific. In one embodiment, a specific antibody is one that only binds the STEAP-1 antigen but does not bind to any other irrelevant antigen. In another embodiment, a specific antibody is one that binds human STEAP-1 antigen but does not bind a non-human STEAP-1 antigen with 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or greater amino acid homology with the STEAP-1 antigen. In another embodiment, a specific antibody is one that binds human STEAP-1 antigen but does not bind a non-human STEAP-1 antigen with 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or greater percent identity with the amino acid sequence of the STEAP-1 antigen. In another embodiment, a specific antibody is one that binds human STEAP-1 antigen and binds murine STEAP-1 antigen, but with a higher degree of binding the human antigen. In another embodiment, a specific antibody is one that binds human STEAP-1 antigen and binds primate STEAP-1 antigen, but with a higher degree of binding the human antigen. In another embodiment, the specific antibody binds to human STEAP-1 antigen and any non-human STEAP-1 antigen, but with a higher degree of binding the human antigen or any combination thereof. As used herein “to treat” or “therapeutic” and grammatically related terms, refer to any improvement of any consequence of disease, such as prolonged survival, less morbidity, and / or a lessening of side effects which are the byproducts of an alternative therapeutic modality; as is readily appreciated in the art, full eradication of disease is a preferred but albeit not a requirement for a treatment act. The term “variant” refers to a molecule that exhibits a variation from a described type or norm, such as a protein that has one or more different amino acid residues in the corresponding position(s) of a specifically described protein (e.g., STEAP-1 protein as shown in Table IV). An analog is an example of a variant protein. Splice isoforms and single nucleotides polymorphisms (SNPs) are further examples of variants. The phrases “isolated” or “biologically pure” refer to material which is substantially or essentially free from components which normally accompany the material as it is found in its native state. Thus, isolated peptides in accordance with the invention preferably do not contain materials normally associated with the peptides in their in-situ environment. For example, a polynucleotide is said to be “isolated” when it is substantially separated from contaminant polynucleotides that correspond or are complementary to genes other than the STEAP-1 genes or that encode polypeptides other than STEAP-1 gene product or fragments thereof. A skilled artisan can readily employ nucleic acid isolation procedures to obtain an isolated STEAP-1 polynucleotide. A protein is said to be “isolated,” for example, when physical, mechanical, or chemical methods are employed to remove the STEAP-1 proteins from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated STEAP-1 protein. Alternatively, an isolated protein can be prepared by chemical means. Suitable “labels” include radionuclides, enzymes, substrates, cofactors, inhibitors, fluorescent moieties, chemiluminescent moieties, magnetic particles, and the like. Patents teaching the use of such labels include U.S. Pat. Nos.3,817,837; 3,850,752; 3,939,350; 3,996,345; 4,277,437; 4,275,149; and 4,366,241. In addition, the antibodies provided herein can be useful as the antigen-binding component of fluorobodies. (See, e.g., ZEYTUN, et al., Nat. Biotechnol.21:1473-79 (2003). The “STEAP-1 proteins” and / or “STEAP-1 related proteins” of the invention include those specifically identified herein (see, Table IV), as well as allelic variants, conservative substitution variants, analogs and homologs that can be isolated / generated and characterized without undue experimentation following the methods outlined herein or readily available in the art. Fusion proteins that combine parts of different STEAP-1 proteins or fragments thereof, as well as fusion proteins of a STEAP-1 protein and a heterologous polypeptide are also included. Such STEAP-1 proteins are collectively referred to as the STEAP-1-related proteins, the proteins of the invention, or STEAP-1. The term “STEAP-1-related protein” refers to a polypeptide fragment or a STEAP-1 protein sequence of 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 amino acids; or, at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 225, 250, 275, 300, 325, 330, 335, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500, 510, 515, 516, 517, 518, 519 or more amino acids. II.) Antibodies Another aspect of the invention provides antibodies that bind to STEAP-1 as disclosed herein. In one embodiment, the antibody that binds to STEAP-1 (Table IV) and other STEAP-1-related proteins. As is known in the art, STEAP-1 antibodies of the invention are particularly useful in cancer (see, e.g., Table I), for prognostic assays, imaging, diagnostic, and therapeutic methodologies. In one embodiment, a STEAP-1 binding assay is disclosed herein for use in detection of cancer, for example, in an immunoassay. Similarly, such STEAP-1 antibodies are useful (e.g., when combined with a therapeutic agent, such as in an ADC, in the treatment, and / or prognosis of cancer (for example, the cancers set forth in Table I) to the extent STEAP-1 is also expressed or overexpressed in these other cancers. Moreover, intracellularly expressed antibodies (e.g., single chain antibodies) are therapeutically useful in treating cancers in which the expression of STEAP-1 and other targets are involved. Various methods for the preparation of antibodies, specifically monoclonal antibodies, are well known in the art. For example, antibodies can be prepared by immunizing a suitable mammalian host using a STEAP-1-related protein, peptide, or fragment, in isolated or immunoconjugated form (Antibodies: A Laboratory Manual, CSH Press, Eds., Harlow, and Lane (1988); Harlow, Antibodies, Cold Spring Harbor Press, NY (1989)). In addition, fusion proteins of STEAP-1 can also be used, such as a STEAP-1 GST-fusion protein. In a particular embodiment, a GST fusion protein comprising all or most of the amino acid sequence of STEAP-1 is produced and then used as an immunogen to generate appropriate antibodies. In another embodiment, a STEAP-1-related protein is synthesized and used as an immunogen. In addition, naked DNA immunization techniques known in the art are used (with or without purified STEAP-1-related protein or STEAP-1 expressing cells) to generate an immune response to the encoded immunogen (for review, see DONNELLY et. al., 1997, Ann. Rev. Immunol.15: 617-648). Preferred methods for the generation of STEAP-1 antibodies are further illustrated by way of the examples provided herein. Methods for preparing a protein or polypeptide for use as an immunogen are well known in the art. Also well known in the art are methods for preparing immunogenic conjugates of a protein with a carrier, such as BSA, KLH or another carrier protein. In some circumstances, direct conjugation using, for example, carbodiimide reagents are used; in other instances, linking reagents such as those supplied by Pierce Chemical Co., Rockford, Ill., are effective. Administration of a STEAP- 1 immunogen is often conducted by injection over a suitable time period and with use of a suitable adjuvant, as is understood in the art. During the immunization schedule, titers of antibodies can be taken to determine adequacy of antibody formation. STEAP-1 monoclonal antibodies can be produced by various means well known in the art. For example, immortalized cell lines that secrete a desired monoclonal antibody are prepared using the standard hybridoma technology of Kohler and Milstein or modifications that immortalize antibody- producing B cells, as is generally known. Immortalized cell lines that secrete the desired antibodies are screened by immunoassay in which the antigen is a STEAP-1-related protein. When the appropriate immortalized cell culture is identified, the cells can be expanded, and antibodies produced either from in vitro cultures or from ascites fluid. The antibodies or fragments of the invention can also be produced by recombinant means. Regions that bind specifically to the desired regions of a STEAP-1 protein can also be produced in the context of chimeric or complementarity-determining region (CDR) grafted antibodies of multiple species origin. Humanized or human STEAP-1 antibodies can also be produced and are preferred for use in therapeutic contexts. Methods for humanizing murine and other non-human antibodies, by substituting one or more of the non-human antibody CDRs for corresponding human antibody sequences, are well known (see for example, JONES et. al., 1986, Nature 321: 522-525; RIECHMANN et. al., 1988, Nature 332: 323-327; VERHOEYEN et. al., 1988, Science 239: 1534-1536). See also, CARTER et. al., 1993, Proc. Natl. Acad. Sci. USA 89: 4285 and SIMS et. al., 1993, J. Immunol.151: 2296. In one embodiment, human monoclonal antibodies of the invention can be prepared using VelocImmune mice into which genomic sequences bearing endogenous mouse variable segments at the immunoglobulin heavy chain (VH, DH, and JH segments) and / or kappa light chain (VK and JK) loci have been replaced, in whole or in part, with human genomic sequences bearing unrearranged germline variable segments of the human immunoglobulin heavy chain (VH, DH, and JH) and / or kappa light chain (VK and JK) loci (Regeneron, Tarrytown, N.Y.). See, for example, U.S. Pat. Nos.6,586,251, 6,596,541, 7,105,348, 6,528,313, 6,638,768, and 6,528,314. In addition, human antibodies of the invention can be generated using the HuMAb mouse (Medarex, Inc.) which contains human immunoglobulin gene miniloci that encode unrearranged human heavy (mu and gamma) and kappa light chain immunoglobulin sequences, together with targeted mutations that inactivate the endogenous mu and kappa chain loci (see e.g., LONBERG, et. al. (1994) Nature 368(6474): 856-859). In another embodiment, fully human antibodies of the invention can be raised using a mouse that carries human immunoglobulin sequences on transgenes and transchromosomes, such as a mouse that carries a human heavy chain transgene and a human light chain transchromosome. Such mice, referred to herein as “KM mice,” such mice are described in TOMIZUKA et. al. (2000) Proc. Natl. Acad. Sci. USA 97:722-727 and PCT Publication WO 02 / 43478 to TOMIZUKA, et. al. Human monoclonal antibodies of the invention can also be prepared using phage or yeast display methods for screening libraries of human immunoglobulin genes. Such phage display methods for isolating human antibodies are established in the art. See for example: U.S. Pat. Nos.5,223,409; 5,403,484; and U.S. Pat. No.5,571,698 to LADNER et. al.; U.S. Pat. Nos.5,427,908 and 5,580,717 to DOWER et. al.; U.S. Pat. Nos.5,969,108 and 6,172,197 to MCCAFFERTY et. al.; and U.S. Pat. Nos. 5,885,793; 6,521,404; 6,544,731; 6,555,313; 6,582,915 and 6,593,081 to GRIFFITHS et. al. Human monoclonal antibodies of the invention can also be prepared using SCID mice into which human immune cells have been reconstituted such that a human antibody response can be generated upon immunization. Such mice are described in, for example, U.S. Pat. Nos.5,476,996 and 5,698,767 to WILSON, et. al. Additionally, human antibodies of the present invention can be made with techniques using transgenic mice, inactivated for antibody production, engineered with human heavy and light chains loci referred to as Xenomouse (Amgen Fremont, Inc., formerly Abgenix, Inc.). An exemplary description of preparing transgenic mice that produce human antibodies can be found in U.S. Pat. No.6,657,103. See, also, U.S. Pat. Nos.5,569,825; 5,625,126; 5,633,425; 5,661,016; and 5,545,806; and MENDEZ, et. al. Nature Genetics, 15: 146-156 (1998); KELLERMAN, S. A. & GREEN, L. L., Curr. Opin. Biotechnol 13, 593-597 (2002). Any of the methods of production above result in antibodies that have a certain ability to bind STEAP-1, or homologs or fragments or polypeptide sequences having 85, 90, 91, 92, 93, 94, 95, 96, 9, 98, or 99% sequence identity to STEAP-1. The binding affinity (KD) of the antibodies, binding fragments thereof, and antibody drug conjugates comprising the same for STEAP-1 may be 1 mM or less, 100 nM or less, 10 nM or less, 2 nM or less or 1 nM or less. Alternatively, the KDmay be between 5 and 10 nM; or between 1 and 2 nM. The KDmay be between 1 micromolar and 500 micromolar or between 500 micromolar and 1 nM. The binding affinity of the antigen binding protein is determined by the association constant (Ka) and the dissociation constant (Kd) (KD=Kd / Ka). The binding affinity may be measured by BIACORE for example, by capture of the test antibody onto a protein-A coated sensor surface and flowing STEAP-1 over this surface. Alternatively, the binding affinity can be measured by FORTEBIO for example, with the test antibody receptor captured onto a protein-A coated needle and flowing STEAP-1 over this surface. One skilled in the art can identify other suitable assays known in the art to measure binding affinity. Engineered antibodies of the invention include those in which modifications have been made to framework residues within VH and / or VL (e.g., to improve the properties of the antibody). Typically, such framework modifications are made to decrease the immunogenicity of the antibody. For example, one approach is to “backmutate” one or more framework residues to the corresponding germline sequence. More specifically, an antibody that has undergone somatic mutation may contain framework residues that differ from the germline sequence from which the antibody is derived. Such residues can be identified by comparing the antibody framework sequences to the germline sequences from which the antibody is derived. To return the framework region sequences to their germline configuration, the somatic mutations can be “backmutated” to the germline sequence by, for example, site-directed mutagenesis or PCR-mediated mutagenesis (e.g., “backmutated” from leucine to methionine). Such “backmutated” antibodies are also intended to be encompassed by the invention. Engineering of the VH and / or VL can also be made to modify the binding affinity to the antigen. For example, changing residues within the frameworks and / or CDR regions to increase affinity, or reduce affinity to STEAP-1 are also intended to be encompassed by the invention. Another type of framework modification involves mutating one or more residues within the framework region, or even within one or more CDR regions, to remove T-cell epitopes to thereby reduce the potential immunogenicity of the antibody. This approach is also referred to as “deimmunization” and is described in further detail in U.S. Patent Publication No.2003 / 0153043 by CARR, et. al. In addition, or alternative to modifications made within the framework or CDR regions, antibodies of the invention may be engineered to include modifications within the Fc region, typically to alter one or more functional properties of the antibody, such as serum half-life, complement fixation, Fc receptor binding, and / or antigen-dependent cellular cytotoxicity. Furthermore, a STEAP-1 antibody of the invention may be chemically modified (e.g., one or more chemical moieties can be attached to the antibody) or be modified to alter its glycosylation, again to alter one or more functional properties of the antibody. Each of these embodiments is described in further detail below. In one embodiment, the hinge region of CH1 is modified such that the number of cysteine residues in the hinge region is altered, e.g., increased or decreased. This approach is described further in U.S. Pat. No.5,677,425 by BODMER, et. al. The number of cysteine residues in the hinge region of CH1 is altered to, for example, facilitate assembly of the light and heavy chains or to increase or decrease the stability of the STEAP-1 antibody. In another embodiment, the Fc hinge region of an antibody is mutated to decrease the biological half-life of the STEAP-1 antibody. More specifically, one or more amino acid mutations are introduced into the CH2-CH3 domain interface region of the Fc-hinge fragment such that the antibody has impaired Staphylococcyl protein A (SpA) binding relative to native Fc-hinge domain SpA binding. This approach is described in further detail in U.S. Pat. No.6,165,745 by WARD, et. al. In another embodiment, the STEAP-1 antibody is modified to increase its biological half-life. Various approaches are possible. For example, mutations can be introduced as described in U.S. Pat. No.6,277,375 to Ward. Alternatively, to increase the biological half-life, the antibody can be altered within the CH1 or CL region to contain a salvage receptor binding epitope taken from two loops of a CH2 domain of an Fc region of an IgG, as described in U.S. Pat. Nos.5,869,046 and 6,121,022 by PRESTA et. al. In another embodiment, the STEAP-1 antibody comprises the antibody heavy chain sequence set forth in Table VI(A). In another embodiment, the STEAP-1 antibody comprises the antibody light chain sequence set forth in Table VI(B). In another embodiment, the STEAP-1 antibody comprises the antibody heavy chain variable region sequence(s) set forth in Table VIII. In another embodiment, the STEAP-1 antibody comprises the antibody light chain variable region sequence(s) set forth in Table IX. In another embodiment, the STEAP-1 antibody comprises the antibody CDR sequence(s) set forth in Table X. In another embodiment, the STEAP-1 antibody is conjugated to a therapeutic agent. Reactivity of the STEAP-1 antibodies can be established by a number of well-known means, including Western blot, immunoprecipitation, ELISA, and FACS analyses using, as appropriate, STEAP- 1-related proteins, STEAP-1 expressing cells or extracts thereof. A STEAP-1 antibody or fragment thereof can be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers include, but are not limited to, a radioisotope, a fluorescent compound, a bioluminescent compound, chemiluminescent compound, a metal chelator, or an enzyme. III.) Antibody Drug Conjugates In another aspect, the invention provides antibody-drug conjugates (ADCs), comprising an antibody (preferably a STEAP-1 antibody disclosed herein) conjugated to a therapeutic agent. The therapeutic agent maybe a cytotoxic agent, a cytostatic agent, a chemotherapeutic agent, a drug, a growth inhibitory agent, a toxin (e.g., an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof), or a radioactive isotope (i.e., a radio-conjugate). In another aspect, the invention further provides methods of using the ADCs. In one aspect, an ADC comprises any of the above STEAP-1 antibodies covalently attached or attached via oxime bond to a cytotoxic agent or a detectable agent. In a further embodiment, an ADC comprises a STEAP-1 antibody conjugated to a therapeutic agent using self-hydrolyzing maleimides for cysteine modification (See, WO 2013 / 173337). In a further embodiment, an ADC comprises a STEAP-1 antibody conjugated to a therapeutic agent using a cysteine modification and further comprises reducing the cysteine residue to form a sulfhydryl moiety. In a further embodiment, an ADC comprises a STEAP-1 antibody conjugated to a therapeutic agent using a polypeptide moiety and a self-immolative moiety. In a further embodiment, an ADC comprises a STEAP-1 antibody conjugated to a therapeutic agent wherein the ADC has a high drug antibody ratio (DAR). By way of background, the use of antibody-drug conjugates for the local delivery of cytotoxic or cytostatic agents in the treatment of cancer (SYRIGOS and EPENETOS (1999) Anticancer Research 19:605-614; NICULESCU-DUVAZ and SPRINGER (1997) Adv. Drug Del. Rev.26:151-172; U.S. Pat. No.4,975,278) allows targeted delivery of the drug moiety to tumors, and intracellular accumulation therein, where systemic administration of these unconjugated drug agents may result in unacceptable levels of toxicity to normal cells as well as the tumor cells sought to be eliminated (BALDWIN, et. al., (1986) Lancet pp. (Mar.15, 1986):603-05; THORPE, (1985) “Antibody Carriers of Cytotoxic Agents in Cancer Therapy: A Review,” in Monoclonal Antibodies '84: Biological and Clinical Applications, A. PINCHERA, et. al. (ed.), pp.475-506). Maximal efficacy with minimal toxicity is sought thereby. Both polyclonal antibodies and monoclonal antibodies have been reported as useful in these strategies (ROWLAND, et al., (1986) Cancer Immunol. Immunother., 21:183-87). Drugs used in these methods include daunomycin, doxorubicin, methotrexate, and vindesine (ROWLAND, et. al., (1986) supra). Toxins used in antibody-toxin conjugates include bacterial toxins such as diphtheria toxin, plant toxins such as ricin, small molecule toxins such as geldanamycin (MANDLER, et. al. (2000) Jour. of the Nat. Cancer Inst.92(19):1573-1581; MANDLER, et. al. (2000) Bioorganic & Med. Chem. Letters 10:1025- 1028; MANDLER, et. al. (2002) Bioconjugate Chem.13:786-791), maytansinoids (EP 1391213; LIU, et. al., (1996) Proc. Natl. Acad. Sci. USA 93:8618-8623), and calicheamicin (LODE, et. al. (1998) Cancer Res.58:2928; HINMAN, et. al. (1993) Cancer Res.53:3336-3342). The toxins may affect their cytotoxic and cytostatic effects by mechanisms including tubulin binding, DNA binding, or topoisomerase inhibition. Some cytotoxic drugs tend to be inactive or less active when conjugated to large antibodies or protein receptor ligands. To date, the FDA has approved twelve (12) ADCs, including gemtuzumab ozogamicin (MYLOTARG, Wyeth Pharmaceuticals), which was the first ADC approved by the FDA in 2000. (See, e.g., Drago et al.2021 Nature Reviews 18, 327-344; MCKERTISH, et al., 2021 Biomedicines 9, 872; KHONGORZUI, et al., 2020 Molecular Cancer Res.18:3–19; BROSS, et al., 2001 Clin. Cancer Res.7, 1490–1496; HAMANN, et al., 2002 Bioconjug. Chem.13, 47–58; LAMB, 2017 Drugs 77, 1603–1610.). Additional, examples of commercial antibody drug conjugates are, ADCETRIS (brentuximab vedotin, Seattle Genetics,), ZEVALIN® (ibritumomab tiuxetan, Biogen / Idec), KADCYLA® (ado- trastuzumab emtansine, Genentech), BESPONSA® (inotuzumab ozogamicin, Pfizer / Wyeth), POLIVY (polatuzumab vedotin, Genentech / Roche), Cantuzumab mertansine (Immunogen, Inc.), MLN-2704 (Millennium Pharm., BZL Biologics, Immunogen Inc.), and PADCEV (enfortumab vedotin-ejfv, Seattle Genetics / Astellas (Agensys, Inc., Santa Monica, California). Further, therapeutic agents including but not limited to chemotherapeutic agents useful in the generation of ADCs are described herein. Enzymatically active toxins and fragments thereof that can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. See, e.g., WO 93 / 21232 published Oct.28, 1993. A variety of radionuclides are available for the production of radio-conjugated antibodies. Examples include177Lu,89Zr,212Bi,131I,131In,90Y, and186Re. Conjugates of the antibody and cytotoxic agent are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCl), active esters (such as disuccinimidyl suberate), aldehydes (such as glutaraldehyde), bis-azido compounds (such as bis (p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as toluene 2,6-diisocyanate), and bis- active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). Carbon-14-labeled 1- isothiocyanatobenzyl-3-methyldiethylene triaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for conjugation of radionucleotide to the antibody (WO94 / 11026). Other antitumor agents that can be conjugated to the antibodies of the invention include BCNU, streptozoicin, vincristine and 5-fluorouracil, the family of agents known collectively LL-E33288 complex described in U.S. Pat. Nos.5,053,394, 5,770,710, as well as esperamicins (U.S. Pat. No.5,877,296). Enzymatically active toxins and fragments thereof which can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin, Aleurites fordii proteins, dianthin proteins, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin and the tricothecenes. For example, a ricin immunotoxin can be prepared as described in Vitetta et al (1987) Science, 238:1098. See, for example, WO 93 / 21232 (published Oct.28, 1993). The present invention further contemplates an ADC formed between an antibody and a compound with nucleolytic activity (e.g., a ribonuclease or a DNA endonuclease such as a deoxyribonuclease; DNase). For selective destruction of the tumor, the antibody may comprise a highly radioactive atom. A variety of radioactive isotopes are available for the production of radio-conjugated antibodies. Examples include At211, I131, I125, Y90, Re186, Re88, Sm53, Bi212, P32, Pb212and radioactive isotopes of Lu. When the conjugate is used for detection, it may comprise a radioactive atom for scintigraphic studies, for example tc99mor I123, or a spin label for nuclear magnetic resonance (NMR) imaging (also known as magnetic resonance imaging (MRI)), such as iodine-123 again, iodine-131, indium-111, fluorine-19, carbon-13, nitrogen-15, oxygen-17, gadolinium, manganese, or iron. The radio- or other labels may be incorporated in the conjugate in known ways. For example, the peptide may be biosynthesized or may be synthesized by chemical amino acid synthesis using suitable amino acid precursors involving, for example, fluorine-19 in place of hydrogen. Labels such as tc99mor I123, Re186, Re188and In111can be attached via a cysteine residue in the peptide. Yttrium-90 can be attached via a lysine residue. The IODOGEN method (FRAKER, et. al. (1978) Biochem. Biophys. Res. Commun.80: 49-57 can be used to incorporate iodine-123. “Monoclonal Antibodies in Immunoscintigraphy” (CHATAL, CRC Press 1989) describes other methods in detail. The present invention provides, inter alia, antibody-drug conjugate compounds for targeted delivery of therapeutic agents. The inventors have made the discovery that the antibody-drug conjugate compounds have potent cytotoxic and / or cytostatic activity against cells expressing STEAP-1 and variants thereof. The antibody-drug conjugate compounds comprise an Antibody unit covalently linked to at least one Drug unit. The Drug units can be covalently linked directly to the Antibody unit or via a Linker unit (- LU-). In some embodiments, the antibody drug conjugate compound has the following formula: Ab-(LU-D)pADC Schema (I) or a pharmaceutically acceptable salt or solvate thereof; wherein: • Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; • (LU-D) is a Linker Unit-Drug unit moiety, wherein: • LU- is a Linker unit, and • -D is a drug unit having cytostatic or cytotoxic activity against a target cell; and • p ranges from 1 to 20 or alternatively 1-50. In some embodiments, the antibody drug conjugate compound has the following formula: Ab-(Aa-Ww—Yy-D)pADC Schema (II) or a pharmaceutically acceptable salt or solvate thereof, wherein: • Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; and • -Aa-Ww—Yy— is a Linker unit (LU), wherein: • -A- is a Stretcher unit, • a is 0 or 1 or 2 or 3, • each —W— is independently an Amino Acid unit, • w is an integer ranging from 0 to 12, • —Y— is a self-immolative spacer unit, • y is 0, 1 or 2; • -D is a drug unit having cytostatic or cytotoxic activity against the target cell; and • p is an integer from 1 to 20 or alternatively 1-50. In some embodiments, the antibody drug conjugate compound has the following formula: or a pharmaceutically acceptable salt or solvate thereof, wherein: • Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; • each R is independently selected from N, CH, or C; • R’ is C or CH; • W is selected from: In some embodiments, the antibody drug conjugate compound has the following formula: • Ab is the antibody unit, e.g., anti-STEAP-1 antibody of the present invention. • Each R is independently selected from N, CH, or C. • W is selected from: • Xbis a spacer moiety selected from the group consisting of an alkyl, a heteroalkyl, polyethylene glycol (PEG), and a peptide. • b is 0, 1 or 2. • Ybis a polypeptide moiety that comprises about 1 to about 6 amino acids that are natural and / or unnatural amino acids. • Zbis a self-immolative moiety including but not limited to: • D is a drug unit having cytostatic or cytotoxic activity against the target cell. • p is an integer from 1 to 20 or alternatively 1-50. In some embodiments, the antibody drug conjugate compound has the following formula: ADC Schema (VII) or a pharmaceutically acceptable salt or solvate thereof, wherein: • Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; R1 • is , wherein R2is a unsubstituted or substituted C1-C6alkyl, heteroalkyl, cycloalkyl or cycloheteroalkyl; • each of Rxand Ryis independently selected from R and L-Rz, provided that when one of Rxand Ryis NRz, the other is R; • R5is H or CR’3, wherein each R’ is independently H or F; • R6is H or CH2CN; • LU is a linker unit; and • R is H or a C1-C3alkyl; and • i is an integer in the range of 1 to about 20. In some embodiments, the antibody drug conjugate compound has the following formula: ADC Schema (XIII) or a pharmaceutically acceptable salt or solvate thereof, wherein: Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; 1 R is , wherein R2is a unsubstituted or substituted C1-C6alkyl, heteroalkyl, cycloalkyl or cycloheteroalkyl; each of Rxand Ryis independently selected from R and L-Rz, provided that when one of Rxand Ryis NRz, the other is R; R5is H or CR’3, wherein each R’ is independently H or F; R6is H or CH2CN; LU is a linker unit; and R is H or a C1-C3alkyl; and j is an integer in the range of 1 to about 20. In some embodiments, the antibody drug conjugate compound has the following formula: ADC Schema (IX) or a pharmaceutically acceptable salt or solvate thereof, wherein: Ab is the Antibody unit, e.g., a STEAP-1 antibody of the present invention; 1 R is , wherein R2is a unsubstituted or substituted C1-C6alkyl, heteroalkyl, cycloalkyl or cycloheteroalkyl; each of Rxand Ryis independently selected from R and L-Rz, provided that when one of Rxand Ryis NRz, the other is R; R5is H or CR’3, wherein each R’ is independently H or F; R6is H or CH2CN; LU is a linker unit; and R is H or a C1-C3alkyl; and k is an integer in the range of 1 to about 20. In some embodiments, the antibody drug conjugate compound has the following formula: • R1isO wherein R2 is a substituted or unsubstituted C1-C6 alkyl, heteroalkyl, cycloalkyl orcycloheteroalkyl; • R3is H or a C1-C3alkyl; • R5is H or CR’3wherein each R’ is independently H or F; • R6is H or CH2CN; • Ab is the antibody unit, e.g., anti-STEAP-1 antibody of the present invention. • Each R is independently selected from N, CH, or C. • J is a conjugation moiety. • Xbis a spacer moiety selected from the group consisting of an alkyl, a heteroalkyl, polyethylene glycol (PEG), and a peptide. • b is 0, 1 or 2. • Ybis a polypeptide moiety that comprises about 1 to about 6 amino acids that are natural and / or unnatural amino acids. • Zbis a self-immolative moiety including but not limited to: For compositions comprising a plurality of antibodies, the drug loading is represented by p, the average number of drug molecules per Antibody. Drug loading may range from 1 to 24 drugs (D) per Antibody. The average number of drugs per antibody in preparation of conjugation reactions may be characterized by conventional means such as mass spectroscopy, ELISA assay, and HPLC. The quantitative distribution of Antibody-Drug-Conjugates in terms of p may also be determined. In some instances, separation, purification, and characterization of homogeneous Antibody-Drug-conjugates where p is a certain value from Antibody-Drug-Conjugates with other drug loadings may be achieved by means such as reverse phase HPLC or electrophoresis. In exemplary embodiments, p is from 2 to 8. In some embodiments, p is from 2 to 24. The generation of Antibody-drug conjugate compounds can be accomplished by any technique known to the skilled artisan. Briefly, the Antibody-drug conjugate compounds comprise STEAP-1 antibodies. In one embodiment, the STEAP-1 ADC comprises the antibody heavy chain sequence set forth in Table VI(A). In another embodiment, the STEAP-1 ADC comprises the antibody light chain sequence set forth in Table VI(B). In another embodiment, the STEAP-1 ADC comprises the antibody heavy chain variable region sequence(s) set forth in Table VIII. In another embodiment, the STEAP-1 ADC comprises the antibody light chain variable region sequence(s) set forth in Table IX. In another embodiment, the STEAP-1 ADC comprises the antibody CDR sequence(s) set forth in Table X. In another embodiment, the aforementioned STEAP-1 antibodies are conjugated to a therapeutic agent. In one embodiment, the therapeutic agent is a Drug-Linker (DL) payload set forth in Figure 12. In one embodiment, the DL payload is set forth in Figure 12(A) and has the following chemical structure: ADL-32-132 or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(B) and has the following chemical structure: or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(C) and has the following chemical structure: ADL-79-103 or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(D) and has the following chemical structure: Mall--AA- -PABC- -PC- -exxatteccan or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(E) and has the following chemical structure: Maall--GGFG --PABC--eexxaatteeccaann or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(F) and has the following chemical structure: Mal-AA-PABC-gluc-exatecan or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 12(G) and has the following chemical structure: In one embodiment, the DL payload is set forth in Figure 12(H) and has the following chemical structure: In one embodiment, the DL payload is set forth in Figure 12(I) and has the following chemical structure: In one embodiment, the DL payload is set forth in Figure 12(J) and has the following chemical structure: In one embodiment, the DL payload is set forth in Figure 13(A) and has the following chemical structure: or a pharmaceutically acceptable salt or solvate form thereof. In one embodiment, the DL payload is set forth in Figure 13(B) and has the following chemical structure: MC-vcMMAE or a pharmaceutically acceptable salt or solvate form thereof. A number of different reactions are available for covalent attachment of drugs and / or linkers to binding agents. This is often accomplished by reaction of the amino acid residues of the binding agent, e.g., antibody molecule, including the amine groups of lysine, the free carboxylic acid groups of glutamic and aspartic acid, the sulfhydryl groups of cysteine and the various moieties of the aromatic amino acids. One of the most commonly used non-specific methods of covalent attachment is the carbodiimide reaction to link a carboxy (or amino) group of a compound to amino (or carboxy) groups of the antibody. Additionally, bifunctional agents such as dialdehydes or imidoesters have been used to link the amino group of a compound to amino groups of an antibody molecule. Also available for attachment of drugs to binding agents is the Schiff base reaction. This method involves the periodate oxidation of a drug that contains glycol or hydroxy groups, thus forming an aldehyde which is then reacted with the binding agent. Attachment occurs via formation of a Schiff base with amino groups of the binding agent. Isothiocyanates can also be used as coupling agents for covalently attaching drugs to binding agents. Other techniques are known to the skilled artisan and within the scope of the present invention. In certain embodiments, an intermediate, which is the precursor of the linker, is reacted with the drug under appropriate conditions. In certain embodiments, reactive groups are used on the drug and / or the intermediate. The product of the reaction between the drug and the intermediate, or the derivatized drug, is subsequently reacted with the STEAP-1 antibodies under appropriate conditions. IV.) Linker Units Typically, the antibody-drug conjugate compounds comprise a Linker unit between the drug unit and the antibody unit. In some embodiments, the linker is cleavable under intracellular conditions, such that cleavage of the linker releases the drug unit from the antibody in the intracellular environment. In yet other embodiments, the linker unit is not cleavable, and the drug is released, for example, by antibody degradation. In a preferred embodiment, the linker is conjugated to a STEAP-1 antibody described herein. In some embodiments, the linker is cleavable by a cleaving agent that is present in the intracellular environment (e.g., within a lysosome or endosome or caveolea). The linker can be, e.g., a peptidyl linker that is cleaved by an intracellular peptidase or protease enzyme, including, but not limited to, a lysosomal or endosomal protease. The linker can also be cleaved by a cleaving agent that is present in the extracellular environment (e.g., in the vicinity to the cellular membrane or tissue space). The linker can be, e.g., a peptidyl linker that is cleaved by an extracellular peptidase or protease enzyme, including, but not limited to, a cathepsin family enzyme or matrix metalloproteinases). In other embodiments, the cleavable linker is pH-sensitive, i.e., sensitive to hydrolysis at certain pH values. Typically, the pH-sensitive linker hydrolyzable under acidic conditions. For example, an acid- labile linker that is hydrolyzable in the lysosome (e.g., an oxime, hydrazone, semi-carbazone, thiosemicarbazone, cis-aconitic amide, ortho ester, acetal, ketal, or the like) can be used. (See, e.g., U.S. Pat. Nos.5,122,368; 5,824,805; 5,622,929; DUBOWCHIK AND WALKER, 1999, Pharm. Therapeutics 83:67-123; NEVILLE et. al., 1989, Biol. Chem.264:14653-14661.) In yet other embodiments, the linker is cleavable under reducing conditions known in the art. (See, e.g., Thorpe et al., 1987, Cancer Res.47:5924-5931; WAWRZYNCZAK et. al., In Immunoconjugates: Antibody Conjugates in Radioimagery and Therapy of Cancer (C. W. VOGEL ed., Oxford U. Press, 1987. See also U.S. Pat. No.4,880,935.). The linker can also be cleaved under reducing conditions found intra-cellularly (or extra-cellularly). For example, in a preferred embodiment, the specific linker N—O bond may be formally reduced and broken to result in a cleavage of the linker. In yet other specific embodiment, the linker is a malonate linker (Johnson et al., 1995, Anticancer Res.15:1387-93), a maleimidobenzoyl linker (LAU, et al., 1995, Bioorg-Med- Chem.3(10):1299-1304), or a 3′-N-amide analog (LAU, et al., 1995, Bioorg-Med-Chem.3(10):1305-12). In yet other embodiments, the linker unit is not cleavable, and the drug is released by antibody degradation. (See, PCT Publication No. WO2012 / 166560 (Ambrx, Inc.) incorporated by reference herein in its entirety and for all purposes). Typically, the linker is not substantially sensitive to the extracellular environment. As used herein, “not substantially sensitive to the extracellular environment,” in the context of a linker, means that no more than about 20%, typically no more than about 15%, more typically no more than about 10%, and even more typically no more than about 5%, no more than about 3%, or no more than about 1% of the linkers, in a sample of antibody-drug conjugate compound, are cleaved when the antibody- drug conjugate compound presents in an extracellular environment (e.g., in plasma). Whether a linker is not substantially sensitive to the extracellular environment can be determined, for example, by incubating with plasma the antibody-drug conjugate compound for a predetermined time period (e.g., 2, 4, 8, 16, or 24 hours) and then quantitating the amount of free drug present in the plasma. In other, non-mutually exclusive embodiments, the linker promotes cellular internalization as known in the art. A variety of exemplary linkers that can be used with the present compositions and methods are described in WO 2004 / 010957, U.S. Publication No.2006 / 0074008, U.S. Publication No.20050238649, and U.S. Publication No.2006 / 0024317 (each of which is incorporated by reference herein in its entirety and for all purposes). For the purposes of the disclosure, a “Linker unit” (LU) is a bifunctional compound that can be used to link a Drug unit and an Antibody unit to form an antibody-drug conjugate compound. In some embodiments, the Linker unit has the formula: -Aa-Ww—Yy— o wherein: -A- is a Stretcher unit, o a is 0 or 1, o each —W— is independently an Amino Acid unit, o w is an integer ranging from 0 to 12, o —Y— is a self-immolative Spacer unit, and o y is 0, 1 or 2. In some embodiments, a is 0 or 1, w is 0 or 1, and y is 0, 1 or 2. In some embodiments, a is 0 or 1, w is 0 or 1, and y is 0 or 1. In some embodiments, when w is 1 to 12, y is 1 or 2. In some embodiments, w is 2 to 12 and y is 1 or 2. In some embodiments, a is 1 and w and y are 0. V.) The Stretcher Unit The Stretcher unit (A), when present, is capable of linking an Antibody unit to an Amino Acid unit (—W—), if present, to a Spacer unit (—Y—), if present; or to a Drug unit (-D). Useful functional groups that can be present on a STEAP-1 antibody, either naturally or via chemical manipulation include, but are not limited to, keto, aldehyde, sulfhydryl, amino, hydroxyl, the anomeric hydroxyl group of a carbohydrate, and carboxyl. Suitable functional groups are keto, aldehyde, sulfhydryl, and amino. In one example, the keto group is on a non-natural amino acid (nnAA) incorporated into the antibody of the invention. In a further example, the aldehyde group is on a nnAA incorporated into the antibody of the invention. In another example, sulfhydryl groups can be generated by reduction of the intramolecular disulfide bonds of a STEAP-1 antibody. In another embodiment, sulfhydryl groups can be generated by reaction of an amino group of a lysine moiety of a STEAP-1 antibody with 2-iminothiolane (Traut's reagent) or other sulfhydryl generating reagents. In certain embodiments, the STEAP-1 antibody is a recombinant antibody and is engineered to carry one or more lysines. In certain other embodiments, the recombinant STEAP-1antibody is engineered to carry additional sulfhydryl groups, e.g., additional cysteines. In one embodiment, the Stretcher unit forms a bond with a sulfur atom of the Antibody unit. The sulfur atom can be derived from a sulfhydryl group of an antibody. In certain embodiments, the Stretcher unit is linked to the Antibody unit via a disulfide bond between a sulfur atom of the Antibody unit and a sulfur atom of the Stretcher unit. In yet other embodiments, the Stretcher contains a reactive site that can form a bond with a primary or secondary amino group of an antibody. Examples of these reactive sites include, but are not limited to, activated esters such as succinimide esters, 4 nitrophenyl esters, pentafluorophenyl esters, tetrafluorophenyl esters, anhydrides, acid chlorides, sulfonyl chlorides, isocyanates and isothiocyanates. In some embodiments, the Stretcher contains a reactive site that is reactive to a modified carbohydrate's (—CHO) group that can be present on an antibody. For example, a carbohydrate can be mildly oxidized using a reagent such as sodium periodate and the resulting (—CHO) unit of the oxidized carbohydrate can be condensed with a Stretcher that contains a functionality such as a hydrazide, an oxime, a primary or secondary amine, a hydrazine, a thiosemicarbazone, a hydrazine carboxylate, and an arylhydrazide such as those described by KANEKO, et al., 1991, Bioconjugate Chem.2:133-41. VI.) The Amino Acid Unit The Amino Acid unit (—W—), when present, links the Stretcher unit to the Spacer unit if the Spacer unit is present, links the Stretcher unit to the Drug moiety if the Spacer unit is absent, and links the Antibody unit to the Drug unit if the Stretcher unit and Spacer unit are absent. In certain embodiments, the Amino Acid unit can comprise natural amino acids. In other embodiments, the Amino Acid unit can comprise non-natural amino acids. In some embodiments, the Amino Acid unit can be enzymatically cleaved by one or more enzymes, including a cancer or tumor-associated protease, to liberate the Drug unit (-D), which in one embodiment is protonated in vivo upon release to provide a Drug (D). In one aspect of the Amino Acid unit, the Amino Acid unit is valine-citrulline (denoted “vc” or “Val-Cit”). In another aspect, the Amino Acid unit is phenylalanine-lysine. In yet another aspect of the Amino Acid unit, the Amino Acid unit is N-methylvaline-citrulline. In yet another aspect, the Amino Acid unit is 5-aminovaleric acid, homo phenylalanine lysine, tetraisoquinolinecarboxylate lysine, cyclohexylalanine lysine, isonepecotic acid lysine, beta-alanine lysine, glycine serine valine glutamine and isonepecotic acid. VII.) The Spacer Unit The Spacer unit (—Y—), when present, links an Amino Acid unit to the Drug unit when an Amino Acid unit is present. Alternately, the Spacer unit links the Stretcher unit to the Drug unit when the Amino Acid unit is absent. The Spacer unit also links the Drug unit to the Antibody unit when both the Amino Acid unit and Stretcher unit are absent. Spacer units are of two general types: non self- immolative or self-immolative. Examples of possible spacers of the invention are known in the art. See, TOKI, et. al., 2002, J. Org. Chem.67:1866-1872 and Nature Biotechnology 21(7):778-784). Other examples of self-immolative spacers include, but are not limited to, aromatic compounds that are electronically similar to the PAB group such as 2-aminoimidazol-5-methanol derivatives (HAY, et. al., 1999, Bioorg. Med. Chem. Lett.9:2237) and ortho or para-aminobenzylacetals. Spacers can be used that undergo cyclization upon amide bond hydrolysis, such as substituted and unsubstituted 4-aminobutyric acid amides (RODRIGUES, et. al., 1995, Chemistry Biology 2:223), appropriately substituted bicyclo[2.2.1] and bicyclo[2.2.2] ring systems (STORM, et. al., 1972, J. Amer. Chem. Soc.94:5815) and 2-aminophenylpropionic acid amides (AMSBERRY, et. al., 1990, J. Org. Chem.55:5867). Elimination of amine-containing drugs that are substituted at the a-position of glycine (KINGSBURY, et. al., 1984, J. Med. Chem.27:1447) are also examples of self-immolative spacers. VIII.) The Drug Unit The Drug moiety (D) can be any cytotoxic, cytostatic, or immunomodulatory (e.g., immunosuppressive) drug. (D) is a Drug unit (moiety) having an atom that can form a bond with the Spacer unit, with the Amino Acid unit, with the Stretcher unit, or with the Antibody unit. In some embodiments, the Drug unit (D) has a nitrogen atom that can form a bond with the Spacer unit. As used herein, the terms “Drug unit” and “Drug moiety” are synonymous and used interchangeably. Useful classes of cytotoxic, cytostatic, or immunomodulatory agents include, for example, antitubulin agents, DNA minor groove binders, DNA replication inhibitors, and alkylating agents. In some embodiments, the Drug is an auristatin, such as auristatin E (also known in the art as a derivative of dolastatin-10) or a derivative thereof. The auristatin can be, for example, an ester formed between auristatin E and a keto acid. For example, auristatin E can be reacted with paraacetyl benzoic acid or benzoylvaleric acid to produce AEB and AEVB, respectively. In some embodiments, the Drug Unit is a calicheamicin, camptothecin, a maytansinoid, or an anthracycline. In some embodiments the drug is a taxane, a topoisomerase inhibitor, a vinca alkaloid. In some typical embodiments, suitable cytotoxic agents include, for example, DNA minor groove binders (e.g., enediynes and lexitropsins, a CBI compound; see also U.S. Pat. No.6,130,237), duocarmycins, taxanes (e.g., paclitaxel and docetaxel), puromycins, and vinca alkaloids. Other cytotoxic agents include, for example, CC-1065, SN-38, topotecan, morpholino-doxorubicin, rhizoxin, cyanomorpholino-doxorubicin, echinomycin, combretastatin, netropsin, epothilone A and B, estramustine, cryptophysins, cemadotin, maytansinoids, discodermolide, eleutherobin, and mitoxantrone. In some embodiments, the Drug is an anti-tubulin agent. Examples of anti-tubulin agents include, auristatins, taxanes (e.g., Taxol® (paclitaxel), Taxotere® (docetaxel)), T67 (Tularik) and vinca alkyloids (e.g., vincristine, vinblastine, vindesine, and vinorelbine). Other antitubulin agents include, for example, baccatin derivatives, taxane analogs (e.g., epothilone A and B), nocodazole, colchicine and colcimid, estramustine, cryptophycins, cemadotin, maytansinoids, combretastatins, discodermolide, and eleutherobin. In certain embodiments, the cytotoxic agent is a maytansinoid, another group of anti-tubulin agents. For example, in specific embodiments, the maytansinoid is maytansine or DM-1 (ImmunoGen, Inc.; see also Chari et al., 1992, Cancer Res.52:127-131). In certain embodiments, the cytotoxic or cytostatic agent is a dolastatin. In certain embodiments, the cytotoxic or cytostatic agent is of the auristatin class, for example, Dolastatin-10, Auristatin e, or Auristatin PHE, etc. In certain embodiments, the Drug Unit (D) is an auristatin analog having the following structural formula: or a pharmaceutically acceptable salt thereof, wherein R1is , wherein R2is a unsubstituted or substituted C1-C6alkyl, heteroalkyl, cycloalkyl or cycloheteroalkyl; each of Ra, Rband Rcis selected from H and NRxRy, provided that only one of Ra, Rband Rcis NRxRyand each of the others is H; each of Rxand Ryis independently selected from R, Rrand L-Rz, provided that when one of Rxand Ryis L-Rzor Rr, the other is R; R5is H or CR’3, wherein each R’ is independently H or F; R6is H or CH2CN; L is a linker; Rris (C=O)-O-(CH2)p-Rvor (C=O)-(CH2)q-Rv; Rvis R, OR, NHR, NR2, an aryl group or an amino acid; p is 0, 1, 2, 3, 4, 5 or 6; q is 0, 1, 2, 3, 4, 5 or 6; Rzcomprises a functional or reactive group; and R is H or a C1-C3alkyl. IX.) Drug Loading Drug loading is represented by p and is the average number of Drug moieties per antibody in a molecule. Drug loading may range from 1 to 24 drug moieties (D) per antibody. ADCs of the invention include collections of antibodies conjugated with a range of drug moieties, from 1 to 24. The average number of drug moieties per antibody in preparations of ADC from conjugation reactions may be characterized by conventional means such as mass spectroscopy and, ELISA assay. The quantitative distribution of ADC in terms of p may also be determined. In some instances, separation, purification, and characterization of homogeneous ADC where p is a certain value from ADC with other drug loadings may be achieved by means such as electrophoresis. For some antibody-drug conjugates, p may be limited by the number of attachment sites on the antibody. For example, where the attachment is a cysteine thiol, as in the exemplary embodiments above, an antibody may have only one or several cysteine thiol groups, or may have only one or several sufficiently reactive thiol groups through which a linker may be attached. In certain embodiments, higher drug loading, e.g., p>5, may cause aggregation, insolubility, toxicity, or loss of cellular permeability of certain antibody-drug conjugates. In certain embodiments, the drug loading for an ADC of the invention ranges from 1 to about 8; from about 2 to about 6; from about 3 to about 5; from about 3 to about 4; from about 3.1 to about 3.9; from about 3.2 to about 3.8; from about 3.2 to about 3.7; from about 3.2 to about 3.6; from about 3.3 to about 3.8; or from about 3.3 to about 3.7. Indeed, it has been shown that for certain ADCs, the optimal ratio of drug moieties per antibody may be less than 8 and may be about 2 to about 5. See U.S. Pat. No.7,498,298 (herein incorporated by reference in its entirety). In certain embodiments, fewer than the theoretical maximum of drug moieties are conjugated to an antibody during a conjugation reaction. An antibody may contain, for example, lysine residues that do not react with the drug-linker intermediate or linker reagent, as discussed below. Generally, antibodies do not contain many free and reactive cysteine thiol groups which may be linked to a drug moiety; indeed, most cysteine thiol residues in antibodies exist as disulfide bridges. In certain embodiments, an antibody may be reduced with a reducing agent such as dithiothreitol (DTT) or tricarbonylethylphosphine (TCEP), under partial or total reducing conditions, to generate reactive cysteine thiol groups. In certain embodiments, an antibody is subjected to denaturing conditions to reveal reactive nucleophilic groups such as lysine or cysteine. The loading (drug to antibody ratio) of an ADC may be controlled in different ways, e.g., by: (i) limiting the molar excess of drug-linker intermediate or linker reagent relative to antibody, (ii) limiting the conjugation reaction time or temperature, (iii) partial or limiting reductive conditions for cysteine thiol modification, (iv) engineering by recombinant techniques the amino acid sequence of the antibody such that the number and position of cysteine residues is modified for control of the number and / or position of linker-drug attachments (such as thioMab or thioFab prepared as disclosed herein and in WO2006 / 034488 (herein incorporated by reference in its entirety)). It is to be understood that where more than one nucleophilic group reacts with a drug-linker intermediate or linker reagent followed by drug moiety reagent, then the resulting product is a mixture of ADC compounds with a distribution of one or more drug moieties attached to an antibody. The average number of drugs per antibody may be calculated from the mixture by a dual ELISA antibody assay, which is specific for antibody and specific for the drug. Individual ADC molecules may be identified in the mixture by mass spectroscopy and separated by HPLC, e.g. hydrophobic interaction chromatography (see, e.g., HAMBLETT, K. J., et al., “Effect of drug loading on the pharmacology, pharmacokinetics, and toxicity of an anti-CD30 antibody-drug conjugate,” Abstract No.624, American Association for Cancer Research, 2004 Annual Meeting, Mar.27-31, 2004, Proceedings of the AACR, Volume 45, March 2004; ALLEY, S.C., et al., “Controlling the location of drug attachment in antibody-drug conjugates,” Abstract No.627, American Association for Cancer Research, 2004 Annual Meeting, Mar.27-31, 2004, Proceedings of the AACR, Volume 45, March 2004). In certain embodiments, a homogeneous ADC with a single loading value may be isolated from the conjugation mixture by electrophoresis or chromatography. X.) Methods of Determining Cytotoxic Effect of ADCs Methods of determining whether a Drug or Antibody-Drug conjugate exerts a cytostatic and / or cytotoxic effect on a cell are known. Generally, the cytotoxic or cytostatic activity of an ADC can be measured by: (i) exposing mammalian cells expressing a target protein of the Antibody Drug conjugate in a cell culture medium; (ii) culturing the cells for a period from about 6 hours to about 5 days; and (iii) measuring cell viability. Cell-based in vitro assays can be used to measure viability (proliferation), cytotoxicity, and induction of apoptosis (caspase activation) of the Antibody Drug Conjugate. For determining whether an ADC exerts a cytostatic effect, a thymidine incorporation assay may be used. For example, cancer cells expressing a target antigen at a density of 5,000 cells / well of a 96-well plated can be cultured for a 72-hour period and exposed to 0.5 μCi of3H-thymidine during the final 8 hours of the 72-hour period. The incorporation of3H-thymidine into cells of the culture is measured in the presence and absence of the ADC. For determining cytotoxicity, necrosis, or apoptosis (programmed cell death) can be measured. Necrosis is typically accompanied by increased permeability of the plasma membrane; swelling of the cell, and rupture of the plasma membrane. Apoptosis is typically characterized by membrane blebbing, condensation of cytoplasm, and the activation of endogenous endonucleases. Determination of any of these effects on cancer cells indicates that an ADC is useful in the treatment of cancers. Cell viability can be measured by determining in a cell the uptake of a dye such as neutral red, trypan blue, or ALAMAR™ blue (see, e.g., PAGE, et. al., 1993, Intl. J. Oncology 3:473-476). In such an assay, the cells are incubated in media containing the dye, the cells are washed, and the remaining dye, reflecting cellular uptake of the dye, is measured spectrophotometrically. The protein-binding dye sulforhodamine B (SRB) can also be used to measure cytoxicity (SKEHAN, et. al., 1990, J. Natl. Cancer Inst.82:1107-12). Alternatively, a tetrazolium salt, such as MTT, or CellTiter-Glo^, is used in a quantitative assay for mammalian cell survival and proliferation by detecting living, but not dead, cells (see, e.g., MOSMANN, 1983, J. Immunol. Methods 65:55-63). Apoptosis can be quantitated by measuring, for example, DNA fragmentation. Commercial photometric methods for the quantitative in vitro determination of DNA fragmentation are available. Examples of such assays, including TUNEL (which detects incorporation of labeled nucleotides in fragmented DNA) and ELISA-based assays, are described in Biochemica, 1999, no.2, pp.34-37 (Roche Molecular Biochemicals). Apoptosis can also be determined by measuring morphological changes in a cell. For example, as with necrosis, loss of plasma membrane integrity can be determined by measuring the uptake of certain dyes (e.g., a fluorescent dye such as, for example, acridine orange or ethidium bromide). A method for measuring apoptotic cell number has been described by Duke and Cohen, Current Protocols in Immunology (COLIGAN, et. al., eds., 1992, pp.3.17.1-3.17.16). Cells also can be labeled with a DNA dye (e.g., acridine orange, ethidium bromide, or propidium iodide) and the cells observed for chromatin condensation and margination along the inner nuclear membrane. Other morphological changes that can be measured to determine apoptosis include, e.g., cytoplasmic condensation, increased membrane blebbing, and cellular shrinkage. The presence of apoptotic cells can be measured in both the attached and “floating” compartments of the cultures. For example, both compartments can be collected by removing the supernatant, trypsinizing the attached cells, combining the preparations following a centrifugation wash step (e.g., 10 minutes at 2000 rpm), and detecting apoptosis (e.g., by measuring DNA fragmentation). (See, e.g., PIAZZA, et. al., 1995, Cancer Research 55:3110-16). In vivo, the effect of a STEAP-1 antibody therapeutic composition can be evaluated in a suitable animal model. For example, xenogeneic cancer models can be used, wherein cancer explants or passaged xenograft tissues are introduced into immune compromised animals, such as nude or SCID mice (KLEIN, et. al., 1997, Nature Medicine 3: 402-408). For example, PCT Patent Application WO98 / 16628 and U.S. Pat. No.6,107,540 describe various xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micro-metastasis, and the formation of osteoblastic metastases characteristic of late-stage disease. Efficacy can be predicted using assays that measure inhibition of tumor formation, tumor regression or metastasis, and the like. In vivo assays that evaluate the promotion of apoptosis are useful in evaluating therapeutic compositions. In one embodiment, xenografts from tumor bearing mice treated with therapeutic composition can be examined for the presence of apoptotic foci and compared to untreated control xenograft-bearing mice. The extent to which apoptotic foci are found in the tumors of the treated mice provides an indication of the therapeutic efficacy of the composition. The therapeutic compositions used in the practice of the foregoing methods can be formulated into pharmaceutical compositions comprising a carrier suitable for the desired delivery method. Suitable carriers include any material that when combined with the therapeutic composition retains the anti-tumor function of the therapeutic composition and is generally non-reactive with the patient's immune system. Examples include, but are not limited to, any of a number of standard pharmaceutical carriers such as sterile phosphate buffered saline solutions, bacteriostatic water, and the like (See, generally, Remington's Pharmaceutical Sciences, 16th Edition, A. Osal., Ed., 1980). Therapeutic formulations can be solubilized and administered via any route capable of delivering the therapeutic composition to the tumor site. Potentially effective routes of administration include, but are not limited to, intravenous, parenteral, intraperitoneal, intramuscular, intratumor, intradermal, intra-organ, orthotopic, and the like. A preferred formulation for intravenous injection comprises the therapeutic composition in a solution of preserved bacteriostatic water, sterile unpreserved water, and / or diluted in polyvinylchloride or polyethylene bags containing 0.9% sterile Sodium Chloride for Injection, USP. Therapeutic protein preparations can be lyophilized and stored as sterile powders, preferably under vacuum, and then reconstituted in bacteriostatic water (containing for example, benzyl alcohol preservative) or in sterile water prior to injection. Dosages and administration protocols for the treatment of cancers using the foregoing methods will vary with the method and the target cancer, and will generally depend on a number of other factors appreciated in the art. In one embodiment, the pharmaceutical composition of the present invention may comprise more than one species of ADC of the invention due to modification of a STEAP-1 antibody. For example, the present invention includes a pharmaceutical composition comprising the ADC of the invention, wherein the STEAP-1 antibody is an antibody with a C-terminal lysine partially removed or completely removed an antibody having N-terminal post-translational modification, an antibody lacking heavy chain C-terminal lysine and having N-terminal post-translational modification, and / or an antibody having heavy chain C-terminal lysine and not having N-terminal post-translational modification. In a preferred embodiment, STEAP-1 antibody is set forth in Table(s) VI and Table VII. XI.) Treatment of Cancer(s) Expressing STEAP-1 The identification of STEAP-1 as a protein that is normally expressed in a restricted set of tissues or cells, but which is also expressed in cancers such as those listed in Table I, opens a number of therapeutic approaches to the treatment of such cancers. Of note, targeted antitumor therapies have been useful even when the targeted protein is expressed on normal tissues or cells, even vital normal organ tissues. A vital organ is one that is necessary to sustain life, such as the heart or colon. A non-vital organ is one that can be removed whereupon the individual is still able to survive. Examples of non-vital organs are ovary, breast, and prostate. Expression of a target protein in normal tissue, even vital normal tissue, does not defeat the utility of a targeting agent for the protein as a therapeutic for certain tumors in which the protein is also overexpressed. For example, expression in vital organs is not in and of itself detrimental. In addition, organs regarded as dispensable, such as the prostate and ovary, can be removed without affecting mortality. Finally, some vital organs are not affected by normal organ expression because of an immunoprivilege. Immunoprivileged organs are organs that are protected from blood by a blood-organ barrier and thus are not accessible to immunotherapy. Examples of immunoprivileged organs are the brain and testis. Accordingly, therapeutic approaches that inhibit the activity of a STEAP-1 protein are useful for patients suffering from cancer that expresses STEAP-1 (such as, for example, those cancers set forth in Table I). These therapeutic approaches generally fall into three classes. The first class modulates STEAP-1 function as it relates to tumor cell growth leading to inhibition or retardation of tumor cell growth or inducing its killing. The second class comprises various methods for inhibiting the binding or association of a STEAP-1 protein with its binding partner or with other proteins. The third class comprises a variety of methods for inhibiting the transcription of a STEAP-1 gene or translation of STEAP-1 mRNA. Accordingly, cancer patients can be evaluated for the presence and level of STEAP-1 expression, preferably using immunohistochemical assessments of tumor tissue, quantitative STEAP-1 imaging, or other techniques that reliably indicate the presence and degree of STEAP-1 expression. Immunohistochemical analysis of tumor biopsies or surgical specimens is preferred for this purpose, if applicable. Methods for immunohistochemical analysis of tumor tissues are well known in the art. XII.) STEAP-1 ADC Cocktails Therapeutic methods of the invention contemplate the administration of single STEAP-1 ADCs as well as combinations, or cocktails, of different antibodies (i.e., STEAP-1 antibodies or antibodies that bind another protein). Such antibody cocktails can have certain advantages in as much as they contain antibodies that target different epitopes, exploit different effector mechanisms, or combine directly cytotoxic antibodies with antibodies that rely on immune effector functionality. Such antibodies in combination can exhibit synergistic therapeutic effects. In addition, STEAP-1 antibodies can be administered concomitantly with other therapeutic modalities, including but not limited to various chemotherapeutic and biologic agents, androgen-blockers, immune modulators (e.g., IL-2, GM-CSF, PD1, PD-L1), surgery or radiation. In a preferred embodiment, the STEAP-1 antibodies are administered in conjugated form. In a further preferred embodiment, the STEAP-1 antibodies are set forth in Table VI and Table VII. STEAP-1 ADC formulations are administered via any route capable of delivering the antibodies to a tumor cell. Routes of administration include, but are not limited to, intravenous, intraperitoneal, intramuscular, intratumor, intradermal, and the like. Treatment generally involves repeated administration of the STEAP-1 ADC preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range, including but not limited to, 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, or 25 mg / kg body weight. In general, doses in the range of 10-1000 mg MAb per week are effective and well tolerated. Based on clinical experience with the Herceptin® (Trastuzumab) in the treatment of metastatic breast cancer, an initial loading dose of approximately 4 mg / kg patient body weight IV, followed by weekly doses of about 2 mg / kg IV of the MAb preparation represents an acceptable dosing regimen. Preferably, the initial loading dose is administered as a 90-minute or longer infusion. The periodic maintenance dose is administered as a 30 minute or longer infusion, provided the initial dose was well tolerated. As appreciated by those of skill in the art, numerous factors can influence the ideal dose regimen in a particular case. Such factors include, for example, the binding affinity and half-life of the antibodies used, the degree of STEAP-1 expression in the patient, the extent of circulating shed STEAP-1 antigen, the desired steady-state antibody concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Optionally, patients should be evaluated for the levels of STEAP-1 in a given sample (e.g., the levels of circulating STEAP-1 antigen and / or STEAP-1 expressing cells) in order to assist in the determination of the most effective dosing regimen, etc. Such evaluations are also used for monitoring purposes throughout therapy and are useful to gauge therapeutic success in combination with the evaluation of other parameters (for example, urine cytology and / or ImmunoCyt levels in bladder cancer therapy, or by analogy, serum PSA levels in prostate cancer therapy). An object of the present invention is to provide STEAP-1 ADCs, which inhibit or retard the growth of tumor cells expressing STEAP-1. A further object of this invention is to provide methods to inhibit angiogenesis and other biological functions and thereby reduce tumor growth in mammals, preferably humans, using such STEAP-1 ADCs, and in particular using such STEAP-1 ADCs combined with other drugs or immunologically active treatments. XIII.) Combination Therapy In one embodiment, there is synergy when tumors, including human tumors, are treated with STEAP-1 ADCs in conjunction with chemotherapeutic agents or other targeted cancer drug(s) or radiation or combinations thereof. In other words, the inhibition of tumor growth by a STEAP-1 ADC is enhanced more than expected when combined with chemotherapeutic agents or other targeted cancer drug(s) or radiation or combinations thereof. Synergy may be shown, for example, by greater inhibition of tumor growth with combined treatment than would be expected from a treatment of only STEAP-1 ADC or the additive effect of treatment with a STEAP-1 ADC and a chemotherapeutic agent or other targeted cancer drug(s) or radiation. One of skill in the art will understand that the specific combination of therapeutic modality used will be primarily based on the STEAP-1 expression profile and the type of cancer for any particular patient. For example, STEAP-1 promotes metastasis and EMT in lung adenocarcinoma by activating the JAK2 / STAT3 pathway. In hepatocellular carcinoma, STEAP-1 may influence cell proliferation and cell cycle arrest via the c-Myc pathway. In gastric cancer, STEAP-1 may promote invasion through the AKT / FOXO1 and / or EIF4E signaling pathways. In colorectal cancer, STEAP-1 may influence cell apoptosis via the NRF2 pathway and its interactions with ROS. NKX2-2, a known marker for Ewing's sarcoma (ES), and has been shown to regulate STEAP-1 expression in ES. Preferably, synergy is demonstrated by remission of the cancer where remission is not expected from treatment either from a STEAP-1 ADC or with treatment using an additive combination of a STEAP-1 ADC and a chemotherapeutic agent or other targeted cancer drug(s) or radiation or an immunotherapy such as CAR-T or NK cell therapy. The method for inhibiting growth of tumor cells using a STEAP-1 ADC and a combination of chemotherapy or radiation or both comprises administering the STEAP-1 ADC before, during, or after commencing chemotherapy or radiation therapy, as well as any combination thereof (i.e. before and during, before and after, during and after, or before, during, and after commencing the chemotherapy and / or radiation therapy). For example, the STEAP-1 ADC is typically administered between 1 and 60 days, preferably between 3 and 40 days, more preferably between 5 and 12 days before commencing radiation therapy and / or chemotherapy. However, depending on the treatment protocol and the specific patient’s needs, the method is performed in a manner that will provide the most efficacious treatment and ultimately prolong the life of the patient. The administration of chemotherapeutic agents can be accomplished in a variety of ways including systemically by the parenteral and enteral routes. In one embodiment, the STEAP-1 ADCs and the chemotherapeutic agent are administered as separate molecules. Particular examples of chemotherapeutic agents or chemotherapy include cisplatin, dacarbazine (DTIC), dactinomycin, mechlorethamine (nitrogen mustard), streptozocin, cyclophosphamide, carmustine (BCNU), lomustine (CCNU), doxorubicin (adriamycin), daunorubicin, procarbazine, mitomycin, cytarabine, etoposide, methotrexate, 5-fluorouracil, vinblastine, vincristine, bleomycin, paclitaxel (taxol), docetaxel (taxotere), aldesleukin, asparaginase, busulfan, carboplatin, cladribine, dacarbazine, floxuridine, fludarabine, hydroxyurea, ifosfamide, interferon alpha, leuprolide, megestrol, melphalan, mercaptopurine, plicamycin, mitotane, pegaspargase, pentostatin, pipobroman, plicamycin, streptozocin, tamoxifen, teniposide, testolactone, thioguanine, thiotepa, uracil mustard, vinorelbine, gemcitabine, chlorambucil, taxol and combinations thereof. The source of radiation, used in combination with a STEAP-1 ADC, can be either external or internal to the patient being treated. When the source is external to the patient, the therapy is known as external beam radiation therapy (EBRT). When the source of radiation is internal to the patient, the treatment is called brachytherapy (BT). In one embodiment, the radiation therapy is boron neutron capture therapy. In one embodiment, the radiation is Proton Boron Fusion Therapy. The above-described therapeutic regimens may be further combined with additional cancer treating agents and / or regimes, for example additional chemotherapy, cancer vaccines, signal transduction inhibitors, agents useful in treating abnormal cell growth or cancer, agents that interfere with DNA repair mechanism (e.g. inhibitors of the enzyme poly ADP ribose polymerase (PARP)), antibodies (e.g., Anti-CTLA-4 antibodies as described in WO / 2005 / 092380 (Pfizer)) or other ligands that inhibit tumor growth by binding to IGF-1R, and cytokines. Examples of PARP inhibitors include, but are not limited to, olaparib, niraparib, rucaparib, and talazoparib. In addition, HRAS may be targeted using salirasib and small interfering RNA (siRNA). Additionally, many KRAS inhibitors have been developed included approved drugs targeting specific mutations as well as current developing candidates targeting pan-KRAS. In another embodiment, PI3KA mutants have also been targeted including those inhibitors that can also lead to degradation of the mutant protein, for example, inavolisib and taselisib. Additional PI3KA mutant targeted drugs include alpelisib, pictilisib, STX-478, etc. When the mammal is subjected to additional chemotherapy, chemotherapeutic agents described above may be used. Additionally, growth factor inhibitors, biological response modifiers, anti- hormonal therapy, selective estrogen receptor modulators (SERMs), angiogenesis inhibitors, and anti- androgens may be used. For example, anti-hormones, for example anti-estrogens such as Nolvadex (tamoxifen) or, anti-androgens such as Casodex (4′-cyano-3-(4-fluorophenylsulphonyl)-2-hydroxy-2- methyl-3-′-(trifluoromethyl)propionanilide) may be used. The above therapeutic approaches can be combined with any one of a wide variety of surgical, chemotherapy or other targeted drugs(s) or radiation therapy regimens. The therapeutic approaches of the invention can enable the use of reduced dosages of chemotherapy (or other therapies) and / or less frequent administration, an advantage for all patients and particularly for those that do not tolerate the toxicity of the chemotherapeutic agent well. XIV.) Kits / Articles of Manufacture For use in the laboratory, prognostic, prophylactic, diagnostic and therapeutic applications described herein, kits are within the scope of the invention. Such kits can comprise a carrier, package, or container that is compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used in the method, along with a label or insert comprising instructions for use, such as a use described herein. For example, the container(s) can comprise a STEAP-1 antibody or several STEAP-1 antibodies (See, Tables VI and VII) of the disclosure. Kits can comprise a container comprising a drug unit. The kit can include all or part of the STEAP-1 ADCs and / or diagnostic assays for detecting cancer and / or other immunological disorders. The kit of the invention will typically comprise the container described above, and one or more other containers associated therewith that comprise materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes; carrier, package, container, vial and / or tube labels listing contents and / or instructions for use, and package inserts with instructions for use. A label can be present on or with the container to indicate that the composition is used for a specific therapy or non-therapeutic application, such as a prognostic, prophylactic, diagnostic or laboratory application, and can also indicate directions for either in vivo or in vitro use, such as those described herein. Directions and or other information can also be included on an insert(s) or label(s) which is included with or on the kit. The label can be on or associated with the container. A label can be on a container when letters, numbers or other characters forming the label are molded or etched into the container itself; a label can be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package insert. The label can indicate that the composition is used for diagnosing, treating, prophylaxing, or prognosing a condition, such as a cancer or other immunological disorder. The terms “kit” and “article of manufacture” can be used as synonyms. In another embodiment of the invention, an article(s) of manufacture containing compositions, such as STEAP-1 ADCs of the disclosure. The article of manufacture typically comprises at least one container and at least one label. Suitable containers include, for example, bottles, vials, syringes, and test tubes. The containers can be formed from a variety of materials such as glass, metal, or plastic. The container can hold one or several STEAP-1 ADCs and / or one or more therapeutics doses of STEAP-1 ADCs. The container can alternatively hold a composition that is effective for treating, diagnosis, prognosing or prophylaxing a condition and can have a sterile access port (for example the container can be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). The active agents in the composition can be a STEAP-1 antibody or ADC of the present disclosure. The article of manufacture can further comprise a second container comprising a pharmaceutically acceptable buffer, such as phosphate-buffered saline, Ringer's solution, and / or dextrose solution. It can further include other materials desirable from a commercial and user standpoint, including other buffers, diluents, filters, stirrers, needles, syringes, and / or package inserts with indications and / or instructions for use. EXEMPLARY EMBODIMENTS 1) An antibody drug conjugate (ADC) comprising a STEAP-1 antibody or antigen binding fragment thereof conjugated to a Drug-Linker (DL) payload, wherein the antibody or antigen binding fragment thereof comprises a heavy chain CDR region comprising an amino acid sequence set forth in any of SEQ ID NO: 12, SEQ ID NO: 13, and SEQ ID NO: 14: 69. 2) The ADC of claim 1, further comprising a STEAP-1 antibody or antigen binding fragment thereof wherein the antibody or antigen binding fragment thereof comprises a light chain CDR region comprising an amino acid sequence set forth in any of SEQ ID NO: 15, SEQ ID NO: 16, and SEQ ID NO: 17. 3) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: ADL-32-132 .4) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: .) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: .) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure:

[0002] Mall--AA- -PABC- -PC- -exxatteccan.) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: Maall--GGFG --PABC--eexxaatteeccaann.) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: Mal-AA-PABC-gluc-exatecan . ) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: . 0) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: .) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: .) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure:

[0003] ) A pharmaceutical composition comprising the ADCs of any of claims 1 through 12 and a pharmaceutically acceptable excipient. ) A kit comprising the ADC of any of claims 1-12. ) A kit comprising the pharmaceutical composition of claim 13. ) A method of treating cancer in a subject, comprising administering to the subject a therapeutically effective amount of an ADC of any of claims 1-12. ) A method of treating cancer in a subject, comprising administering to the subject a therapeutically effective amount of the pharmaceutical composition of claim 13. ) The method of claim 16, wherein the subject is a human. ) The method of claim 17, wherein the subject is a human. ) The method of claim 16, wherein the cancer is set forth in Table I. ) The method of claim 17, wherein the cancer is set forth in Table I. ) The method of claim 16, wherein the method further comprises administering radiation or other targeted cancer drug(s) or a chemotherapeutic agent or CAR-T therapy, or NK cell therapy. ) The method of claim 17, wherein the method further comprises administering radiation or other targeted cancer drug(s) or a chemotherapeutic agent or CAR-T therapy, or NK cell therapy. EXAMPLES: Various aspects of the invention are further described and illustrated by way of the several examples that follow, none of which is intended to limit the scope of the invention. Example 1: Methods of Generating Antibodies. The STEAP-1 antibody was generated by immunizing mice with cells expressing STEAP-1. Following standard hybridoma generation and screening, mouse anti-STEAP1 antibody was selected and sequenced. The selected antibody was humanized conserving specific binding to STEAP1. The humanized anti-STEAP1 antibody (STP1-Ab) was expressed recombinantly by cloning the antibody variable heavy and light chain sequences upstream of the human heavy chain IgG1 and human light chain Igκ constant regions, respectively. Signal peptides were inserted upstream of the heavy and light chains to allow secretion of the antibodies. The complete STP1-Ab human heavy chain and light chain cassettes were cloned downstream of the CMV promoter / enhancer in a cloning vector. A polyadenylation site was included downstream of the MAb coding sequence. The recombinant STP1-Ab heavy and light chain expressing constructs were transfected into CHO cells. Stably transfected Chinese Hamster Ovary (CHO) cells underwent selection and recovery process for the generation of stable pools expressing recombinant antibodies and Fc variants. For the antibody generation, fed-batch production process with typical culture duration of 8 to 15 days was used for stably transfected pools prior to harvest of the culture media. Alternatively, transiently transfected cells were cultured for a typical duration of 3-15 days prior to harvest of the culture media. Subsequently, Protein-A affinity purification was performed for harvested cell culture fluid and purified materials were buffer exchanged into phosphate-buffered saline (PBS) or other preferred antibody formulation buffer. The quality of recombinant antibodies was assessed by size-exclusion chromatography, SDS-PAGE and other methods known in the art. The resulting STEAP-1 antibody is set forth in Table VI, Table VII and comprise (SEQ ID NO: 4) through (SEQ ID NO: 7). Example 2: Binding Assays of STEAP-1 Antibodies. The binding affinity of STEAP-1 antibody of the invention was assessed using the following protocols. Briefly, tumor cell lines were harvested, and cells re-suspended in FACS buffer (2% FBS + 5 mM EDTA in PBS). Cells were plated into 96-well round bottom plates and incubated with antibody (10 µg / mL) for one (1) hour on ice. For cell binding affinity determinations, antibodies were added at 10 µg / mL with 3-fold dilutions. After incubation, cells were pelleted by centrifugation at 200×g for 5 minutes, washed twice with FACS buffer, and counterstained with R-PE labeled goat anti-human Fc gamma fragment specific secondary antibody (Jackson Immuno Research; West Grove, PA) for an additional one (1) hour on ice, protected from light. Labeled cells were then washed twice with FACS buffer and analyzed by flow cytometry using an Attune NxT flow cytometer (Thermo Fisher Scientific; Carlsbad, CA). The results show the STEAP-1 antibody (STP1-Ab) binds specifically to STEAP-1 target expressed on the cell-surface of human cancer cell lines on multiple cancer cell lines. (See, Figure(s) 1). Example 3: Binding Assays of STEAP-1 Antibodies. In another example, the binding affinity of STEAP-1 antibody of the invention was assessed using the following protocols. Briefly, tumor cell lines were harvested, and cells re-suspended in FACS buffer (2% FBS + 5 mM EDTA in PBS). Cells were plated into 96-well round bottom plates and incubated with antibody (10 µg / mL) for one (1) hour on ice. For cell binding affinity determinations, antibodies were added at 10 µg / mL with 3-fold dilutions. After incubation, cells were pelleted by centrifugation at 200×g for 5 minutes, washed twice with FACS buffer, and counterstained with R-PE labeled goat anti-human Fc gamma fragment specific secondary antibody (Jackson Immuno Research; West Grove, PA) for an additional one (1) hour on ice, protected from light. Labeled cells were then washed twice with FACS buffer and analyzed by flow cytometry using an Attune NxT flow cytometer (Thermo Fisher Scientific; Carlsbad, CA). The results show binding by of STP1-Ab (open histogram) compared to isotype control antibody (grey histogram) to STEAP1 on the cell-surface of human cancer cell lines 22RV1 (Figure 2(A)), LNCaP (Figure 2(B)), EBC-1 (Figure 2(C)), SU-DHL-1 (Figure 2(D)), as well as recombinantly expressed STEAP1 in CHO-K1 (Figure 2(E)), 293T (Figure 2(F)), and PC-3 (Figure 2(G)). (See, Figure(s) 2). Example 4: Binding Assays of STEAP-1 Antibodies. In another example, the binding affinity of STEAP-1 antibody of the invention was assessed using the following protocols. Briefly, tumor cell lines were harvested, and cells re-suspended in FACS buffer (2% FBS + 5 mM EDTA in PBS). Cells were plated into 96-well round bottom plates and incubated with antibody (10 µg / mL) for one (1) hour on ice. For cell binding affinity determinations, antibodies were added at 10 µg / mL with 3-fold dilutions. After incubation, cells were pelleted by centrifugation at 200×g for 5 minutes, washed twice with FACS buffer, and counterstained with R-PE labeled goat anti-human Fc gamma fragment specific secondary antibody (Jackson Immuno Research; West Grove, PA) for an additional one (1) hour on ice, protected from light. Labeled cells were then washed twice with FACS buffer and analyzed by flow cytometry using an Attune NxT flow cytometer (Thermo Fisher Scientific; Carlsbad, CA). The results in Figure 3(A) show binding affinity of STP1-Ab to STEAP1 on the cell-surface of a human prostate cancer cell line LNCaP by flow cytometry compared to isotype control antibody. Figure 3(B) presents binding affinity of STP1-Ab and STP1-ADC3 to STEAP1 on the cell-surface of a human cancer cell line SU-DHL-1 by flow cytometry. (See, Figure(s) 3 and Table XII and Table XIII). Example 5: Binding Assays of STEAP-1 Antibodies. In another example, the binding affinity of STEAP-1 antibody of the invention were assessed using the following protocols. Briefly, tumor cell lines were harvested, and cells re-suspended in FACS buffer (2% FBS + 5 mM EDTA in PBS). Cells were plated into 96-well round bottom plates and incubated with antibody (10 µg / mL) for one (1) hour on ice. For cell binding affinity determinations, antibodies were added at 10 µg / mL with 3-fold dilutions. After incubation, cells were pelleted by centrifugation at 200×g for 5 minutes, washed twice with FACS buffer, and counterstained with R-PE labeled goat anti-human Fc gamma fragment specific secondary antibody (Jackson Immuno Research; West Grove, PA) for an additional one (1) hour on ice, protected from light. Labeled cells were then washed twice with FACS buffer and analyzed by flow cytometry using an Attune NxT flow cytometer (Thermo Fisher Scientific; Carlsbad, CA). The results in Figure 4(A) shows binding affinity of STP1-Ab compared to isotype control antibody. Figure 4(B) shows binding to human and cynomolgus monkey STEAP1 recombinantly expressed on the cell-surface of 293T cells by flow cytometry. (See, Figure(s) 4 and Table XIV). Example 6: Cytotoxicity of STEAP-1 ADCs In Vitro. The in vitro cytotoxicity of the STEAP-1 ADCs was determined using the following protocols. Briefly, tumor cell lines were harvested, plated into 384-well white flat-bottom plates, and allowed to re- attach for 2-4 hours while incubating at 37°C. Cells were then treated with ADC or free payload test articles over a dose-titration (500 nM max with 5-fold dilutions). After 5-day treatment, the remaining cell viability was determined by CellTiter Glo assay based on the manufacturer’s instructions (Promega; Madison, WI). Data were normalized to non-treated control cells and dose-response curves were fitted using a 4-parameter logistic equation using GraphPad Prism software (version 9; La Jolla, CA). The results show that the STEAP-1 ADCs have cytotoxic effects in vitro on CHO-K1 cells expressing human STEAP-1 (See, Figure(s) 5 and Table XV). In another set of experiment(s) using the protocols set forth above, the in vitro cytotoxicity of STP1-ADC3 is shown compared to unconjugated STP-1 Ab and corresponding isotype controls, as well as free payload on 293T cells expressing human STEAP1 (See, Figure 6(A)) and monkey STEAP1 (See, Figure 6 (B)). The IC50(nM) is set forth in Table XVI. These results further affirm that the STEAP-1 ADCs have cytotoxic effects in vitro. Example 7: Efficacy of STEAP-1 ADCs Using Multiple Payloads in an EBC-1 NSCLC Xenograft Model In Vivo. In vivo efficacy of the STEAP-1 ADCs was performed using the following protocols. Briefly, EBC-1 cell suspension was mixed 1:1 with Matrigel. 2,000,000 viable cells were subcutaneously injected into the rear flank of female BALB / c nude mice. When the mean tumor size reached approximately 120 mm3, mice were randomized into groups, 5 mice per group. Vehicle control or test articles at either 5 mg / kg, 3 mg / kg, or 9 mg / kg were dosed once. Tumor volumes were measured three times per week after randomization in two dimensions using a caliper, and the volume was expressed in mm3using the formula: V = (L x W x W) / 2, where V is tumor volume, L is tumor length (the longest tumor dimension) and W is tumor width (the longest tumor dimension perpendicular to L). The results show superior in vivo efficacy of STP1-ADC1 and STP1-ADC2 compared to STP1- GGFG-Dxd in lung squamous carcinoma EBC-1 NSCLC xenograft model. (See, Figure(s) 7). In another set of experiment(s) using the protocols set forth above, the results show superior in vivo efficacy of STP1-ADC3 compared to STP1-Ab conjugated to different linker-payload entities (STP1-GGFG-Dxd and STEAP1-vcMMAE) in lung squamous carcinoma EBC-1 NSCLC xenograft model. (See, Figure(s) 8). Example 8: Efficacy of STEAP-1 ADCs in a Prostate Cancer Patient-Derived Xenograft Model (PDX) In Vivo. Further In vivo efficacy of a STEAP-1 ADC (STP1-ADC3) was performed using the following protocols. Briefly, PDX derived from patients with prostate adenocarcinoma, NSCLC, and gastric cancer were propagated in vivo in immunodeficient mice. Tumor fragments (2-3mm in diameter) from stock mice were harvested and used for subcutaneous inoculation into male immunodeficient mice (prostate cancer PDX) or female immunodeficient mice (NSCLC and gastric cancer PDX). When the mean tumor size reached approximately 150 mm3, mice were randomized into 2 groups. Vehicle control, or STP1-ADC3 at 10mg / kg weekly for 3 doses, were injected intravenously. Tumor volumes were measured three times per week in two dimensions using a caliper, and the volume was expressed in mm3 using the formula: V = (L x W x W) / 2, where V is tumor volume, L is tumor length (the longest tumor dimension) and W is tumor width (the longest tumor dimension perpendicular to L). The results show in vivo efficacy of a STP1-ADC3 compared to vehicle control in 3 different prostate cancer patient-derived xenograft models, PDX82 (Figure 9(A)), PDX87 (Figure 9(B)) and PDX11 (Figure 9(C)). Immunohistochemistry confirming STEAP-1 expression in all 3 models is presented. (See, Figure(s) 9). Example 9: Efficacy of STEAP-1 ADC (STP1-ADC3) Compared to Vehicle Control in a Patient Derived NSCLC Cancer Patient Derived Xenograft Model (PDX58) In Vivo. Further In vivo efficacy of a STEAP-1 ADC (STP1-ADC3) was performed using the following protocols. Briefly, PDX derived from patients with prostate adenocarcinoma, NSCLC, and gastric cancer were propagated in vivo in immunodeficient mice. Tumor fragments (2-3mm in diameter) from stock mice were harvested and used for subcutaneous inoculation into male immunodeficient mice (prostate cancer PDX) or female immunodeficient mice (NSCLC and gastric cancer PDX). When the mean tumor size reached approximately 150 mm3, mice were randomized into 2 groups. Vehicle control, or STP1-ADC3 at 10mg / kg weekly for 3 doses, were injected intravenously. Tumor volumes were measured three times per week in two dimensions using a caliper, and the volume was expressed in mm3 using the formula: V = (L x W x W) / 2, where V is tumor volume, L is tumor length (the longest tumor dimension) and W is tumor width (the longest tumor dimension perpendicular to L). The results show in vivo efficacy of a STP1-ADC3 compared to vehicle control in a NSCLC cancer patient-derived xenograft model PDX58. Immunohistochemistry confirming STEAP-1 expression in this model is presented. (See, Figure(s) 10). Example 10: Efficacy of STEAP-1 ADC (STP1-ADC3) Compared to Vehicle Control in a Patient Derived Gastric Cancer Patient Derived Xenograft Model (PDX10) In Vivo. Further In vivo efficacy of a STEAP-1 ADC (STP1-ADC3) was performed using the following protocols. Briefly, PDX derived from patients with prostate adenocarcinoma, NSCLC, and gastric cancer were propagated in vivo in immunodeficient mice. Tumor fragments (2-3mm in diameter) from stock mice were harvested and used for subcutaneous inoculation into male immunodeficient mice (prostate cancer PDX) or female immunodeficient mice (NSCLC and gastric cancer PDX). When the mean tumor size reached approximately 150 mm3, mice were randomized into 2 groups. Vehicle control, or STP1-ADC3 at 10mg / kg weekly for 3 doses, were injected intravenously. Tumor volumes were measured three times per week in two dimensions using a caliper, and the volume was expressed in mm3 using the formula: V = (L x W x W) / 2, where V is tumor volume, L is tumor length (the longest tumor dimension) and W is tumor width (the longest tumor dimension perpendicular to L). The results show in vivo efficacy of a STP1-ADC3 compared to vehicle control in a gastric cancer patient-derived xenograft model PDX10. Immunohistochemistry confirming STEAP-1 expression in this model is presented. (See, Figure(s) 11). Example 11: Use of Chimeric Antigen Receptor (CAR) T Cell Therapy in Cancers Expressing STEAP-1. Generally speaking, T cells help find and fight off infections and diseases, such as cancer in the body. Many cancers can hide from T cells, thus when T cells cannot “see” cancer, the cancer may grow in the body. A promising form of immunotherapy in cancer is known as CAR-T therapy. In CAR-T therapy, a chimeric antigen receptor (CAR) is designed to recognize specific markers that are expressed in cancer (e.g., STEAP-1). Studies have shown that when a CAR is attached to a specific antigen an immune response is induced, and the T cells recognize cancer and can inhibit cancer growth. By way of a non-limiting example, blood is collected from a patient having cancer that expresses STEAP-1. The T cells from the patient’s blood are isolated and genetically engineered to generate CAR-T cells. The CAR-T cells are cultivated and expanded using techniques known in the art. Finally, the CAR-T cells are infused into the patients’ bloodstream. See, JIN, et. al., Cancer Cell Int., 21:83 (2021). Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trials are open label comparing standard chemotherapy with standard therapy plus STEAP-1 CAR-T cells. As will be appreciated, one non-limiting criteria that can be utilized in connection with enrollment of patients is expression levels of STEAP-1 in a tumor as determined by standard detection methods known in the art. Example 12: Use of Natural Killer (NK) Cell Therapy in Cancers Expressing STEAP-1. Similar to CAR-T therapy, Natural Killer (NK) cell therapy is a form of immunotherapy that has shown promise in treating cancer (for example, cancers expressing STEAP-1). Unlike T-cells, NK cells are not tailored to specific antigens. However, while NK cells can recognize and attack cancer cells, the NK cells do not live long enough or multiple quickly enough to fight cancer cells entirely. However, studies have shown that NK cells can be enhanced by treating them with immune system proteins called cytokines. Studies have shown that enhancing NK cells with cytokines allows for a more robust immune response. One advantage of NK cell therapy is the lack of side effects versus CAR-T therapy. In some instances, NK cells are also enhanced with CARs to make them more attuned to fighting cancer. See, LU, et. al., Frontiers in Oncology, vol.11, Art.720501 (Aug.2021). By way of a non-limiting example, several strategies can be used to enhance the efficacy of NK cell therapies. First, NK cells are generated from peripheral blood (PB), umbilical cord blood (UCB), induced pluripotent stem cells (iPSCs), and NK92 cell lines. After isolation from the aforementioned sources, NK cells are stimulated by cytokines such as IL-2, IL-15, and / or IL-18. Moreover, NK cells can be modified ex vivo to express CARs, allowing NK cells to recognize specific tumor associated with antigens such as STEAP-1. Finally, the NK cells are infused into the patients’ bloodstream. See, MEHTA, et. al., Int. J. of Hematology, 107:262-270 (2018). Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trials are open label comparing standard chemotherapy with standard therapy plus STEAP-1 NK cells. As will be appreciated, one non-limiting criteria that can be utilized in connection with enrollment of patients is expression levels of STEAP-1 in a tumor as determined by standard detection methods known in the art. Example 13: STEAP-1 antibodies and STEAP-1 ADCs Characterization Assays. STEAP-1 antibodies and STEAP-1 ADC compositions of the invention were further characterized using assays known in the art. The results shown in Figure 14(A) through Figure 14(F) confirm an improved therapeutic window and safety profile relative to other STEAP-1 antibodies and STEAP-1 ADCs known in the art. Specifically, STEAP-1 ADCs of the invention show that STEAP1 is an ideal target for mCRPC with a differential expression profile. Additionally, a DAR8 conjugation ensures high exposures driving excellent efficacy. Finally, a stable PK translates to an excellent safety profile which provides a significant unmet medical need in mCRPC patients. Example 14: Human Clinical Trials for the Treatment of Human Carcinomas through the Use of STEAP-1 antibodies and STEAP-1 ADCs. STEAP-1 antibodies and STEAP-1 ADCs are synthesized in accordance with the present invention which specifically accumulate in a tumor cell and are used in the treatment of certain tumors and other immunological disorders and / or other diseases (See, Table I). In connection with each of these indications, two clinical approaches are successfully pursued. I.) Adjunctive therapy: In adjunctive therapy, patients are treated with STEAP-1 antibodies and STEAP-1 ADCs in combination with a chemotherapeutic or pharmaceutical or biopharmaceutical agent or a combination thereof. Primary cancer targets are treated under standard protocols by the addition of STEAP-1 antibodies and STEAP-1 ADCs. Protocol designs address effectiveness as assessed by the following examples, including but not limited to, reduction in tumor mass of primary or metastatic lesions, increased progression free survival, overall survival, improvement of patient’s health, disease stabilization, as well as the ability to reduce usual doses of standard chemotherapy and other biologic agents. These dosage reductions allow additional and / or prolonged therapy by reducing dose-related toxicity of the chemotherapeutic or biologic agent. II.) Monotherapy: In connection with the use of the STEAP-1 antibodies and STEAP-1 ADCs in monotherapy of tumors, the STEAP-1 antibodies and STEAP-1 ADCs are administered to patients without a chemotherapeutic or pharmaceutical or biological agent. In one embodiment, monotherapy is conducted clinically in end-stage cancer patients with extensive metastatic disease. Protocol designs address effectiveness as assessed by the following examples, including but not limited to, reduction in tumor mass of primary or metastatic lesions, increased progression free survival, overall survival, improvement of patient’s health, disease stabilization, as well as the ability to reduce usual doses of standard chemotherapy and other biologic agents. Dosage Dosage regimens may be adjusted to provide the optimum desired response. For example, a single STEAP-1 antibodie(s) and STEAP-1 ADC injection may be administered, several divided doses may be administered over time, or the dose may be proportionally reduced or increased as indicated by the exigencies of the therapeutic situation. “Dosage Unit Form” as used herein refers to physically discrete units suited as unitary dosages for the mammalian subjects to be treated; each unit containing a predetermined quantity of active compound calculated to produce the desired therapeutic effect in association with the required pharmaceutical carrier. The specification for the dosage unit forms of the invention are dictated by and directly dependent on (a) the unique characteristics of the STEAP-1 antibodie(s) and STEAP-1 ADC, the individual mechanics of the irradiation mechanism (reactor) and the particular therapeutic or prophylactic effect to be achieved, and (b) the limitations inherent in the art of compounding such an compound for the treatment of sensitivity in individuals. Clinical Development Plan (CDP) The CDP follows and develops treatments of cancer(s) and / or immunological disorders (See, Table I) using STEAP-1 antibodies and STEAP-1 ADCs of the disclosure. Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trials are open label comparing standard chemotherapy with standard therapy plus STEAP-1 antibodie(s) and STEAP-1 ADCs. As will be appreciated, one non-limiting criteria that can be utilized in connection with enrollment of patients is concentration of STEAP-1 antibodie(s) and STEAP-1 ADCs in a tumor as determined by standard detection methods known in the art. The present invention is not to be limited in scope by the embodiments disclosed herein, which are intended as single illustrations of individual aspects of the invention, and any that are functionally equivalent are within the scope of the invention. Various modifications to the models, methods, and life cycle methodology of the invention, in addition to those described herein, will become apparent to those skilled in the art from the foregoing description and teachings, and are similarly intended to fall within the scope of the invention. Such modifications or other embodiments can be practiced without departing from the true scope and spirit of the invention.

[0004] Table I. Representative List of Cancer(s) to be Treated. Table II. Amino Acid Abbreviations. Table III. Amino Acid Substitution Matrix.

[0005] Table IV. Nucleic acid sequence (SEQ ID NO: 1) and amino acid sequence (SEQ ID NO: 2) of human six-transmembrane epithelial antigen of prostate 1 (STEAP-1). 1 - ATGGAAAGCAGAAAAGACATCACAAACCAAGAAGAACTTTGGAAAATGAAGCCTAGGAGA - 60 1 - M E S R K D I T N Q E E L W K M K P R R - 20 61 - AATTTAGAAGAAGACGATTATTTGCATAAGGACACGGGAGAGACCAGCATGCTAAAAAGA - 120 21 - N L E E D D Y L H K D T G E T S M L K R - 40 121 - CCTGTGCTTTTGCATTTGCACCAAACAGCCCATGCTGATGAATTTGACTGCCCTTCAGAA - 180 41 - P V L L H L H Q T A H A D E F D C P S E - 60 181 - CTTCAGCACACACAGGAACTCTTTCCACAGTGGCACTTGCCAATTAAAATAGCTGCTATT - 240 61 - L Q H T Q E L F P Q W H L P I K I A A I - 80 241 - ATAGCATCTCTGACTTTTCTTTACACTCTTCTGAGGGAAGTAATTCACCCTTTAGCAACT - 300 81 - I A S L T F L Y T L L R E V I H P L A T - 100 301 - TCCCATCAACAATATTTTTATAAAATTCCAATCCTGGTCATCAACAAAGTCTTGCCAATG - 360 101 - S H Q Q Y F Y K I P I L V I N K V L P M - 120 361 - GTTTCCATCACTCTCTTGGCATTGGTTTACCTGCCAGGTGTGATAGCAGCAATTGTCCAA - 420 121 - V S I T L L A L V Y L P G V I A A I V Q - 140 421 - CTTCATAATGGAACCAAGTATAAGAAGTTTCCACATTGGTTGGATAAGTGGATGTTAACA - 480 141 - L H N G T K Y K K F P H W L D K W M L T - 160 481 - AGAAAGCAGTTTGGGCTTCTCAGTTTCTTTTTTGCTGTACTGCATGCAATTTATAGTCTG - 540 161 - R K Q F G L L S F F F A V L H A I Y S L - 180 541 - TCTTACCCAATGAGGCGATCCTACAGATACAAGTTGCTAAACTGGGCATATCAACAGGTC - 600 181 - S Y P M R R S Y R Y K L L N W A Y Q Q V - 200 601 - CAACAAAATAAAGAAGATGCCTGGATTGAGCATGATGTTTGGAGAATGGAGATTTATGTG - 660 201 - Q Q N K E D A W I E H D V W R M E I Y V - 220 661 - TCTCTGGGAATTGTGGGATTGGCAATACTGGCTCTGTTGGCTGTGACATCTATTCCATCT - 720 221 - S L G I V G L A I L A L L A V T S I P S - 240 721 - GTGAGTGACTCTTTGACATGGAGAGAATTTCACTATATTCAGAGCAAGCTAGGAATTGTT - 780 241 - V S D S L T W R E F H Y I Q S K L G I V - 260 781 - TCCCTTCTACTGGGCACAATACACGCATTGATTTTTGCCTGGAATAAGTGGATAGATATA - 840 261 - S L L L G T I H A L I F A W N K W I D I - 280 841 - AAACAATTTGTATGGTATACACCTCCAACTTTTATGATAGCTGTTTTCCTTCCAATTGTT - 900 281 - K Q F V W Y T P P T F M I A V F L P I V - 300 901 - GTCCTGATATTTAAAAGCATACTATTCCTGCCATGCTTGAGGAAGAAGATACTGAAGATT - 960 301 - V L I F K S I L F L P C L R K K I L K I - 320 961 - AGACATGGTTGGGAAGACGTCACCAAAATTAACAAAACTGAGATATGTTCCCAGTTGTAG - 1020 321 - R H G W E D V T K I N K T E I C S Q L * - 340 Table V. Amino acid sequence (SEQ ID NO: 3) of the human six-transmembrane epithelial antigen of prostate 1 (STEAP-1). Signal peptide is underlined. MESRKDITNQEELWKMKPRRNLEEDDYLHKDTGETSMLKRPVLLHLHQTAHADEFDCPSELQ HTQELFPQWHLPIKIAAIIASLTFLYTLLREVIHPLATSHQQYFYKIPILVINKVLPMVSIT LLALVYLPGVIAAIVQLHNGTKYKKFPHWLDKWMLTRKQFGLLSFFFAVLHAIYSLSYPMRR SYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWR EFHYIQSKLGIVSLLLGTIHALIFAWNKWIDIKQFVWYTPPTFMIAVFLPIVVLIFKSILFL PCLRKKILKIRHGWEDVTKINKTEICSQL*

[0006] Table(s) VI(A). Sequences of Antibody Heavy Chains. Table VI(A). The cDNA sequence (SEQ ID NO: 4) and amino acid sequence (SEQ ID NO: 5) of STP1-Ab heavy chain. The nucleotide sequence encoding the variable region is underlined. 1 - GAGGTGCAGCTGGTGGAGAGCGGAGGAGGACTGGTGCAGCCAGGGGGAAGCCTGAGGCTG - 60 1 - E V Q L V E S G G G L V Q P G G S L R L - 20 61 - TCCTGTGCCGTGTCCGGGTACTCCATTACCTCCGACTATGCCTGGAACTGGGTGAGACAG - 120 21 - S C A V S G Y S I T S D Y A W N W V R Q - 40 121 - GCTCCTGGCAAGGGCCTGGAGTGGGTGGGATATATCTCCAACTCTGGATCTACCTCCTAC - 180 41 - A P G K G L E W V G Y I S N S G S T S Y - 60 181 - AACCCCTCCCTGAAATCCCGGTTCACCATCTCCCGGGATACTTCCAAGAATACCCTCTAC - 240 61 - N P S L K S R F T I S R D T S K N T L Y - 80 241 - CTCCAGATGAATAGCCTGCGGGCCGAGGACACCGCCGTGTATTACTGCGCCCGGGAAAGA - 300 81 - L Q M N S L R A E D T A V Y Y C A R E R - 100 301 - AACTACGACTACGACGACTACTACTACGCTATGGATTACTGGGGCCAGGGCACACTGGTG - 360 101 - N Y D Y D D Y Y Y A M D Y W G Q G T L V - 120 361 - ACAGTGAGCTCCGCTAGCACCAAGGGCCCATCGGTCTTCCCCCTGGCACCCTCCTCCAAG - 420 121 - T V S S A S T K G P S V F P L A P S S K - 140 421 - AGCACCTCTGGGGGCACAGCGGCCCTGGGCTGCCTGGTCAAGGACTACTTCCCCGAACCG - 480 141 - S T S G G T A A L G C L V K D Y F P E P - 160 481 - GTGACGGTGTCGTGGAACTCAGGCGCCCTGACCAGCGGCGTGCACACCTTCCCGGCTGTC - 540 161 - V T V S W N S G A L T S G V H T F P A V - 180 541 - CTACAGTCCTCAGGACTCTACTCCCTCAGCAGCGTGGTGACCGTGCCCTCCAGCAGCTTG - 600 181 - L Q S S G L Y S L S S V V T V P S S S L - 200 601 - GGCACCCAGACCTACATCTGCAACGTGAATCACAAGCCCAGCAACACCAAGGTGGACAAG - 660 201 - G T Q T Y I C N V N H K P S N T K V D K - 220 661 - AAAGTTGAGCCCAAATCTTGTGACAAAACTCACACATGCCCACCGTGCCCAGCACCTGAA - 720 221 - K V E P K S C D K T H T C P P C P A P E - 240 721 - CTCCTGGGGGGACCGTCAGTCTTCCTCTTCCCCCCAAAACCCAAGGACACCCTCATGATC - 780 241 - L L G G P S V F L F P P K P K D T L M I - 260 781 - TCCCGGACCCCCGAGGTCACATGCGTGGTGGTGGACGTGAGCCACGAAGACCCTGAGGTC - 840 261 - S R T P E V T C V V V D V S H E D P E V - 280 841 - AAGTTCAACTGGTACGTGGACGGCGTGGAGGTGCATAATGCCAAGACAAAGCCGCGGGAG - 900 281 - K F N W Y V D G V E V H N A K T K P R E - 300 901 - GAGCAGTACAACAGCACGTACCGTGTGGTCAGCGTCCTCACCGTCCTGCACCAGGACTGG - 960 301 - E Q Y N S T Y R V V S V L T V L H Q D W - 320 961 - CTGAATGGCAAGGAGTACAAGTGCAAGGTCTCCAACAAAGCCCTCCCAGCCCCCATCGAG - 1020 321 - L N G K E Y K C K V S N K A L P A P I E - 340 1021 - AAAACCATCTCCAAAGCCAAAGGGCAGCCCCGAGAACCACAGGTGTACACCCTGCCCCCA - 1080 341 - K T I S K A K G Q P R E P Q V Y T L P P - 360 1081 - TCCCGGGAGGAGATGACCAAGAACCAGGTCAGCCTGACCTGCCTGGTCAAAGGCTTCTAT - 1140 361 - S R E E M T K N Q V S L T C L V K G F Y - 380 1141 - CCCAGCGACATCGCCGTGGAGTGGGAGAGCAATGGGCAGCCGGAGAACAACTACAAGACC - 1200 381 - P S D I A V E W E S N G Q P E N N Y K T - 400 1201 - ACGCCTCCCGTGCTGGACTCCGACGGCTCCTTCTTCCTCTACAGCAAGCTCACCGTGGAC - 1260 401 - T P P V L D S D G S F F L Y S K L T V D - 420 1261 - AAGAGCAGGTGGCAGCAGGGGAACGTCTTCTCATGCTCCGTGATGCATGAGGCTCTGCAC - 1320 421 - K S R W Q Q G N V F S C S V M H E A L H - 440 1321 - AACCACTACACGCAGAAGAGCCTCTCCCTGTCTCCGGGTAAATGA - 1365 441 - N H Y T Q K S L S L S P G K * - 454

[0007] Table(s) VI(B). Sequences of Antibody Light Chains. Table VI(B). The cDNA sequence (SEQ ID NO: 6) and amino acid sequence (SEQ ID NO: 7) of STP-1 Ab light chain. The nucleotide sequence encoding the variable region is underlined. 1 - GACATCCAGATGACCCAGTCCCCCTCCTCCCTGTCCGCCTCTGTGGGAGACAGAGTGACC - 60 1 - D I Q M T Q S P S S L S A S V G D R V T - 20 61 - ATCACCTGCAAGTCCTCCCAGTCCCTGCTGTATAGGTCCAACCAGAAAAACTACCTGGCC - 120 21 - I T C K S S Q S L L Y R S N Q K N Y L A - 40 121 - TGGTACCAGCAGAAACCCGGCAAGGCCCCCAAGCTGCTGATCTATTGGGCCTCTACCCGC - 180 41 - W Y Q Q K P G K A P K L L I Y W A S T R - 60 181 - GAATCCGGCGTGCCTTCCCGCTTCTCCGGGTCAGGAAGCGGCACAGACTTCACCCTGACT - 240 61 - E S G V P S R F S G S G S G T D F T L T - 80 241 - ATCTCCTCCCTCCAGCCCGAGGATTTCGCCACCTACTACTGCCAGCAGTACTACAACTAT - 300 81 - I S S L Q P E D F A T Y Y C Q Q Y Y N Y - 100 301 - CCCAGGACCTTCGGCCAGGGCACCAAGGTGGAAATCAAACGTACGGTGGCTGCACCATCT - 360 101 - P R T F G Q G T K V E I K R T V A A P S - 120 361 - GTCTTCATCTTCCCGCCATCTGATGAGCAGTTGAAATCTGGAACTGCCTCTGTTGTGTGC - 420 121 - V F I F P P S D E Q L K S G T A S V V C - 140 421 - CTGCTGAATAACTTCTATCCCAGAGAGGCCAAAGTACAGTGGAAGGTGGATAACGCCCTC - 480 141 - L L N N F Y P R E A K V Q W K V D N A L - 160 481 - CAATCGGGTAACTCCCAGGAGAGTGTCACAGAGCAGGACAGCAAGGACAGCACCTACAGC - 540 161 - Q S G N S Q E S V T E Q D S K D S T Y S - 180 541 - CTCAGCAGCACCCTGACGCTGAGCAAAGCAGACTACGAGAAACACAAAGTCTACGCCTGC - 600 181 - L S S T L T L S K A D Y E K H K V Y A C - 200 601 - GAAGTCACCCATCAGGGCCTGAGTTCGCCCGTCACAAAGAGCTTCAACAGGGGAGAGTGT - 660 T H Q G L S S P V T K S F N R G E C - 220 663 220

[0008] Table(s) VII(A) thru VII(F). Amino Acid Sequences of Antibody Heavy Chains. Table VII(A). Amino acid sequence (SEQ ID NO: 8) of STP1-Ab heavy chain. The variable region is underlined, and the Kabat CDR regions are boxed. MHEALHNHYTQKSLSLSPGK Table(s) VII(B). Amino Acid Sequences of Antibody Light Chains. Table VII(B). Amino acid sequence (SEQ ID NO: 9) of STP1-Ab light chain. The variable region is underlined, and the Kabat CDR regions are boxed. PPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC Table VIII. Amino Acid Sequences of Antibody Heavy Chain Variable Region(s). STP1-Ab EVQLVESGGGLVQPGGSLRLSCAVSGYSITSDYAWNWVRQAPGKGLEWVGYISNSGSTSYNP SLKSRFTISRDTSKNTLYLQMNSLRAEDTAVYYCARERNYDYDDYYYAMDYWGQGTLVTVSS (SEQ ID NO: 10) Table IX. Amino Acid Sequences of Antibody Light Chain Variable Region(s). STP1-Ab GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYNYPRTFGQGTKVEIK (SEQ ID NO: 11) Table X. Amino Acid Sequences of Antibody CDRs.

[0009] Table XI(A). Alignment of Amino Acid Variable Heavy Chain Regions with Corresponding Germline Sequences. Table XI(A). Alignment of amino acid sequence of STP1-Ab heavy chain variable region (SEQ ID NO: 18) with corresponding top V (SEQ ID NO: 19), D (SEQ ID NO: 20) and J (SEQ ID NO: 21) germline sequences. The Kabat CDR regions are boxed. STP1-Ab 59 IGHV3-66*01 58 IGHD5-12*01 0 IGHJ1*01 0 STP1-Ab 118 IGHV3-66*01 97 IGHD5-12*01 7 IGHJ1*01 11 STP1-Ab LVTVSS 124 IGHV3-66*01 ------ 97 IGHD5-12*01 ------ 7 IGHJ1*01 LVTVSS 17 Table XI(B). Alignment of Amino Acid Variable Light Chain Regions with Corresponding Germline Sequences Table XI(B). Alignment of amino acid sequence of STP1-Ab light chain variable region (SEQ ID NO: 22) with corresponding top V (SEQ ID NO: 23) and J (SEQ ID NO: 24) germline sequences. The Kabat CDR regions are boxed.

[0010] Table XII. Summarizes the binding parameters Bmax, KD, and Fit curve R2of STP1-Ab antibody to the human prostate cancer cell line LNCaP. ND* = Not Defined. Table XIII. Summarizes the binding parameters Bmax, KD, and Fit curve R2of STP1-Ab antibody and STP1-ADC3 to the cancer cell line SU-DHL-1. Table XIV. Summarizes the binding parameters Bmax, KD, and Fit curve R2of STP1-Ab antibody on 293T cells expressing human STEAP1 and monkey STEAP1. Table XV. Summarizes the in vitro cytotoxicity potencies (IC50) of STP1-ADC2, STP1-ADC3 and STP1- GGFG-Dxd on STEAP1 expressing CHO-K1 / Human STEAP1 cells. Table XVI. Summarizes the in vitro cytotoxicity potencies (IC50) of STP1-ADC3, STP1-Ab, isotype control antibody, isotype control ADC as well as free payload on 293T cells recombinantly expressing human STEAP1 and monkey STEAP1.

Claims

1. CLAIMS: 1) An antibody drug conjugate (ADC) comprising a STEAP-1 antibody or antigen binding fragment thereof conjugated to a Drug-Linker (DL) payload, wherein the antibody or antigen binding fragment thereof comprises a heavy chain CDR region comprising an amino acid sequence set forth in any of SEQ ID NO: 12, SEQ ID NO: 13, and SEQ ID NO:

14. 2) The ADC of claim 1, further comprising a STEAP-1 antibody or antigen binding fragment thereof wherein the antibody or antigen binding fragment thereof comprises a light chain CDR region comprising an amino acid sequence set forth in any of SEQ ID NO: 15, SEQ ID NO: 16, and SEQ ID NO:

17. 3) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: O NO2O O.4) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: O MeO2S O O .15) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: HOO H O N N O O O N N N P N. 6) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: OHOO H O N N-- - - .7) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: 2O O HHOH N N N N N N O O.8) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: OH OH HO O O. 9) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: 3NO2MeO2S HOH O .10) The or structure: N BrHOH O O N N N .11) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: 4OH OH HO NO2O O O .12) The ADC of claim 1 or 2, wherein the DL payload comprises the following chemical structure: OH OH HO O O13) A pharmaceutical composition comprising the ADCs of any of claims 1 through 12 and a pharmaceutically acceptable excipient. 14) A kit comprising the ADC of any of claims 1-12. 15) A method of treating cancer in a subject, comprising administering to the subject a therapeutically effective amount of an ADC of any of claims 1-12. 516) The method of claim 15, wherein the subject is a human. 17) The method of claim 15, wherein the cancer is set forth in Table I. 18) The method of claim 17, wherein the cancer is prostate cancer. 19) The method of claim 15, wherein the method further comprises administering radiation or a chemotherapeutic agent or CAR-T therapy, or NK cell therapy or other targeted cancer drug(s). 20) The method of claim 15, wherein the method further comprises administering radiation or a chemotherapeutic agent or CAR-T therapy, or NK cell therapy or other targeted cancer drug(s). 6

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