Therapeutic antibodies and their uses

Abstract

The present invention relates to antibodies, e.g., full length antibodies or antigen binding fragments thereof, that specifically bind to BCMA (B­Cell Maturation Antigen) and CD3 (Cluster of Differentiation 3). The invention also relates to antibody conjugates (e.g., antibody­drug­conjugates) comprising the BCMA antibodies, compositions comprising the BCMA antibodies, and methods of using the BCMA antibodies and their conjugates for treating conditions associated with cells expressing BCMA (e.g., cancer or autoimmune disease). The invention further relates to heteromultimeric antibodies that specifically bind to CD3 and a tumor cell antigen, (e.g., bispecific antibodies that specifically bind to CD3 and BCMA). Compositions comprising such heteromultimeric antibodies, methods for producing and purifying such heterodimeric antibodies, and their use in diagnostics and therapeutics are also provided.

Description

THERAPEUTIC ANTIBODIES AND THEIR USESFieldThe present invention relates to antibodies, e.g., full length antibodies or antigen binding fragments thereof, that specifically bind to BCMA (B-Cell Maturation Antigen) and / or CD3 (Cluster of Differentiation 3). The invention also relates to antibody conjugates (e.g., antibody-drug-conjugates) comprising the BCMA antibodies, compositions comprising the BCMA antibodies, and methods of using the BCMA antibodies and their conjugates for treating conditions associated with cells expressing BCMA (e.g., cancer or autoimmune disease). The invention further relates to heteromultimeric antibodies that specifically bind to CD3 and a tumor cell antigen, (e.g., bispecific antibodies that specifically bind to CD3 and BCMA). Compositions comprising such heteromultimeric antibodies, methods for producing and purifying such heterodimeric antibodies, and their use in diagnostics and therapeutics are also provided.BackgroundB-cell maturation antigen (BCMA, CD269, or TNFRSF17) is a member of the tumor necrosis factor receptor (TNFR) superfamily. BCMA was identified in a malignant human T cell lymphoma containing a t(4; 16) translocation. The gene is selectively expressed in the B-cell lineage with the highest expression in plasma blasts and plasma cells, antibody secreting cells. BCMA binds two ligands, B-cell activation factor (BAFF) (also called B-lymphoctye stimulator (BLyS) and APOL-related leukocyte expressed ligand (TALL-1 )) and a proliferation-inducing ligand (APRIL) with affinity of 1 uM and 16nM, respectively. Binding of APRIL or BAFF to BCMA promotes a signaling cascade involving NF-kappa B, Elk-1 , c-Jun N-terminal kinase and the p38 mitogen-activated protein kinase, which produce signals for cell survival and proliferation.BCMA is also expressed on malignant B cells and several cancers that involve B lymphocytes including multiple myeloma, plasmacytoma, Hodgkin's Lymphoma, and chronic lymphocytic leukemia. In autoimmune diseases where plasmablasts are involved such as systemic lupus erythematosus (SLE) and rheumatoid arthritis, BCMA expressing antibody-producing cells secrete autoantibodies that attack self.In the case of multiple myeloma, about 24,000 new cases are newly diagnosed in the United States each year, and this number represents about 15% of the newly diagnosed hematological cancers in the United States. An average of 1 1 ,000 deaths result from multiple myeloma each year, and the average 5-year survival rate is about 44%, with median survival of 50-55 months. Current treatment for multiple myeloma is focused on plasma cells apoptosis and / or decreasing osteoclast activity (e.g., chemotherapy, thalidomide, lenalidomide, bisphosphonates, and / or proteasome inhibitors such as bortezomib (VELCADE®) or carfilzomib). However, multiple myeloma remains an incurable disease, and almost all patients have developed resistance to these agents and eventually relapse. Accordingly, an alternative treatment to multiple myeloma, such as using an anti-BCMA antagonist including antibodies and other immunotherapeutic agents (e.g. bispecific antibodies or antibody- drug conjugates), would make a superior therapeutic agent. SummaryThe invention disclosed herein is directed to therapeutic antibodies that bind to BCMA and / or CD3. Antibody conjugates (e.g., antibody-drug conjugates) comprising BCMA are also provided. Further, the heteromultimeric antibodies (e.g., bispecific antibodies) that specifically bind to CD3 and a tumor cell antigen (e.g., bispecific antibodies that specifically bind to CD3 and BCMA) are also provided.In one aspect, the invention provides an isolated antibody, or an antigen binding fragment thereof, which specifically binds to B-Cell Maturation Antigen (BCMA), wherein the antibody comprises (a) a heavy chain variable (VH) region comprising (i) a VH complementary determining region one (CDR1 ) comprising the sequence SYX-| MX2, wherein is A or P; and X2is T, N, or S (SEQ ID NO: 301 ), GFTFXiSY, wherein is G or S (SEQ ID NO: 302), or GFTFX1SYX2MX3, wherein X-, is G or S, X2is A or P; and X3is T, N, or S (SEQ ID NO: 303); (ii) a VH CDR2 comprising the sequence AX.iX2X3X4GX5X6X7XeYADX9X.i0KG, wherein X is I, V, T, H, L, A, or C; X2is S, D, G, T, I, L, F, M, or V; X3is G, Y, L, H, D, A, S, or M; X4is S, Q, T, A, F, or W; X5is G or T;X6is N, S, P, Y, W, or F; X7is S, T, I, L, T, A, R, V, K, G, or C; X8is F, Y, P, W, H, or G; X9is V, R, or L; and X10is G or T (SEQ ID NO: 305), or X.1X2X3X4X5X6,wherein X-, is S, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M; X3is S, G, F, or W; X4is G or S; X5is G or T; and X6is N, S, P, Y, or W (SEQ ID NO: 306); and iii) a VH CDR3 comprisingthe sequence VSPIXiX2X3X4,wherein Xi is A or Y; X2is A or S; and X3is G, Q, L, P, or E (SEQ ID NO: 307), or YWPMX1X2,wherein Xi is D, S, T, or A; and X2is I, S, L, P, or D (SEQ ID NO: 308); and / or (b) a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence X X2X3X4X5X6X7X8X9XioXiiXi2, wherein X-i is R, G, W, A, or C; X2is A, P, G, L, C, or S; X3is S, G, or R; X4is Q, C, E, V, or I; X5is S, P, G, A, R, or D; X6is V, G, I, or L; X7is S, E, D, P, or G; X8is S, P, F, A, M, E, V, N, D, or Y; X9is I, T, V, E, S, A, M, Q, Y, H, R, or F; X10is Y or F; Xn is L, W, or P; and X12is A, S, or G (SEQ ID NO: 309); (ii) a VL CDR2 comprising the sequence X ASX2RAX3, wherein X is G or D; X2is S or I; and X3is T or P (SEQ ID NO: 310); and (iii) a VL CDR3 comprising the sequence QQYX^XaPX-fT, wherein is G, Q, E, L, F, A, S, M, K, R, or Y; X2is S, R, T, G, V, F, Y, D, A, H, V, E, K, or C; X3is W, F, or S; and X4is L or I (SEQ ID NO: 31 1 ), or QQYX1X2X3PX4, wherein X-, is G, Q, E, L, F, A, S, M, R, K, or Y; X2is S, R, T, G, R, V, D, A, H, E, K, C, F, or Y; X3is W, S, or F; and X4is L or I (SEQ ID NO: 312).In another aspect, the invention provides an isolated antibody, or an antigen binding fragment thereof, which specifically binds to BCMA, wherein the antibody comprises: a VH region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 2, 3, 7, 8, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 35, 37, 39, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 83, 87, 92, 95, 97, 99, 101 , 104, 106, 1 10, 1 12, 1 14, 1 18, 120, 122, 125, 127, 313, 314, 363, or 365; and / or a VL region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 1 , 4, 5, 6, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 34, 36, 38, 40, 41 , 43, 45, 47, 49, 51 , 53, 55, 57, 59, 61 , 63, 65, 67, 69, 71 , 73, 75, 77, 79, 317, 81 , 82, 84, 85, 86, 88, 89, 90, 91 , 93, 94, 96, 98, 100, 102, 103, 105, 107, 108, 109, 1 1 1 , 1 13, 1 15, 1 16, 1 17, 1 19, 121 , 123, 124, 126, 128, 315, 316, or 364. In some embodiments, the VH region comprises (i) a VH CDR1 comprising SEQ ID NO: 150, 151 , 152, 156, or 157; (ii) a VH CDR2 comprising SEQ ID NO: 169, 154, 194, 159, 195, 196, 162, 158, 198, 177, 178, 199, 200, 201 , 202, 203, 204, 206, 207,208, 172, 203, or 204 ; and (iii) a VH CDR3 comprising SEQ ID NO: 155, 161 , 197, 205, or 164; and / or wherein the VL region comprises (i) a VL CDR1 comprising SEQ ID NO:209, 271 , 273, 275, 251 , 277, 260, 279, 245, 283, 285, 287, 290, 292, 235, 297, or 299; (ii) a VL CDR2 comprising SEQ ID NO: 221 ; and (iii) a VL CDR3 comprising SEQ ID NO: 225, 272, 274, 276, 278, 280, 281 , 282, 284, 286, 288, 289, 291 , 293, 294, 229,296, 298, or 300. In some embodiments, the VH region comprises the sequence shown in SEQ ID NO: 1 12 or a variant with one or several conservative amino acid substitutions in residues that are not within a CDR and / or the VL region comprises the amino acid sequence shown in SEQ ID NO: 38 or a variant thereof with one or several amino acid substitutions in amino acids that are not within a CDR. In some embodiments, the antibody comprises a light chain comprising the sequence shown in SEQ ID NO: 357 and a heavy chain comprising the sequence shown in SEQ ID NO: 358. In some embodiments, the antibody comprises a VH region produced by the expression vector with ATCC Accession No. PTA-122094. In some embodiments, the antibody comprises a VL region produced by the expression vector with ATCC Accession No. PTA-122093.In another aspect, the invention provides an isolated antibody comprising an acyl donor glutamine-containing tag engineered at a specific site of the BCMA antibody of the present invention. In some embodiments, the tag comprises an amino acid sequence selected from the group consisting of Q, LQG, LLQGG (SEQ ID NO:318), LLQG (SEQ ID NO:454), LSLSQG (SEQ ID NO: 455), GGGLLQGG (SEQ ID NO: 456), GLLQG (SEQ ID NO: 457), LLQ, GSPLAQSHGG (SEQ ID NO: 458), GLLQGGG (SEQ ID NO: 459), GLLQGG (SEQ ID NO: 460), GLLQ (SEQ ID NO: 461 ), LLQLLQGA (SEQ ID NO: 462), LLQGA (SEQ ID NO: 463), LLQYQGA (SEQ ID NO: 464), LLQGSG (SEQ ID NO: 465), LLQYQG (SEQ ID NO: 466), LLQLLQG (SEQ ID NO: 467), SLLQG (SEQ ID NO: 468), LLQLQ (SEQ ID NO: 469), LLQLLQ (SEQ ID NO: 470), LLQGR (SEQ ID NO: 471 ), LLQGPP (SEQ ID NO: 472), LLQGPA (SEQ ID NO: 473), GGLLQGPP (SEQ ID NO: 474), GGLLQGA (SEQ ID NO: 475), LLQGPGK (SEQ ID NO: 476), LLQGPG (SEQ ID NO: 477), LLQGP (SEQ ID NO: 478), LLQP (SEQ ID NO: 479), LLQPGK (SEQ ID NO: 480), LLQAPGK (SEQ ID NO: 481 ), LLQGAPG (SEQ ID NO: 482), LLQGAP (SEQ ID NO: 483), and LLQLQG (SEQ ID NO: 484).In one variation, the invention provides an isolated antibody comprising an acyl donor glutamine-containing tag and an amino acid modification at position 222, 340, or 370 of the BCMA antibody of the present invention. In some embodiments, the amino acid modification is a substitution from lysine to arginine.In some embodiments, the BCMA antibody of the present invention further comprises a linker. In some embodiments, the linker is selected from the group consisting of Ac-Lys-Gly (acetyl-lysine-glycine), aminocaproic acid, Ac-Lys-p-Ala(acetyl-lysine-p-alanine), amino-PEG2 (polyethylene glycol)-C2, amino-PEG3-C2, amino-PEG6-C2, Ac-Lys-Val-Cit-PABC (acetyl-lysine-valine-citrulline-p- aminobenzyloxycarbonyl), amino-PEG6-C2-Val-Cit-PABC, aminocaproyl-Val-Cit-PABC, [(3R,5R)-1 -{3-[2-(2-aminoethoxy)ethoxy]propanoyl}pipendine-3,5-diyl]bis-Val-Cit-PABC, [(3S,5S)-1 -{3-[2-(2-aminoethoxy)ethoxy]propanoyl}pipendine-3,5-diyl]bis-Val-Cit-PABC, putrescine, and Ac-Lys-putrescine.In another aspect, the invention provides a conjugate of the BCMA antibody or the antigen binding fragment as described herein, wherein the antibody or the antigen binding fragment is conjugated to an agent, wherein the agent is selected from the group consisting of a cytotoxic agent, an immunomodulating agent, an imaging agent, a therapeutic protein, a biopolymer, and an oligonucleotide. In some embodiments, the agent is a cytotoxic agent including, but not limited to, an anthracycline, an auristatin, a camptothecin, a combretastatin, a dolastatin, a duocarmycin, an enediyne, a geldanamycin, an indolino-benzodiazepine dimer, a maytansine, a puromycin, a pyrrolobenzodiazepine dimer, a taxane, a vinca alkaloid, a tubulysin, a hemiasterlin, a spliceostatin, a pladienolide, and stereoisomers, isosteres, analogs, or derivatives thereof. For example, the cytotoxic agent is MMAD (Monomethyl Auristatin D), 0101 (2- methylalanyl- / V-[(3 4S,5S)-3-methoxy-1 -{(2S)-2-[(1 2 )-1-methoxy-2-methyl-3-oxo-3- {[(1 S)-2-phenyl-1 -(1 ,3-thiazol-2-yl)ethyl]amino}propyl]pyrrolidin-1 -yl}-5-methyl-1 - oxoheptan-4-yl]- / V-methyl-L-valinamide), 3377 (N,2-dimethylalanyl-N-{(1 S,2R)-4-{(2S)- 2-[(1 R,2R)-3-{[(1 S)-1 -carboxyl-2-phenylethyl]amino}-1 -methoxy-2-methyl-3- oxopropyl]pyrrolidin-1 -yl}-2-methoxy-1-[(1 S)-1 -methylpropyl]-4-oxobutyl}-N-methyl-L- valinamide), 0131 (2-methyl-L-proly-N-[(3R,4S,5S)-1 -{(2S)-2-[(1 R,2R)-3-{[(1 S)-1 - carboxy-2-phenylethyl]amino}-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}-3- methoxy-5-methyl-1-oxoheptan-4-yl]-N-methyl-L-valinamide), or 0121 (2-methyl-L-proly- N-[(3R,4S,5S)-1 -{(2S)-2-[(1 R,2R)-3-{[(2S)-1-methoxy-1-oxo-3-phenylpropan-2- yl]amino}-1 -methoxy-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}-3-methoxy-5-methyl-1 - oxoheptan-4-yl]-N-methyl-L-valinamide).In some embodiments, the present invention provides a conjugate comprising the formula: antibody-(acyl donor glutamine-containing tag)-(linker)-(cytotoxic agent). In some embodiments, the acyl donor glutamine-containing tag comprises an amino acid sequence LLQG (SEQ ID NO: 319) and / or GGLLQGPP (SEQ ID NO: 339) and wherein the linker comprises acetyl-lysine-valine-citrulline-p-aminobenzyloxycarbonyl or amino-PEG6-C2. In some embodiments, the conjugate is selected from the group consisting of 1 ) antibody-GGLLQGPP (SEQ ID NO: 339)-(acetyl-lysine-valine-citrulline-p- aminobenzyloxycarbonyl (AcLys-VC-PABC))-0101 ; 2) antibody-LLQG (SEQ ID NO: 319)-amino-PEG6-C2-0131 ; and 3) antibody-LLQG (SEQ ID NO: 319)-amino-PEG6- C2-3377. In some embodiments, the conjugate further comprises an amino acid substitution from lysine to arginine at antibody position 222. In some embodiments, the conjugate further comprises amino acid substitutions at antibody position N297Q or N297A.In another aspect, provided is a method of producing the BCMA antibody as described herein, comprising culturing the host cell under conditions that result in production of the BCMA antibody, and isolating the BCMA antibody from the host cell or culture.In another aspect, the invention provides a use of the BCMA antibodies or the BCMA antibody conjugates as described herein in the manufacture of a medicament for treating a condition (e.g., cancer or autoimmune disorder) associated with BCMA expression. In some embodiments, provided is a use of the BCMA antibodies or the BCMA antibody conjugates as described herein in the manufacture of a medicament for inhibiting tumor growth or progression. In some embodiments, provided is a use of the BCMA antibodies or the BCMA antibody conjugates as described herein in the manufacture of a medicament for inhibiting metastasis of malignant cells expressing BCMA. In some embodiments, provided is a use of the BCMA antibodies or the BCMA antibody conjugates as described herein in the manufacture of a medicament for inducing tumor regression.In another aspect, the invention provides an isolated antibody, or an antigen binding fragment thereof, which specifically binds to CD3, wherein the antibody comprises a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399. In some embodiments, the antibody comprises a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 324 or 388; and / or a light chain variable (VL) region comprising VLCDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 323 or 387. In some embodiments, the VH region comprises (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 414, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453. In some embodiments, the VH region comprises (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 407, or 408 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 336, 404, 405, or 417; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335 or 406; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 343 or 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342 or 439. In some embodiments, the antibody comprises a VH region produced by the expression vector with ATCC Accession No. PTA-122513. In some embodiments, the antibody comprises a VL region produced by the expression vector with ATCC Accession No. PTA-122512.In another aspect, provided is an isolated antibody which specifically binds to CD3 and competes with the anti-CD3 antibody of the present invention as described herein.In another aspect, the invention provides a bispecific antibody wherein the bispecific antibody is a full-length human antibody, comprising a first antibody variable domain of the bispecific antibody capable of recruiting the activity of a human immune effector cell by specifically binding to an effector antigen located on the human immune effector cell, and comprising a second antibody variable domain of the bispecific antibody capable of specifically binding to a target antigen, wherein the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324,326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399. In some embodiments, the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 414, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453. In some embodiments, the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 324 or 388; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 323 or 387; and the second antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 1 12; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 38.In some embodiments, the second antibody variable domain comprises (a) a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one (CDR1 ) comprising the sequence SYXi MX2, wherein Xi is A or P; and X2is T, N, or S (SEQ ID NO: 301 ), GFTFX-iSY, wherein Χτ is G or S (SEQ ID NO: 302), or GFTFX1SYX2MX3, wherein Χτ is G or S, X2is A or P; and X3is T, N, or S (SEQ ID NO: 303); (ii) a VH CDR2 comprising the sequencewherein Χτ is I, V, T, H, L, A, or C; X2is S, D, G, T, I, L, F, M, or V; X3is G, Y, L, H, D, A, S, or M; X4is S, Q, T, A, F, or W; X5is G or T;X6is N, S, P, Y, W, or F; X7is S, T, I, L, T, A, R, V, K, G, or C; X8is F, Y, P, W, H, or G; X9is V, R, or L; and X10is G or T(SEQ ID NO: 305), or X^XsX^sXe,wherein Χτ is S, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M; X3is S, G, F, or W; X4is G or S; X5is G or T; and X6is N, S, P, Y, or W (SEQ ID NO: 306); and iii) a VH CDR3 comprising the sequence VSPIX X2X3X4wherein X^ is A or Y; X2is A or S; and X3is G, Q, L, P, or E (SEQ ID NO: 307), or YWPMX^s,wherein Χτ is D, S, T, or A; and X2is I, S, L, P, or D (SEQ ID NO: 308); and / or (b) a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence X X2X3X4X5X6X7X8X9XioXiiXi2, wherein Χτ is R, G, W, A, or C; X2is A, P, G, L, C, or S; X3is S, G, or R; X4is Q, C, E, V, or I; X5is S, L, P, G, A, R, or D; X6is V, G, or I; X7is S, E, D, or P; X8is S, P, F, A, M, E, V, N, D, or Y; X9is I, T, V, E, S, A, M, Q, Y, H, or R; X10is Y or F; Xn is L, W, or P; and X12is A, S, or G (SEQ ID NO: 309); (ii) a VL CDR2 comprising the sequence X ASX2RAX3, wherein X-i is G or D; X2is S or I; and X3is T or P (SEQ ID NO: 310); and (iii) a VL CDR3 comprising the sequence QQYXiX2X3PX4T, wherein X is G, Q, E, L, F, A, S, M, K, R, or Y; X2is S, R, T, G, V, F, Y, D, A, H, V, E, K, or C; X3is W, F, or S; and X4is L or I (SEQ ID NO: 31 1 ), or QQYX^XsPX^ wherein Χτ is G, Q, E, L, F, A, S, M, R, K, or Y; X2is S, R, T, G, R, V, D, A, H, E, K, C, F, or Y; X3is W, S, or F; and X4is L or I (SEQ ID NO: 312). In some embodiments, the second antibody variable domain comprises a heavy chain variable (VH) region comprising (i) a VH CDR1 comprising the sequence shown in SEQ ID NO: 150, 151 , 152, 156, 157, 348, 349, 353, 354, or 355; (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 169, 154, 194, 159, 195, 196, 162, 158, 198, 177, 178, 199, 200, 201 , 202, 203, 204, 206, 207, 208, 172, 203, 204, 350, 351 , 356 or 357; and (iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 155, 161 , 197, 205, 164, or 352, or 358; and / or wherein the light chain variable (VL) region comprises (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 209, 271 , 273, 275, 251 , 277, 260, 279, 245, 283, 285, 287, 290, 292, 235, 297, 299, or 361 ; (ii) a VL CDR2 comprising the sequence shown in SEQ I D NO: 221 , 359 or 362; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 21 1 , 225, 272, 274, 276, 278, 280, 281 , 282, 284, 286, 288, 289, 291 , 293, 294, 229, 296, 298, 300 or 360.In some embodiments, (a) the first antibody variable domain comprises a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 407, or 408(H) a VH CDR2 comprising the sequence shown in SEQ ID NO: 336, 417, 404, or 405; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335 or406; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 343 or 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342 or 439; and (b) the second antibody variable domain comprises a heavy chain VH region comprising a heavy chain variable (VH) region comprising (i) a VH CDR1 comprising the sequence shown in SEQ ID NO: 151 , 156, or 157; (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 158 or 159; and (iii) a VH CDR3 comprising SEQ ID NO: 155; and / or wherein the light chain variable (VL) region comprises (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 209; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 221 ; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 225.In some embodiments, both the first and the second antibody variable domains of the bispecific antibody comprise amino acid modifications at positions 223, 225, and 228 in the hinge region and at position 409 or 368 (EU numbering scheme) in the CH3 region of a human lgG2 (SEQ ID NO: 493). In some embodiments, the bispecific antibody as described herein further comprises an amino acid modification at position 265 of the human lgG2.In another aspect, the invention provides pharmaceutical compositions comprising any of the antibodies (e.g., BCMA, CD3, or bispecific) or the conjugates thereof (e.g., BCMA antibody-drug conjugate) described herein.In another aspect, the invention also provides cell lines that recombinantly produce any of the antibodies (e.g., BCMA, CD3, or bispecific) or the conjugates thereof (e.g., BCMA antibody-drug conjugate) described herein.In another aspect, the invention also provides nucleic acids encoding any of the antibodies (e.g., BCMA, CD3, or bispecific) or the conjugates thereof (e.g., BCMA antibody-drug conjugate) described herein. The invention also provides nucleic acids encoding a heavy chain variable region and / or a light chain variable region of any of these antibodies described herein.The invention also provides kits comprising an effective amount of any of the antibodies (e.g., BCMA, CD3, or bispecific) or the conjugates thereof (e.g., BCMA antibody-drug conjugate) described herein.The invention also provides methods of treating a condition (e.g., tumor growth / progression inhibition; metastasis of maliginant cells expressing BCMA inhibition;tumor regression induction in subjects with malignant cells expressing BCMA) in subjects in need thereof comprising providing the isolated antibodies (e.g., BCMA) or binding fragments, bispecific antibodies (BCMA-CD3 bispecifics), or the conjugates thereof (e.g., BCMA antibody-drug conjugates) thereof described herein and administering said antibodies or conjugates to said subject.Also provided are methods of treating a condition associated with malignant cells expressing a tumor antigen in a subject comprising administering to a subject in need thereof an effective amount of the pharmaceutical compositions of the invention. In some embodiments, the condition is cancer. In some embodiments, the cancer is a B- cell related cancer selecting from the group consisting of multiple myeloma, malignant plasma cell neoplasm, Hodgkin's lymphoma, nodular lymphocyte predominant Hodgkin's lymphoma, Kahler's disease and Myelomatosis, plasma cell leukemia, plasmacytoma, B-cell prolymphocytic leukemia, hairy cell leukemia, B-cell non- Hodgkin's lymphoma (NHL), acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), follicular lymphoma, Burkitt's lymphoma, marginal zone lymphoma, mantle cell lymphoma, large cell lymphoma, precursor B-lymphoblastic lymphoma, myeloid leukemia, Waldenstrom's macroglobulienemia, diffuse large B cell lymphoma, follicular lymphoma, marginal zone lymphoma, mucosa-associated lymphatic tissue lymphoma, small cell lymphocytic lymphoma, mantle cell lymphoma, Burkitt lymphoma, primary mediastinal (thymic) large B-cell lymphoma, lymphoplasmactyic lymphoma, Waldenstrom macroglobulinemia, nodal marginal zone B cell lymphoma, splenic marginal zone lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, lymphomatoid granulomatosis, T cell / histiocyte-rich large B-cell lymphoma, primary central nervous system lymphoma, primary cutaneous diffuse large B-cell lymphoma (leg type), EBV positive diffuse large B-cell lymphoma of the elderly, diffuse large B-cell lymphoma associated with inflammation, intravascular large B-cell lymphoma, ALK-positive large B-cell lymphoma, plasmablastic lymphoma, large B-cell lymphoma arising in HHV8-associated multicentric Castleman disease, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and Burkitt lymphoma, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and classical Hodgkin lymphoma,and other B-cell related lymphoma. In some embodiments, the condition is an autoimmune disorder, such as systemic lupus erythematosus or rheumatoid arthritis.In some embodiments, the antibodies described herein comprise a constant region. In some embodiments, the antibodies described herein are of the human lgG1 , lgG2 or lgG2Aa, lgG3, or lgG4 subclass. In some embodiments, the antibodies described herein comprise a glycosylated constant region. In some embodiments, the antibodies described herein comprise a constant region having increased binding affinity to one or more human Fc gamma receptor(s). Brief Description of the Figures / DrawingsFigure 1A - Figure 1 D depict the double-referenced sensorgrams with fit curves for interactions between selected anti-BCMA antibodies of the present invention and human BCMA.Figure 2 depicts in vivo efficacy studies of various anti-BCMA ADCs in the MM1 S orthotopic multiple myeloma model, including P6E01_VHVL-AcLys-Val-Cit-PABC- Aur0101 ; P5A2_VHVL-AcLys-Val-Cit-PABC-Aur0101 ; P5C1_VHVL-Acl_ys-Val-Cit- PABC-Aur0101 ; P4G4-AcLys-Val-Cit-PABC-Aur0101 ; and P1A1 1 -AcLys-Val-Cit-PABC- Aur0101. NNC is a negative control non-BCMA antibody. "LCQ05" and "LCQ04" correspond to glutamine-containing transglutaminase tag SEQ ID NOs: 474 and 475, respectively.Figure 3 depicts in vivo efficacy of the anti-BCMA ADCs in the MM1 S orthotopic multiple myeloma model, including L3.PY / P6E01 antibody conjugated with 1 ) H7c / N297A / K222R-amino-PEG6-C2-3377, 2) N297Q / K222R-AcLys-Val-Cit-PABC- 0101 , 3) LCQ05 / K222R-AcLys-Val-Cit-PABC-0101 , 4) H7c / N297A / K222R-amino- PEG6-C2-0131 , and 5) N297Q / K222R / LCQ05-AcLys-Val-Cit-PABC-Aur0101. NNC is a control non-BCMA antibody. "LCQ05" and H7c correspond to glutamine-containing transglutaminase tag SEQ ID NO: 474 and SEQ ID NO: 454, respectivelyFigure 4 also depicts in vivo efficacy of the anti-BCMA ADCs in the MM1 S orthotopic multiple myeloma model, including L3.PY / P6E01 antibody conjugated with 1 ) H7c / N297A / K222R-amino-PEG6-C2-3377, 2) N297Q / K222R-AcLys-Val-Cit-PABC- Aur0101 , 3) LCQ05 / K222R-AcLys-Val-Cit-PABC-Aur0101 , 4) H7c / N297A / K222R- amino-PEG6-C2-0131 , and 5) N297Q / K222R / LCQ05-AcLys-Val-Cit-PABC-Aur0101. NNC is a control non-BCMA antibody (antibody-N297Q / K222R-AcLys-VC-PABC-0101 )."LCQ05" and H7c correspond to glutamine-containing transglutaminase tag SEQ ID NO: 474 and SEQ ID NO: 454, respectively.Figure 5 also depicts in vivo efficacy of an anti-BCMA ADC in the MM1 S orthotopic multiple myeloma model. Anti-BCMA antibody COMBO_Rd4_0.6nM-C29 ("Combo C29 Dl) is conjugated to H7c / N297A / K222R-amino-PEG6-C2-131 at doses ranging from 0.1 mg / kg, 0.38 mg / kg, 0.75 mg / kg, 1.5 mg / kg in comparison to NNC, a control non-BCMA antibody (antibody-N297Q / K222R-AcLys-VC-PABC-0101 ) at 3 mg / kg. H7c correspond to glutamine-containing transglutaminase tag SEQ ID NO: 454.Figure 6A - Figure 6F depict the in vivo efficacy of an anti-CD3 / anti-CD20 bispecific antibody in cynomolgus monkeys. B cell depletion following a single dose of bispecific antibody is shown as a percentage of prestudy counts.Figure 7A - Figure 7F depict the in vivo efficacy of an anti-CD3 / anti-CD20 bispecific antibody in cynomolgus monkeys. CD8+ T cell kinetics were tracked following a single dose of bispecific antibody.Figure 8A and Figure 8B depict the in vivo efficacy of an anti-CD3 / anti-CD20 bispecific antibody in cynomolgus monkeys. The effect of the monovalent CD3 antibody on T cell kinetics and proliferation was analyzed.Figures 9A - Figure 9D depict the in vivo efficacy of an anti-CD3 / anti-CD20 bispecific antibody in cynomolgus monkeys. The effect of anti-CD3 arm affinity on B cell depletion was analyzed.Figures 10A and 10B show that the selected anti-CD3 antibodies had Thymidine incorporation reading on human and cynomolgus PBMC.Figure 1 1 A - Figure 1 1 D show that all human anti-EpCam_h2B4 bispecific antibodies have cell killing activity on in vitro setting.Figure 12 shows that a single dose of human anti-BCMA / CD3 bispecific antibody resulted in tumor regression in a dose-dependent manner in an orthotopic MM1.S myeloma model.Figure 13 shows that two doses of human anti-BCMA / CD3 bispecific antibody resulted in increased tumor regression in an orthotopic Molp8 myeloma model.Figure 14 shows that anti-BCMA / CD3 bispecific antibody alone or in combination with standard of care for multiple myeloma (lenalidomide or bortezomib) is more efficacious than lenalidomide and bortezomib combined in orthotopic Molp8 tumor model.Figure 15A - Figure 15C, respectively, show that carfilzomib, lenalidomide, and doxorubicin do not have a negative effect on the function of the anti-BCMA / CD3 bispecific antibody on OPM2 cells as compared to the anti-BCMA / CD3 bispecific antibody alone.Figure 16 shows synergistic effects on the function of anti-BCMA / CD3 bispecific antibody when combined with carfilzomib and lenalidomide in comparison to each molecule alone.Detailed DescriptionThe invention disclosed herein provides antibodies and antibody conjugates (e.g., antibody-drug conjugates) that specifically bind to BCMA (e.g., human BCMA). The invention also provides polynucleotides encoding these antibodies and conjugates, compositions comprising these antibodies and conjugates, and methods of making these antibodies and conjugates. Further, the invention disclosed herein provides antibodies that specifically bind to CD3 (e.g., human CD3) as well as heterodimeric antibodies (e.g., bispecific antibodies) that specifically bind to CD3 and a tumor antigen (e.g., BCMA). The invention also provides polynucleotides encoding these antibodies, compositions comprising these antibodies, and methods of making and using these antibodies. The invention further provides methods for treating a condition associated with malignant BCMA expression in a subject, such as cancer or autoimmune disease, using the antibodies (e.g, BCMA, CD3, or bispecific antibody) or conjugates thereof (BCMA antibody-drug conjugates) as described herein.General TechniquesThe practice of the present invention will employ, unless otherwise indicated, conventional techniques of molecular biology (including recombinant techniques), microbiology, cell biology, biochemistry and immunology, which are within the skill of the art. Such techniques are explained fully in the literature, such as, Molecular Cloning: A Laboratory Manual, second edition (Sambrook et al., 1989) Cold Spring Harbor Press; Oligonucleotide Synthesis (M.J. Gait, ed., 1984); Methods in Molecular Biology, Humana Press; Cell Biology: A Laboratory Notebook (J.E. Cellis, ed., 1998) Academic Press; Animal Cell Culture (R. I. Freshney, ed., 1987); Introduction to Cell and Tissue Culture (J. P. Mather and P.E. Roberts, 1998) Plenum Press; Cell and TissueCulture: Laboratory Procedures (A. Doyle, J.B. Griffiths, and D.G. Newell, eds., 1993- 1998) J. Wiley and Sons; Methods in Enzymology (Academic Press, Inc.); Handbook of Experimental Immunology (D.M. Weir and C.C. Blackwell, eds.); Gene Transfer Vectors for Mammalian Cells (J.M. Miller and M.P. Calos, eds., 1987); Current Protocols in Molecular Biology (F.M. Ausubel et al., eds., 1987); PCR: The Polymerase Chain Reaction, (Mullis et al., eds., 1994); Current Protocols in Immunology (J.E. Coligan et al., eds., 1991); Short Protocols in Molecular Biology (Wiley and Sons, 1999); Immunobiology (C.A. Janeway and P. Travers, 1997); Antibodies (P. Finch, 1997); Antibodies: a practical approach (D. Catty., ed., IRL Press, 1988-1989); Monoclonal antibodies: a practical approach (P. Shepherd and C. Dean, eds., Oxford University Press, 2000); Using antibodies: a laboratory manual (E. Harlow and D. Lane (Cold Spring Harbor Laboratory Press, 1999); The Antibodies (M. Zanetti and J.D. Capra, eds., Harwood Academic Publishers, 1995). DefinitionsAn "antibody" is an immunoglobulin molecule capable of specific binding to a target, such as a carbohydrate, polynucleotide, lipid, polypeptide, etc., through at least one antigen recognition site, located in the variable region of the immunoglobulin molecule. As used herein, the term encompasses not only intact polyclonal or monoclonal antibodies, but also fragments thereof (such as Fab, Fab', F(ab')2, Fv), single chain (ScFv) and domain antibodies (including, for example, shark and camelid antibodies), and fusion proteins comprising an antibody, and any other modified configuration of the immunoglobulin molecule that comprises an antigen recognition site. An antibody includes an antibody of any class, such as IgG, IgA, or IgM (or sub- class thereof), and the antibody need not be of any particular class. Depending on the antibody amino acid sequence of the constant region of its heavy chains, immunoglobulins can be assigned to different classes. There are five major classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, and several of these may be further divided into subclasses (isotypes), e.g., lgG1 , lgG2, lgG3, lgG4, lgA1 and lgA2. The heavy-chain constant regions that correspond to the different classes of immunoglobulins are called alpha, delta, epsilon, gamma, and mu, respectively. The subunit structures and three-dimensional configurations of different classes of immunoglobulins are well known.The term "antigen binding fragment" or "antigen binding portion" of an antibody, as used herein, refers to one or more fragments of an intact antibody that retain the ability to specifically bind to a given antigen (e.g., BCMA or CD3). Antigen binding functions of an antibody can be performed by fragments of an intact antibody. Examples of binding fragments encompassed within the term "antigen binding fragment" of an antibody include Fab; Fab'; F(ab')2; an Fd fragment consisting of the VH and CH1 domains; an Fv fragment consisting of the VL and VH domains of a single arm of an antibody; a single domain antibody (dAb) fragment (Ward et al., Nature 341 :544- 546, 1989), and an isolated complementarity determining region (CDR).An antibody, an antibody conjugate, or a polypeptide that "preferentially binds" or"specifically binds" (used interchangeably herein) to a target (e.g., BCMA protein or CD3 protein) is a term well understood in the art, and methods to determine such specific or preferential binding are also well known in the art. A molecule is said to exhibit "specific binding" or "preferential binding" if it reacts or associates more frequently, more rapidly, with greater duration and / or with greater affinity with a particular cell or substance than it does with alternative cells or substances. An antibody "specifically binds" or "preferentially binds" to a target if it binds with greater affinity, avidity, more readily, and / or with greater duration than it binds to other substances. For example, an antibody that specifically or preferentially binds to a BCMA epitope or CD3 epitope is an antibody that binds this epitope with greater affinity, avidity, more readily, and / or with greater duration than it binds to other BCMA epitopes, non-BCMA epitopes, CD3 epitopes, or non-CD3 epitopes. It is also understood that by reading this definition, for example, an antibody (or moiety or epitope) that specifically or preferentially binds to a first target may or may not specifically or preferentially bind to a second target. As such, "specific binding" or "preferential binding" does not necessarily require (although it can include) exclusive binding. Generally, but not necessarily, reference to binding means preferential binding.A "variable region" of an antibody refers to the variable region of the antibody light chain or the variable region of the antibody heavy chain, either alone or in combination. As known in the art, the variable regions of the heavy and light chain each consist of four framework regions (FR) connected by three complementarity determining regions (CDRs) also known as hypervariable regions. The CDRs in each chain are held together in close proximity by the FRs and, with the CDRs from the otherchain, contribute to the formation of the antigen binding site of antibodies. There are at least two techniques for determining CDRs: (1 ) an approach based on cross-species sequence variability (i.e., Kabat et al. Sequences of Proteins of Immunological Interest, (5th ed., 1991 , National Institutes of Health, Bethesda MD)); and (2) an approach based on crystallographic studies of antigen-antibody complexes (Al-lazikani et al., 1997, J. Molec. Biol. 273:927-948). As used herein, a CDR may refer to CDRs defined by either approach or by a combination of both approaches.A "CDR" of a variable domain are amino acid residues within the variable region that are identified in accordance with the definitions of the Kabat, Chothia, the accumulation of both Kabat and Chothia, AbM, contact, and / or conformational definitions or any method of CDR determination well known in the art. Antibody CDRs may be identified as the hypervariable regions originally defined by Kabat et al. See, e.g., Kabat et al., 1992, Sequences of Proteins of Immunological Interest, 5th ed., Public Health Service, NIH, Washington D.C. The positions of the CDRs may also be identified as the structural loop structures originally described by Chothia and others. See, e.g., Chothia et al., Nature 342:877-883, 1989. Other approaches to CDR identification include the "AbM definition," which is a compromise between Kabat and Chothia and is derived using Oxford Molecular's AbM antibody modeling software (now Accelrys®), or the "contact definition" of CDRs based on observed antigen contacts, set forth in MacCallum et al., J. Mol. Biol., 262:732-745, 1996. In another approach, referred to herein as the "conformational definition" of CDRs, the positions of the CDRs may be identified as the residues that make enthalpic contributions to antigen binding. See, e.g., Makabe et al., Journal of Biological Chemistry, 283: 1 156-1166, 2008. Still other CDR boundary definitions may not strictly follow one of the above approaches, but will nonetheless overlap with at least a portion of the Kabat CDRs, although they may be shortened or lengthened in light of prediction or experimental findings that particular residues or groups of residues or even entire CDRs do not significantly impact antigen binding. As used herein, a CDR may refer to CDRs defined by any approach known in the art, including combinations of approaches. The methods used herein may utilize CDRs defined according to any of these approaches. For any given embodiment containing more than one CDR, the CDRs may be defined in accordance with any of Kabat, Chothia, extended, AbM, contact, and / or conformational definitions.As used herein, "monoclonal antibody" 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 site. Furthermore, in contrast to polyclonal antibody preparations, which typically include different antibodies directed against different determinants (epitopes), each monoclonal antibody is directed against a single determinant on the antigen. 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 and Milstein, Nature 256:495, 1975, or may be made by recombinant DNA methods such as described in U.S. Pat. No. 4,816,567. The monoclonal antibodies may also be isolated from phage libraries generated using the techniques described in McCafferty et al. , Nature 348:552-554, 1990, for example.As used herein, "humanized" antibody refers to forms of non-human (e.g. murine) antibodies that are chimeric immunoglobulins, immunoglobulin chains, or fragments thereof (such as Fv, Fab, Fab', F(ab')2or other antigen binding subsequences of antibodies) that contain minimal sequence derived from non-human immunoglobulin. Preferably, humanized antibodies are human immunoglobulins (recipient antibody) in which residues from a complementarity determining region (CDR) of the recipient are replaced by residues from a CDR of a non-human species (donor antibody) such as mouse, rat, or rabbit having the desired specificity, affinity, and capacity. In some instances, Fv framework region (FR) residues of the human immunoglobulin are replaced by corresponding non-human residues. Furthermore, the humanized antibody may comprise residues that are found neither in the recipient antibody nor in the imported CDR or framework sequences, but are included to further refine and optimize antibody performance. 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 CDR regions correspond to those of a non-human immunoglobulin and all or substantially all of the FR regions are those of a human immunoglobulin consensus sequence. The humanized antibody optimally also willcomprise at least a portion of an immunoglobulin constant region or domain (Fc), typically that of a human immunoglobulin. Preferred are antibodies having Fc regions modified as described in WO 99 / 58572. Other forms of humanized antibodies have one or more CDRs (CDR L1 , CDR L2, CDR L3, CDR H1 , CDR H2, or CDR H3) which are altered with respect to the original antibody, which are also termed one or more CDRs "derived from" one or more CDRs from the original antibody.As used herein, "human antibody" means an antibody having an amino acid sequence corresponding to that of an antibody produced by a human and / or which has been made using any of the techniques for making human antibodies known to those skilled in the art or disclosed herein. This definition of a human antibody includes antibodies comprising at least one human heavy chain polypeptide or at least one human light chain polypeptide. One such example is an antibody comprising murine light chain and human heavy chain polypeptides. Human antibodies can be produced using various techniques known in the art. In one embodiment, the human antibody is selected from a phage library, where that phage library expresses human antibodies (Vaughan et al., Nature Biotechnology, 14:309-314, 1996; Sheets et al., Proc. Natl. Acad. Sci. (USA) 95:6157-6162, 1998; Hoogenboom and Winter, J. Mol. Biol., 227:381 , 1991 ; Marks et al., J. Mol. Biol., 222:581 , 1991 ). Human antibodies can also be made by immunization of animals into which human immunoglobulin loci have been transgenically introduced in place of the endogenous loci, e.g., mice in which the endogenous immunoglobulin genes have been partially or completely inactivated. This approach is described in U.S. Pat. Nos. 5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; and 5,661 ,016. Alternatively, the human antibody may be prepared by immortalizing human B lymphocytes that produce an antibody directed against a target antigen (such B lymphocytes may be recovered from an individual or from single cell cloning of the cDNA, or may have been immunized in vitro). See, e.g., Cole et al. Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, p. 77, 1985; Boerner et al., J. Immunol., 147 (1 ):86-95, 1991 ; and U.S. Pat. No. 5,750,373.The term "chimeric antibody" is intended to refer to antibodies in which the variable region sequences are derived from one species and the constant region sequences are derived from another species, such as an antibody in which the variable region sequences are derived from a mouse antibody and the constant region sequences are derived from a human antibody.The terms "polypeptide", "oligopeptide", "peptide" and "protein" are used interchangeably herein to refer to chains of amino acids of any length, preferably, relatively short (e.g., 10-100 amino acids). The chain may be linear or branched, it may comprise modified amino acids, and / or may be interrupted by non-amino acids. The terms also encompass an amino acid chain that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as conjugation with a labeling component. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid (including, for example, unnatural amino acids, etc.), as well as other modifications known in the art. It is understood that the polypeptides can occur as single chains or associated chains.A "monovalent antibody" comprises one antigen binding site per molecule (e.g., IgG or Fab). In some instances, a monovalent antibody can have more than one antigen binding sites, but the binding sites are from different antigens.A "monospecific antibody" comprises two identical antigen binding sites per molecule (e.g. IgG) such that the two binding sites bind identical epitope on the antigen. Thus, they compete with each other on binding to one antigen molecule. Most antibodies found in nature are monospecific. In some instances, a monospecific antibody can also be a monovalent antibody (e.g. Fab)A "bivalent antibody" comprises two antigen binding sites per molecule (e.g.,IgG). In some instances, the two binding sites have the same antigen specificities. However, bivalent antibodies may be bispecific.A "bispecific" or "dual-specific" is a hybrid antibody having two different antigen binding sites. The two antigen binding sites of a bispecific antibody bind to two different epitopes, which may reside on the same or different protein targets.A "Afunctional" is antibody is an antibody having identical antigen binding sites (i.e., identical amino acid sequences) in the two arms but each binding site can recognize two different antigens.A "heteromultimer", "heteromultimeric complex", or "heteromultimeric polypeptide" is a molecule comprising at least a first polypeptide and a second polypeptide, wherein the second polypeptide differs in amino acid sequence from the first polypeptide by at least one amino acid residue. The heteromultimer can comprise a "heterodimer" formed by the first and second polypeptide or can form higher ordertertiary structures where polypeptides in addition to the first and second polypeptide are present.A "heterodimer," "heterodimeric protein," "heterodimeric complex," or "heteromultimeric polypeptide" is a molecule comprising a first polypeptide and a second polypeptide, wherein the second polypeptide differs in amino acid sequence from the first polypeptide by at least one amino acid residue.The "hinge region," "hinge sequence", and variations thereof, as used herein, includes the meaning known in the art, which is illustrated in, for example, Janeway et al., ImmunoBiology: the immune system in health and disease, (Elsevier Science Ltd., NY) (4th ed., 1999); Bloom et al., Protein Science (1997), 6:407-415; Humphreys et al., J. Immunol. Methods (1997), 209:193-202.The "immunoglobulin-like hinge region," "immunoglobulin-like hinge sequence," and variations thereof, as used herein, refer to the hinge region and hinge sequence of an immunoglobulin-like or an antibody-like molecule (e.g., immunoadhesins). In some embodiments, the immunoglobulin-like hinge region can be from or derived from any lgG1 , lgG2, lgG3, or lgG4 subtype, or from IgA, IgE, IgD or IgM, including chimeric forms thereof, e.g., a chimeric lgG1 / 2 hinge region.The term "immune effector cell" or "effector cell as used herein refers to a cell within the natural repertoire of cells in the human immune system which can be activated to affect the viability of a target cell. The viability of a target cell can include cell survival, proliferation, and / or ability to interact with other cells.Antibodies of the invention can be produced using techniques well known in the art, e.g., recombinant technologies, phage display technologies, synthetic technologies or combinations of such technologies or other technologies readily known in the art (see, for example, Jayasena, S.D., Clin. Chem., 45: 1628-50, 1999 and Fellouse, F.A., et al, J. Mol. Biol., 373(4):924-40, 2007).As known in the art, "polynucleotide," or "nucleic acid," as used interchangeably herein, refer to chains of nucleotides of any length, and include DNA and RNA. The nucleotides can be deoxyribonucleotides, ribonucleotides, modified nucleotides or bases, and / or their analogs, or any substrate that can be incorporated into a chain by DNA or RNA polymerase. A polynucleotide may comprise modified nucleotides, such as methylated nucleotides and their analogs. If present, modification to the nucleotide structure may be imparted before or after assembly of the chain. The sequence ofnucleotides may be interrupted by non-nucleotide components. A polynucleotide may be further modified after polymerization, such as by conjugation with a labeling component. Other types of modifications include, for example, "caps", substitution of one or more of the naturally occurring nucleotides with an analog, internucleotide modifications such as, for example, those with uncharged linkages (e.g., methyl phosphonates, phosphotriesters, phosphoamidates, carbamates, etc.) and with charged linkages (e.g., phosphorothioates, phosphorodithioates, etc.), those containing pendant moieties, such as, for example, proteins (e.g., nucleases, toxins, antibodies, signal peptides, poly-L-lysine, etc.), those with intercalators (e.g., acridine, psoralen, etc.), those containing chelators (e.g., metals, radioactive metals, boron, oxidative metals, etc.), those containing alkylators, those with modified linkages (e.g., alpha anomeric nucleic acids, etc.), as well as unmodified forms of the polynucleotide(s). Further, any of the hydroxyl groups ordinarily present in the sugars may be replaced, for example, by phosphonate groups, phosphate groups, protected by standard protecting groups, or activated to prepare additional linkages to additional nucleotides, or may be conjugated to solid supports. The 5' and 3' terminal OH can be phosphorylated or substituted with amines or organic capping group moieties of from 1 to 20 carbon atoms. Other hydroxyls may also be derivatized to standard protecting groups. Polynucleotides can also contain analogous forms of ribose or deoxyribose sugars that are generally known in the art, including, for example, 2'-0-methyl-, 2'-0-allyl, 2'-fluoro- or 2'-azido-ribose, carbocyclic sugar analogs, alpha- or beta-anomeric sugars, epimeric sugars such as arabinose, xyloses or lyxoses, pyranose sugars, furanose sugars, sedoheptuloses, acyclic analogs and abasic nucleoside analogs such as methyl riboside. One or more phosphodiester linkages may be replaced by alternative linking groups. These alternative linking groups include, but are not limited to, embodiments wherein phosphate is replaced by P(0)S("thioate"), P(S)S ("dithioate"), (0)NR2("amidate"), P(0)R, P(0)OR', CO or CH2("formacetal"), in which each R or R' is independently H or substituted or unsubstituted alkyl (1-20 C) optionally containing an ether (-0-) linkage, aryl, alkenyl, cycloalkyl, cycloalkenyl or araldyl. Not all linkages in a polynucleotide need be identical. The preceding description applies to all polynucleotides referred to herein, including RNA and DNA.As known in the art a "constant region" of an antibody refers to the constant region of the antibody light chain or the constant region of the antibody heavy chain, either alone or in combination.As used herein, "substantially pure" refers to material which is at least 50% pure (i.e., free from contaminants), more preferably, at least 90% pure, more preferably, at least 95% pure, yet more preferably, at least 98% pure, and most preferably, at least 99% pure.A "host cell" includes an individual cell or cell culture that can be or has been a recipient for vector(s) for incorporation of polynucleotide inserts. Host cells include progeny of a single host cell, and the progeny may not necessarily be completely identical (in morphology or in genomic DNA complement) to the original parent cell due to natural, accidental, or deliberate mutation. A host cell includes cells transfected in vivo with a polynucleotide(s) of this invention.As known in the art, the term "Fc region" is used to define a C-terminal region of an immunoglobulin heavy chain. The "Fc region" may be a native sequence Fc region or a variant Fc region. Although the boundaries of the Fc region of an immunoglobulin heavy chain might vary, the human IgG heavy chain Fc region is usually defined to stretch from an amino acid residue at position Cys226, or from Pro230, to the carboxyl- terminus thereof. The numbering of the residues in the Fc region is that of the EU index as in Kabat. Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md., 1991. The Fc region of an immunoglobulin generally comprises two constant regions, CH2 and CH3.As used in the art, "Fc receptor" and "FcR" describe a receptor that binds to the Fc region of an antibody. The preferred FcR is a native sequence human FcR. Moreover, a preferred FcR is one which binds an IgG antibody (a gamma receptor) and includes receptors of the FcyRI, FcyRII, and FcyRIII subclasses, including allelic variants and alternatively spliced forms of these receptors. FcyRII receptors include FcyRIIA (an "activating receptor") and FcyRIIB (an "inhibiting receptor"), which have similar amino acid sequences that differ primarily in the cytoplasmic domains thereof. FcRs are reviewed in Ravetch and Kinet, Ann. Rev. Immunol., 9:457-92, 1991 ; Capel et al., Immunomethods, 4:25-34, 1994; and de Haas et al., J. Lab. Clin. Med., 126:330-41 , 1995. "FcR" also includes the neonatal receptor, FcRn, which is responsible for thetransfer of maternal IgGs to the fetus (Guyer et al., J. Immunol., 1 17:587, 1976; and Kim et al., J. Immunol., 24:249, 1994).The term "compete", as used herein with regard to an antibody, means that a first antibody, or an antigen binding fragment (or portion) thereof, binds to an epitope in a manner sufficiently similar to the binding of a second antibody, or an antigen binding portion thereof, such that the result of binding of the first antibody with its cognate epitope is detectably decreased in the presence of the second antibody compared to the binding of the first antibody in the absence of the second antibody. The alternative, where the binding of the second antibody to its epitope is also detectably decreased in the presence of the first antibody, can, but need not be the case. That is, a first antibody can inhibit the binding of a second antibody to its epitope without that second antibody inhibiting the binding of the first antibody to its respective epitope. However, where each antibody detectably inhibits the binding of the other antibody with its cognate epitope or ligand, whether to the same, greater, or lesser extent, the antibodies are said to "cross-compete" with each other for binding of their respective epitope(s). Both competing and cross-competing antibodies are encompassed by the present invention. Regardless of the mechanism by which such competition or cross- competition occurs (e.g., steric hindrance, conformational change, or binding to a common epitope, or portion thereof), the skilled artisan would appreciate, based upon the teachings provided herein, that such competing and / or cross-competing antibodies are encompassed and can be useful for the methods disclosed herein.A "functional Fc region" possesses at least one effector function of a native sequence Fc region. Exemplary "effector functions" include C1 q binding; complement dependent cytotoxicity; Fc receptor binding; antibody-dependent cell-mediated cytotoxicity; phagocytosis; down-regulation of cell surface receptors (e.g. B cell receptor), etc. Such effector functions generally require the Fc region to be combined with a binding domain (e.g. an antibody variable domain) and can be assessed using various assays known in the art for evaluating such antibody effector functions.A "native sequence Fc region" comprises an amino acid sequence identical to the amino acid sequence of an Fc region found in nature. A "variant Fc region" comprises an amino acid sequence which differs from that of a native sequence Fc region by virtue of at least one amino acid modification, yet retains at least one effector function of the native sequence Fc region. In some embodiments, the variant Fc regionhas at least one amino acid substitution compared to a native sequence Fc region or to the Fc region of a parent polypeptide, e.g. from about one to about ten amino acid substitutions, and preferably, from about one to about five amino acid substitutions in a native sequence Fc region or in the Fc region of the parent polypeptide. The variant Fc region herein will preferably possess at least about 80% sequence identity with a native sequence Fc region and / or with an Fc region of a parent polypeptide, and most preferably, at least about 90% sequence identity therewith, more preferably, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% sequence identity therewith.The term "effector function" refers to the biological activities attributable to the Fc region of an antibody. Examples of antibody effector functions include, but are not limited to, antibody-dependent cell-mediated cytotoxicity (ADCC), Fc receptor binding, complement dependent cytotoxicity (CDC), phagocytosis, C1 q binding, and down regulation of cell surface receptors (e.g., B cell receptor; BCR). See, e.g., U.S. Pat No. 6,737,056. Such effector functions generally require the Fc region to be combined with a binding domain (e.g., an antibody variable domain) and can be assessed using various assays known in the art for evaluating such antibody effector functions. An exemplary measurement of effector function is through Fcy3 and / or C1 q binding.As used herein "antibody-dependent cell-mediated cytotoxicity" or "ADCC" refers to a cell-mediated reaction in which nonspecific cytotoxic cells that express Fc receptors (FcRs) (e.g. natural killer (NK) cells, neutrophils, and macrophages) recognize bound antibody on a target cell and subsequently cause lysis of the target cell. ADCC activity of a molecule of interest can be assessed using an in vitro ADCC assay, such as that described in U.S. Patent No. 5,500,362 or 5,821 ,337. Useful effector cells for such assays include peripheral blood mononuclear cells (PBMC) and NK cells. Alternatively, or additionally, ADCC activity of the molecule of interest may be assessed in vivo, e.g., in an animal model such as that disclosed in Clynes et al., 1998, PNAS (USA), 95:652-656."Complement dependent cytotoxicity" or "CDC" refers to the lysing of a target in the presence of complement. The complement activation pathway is initiated by the binding of the first component of the complement system (C1 q) to a molecule (e.g. an antibody) complexed with a cognate antigen. To assess complement activation, a CDCassay, e.g. as described in Gazzano-Santoro et al., J. Immunol. Methods, 202: 163 (1996), may be performed.As used herein, "treatment" is an approach for obtaining beneficial or desired clinical results. For purposes of this invention, beneficial or desired clinical results include, but are not limited to, one or more of the following: reducing the proliferation of (or destroying) neoplastic or cancerous cells, inhibiting metastasis of neoplastic cells, remission of a BCMA associated disease (e.g., cancer or autoimmune disease), decreasing symptoms resulting from a BCMA associated disease (e.g., cancer or autoimmune disease), increasing the quality of life of those suffering from a BCMA associated disease (e.g., cancer or autoimmune disease), decreasing the dose of other medications required to treat a BCMA associated disease (e.g., cancer or autoimmune disease), delaying the progression of a BCMA associated disease (e.g., cancer or autoimmune disease), curing a BCMA associated disease (e.g., cancer or autoimmune disease), and / or prolong survival of patients having a BCMA associated disease (e.g., cancer or autoimmune disease)."Ameliorating" means a lessening or improvement of one or more symptoms as compared to not administering a BCMA antibody or a BCMA antibody conjugate. "Ameliorating" also includes shortening or reduction in duration of a symptom.As used herein, an "effective dosage" or "effective amount" of drug, compound, or pharmaceutical composition is an amount sufficient to effect any one or more beneficial or desired results. For prophylactic use, beneficial or desired results include eliminating or reducing the risk, lessening the severity, or delaying the outset of the disease, including biochemical, histological and / or behavioral symptoms of the disease, its complications and intermediate pathological phenotypes presenting during development of the disease. For therapeutic use, beneficial or desired results include clinical results such as reducing incidence or amelioration of one or more symptoms of various BCMA associated diseases or conditions (such as multiple myeloma), decreasing the dose of other medications required to treat the disease, enhancing the effect of another medication, and / or delaying the progression of the BCMA associated disease of patients. An effective dosage can be administered in one or more administrations. For purposes of this invention, an effective dosage of drug, compound, or pharmaceutical composition is an amount sufficient to accomplish prophylactic or therapeutic treatment either directly or indirectly. As is understood in the clinicalcontext, an effective dosage of a drug, compound, or pharmaceutical composition may or may not be achieved in conjunction with another drug, compound, or pharmaceutical composition. Thus, an "effective dosage" may be considered in the context of administering one or more therapeutic agents, and a single agent may be considered to be given in an effective amount if, in conjunction with one or more other agents, a desirable result may be or is achieved.An "individual" or a "subject" is a mammal, more preferably, a human. Mammals also include, but are not limited to, farm animals, sport animals, pets, primates, horses, dogs, cats, mice and rats.As used herein, "vector" means a construct, which is capable of delivering, and, preferably, expressing, one or more gene(s) or sequence(s) of interest in a host cell. Examples of vectors include, but are not limited to, viral vectors, naked DNA or RNA expression vectors, plasmid, cosmid or phage vectors, DNA or RNA expression vectors associated with cationic condensing agents, DNA or RNA expression vectors encapsulated in liposomes, and certain eukaryotic cells, such as producer cells.As used herein, "expression control sequence" means a nucleic acid sequence that directs transcription of a nucleic acid. An expression control sequence can be a promoter, such as a constitutive or an inducible promoter, or an enhancer. The expression control sequence is operably linked to the nucleic acid sequence to be transcribed.As used herein, "pharmaceutically acceptable carrier" or "pharmaceutical acceptable excipient" includes any material which, when combined with an active ingredient, allows the ingredient to retain biological activity and is non-reactive with the subject's immune system. Examples include, but are not limited to, any of the standard pharmaceutical carriers such as a phosphate buffered saline solution, water, emulsions such as oil / water emulsion, and various types of wetting agents. Preferred diluents for aerosol or parenteral administration are phosphate buffered saline (PBS) or normal (0.9%) saline. Compositions comprising such carriers are formulated by well known conventional methods (see, for example, Remington's Pharmaceutical Sciences, 18th edition, A. Gennaro, ed., Mack Publishing Co., Easton, PA, 1990; and Remington, The Science and Practice of Pharmacy 21 st Ed. Mack Publishing, 2005).The term "acyl donor glutamine-containing tag" or "glutamine tag" as used herein refers to a polypeptide or a protein containing one or more Gin residue(s) that acts as a transglutaminase amine acceptor. See, e.g., WO2012059882 and WO2015015448.The term "kon" or "ka", as used herein, refers to the rate constant for association of an antibody to an antigen. Specifically, the rate constants (kon / kaand k0ff / kd) and equilibrium dissociation constants are measured using whole antibody (i.e. bivalent) and monomeric BCMA proteins.The term "koff" or "kd", as used herein, refers to the rate constant for dissociation of an antibody from the antibody / antigen complex.The term "KD", as used herein, refers to the equilibrium dissociation constant of an antibody-antigen interaction.Reference to "about" a value or parameter herein includes (and describes) embodiments that are directed to that value or parameter per se. For example, description referring to "about X" includes description of "X." Numeric ranges are inclusive of the numbers defining the range.It is understood that wherever embodiments are described herein with the language "comprising," otherwise analogous embodiments described in terms of "consisting of and / or "consisting essentially of" are also provided.Where aspects or embodiments of the invention are described in terms of a Markush group or other grouping of alternatives, the present invention encompasses not only the entire group listed as a whole, but each member of the group individually and all possible subgroups of the main group, but also the main group absent one or more of the group members. The present invention also envisages the explicit exclusion of one or more of any of the group members in the claimed invention.Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. In case of conflict, the present specification, including definitions, will control. Throughout this specification and claims, the word "comprise," or variations such as "comprises" or "comprising" will be understood to imply the inclusion of a stated integer or group of integers but not the exclusion of any other integer or group of integers. Unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular.Exemplary methods and materials are described herein, although methods and materials similar or equivalent to those described herein can also be used in the practice or testing of the present invention. The materials, methods, and examples are illustrative only and not intended to be limiting.BCMA Antibodies and Methods of Making ThereofThe present invention provides an antibody that binds to BCMA (e.g., human BCMA (e.g., SEQ ID NO: 353 or accession number: Q02223-2) and characterized by any one or more of the following characteristics: (a) treat, prevent, ameliorate one or more symptoms of a condition associated with malignant cells expressing BCMA in a subject (e.g., B-cell related cancer such as multiple myeloma); (b) inhibit tumor growth or progression in a subject (who has a malignant tumor expressing BCMA); (c) inhibit metastasis of cancer (malignant) cells expressing BCMA in a subject (who has one or more malignant cells expressing BCMA); (f) induce regression (e.g., long-term regression) of a tumor expressing BCMA; (d) exert cytotoxic activity in malignant cells expressing BCMA; and (e) block BCMA interaction with other yet to be identified factors.In one aspect, provided is an isolated antibody, or an antigen binding fragment thereof, which specifically binds to B-Cell Maturation Antigen (BCMA), wherein the antibody comprises (a) a heavy chain variable (VH) region comprising (i) a VH complementary determining region one (CDR1 ) comprising the sequence SYXi MX2, wherein Xi is A or P; and X2is T, N, or S (SEQ ID NO: 301 ), GFTFXiSY, wherein Xi is G or S (SEQ ID NO: 302), or GFTFX SYX2MX3lwherein X is G or S, X2is A or P; and X3is T, N, or S (SEQ ID NO: 303); (ii) a VH CDR2 comprising the sequence AX.iX2X3X4GX5X6X7XeYADX9X.i0KG, wherein X-, is I, V, T, H, L, A, or C; X2is S, D, G, T, I, L, F, M, or V; X3is G, Y, L, H, D, A, S, or M; X4is S, Q, T, A, F, or W; X5is G or T;X6is N, S, P, Y, W, or F; X7is S, T, I, L, T, A, R, V, K, G, or C; X8is F, Y, P, W, H, or G; X9is V, R, or L; and X10is G or T (SEQ ID NO: 305), or X1X2X3X4X5X6,wherein X-, is S, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M; X3is S, G, F, or W; X4is G or S; X5is G or T; and X6is N, S, P, Y, or W (SEQ ID NO: 306); and iii) a VH CDR3 comprising the sequence VSPIX-|X2X3X4,wherein X-i is A or Y; X2is A or S; and X3is G, Q, L, P, or E (SEQ ID NO: 307), or YWPMX X2, wherein X-, is D, S, T, or A; and X2is I, S, L, P, or D (SEQ ID NO: 308); and / or a light chain variable (VL) region comprising (i) a VL CDR1comprising the sequence XiX2X3X4X5X6X7X8X9XioXiiXi2, wherein Xi is R, G, W, A, or C; X2is A, P, G, L, C, or S; X3is S, G, or R; X4is Q, C, E, V, or I; X5is S, P, G, A, R, or D; X6is V, G, I, or L; X7is S, E, D, P, or G; X8is S, P, F, A, M, E, V, N, D, or Y; X9is I, T, V, E, S, A, M, Q, Y, H, R, or F; X10is Y or F; Xn is L, W, or P; and X12is A, S, or G (SEQ ID NO: 309); (ii) a VL CDR2 comprising the sequence X ASX2RAX3, wherein is G or D; X2is S or I; and X3is T or P (SEQ ID NO: 310); and (iii) a VL CDR3 comprising the sequence QQYX X2X3PX4T, wherein X-, is G, Q, E, L, F, A, S, M, K, R, or Y; X2is S, R, T, G, V, F, Y, D, A, H, V, E, K, or C; X3is W, F, or S; and X4is L or I (SEQ ID NO: 31 1 ), or QQYX1X2X3PX4, wherein X-, is G, Q, E, L, F, A, S, M, R, K, or Y; X2is S, R, T, G, R, V, D, A, H, E, K, C, F, or Y; X3is W, S, or F; and X4is L or I (SEQ ID NO: 312).In another aspect, provided is an isolated antibody, or an antigen binding fragment thereof, which specifically binds to BCMA, wherein the antibody comprises: a VH region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 2, 3, 7, 8, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 35, 37, 39, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 83, 87, 92, 95, 97, 99, 101 , 104, 106, 1 10, 1 12, 1 14, 1 18, 120, 122, 1 12, 125, 127, 313, 314, 363, or 365; and / or a VL region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 1 , 4, 5, 6, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 34, 36, 38, 40, 41 , 43, 45, 47, 49, 51 , 53, 55, 57, 59, 61 , 63, 65, 67, 69, 71 , 73, 75, 77, 79, 317, 80, 81 , 82, 84, 85, 86, 88, 89, 90, 91 , 93, 94, 96, 98, 100, 102, 103, 105, 107, 108, 109, 1 1 1 , 1 13, 1 15, 1 16, 1 17, 1 19, 121 , 123, 124, 126, 128, 315, 316, or 364.In some embodiments, provided is an antibody having any one of partial light chain sequence as listed in Table 1 and / or any one of partial heavy chain sequence as listed in Table 1.Table 1mAb Light Chain Heavy ChainP6E01 / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA P6E01 ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YGSPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 1 ) VSS (SEQ ID NO: 2)mAb Light Chain Heavy ChainP6E01 / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H3.AQ ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YGSPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 1 ) VSS (SEQ ID NO: 3)L1 .LG EIVLTQSPGTLSLSPGERATLSC EVQLLESGGGLVQPGGSLRLSCA F / L3.K RASQSLGSFYLAWYQQKPGQA ASGFTFGSYAMTWVRQAPGKGLE W / P6E PRLLIYGASSRATGIPDRFSGSG WVSAISGSGGNTFYADSVKGRFTI 01 SGTDFTLTISRLEPEDFAVYYCKH SRDNSKNTLYLQMNSLRAEDTAVYGWPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 4) VSS (SEQ ID NO: 2)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / P6E RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI 01 GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 5) VSS (SEQ ID NO: 2)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / P6E RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI 01 GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 6) VSS (SEQ ID NO: 2)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AL GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARARVSPIAALMDYWGQGTLNO: 4) VTVSS (SEQ ID NO: 7)mAb Light Chain Heavy ChainL1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AP GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAPMDYWGQGTLVT NO: 4) VSS (SEQ ID NO: 8)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AQ GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAQMDYWGQGTLVT NO: 4) VSS (SEQ ID NO: 3)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.P ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI P GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAPMDYWGQGTLVT ID NO: 9) VSS (SEQ ID NO: 8)EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAL1 .LG ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE F / L3.PRLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIY / H3.AQ GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 9) VSS (SEQ ID NO: 3)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI L GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAALMDYWGQGTLVT ID NO: 10) VSS (SEQ ID NO: 7)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAmAb Light Chain Heavy ChainF / L3.N ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI P GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAPMDYWGQGTLVT ID NO: 10) VSS (SEQ ID NO: 8)L1 .LG EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSLGSFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 10) VSS (SEQ ID NO: 3)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AL GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAALMDYWGQGTLVT NO: 1 1 ) VSS (SEQ ID NO: 7)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AP GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAPMDYWGQGTLVT NO: 1 1 ) VSS (SEQ ID NO: 8)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.K ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE W / H3. RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI AQ GTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAQMDYWGQGTLVT NO: 1 1 ) VSS (SEQ ID NO: 3)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.P ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLEmAb Light Chain Heavy ChainY / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 12) VSS (SEQ ID NO: 3)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI L GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAALMDYWGQGTLVT ID NO: 13) VSS (SEQ ID NO: 7)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI P GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAPMDYWGQGTLVT ID NO: 13) VSS (SEQ ID NO: 8)L1 .GD EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA F / L3.N ASQSVGDFYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Y / H3.A RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 14) VSS (SEQ ID NO: 3)L3.KVW EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA P6E01 ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKHY SRDNSKNTLYLQMNSLRAEDTAV GWPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 15) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA P6E01 ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTImAb Light Chain Heavy ChainGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 2)L3.NY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA P6E01 ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YNYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 17) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE P6E01 RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE P6E01 RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE P6E01 LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE P6E01 RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVmAb Light Chain Heavy ChainYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE P6E01 RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE P6E01 RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H2.QR ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQRKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H2.DY ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAIDYSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H2.YQ ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISYQGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVTmAb Light Chain Heavy ChainID NO: 16) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAH2.LT ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISLTGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVTID NO: 16) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAH2.HA ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISHAGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVTID NO: 16) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAH2.QL ASQS VSSSYLA WYQ QKPGQAPRLLI ASGFTFGSYAMTWVRQAPGKGLEYGASSRATGIPDRFSGSGSGTDFT WVSAISGSGGNTFYADQLKGRFTILTISRLEPED F A VYYC QHYPYPPSFT SRDNSKNTLYLQMNSLRAEDTAVFGQGTKVEIK (SEQ ID NO: 16) YYCARVSPIASGMDYWGQGTLVTVSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAH3.YA ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIYAGMDYWGQGTLVTID NO: 16) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAH3.AE ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAEMDYWGQGTLVTID NO: 16) VSS (SEQ ID NO: 31 )mAb Light Chain Heavy ChainL3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H3.AQ ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA H3.TA ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE Q RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCTRVSPIAAQMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA P6E01 ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLERLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 16) VSS (SEQ ID NO: 2)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QR RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQRKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.DY RLLIYGASSRATGIPDRFSGSGS WVSAIDYSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAmAb Light Chain Heavy ChainLLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.YQ RLLIYGASSRATGIPDRFSGSGS WVSAISYQGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.LT RLLIYGASSRATGIPDRFSGSGS WVSAISLTGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.HA RLLIYGASSRATGIPDRFSGSGS WVSAISHAGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QL RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQLKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.YA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIYAGMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLEmAb Light Chain Heavy ChainH3.AE RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAEMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 31 )L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AQ RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA LLPS / ASQSVSSSYPSWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.TA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCTRVSPIAAQMDYWGQGTLVT ID NO: 18) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QR RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQRKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.DY RLLIYGASSRATGIPDRFSGSGS WVSAIDYSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.YQ RLLIYGASSRATGIPDRFSGSGS WVSAISYQGGNTFYADSVKGRFTImAb Light Chain Heavy ChainGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.LT RLLIYGASSRATGIPDRFSGSGS WVSAISLTGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.HA RLLIYGASSRATGIPDRFSGSGS WVSAISHAGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QL RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQLKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.YA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIYAGMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AE RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAVmAb Light Chain Heavy ChainYPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAEMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 31 )L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AQ RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.AH / ASQSVSAHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.TA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCTRVSPIAAQMDYWGQGTLVT ID NO: 19) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.QR LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADQRKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.DY LLIYGASSRATGIPDRFSGSGSG WVSAIDYSGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.YQ LLIYGASSRATGIPDRFSGSGSG WVSAISYQGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAVmAb Light Chain Heavy ChainYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.LT LLIYGASSRATGIPDRFSGSGSG WVSAISLTGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.HA LLIYGASSRATGIPDRFSGSGSG WVSAISHAGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H2.QL LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADQLKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H3.YA LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIYAGMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H3.AE LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAEMDYWGQGTLVTmAb Light Chain Heavy ChainNO: 20) VSS (SEQ ID NO: 31 )L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H3.AQ LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADSVKGRFTITDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAQMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.FF / ASQSVSSFFLAWYQQKPGQAPR ASGFTFGSYAMTWVRQAPGKGLE H3.TA LLIYGASSRATGIPDRFSGSGSG WVSAISGSGGNTFYADSVKGRFTI Q TDFTLTISRLEPEDFAVYYCQHYP SRDNSKNTLYLQMNSLRAEDTAV YPPSFTFGQGTKVEIK (SEQ ID YYCTRVSPIAAQMDYWGQGTLVT NO: 20) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QR RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQRKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.HA RLLIYGASSRATGIPDRFSGSGS WVSAISHAGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIASGMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AE RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAEMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 31 )mAb Light Chain Heavy ChainL3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AQ RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCARVSPIAAQMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L1.PH / ASQSVSPHYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.TA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YPYPPSFTFGQGTKVEIK (SEQ YYCTRVSPIAAQMDYWGQGTLVT ID NO: 21 ) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QR RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQRKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 24)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.DY RLLIYGASSRATGIPDRFSGSGS WVSAIDYSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.YQ RLLIYGASSRATGIPDRFSGSGS WVSAISYQGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAmAb Light Chain Heavy ChainL3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.LT RLLIYGASSRATGIPDRFSGSGS WVSAISLTGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.HA RLLIYGASSRATGIPDRFSGSGS WVSAISHAGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 28)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QL RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQLKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.YA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIYAGMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KY / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.TA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCKYY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCTRVSPIAAQMDYWGQGTLVT NO: 22) VSS (SEQ ID NO: 32)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLEmAb Light Chain Heavy ChainH2.DY RLLIYGASSRATGIPDRFSGSGS WVSAIDYSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 25)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.YQ RLLIYGASSRATGIPDRFSGSGS WVSAISYQGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 26)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.LT RLLIYGASSRATGIPDRFSGSGS WVSAISLTGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 27)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H2.QL RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADQLKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIASGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 29)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.YA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIYAGMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 30)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLEmAb Light Chain Heavy ChainH3.AE RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAEMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 31 )L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.AQ RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCARVSPIAAQMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 3)L3.PY / EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA L3.KF / ASQSVSSSYLAWYQQKPGQAP ASGFTFGSYAMTWVRQAPGKGLE H3.TA RLLIYGASSRATGIPDRFSGSGS WVSAISGSGGNTFYADSVKGRFTI Q GTDFTLTISRLEPEDFAVYYCKFY SRDNSKNTLYLQMNSLRAEDTAV PYPPSFTFGQGTKVEIK (SEQ ID YYCTRVSPIAAQMDYWGQGTLVT NO: 23) VSS (SEQ ID NO: 32)P5A2_ EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA VHVL ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE RLLMYDASIRATGIPDRFSGSGS WVS Al S D SG G ST YYA DSVKG R FT I GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAV YGSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 34) (SEQ ID NO: 33)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSVIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLE nM_C0 LLMYDASIRATGIPDRFSGSGSG WVSAISDSGGSAWYADSVKGRFT 6 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVQRWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 36) (SEQ ID NO: 35)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE nM_C0 RLLMYDASIRATGIPDRFSGSGS WVSAISDSGGSMWYADSVKGRFmAb Light Chain Heavy Chain9 GTDFTLTISRLEPEDFAVYYCQQ TISRDNSKNTLYLQMNSLRAEDTAYQSWPLTFGQGTKVEIK (SEQ ID VYYCARYWPMSLWGQGTLVTVS NO: 38) S (SEQ ID NO: 37)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSDIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C16 LLMYDASIRATGIPDRFSGSGSG WVSAISdFGGSTYYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAV QTWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 40) (SEQ ID NO: 39)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVS N LYLAWYQ Q KPG Q A P ASGFTFSSYAMNWVRQAPGKGLEM_C03 RLLMYDASIRATGIPDRFSGSGS WVSAISDSGGSTYYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAV YQGWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 41 ) (SEQ ID NO: 33)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSAYYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C01 RLLMYDASIRATGIPDRFSGSGS WVSAITASGGSTYYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAV YERWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 43) (SEQ ID NO: 42)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSSLYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C26 LLMYDASIRATGIPDRFSGSGSG WVSAISDSGGSTYYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAV QVWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 45) (SEQ ID NO: 44)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C25 RLLMYDASIRATGIPDRFSGSGS WVSAISdSGGSRWYADSVKGRFTGTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVmAb Light Chain Heavy ChainYLDWPLTFGQGTKVEIK (SEQ ID YYCARYWPMTPWGQGTLVTVSS NO: 47) (SEQ ID NO: 46)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C22 RLLMYDASIRATGIPDRFSGSGS WVSAVLdSGGSTYYADSVKGRFTGTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAV YQVWPLTFGQGTKVEIK (SEQ ID YYCARYWPMTPWGQGTLVTVSS NO: 49) (SEQ ID NO: 48)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSVIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C19 LLMYDASIRATGIPDRFSGSGSG WVSAISdSGGSRWYADSVKGRFTTDFTLTISRLEPEDFAVYYCQQYL ISRDNSKNTLYLQMNSLRAEDTAV AWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSDWGQGTLVTVSS NO: 51 ) (SEQ ID NO: 50)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE nM_C0 RLLMYDASIRATGIPDRFSGSGS WVSAISdSGGSKWYADSVKGRFT 3 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYFTWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 53) (SEQ ID NO: 52)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSPvYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C07 LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFTTDFTLTISRLEPEDFAVYYCQQYE ISRDNSKNTLYLQMNSLRAEDTAV RWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 55) (SEQ ID NO: 54)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSVEYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C23 RLLMYDASIRATGIPDRFSGSGS WVS AISdSGGSGWYADSVKG R FTGTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAV YARWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSSmAb Light Chain Heavy ChainNO: 57) (SEQ ID NO: 56)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSEIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLE nM_C1 LLMYDASIRATGIPDRFSGSGSG WVSAVLdSGGSTYYADSVKGRFT 8 TDFTLTISRLEPEDFAVYYCQQYF ISRDNSKNTLYLQMNSLRAEDTAVGWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 59) (SEQ ID NO: 58)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVEMSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C10 RLLMYDASIRATGIPDRFSGSGS WVS AISdSGGSCWYADSVKG R FTGTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAV YAHWPLTFGQGTKVEIK (SEQ ID YYCARYWPMTPWGQGTLVTVSS NO: 61 ) (SEQ ID NO: 60)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLEM_C05 RLLMYDASIRATGIPDRFSGSGS WVSAIFaSGGSTYYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAV YQRWPLTFGQGTKVEIK (SEQ ID YYCARYWPMTPWGQGTLVTVSS NO: 63) (SEQ ID NO: 62)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSAQYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE nM_C1 RLLMYDASIRATGIPDRFSGSGS WVS AISqWGGSLPYADSVKG R FT 0 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYQRWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 65) (SEQ ID NO: 64)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSAIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C04 LLMYDASIRATGIPDRFSGSGSG WVSAIMsSGGPLYYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAV QVWPLTFGQGTKVEIK (SEQ ID YYCARYWPMALWGQGTLVTVSS NO: 67) (SEQ ID NO: 66)mAb Light Chain Heavy ChainA02_R EIVLTQSPGTLSLSPGERATLSCG EVQLLESGGGLVQPGGSLRLSCA d4_0.6 PSQSVSSSYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLE nM_C2 LLMYDASIRATGIPDRFSGSGSG WVS Al LmSGGSTYYADSVKG R FT I 6 TDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAVQSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 69) (SEQ ID NO: 68)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSSYWAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE nM_C1 RLLMYDASIRATGIPDRFSGSGS WVSAISdSGGYRYYADSVKGRFTI 3 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYESWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 71 ) (SEQ ID NO: 70)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 GGQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE nM_C0 RLLMYDASIRATGIPDRFSGSGS WVSAILsSGGSTYYADSVKGRFTI 1 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYQSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 73) (SEQ ID NO: 72)A02_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSFIYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLEM_C08 LLMYDASIRATGIPDRFSGSGSG WVSAILdSGGSTYYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAV GSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSPWGQGTLVTVSS NO: 75) (SEQ ID NO: 74)P5C1_ EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA VHVL ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE LLIYDASSRAPGIPDRFSGSGSG WVSAIGGSGGSTYYADSVKGRFT TDFTLTISRLEPEDFAVYYCQQYS ISRDNSKNTLYLQMNSLRAEDTAV TSPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 77) (SEQ ID NO: 76)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAmAb Light Chain Heavy Chaind4_6n ASQSVSPEYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE M_C24 RLLIYDASSRAPGIPDRFSGSGS WVSAIGGSGGSLPYADSVKGRFTGTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAV YSVWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 79) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSAIYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLEM_C26 LLIYDASSRAPGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFTTDFTLTISRLEPEDFAVYYCQQYS ISRDNSKNTLYLQMNSLRAEDTAV AWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 317) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSSvYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLEM_C10 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAV TWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 79) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE nM_C2 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTI 7 TDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAVRWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 81 ) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_6n ASQSVSPIYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLEM_C20 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAV AFPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 82) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSC EVQLLESGGGLVQPGGSLRLSCA d4_6n WLSQSVSSTYLAWYQQKPGQA ASGFTFSSYPMSWVRQAPGKGLEmAb Light Chain Heavy ChainM_C12 PRLLIYDASSRAPGIPDRFSGSG WVSAIGqSGGWSYYADSVKGRFTSGTDFTLTISRLEPEDFAVYYCQ ISRDNSKNTLYLQMNSLRAEDTAV QYSEWPLTFGQGTKVEIK (SEQ YYCARYWPMDSWGQGTLVTVSS ID NO: 84) (SEQ ID NO: 83)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE nM_C1 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTI 6 TDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAVSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 85) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASQSVSSI F LAWYQ Q KP G QA P R ASGFTFSSYPMSWVRQAPGKGLE nM_C0 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTI 9 TDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAVAWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 86) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCA EVQLLESGGGLVQPGGSLRLSCA d4_6n CSQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLEM_C09 LLIYDASSRAPGIPDRFSGSGSG WVSATVqSGGSIGYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAV AWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 88) (SEQ ID NO: 87)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASCDVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE nM_C0 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTI 3 TDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAVMRSPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 89) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA d4_0.6 ASEAVPSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE nM_C0 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGTISRmAb Light Chain Heavy Chain6 TDFTLTISRLEPEDFAVYYCQQYS DNSKNTLYLQMNSLRAEDTAVYYAFPLTFGQGTKVEIK (SEQ ID CARYWPMDSWGQGTLVTVSS NO: 90) (SEQ ID NO: 78)C01_R EIVLTQSPGTLSLSPGERATLSCC EVQLLESGGGLVQPGGSLRLSCA d4_6n SSQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLEM_C04 LLIYDASSRAPGIPDRFSGSGSG WVSAIGqSGGSLPYADSVKGRFTITDFTLTISRLEPEDFAVYYCQQYS SRDNSKNTLYLQMNSLRAEDTAV AFPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 91 ) (SEQ ID NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASVRVSSTYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAISdSGGSRWYADSVKGRFT M_C22 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVMKWPLTFGQGTKVEIK (SEQ ID YYCTRYWPMDIWGQGTLVTVSS NO: 93) (SEQ ID NO: 92)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSAAYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSAIGqSGGSLPYADSVKGRFTI C21 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYMCWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 94) (SEQ ID NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQS VSSS YWGWYQ Q KP G Q A P ASGFTFSSYPMSWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSAIGqSGGSIHYADSVKGRFTI C10 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYQCWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 96) (SEQ ID NO: 95)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAHIqSGGSTYYADSVKGRFTI M_C04 TDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAVmAb Light Chain Heavy ChainQSWPLTFGQGTKVEIK (SEQ I D YYCARYWPMDSWGQGTLVTVSS NO: 98) (SEQ I D NO: 97)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSDYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _6nM_ LLMYDASIRATGI PDRFSGSGSG WVSAIGqSGGSTYYADSVKGRFTI C25 TDFTLTISRLEPEDFAVYYCQQY SRDNSKNTLYLQMNSLRAEDTAVQSWPLTFGQGTKVEIK (SEQ I D YYCARYWPMDPWGQGTLVTVSS NO: 100) (SEQ ID NO: 99)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSAIGqSGGSLPYADSVKGRFTI M_C21 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYQSWPLTFGQGTKVEIK (SEQ I D YYCARYWPMDSWGQGTLVTVSS NO: 38) (SEQ I D NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSPIYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _6nM_ LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLGYADSVKGRFT C1 1 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVKAWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 102) (SEQ ID NO: 101 )COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSYLYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFT M_C20 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVMEWPLTFGQGTKVEIK (SEQ I D YYCARYWPMDSWGQGTLVTVSS NO: 103) (SEQ I D NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSAQYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVS Al FASGGSTYYADSVKGR FTI C09 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYQAWPLTFGQGTKVEIK (SEQ I D YYCARYWPMDSWGQGTLVTVSSmAb Light Chain Heavy ChainNO: 105) (SEQ ID NO: 104)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAO_Rd4 ASQS VSSS YL AWYQ Q KP G Q A P ASGFTFSSYPMSWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSAIGGSGTWTYYADSVKGRFT C08 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYQKWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 107) (SEQ ID NO: 106)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAO_Rd4 ASQSVSAVYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSAIGGSGGSLPYADSVKGRFT M_C19 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYRAWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 108) (SEQ ID NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAO_Rd4 ASIAVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFT M_C02 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVMVWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 109) (SEQ ID NO: 78)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAO_Rd4 PRQSVSSSYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSALFGSGGSTYYADSVKGRFT M_C23 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYQDWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 1 1 1 ) (SEQ ID NO: 1 10)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAO_Rd4 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSAIGGSGGSLPYADSVKGRFT M_C29 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYQSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 38) (SEQ ID NO: 112)mAb Light Chain Heavy ChainCOMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFT M_C09 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVQEWPLTFGQGTKVEIK (SEQ ID YYC A R YWP M Dl WG Q GT LVTVS S NO: 1 13) (SEQ ID NO: 1 12)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSASYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSAALGSGGSTYYADSVKGRF C12 GTDFTLTISRLEPEDFAVYYCQQ TISRDNSKNTLYLQMNSLRAEDTAYMSWPLTFGQGTKVEIK (SEQ ID VYYCARYWPMDSWGQGTLVTVS NO: 1 15) S (SEQ ID NO: 1 14)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSYMYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLIYDASIRATGIPDRFSGSGSG WVSAIGGSGGSTYYADSVKGRFT M_C30 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVKSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 1 16) (SEQ ID NO: 76)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQS VS ALYLAWYQ Q KPG Q A P ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSAIGGSGGSLPYADSVKGRFT M_C14 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYYGWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 1 17) (SEQ ID NO: 1 12)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQPISSSYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _6nM_ LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFT C07 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVQGWPLTFGQGTKVEIK (SEQ ID YYCARYWPMADWGQGTLVTVSS NO: 1 19) (SEQ ID NO: 1 18)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAmAb Light Chain Heavy Chain0_Rd4 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSAISDSGGFVYYADSVKGRFTI C02 GTDFTLTISRLEPEDFAVYYCQQ SRDNSKNTLYLQMNSLRAEDTAVYEFWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 121 ) (SEQ ID NO: 120)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSTYLAWYQQKPGQAPR ASGFTFSSYAMNWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSTYYADSVKGRFT M_C05 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVMSWPLTFGQGTKVEIK (SEQ ID YYCARYWPMSLWGQGTLVTVSS NO: 123) (SEQ ID NO: 122)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQGISSTYLAWYQQKPGQAPR ASGFTFSSYPMSWVRQAPGKGLE _0.6n LLMYDASIRATGIPDRFSGSGSG WVSAIGGSGGSLPYADSVKGRFT M_C17 TDFTLTISRLEPEDFAVYYCQQY ISRDNSKNTLYLQMNSLRAEDTAVAYWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDIWGQGTLVTVSS NO: 124) (SEQ ID NO: 1 12)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMNWVRQAPGKGLE _6nM_ RLLMYDASIRATGIPDRFSGSGS WVSACLDSGGSTYYADSVKGRFT C22 GTDFTLTISRLEPEDFAVYYCQQ ISRDNSKNTLYLQMNSLRAEDTAVYQGWPLTFGQGTKVEIK (SEQ ID YYCARYWPMDSWGQGTLVTVSS NO: 126) (SEQ ID NO: 125)COMB EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCA0_Rd4 ASQSVSVRYLAWYQQKPGQAP ASGFTFSSYPMSWVRQAPGKGLE _0.6n RLLMYDASIRATGIPDRFSGSGS WVSAALGSGGSTYYADSVKGRF M_C1 1 GTDFTLTISRLEPEDFAVYYCQQ TISRDNSKNTLYLQMNSLRAEDTAYGSWPITFGQGTKVEIK (SEQ ID VYYCARYWPMSLWGQGTLVTVS NO: 128) S (SEQ ID NO: 127)Conse EIVLTQSPGTLSLSPGERATLSC EVQLLESGGGLVQPGGSLRLSCA nsus Xi X2X3X4X5 6 7 8 9X10X11 X12 WY ASGFTFX1SYX2MX3WVRQAPGKGmAb Light Chain Heavy ChainQQKPGQAPRLLMYX13ASX14RAX0X11YAD15GIPDRFSGSGSGTDFTLTISRLE X12X13GRFTISRDNSKNTLYLQMNPEDFAVYYCX16X17YX18X19PPSF SLRAEDTAVYYCARVSPIXi4Xi5Xi6TFGQGTKVEIK, wherein is R, MDYWGQGTLVTVSS, wherein X^G, W, A, orC; X2is A, P, G, L, C, is G or S, X2is A or P; X3is T, N, or orS; X3is S, G, or R; X4is Q, C, S; X4isl, V, T, H, L, A, or C; X5is S,E, V, orl;X5is S, P, G, A, R, or D; D, G, T, I, L, F, M, orV;X6is G, Y,X6isV, G, I, orL; X7is S, E, D, P, L, H, D, A, S, orM; X7is S, Q, T, A, orG;X8is S, P, F, A, M, E, V, N, F, or W; X8is G orT; X9is N, S, P,D, orY; X9is I, T, V, E, S, A, M, Q, Y, W, orF;X10is S, T, I, L, T, A, R,Y, H, R, orF; X10isYorF; Xn is V, K, G, orC;Xn is F, Y, P, W, H,L, W, or P; X2is A, S, or G, X3is or G; Xi2is V, R, or L; Xi3is G or T;G or D; X4is S or I; X5is T or P; Xi4is A or Y; X-15 is A or S; and Xi6isX-I6is Q or K; X7is H or Y; X8is G, Q, L, P, or E (SEQ ID NO: 313);G, N, or P; and X9is S, W, or Y or(SEQ ID NO: 315); or EVQLLESGGGLVQPGGSLRLSCAEIVLTQSPGTLSLSPGERATLSC ASGFTFXT SYX2MX3WVRQAPGKGX 1 X2X3X4XsX6X7X8X9X 1 oX 11 Xi 2 WY0X11 YADQQKPGQAPRLLMYX13ASXi4RAX X12X13KGRFTISRDNSKNTLYLQMN15GIPDRFSGSGSGTDFTLTISRLE SLRAEDTAVYYCARYWPMX14X15PEDFAVYYCQQYX16X17X18PX19F WGQGTLVTVSS, wherein X^ is GGQGTKVEIK, wherein X is R, G, or S, X2is A or P; X3is T, N, or S;W, A, orC;X2is A, P, G, L, C, or X4isl, V, T, H, L, A, orC;X5is S, D,S; X3is S, G, or R; X4is Q, C, E, G, T, I, L, F, M, orV; X6is G, Y, L,V, orl;X5is S, L, P, G, A, R, or D; H, D, A, S, orM;X7is S, Q, T, A, F,X6is V, G, orl;X7is S, E, D, or P; orW; X8isG orT; X9is N, S, P, Y,X8isS, P, F, A, M, E, V, N, D, or W, orF; X10isS, T, I, L, T, A, R, V,Y; X9is I, T, V, E, S, A, M, Q, Y, H, K, G, orC; Xn is F, Y, P, W, H, or or R; X0is Y or F; Xn is L, W, or G; X2is V, R, or L; X3is G orT;P; X2is A, S, or G, X3is G or D; X4is D, S, T, or A; and X5is I, S, L,Xn is S or I; X-15 is T or P; Xi6is G, P, or D (SEQ ID NO: 314)Q, E, L, F,A, S, M, R, K, orY; X17mAb Light Chain Heavy Chainis S, R, T, G, R, V, D, A, H, E, K,C, F, or Y; X18is W, S, or F; andX-I 9 is L or I (SEQ ID NO: 316)P4G4 EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAASQSVSSSYLAWYQQKPGQAP ASGFTFSSYAMSWVRQAPGKGLERLLIYGASSRAYGIPDRFSGSGS WVSAISASGGSTYYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YGSPPLFTFGQGTKVEIK (SEQ YYCARLSWSGAFDNWGQGTLVT ID NO: 80) VSS (SEQ ID NO: 363)P1A1 1 EIVLTQSPGTLSLSPGERATLSCR EVQLLESGGGLVQPGGSLRLSCAASQNVSSSYLAWYQQKPGQAP ASGFTFRSYAMSWVRQAPGKGLERLLIYGASYRATGIPDRFSGSGS WVSAISGSGGSTFYADSVKGRFTIGTDFTLTISRLEPEDFAVYYCQH SRDNSKNTLYLQMNSLRAEDTAV YGSPPSFTFGQGTKVEIK (SEQ YYC ATVGTSG AFG I WG Q GTL VTV ID NO: 364) SS (SEQ ID NO: 365)In Table 1 , the underlined sequences are CDR sequences according to Kabat and in bold according to Chothia, except for the heavy chain CDR2 sequences, the Chothia CDR sequence is underlined and the Kabat CDR sequence is in boldThe invention also provides CDR portions of antibodies to BCMA (includingChothia, Kabat CDRs, and CDR contact regions). Determination of CDR regions is well within the skill of the art. It is understood that in some embodiments, CDRs can be a combination of the Kabat and Chothia CDR (also termed "combined CRs" or "extended CDRs"). In some embodiments, the CDRs are the Kabat CDRs. In other embodiments, the CDRs are the Chothia CDRs. In other words, in embodiments with more than one CDR, the CDRs may be any of Kabat, Chothia, combination CDRs, or combinations thereof. Table 2 provides examples of CDR sequences provided herein. Table 2Heavy ChainmAb CDRH1 CDRH2 CDRH3P6E01 SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIASGMDY For thefollowing 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 134) mAbs:P6E01 / P6E GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)01;L1.LGF / NO: 130) (Chothia); (Kabat)L3.KW / P6E GFTFGSYAMT (SEQ01 ; ID NO: 131)L1.LGF / L3.(extended)NY / P6E01 ;L1.GDF / L3.NY / P6E01 ;L3.KW / P6E01;L3.PY / P6E01;L3.NY / P6E01;L3.PY / L1.PS / P6E01 ;L3.PY / L1.AH / P6E01;L3.PY / L1.FF / P6E01;L3.PY / L1.PH / P6E01;L3.PY / L3.KY / P6E01 ;L3.PY / L3.KF / P6E01;andL3.PY / P6E01.H3.AQ SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIAAQMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Kabat) (SEQ ID NO: 135) followingGFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs:P6E01 / H3. NO: 130) (Chothia); (Kabat)AQ; GFTFGSYAMT (SEQL1.LGF / L3.ID NO: 131)KW / H3.AQ;L1.LGF / L3. (extended)PY / H3.AQ;L1 .LGF / L3.NY / H3.AQ;L1 .GDF / L3.KW / H3.AQ;L1 .GDF / L3.PY / H3.AQ;L1 .GDF / L3.NY / H3.AQ;L3.PY / H3.AQ;L3.PY / L1 .PS / H3.AQ;L3.PY / L1 .AH / H3.AQ;L3.PY / L1 .FF / H3.AQ;L3.PY / L1 .PH / H3.AQ;andL3.PY / L3.KF / H3.AQ.H3.AL SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIAALMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 136) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L1 .LGF / L3. GFTFGSYAMT (SEQKW / H3.AL;L1 .LGF / L3. ID NO: 131)NY / H3.AL;and (extended)L1 .GDF / L3.NY / H3.AL.H3.AP SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIAAPMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 137) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L1 .LGF / L3. GFTFGSYAMT (SEQKW / H3.AP; ID NO: 131)L1 .LGF / L3.(extended)PY / H3.AP;L1 .LGF / L3NY / H3.AP;L1 .GDF / L3.KW / H3.AP;andL1 .GDF / L3NY / H3.AP.H2.QR SYAMT (SEQ ID NO: AISGSGGNTFYADQRKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 138) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2. GFTFGSYAMT (SEQQR; ID NO: 131)L3.PY / L1 .P(extended)S / H2.QR;L3.PY / L1 .AH / H2.QR;L3.PY / L1 .FF / H2.QR;L3.PY / L1 .PH / H2.QR;andL3.PY / L3.KY / H2.QR.H2.DY SYAMT (SEQ ID NO: AIDYSGGNTFYADSVKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 139) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID DYSSGN (SEQ ID NO: 140)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2.D GFTFGSYAMT (SEQY; ID NO: 131)L3.PY / L1 .P (extended)S / H2.DY;L3.PY / L1 .AH / H2.DY;L3.PY / L1 .FF / H2.DY;L3.PY / L3.KY / H2.DY;andL3.PY / L3.KF / H2.DY.H2.YQ SYAMT (SEQ ID NO: AISYQGGNTFYADSVKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 141) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID SYQGGN (SEQ ID NO: 142)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2.Y GFTFGSYAMT (SEQQ; ID NO: 131)L3.PY / L1 .P(extended)S / H2.YQ;L3.PY / L1 .AH / H2.YQ;L3.PY / L1 .FF / H2.YQ;L3.PY / L3.KY / H2.YQ;andL3.PY / L3.KF / H2.YQ.H2.LT SYAMT (SEQ ID NO: AISLTGGNTFYADSVKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 143) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID SLTGGN (SEQ ID NO: 144)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2.L GFTFGSYAMT (SEQT; ID NO: 131)L3.PY / L1 .P (extended)S / H2.LT;L3.PY / L1 .AH / H2.LT;L3.PY / L1 .FF / H2.LT;L3.PY / L3.KY / H2.LT;andL3.PY / L3.KF / H2.LT.H2.HA SYAMT (SEQ ID NO: AISHAGGNTFYADSVKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 145) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID SHAGGN (SEQ ID NO:146)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2.H GFTFGSYAMT (SEQA; ID NO: 131)L3.PY / L1 .A(extended)H / H2.HA;L3.PY / L1 .FF / H2.HA;L3.PY / L1 .PH / H2.HA;andL3.PY / L3.KY / H2.HA.H2.QL SYAMT (SEQ ID NO: AISGSGGNTFYADQLKG VSPIASGMDYFor the 129) (Kabat); (SEQ ID NO: 147) (Chothia) (SEQ ID NO: 134) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO: 133)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H2. GFTFGSYAMT (SEQQL; ID NO: 131)L3.PY / L1 .P(extended)S / H2.QL;L3.PY / L1 .AH / H2.QL;L3.PY / L1 .FF / H2.QL;L3.PY / L3.KY / H2.QL;andL3.PY / L3.KF / H2.QL.H3.YA SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIYAGMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 148) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H3.Y GFTFGSYAMT (SEQA; ID NO: 131)L3.PY / L1 .P(extended)S / H3.YA;L3.PY / L1 .AH / H3.YA;L3.PY / L1 .FF / H3.YA;L3.PY / L3.KY / H3.YA;andL3.PY / L3.KF / H3.YA.H3.AE SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIAAEMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 149) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H3.A GFTFGSYAMT (SEQE; ID NO: 131)L3.PY / L1 .A(extended)H / H3.AE;L3.PY / L1 .FF / H3.AE;L3.PY / L1 .PH / H3.AE;andL3.PY / L3.KF / H3.AE.H3.TAQ SYAMT (SEQ ID NO: AISGSGGNTFYADSVKG VSPIAAQMDYFor the 129) (Kabat); (SEQ ID NO: 132) (Chothia) (SEQ ID NO: 135) following GFTFGSY (SEQ ID SGSGGN (SEQ ID NO:133)mAbs: NO: 130) (Chothia); (Kabat)L3.PY / H3.T GFTFGSYAMT (SEQAQ; ID NO: 131 )L3.PY / L1 .P(extended)S / H3.TAQ;L3.PY / L1 .AH / H3.TAQ;L3.PY / L1 .FF / H3.TAQ;L3.PY / L1 .PH / H3.TAQ;andL3.PY / L3.KF / H3.TAQ.P5A2_VH SYAMN (SEQ ID AISDSGGSTYYADSVKG YWPMDI (SEQVL and NO: 150) (Kabat); (SEQ ID NO: 153) (Chothia) ID NO: 155)A02_Rd4 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)_6nM_C0 NO: 151 ) (Chothia); (Kabat)3 GFTFSSYAMN (SEQID NO: 152)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSLPYADSVKG YWPMDI (SEQRd4_0.6n 156) (Kabat); (SEQ ID NO: 158) (Chothia) ID NO: 155)M_C17; GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159COMBO_ NO: 151 ) (Chothia); ) (Kabat)Rd4_0.6n GFTFSSYPMS (SEQM_C14; ID NO: 157)COMBO_ (extended)Rd4_0.6nM_C29;andCOMBO_Rd4_0.6nM_C09C01_Rd4 SYPMS (SEQ ID NO: AIGGSGGSLPYADSVKG YWPMDS (SEQ_6nM_C0 156) (Kabat); (SEQ ID NO: 158) (Chothia) ID NO: 161 ) 4; GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159C01_Rd4 NO: 151 ) (Chothia); ) (Kabat)_0.6nM_ GFTFSSYPMS (SEQC03; ID NO: 157)C01_Rd4 (extended)_0.6nM_C06;COMBO_Rd4_0.6nM_C02;COMBO_Rd4_6nM_C21 ;C01_Rd4_6nM_C2c-D,COMBO_Rd4_0.6nM_C19;C01_Rd4_6nM_C2Λ■C01_Rd4_6nM_C20;C01_Rd4_0.6nM_C09;COMBO_Rd4_0.6nM_C21 ;C01_Rd4_0.6nM_C04_C27C01_Rd4_0.6nM_C16;C01_Rd4_6nM_C1u,COMBO_Rd4_0.6nM_C20P5C1_V SYPMS (SEQ ID NO: AIGGSGGSTYYADSVKG YWPMDS (SEQHVL and 156) (Kabat); (SEQ ID NO: 162) (Chothia) ID NO: 161 )COMBO_ GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159Rd4_0.6n NO: 151 ) (Chothia); ) (Kabat)M_C30 GFTFSSYPMS (SEQID NO: 157)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSAWYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 163) (Chothia) ID NO: 164)C06 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSAWYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 163) (Chothia) ID NO: 164)C09 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDFGGSTYYADSVKG YWPMDI (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 165) (Chothia) ID NO: 155)C16 GFTFSSY (SEQ ID SDFGGS (SEQ ID NO: 166)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AITASGGSTYYADSVKG YWPMSL (SEQ _6nM_C0 NO: 150) (Kabat); (SEQ ID NO: 167) (Chothia) ID NO: 164) 1 GFTFSSY (SEQ ID TASGGS (SEQ ID NO: 168)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSTYYADSVKG YWPMSL (SEQ _6nM_C2 NO: 150) (Kabat); (SEQ ID NO: 153) (Chothia) ID NO: 164) 6 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSRWYADSVKG YWPMTP (SEQ _6nM_C2 NO: 150) (Kabat); (SEQ ID NO: 169) (Chothia) ID NO: 170) 5 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AVLDSGGSTYYADSVKG YWPMTP (SEQ _6nM_C2 NO: 150) (Kabat); (SEQ ID NO: 171) (Chothia) ID NO: 170) 2 GFTFSSY (SEQ ID LDSGGS (SEQ ID NO: 172)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSRWYADSVKG YWPMSD (SEQ _6nM_C1 NO: 150) (Kabat); (SEQ ID NO: 169) (Chothia) ID NO: 173) 9 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSKWYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 174) (Chothia) ID NO: 164)C03 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AIGGSGGSLPYADSVKG(S YWPMDS (SEQ _6nM_C0 NO: 150) (Kabat); EQ ID NO: 158) (Chothia) ID NO: 161 ) 7 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSGWYADSVKG YWPMSL (SEQ _6nM_C2 NO: 150) (Kabat); (SEQ ID NO: 175) (Chothia) ID NO: 164) 3 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AVLDSGGSTYYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 171) (Chothia) ID NO: 164)C18 GFTFSSY (SEQ ID LDSGGS (SEQ ID NO: 172)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGSCWYADSVKG YWPMTP (SEQ _6nM_C1 NO: 150) (Kabat); (SEQ ID NO: 176) (Chothia) ID NO: 170) 0 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AIFASGGSTYYADSVKG YWPMTP (SEQ _6nM_C0 NO: 150) (Kabat); (SEQ ID NO: 177) (Chothia) ID NO: 170) 5 GFTFSSY (SEQ ID FASGGS (SEQ ID NO: 178)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISGWGGSLPYADSVKG YWPMDS (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 304) (Chothia) ID NO: 161 )C10 GFTFSSY (SEQ ID SGWGGS (SEQ ID NO: 179)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AIMSSGGPLYYADSVKG YWPMAL (SEQ _6nM_C0 NO: 150) (Kabat); (SEQ ID NO: 180) (Chothia) ID NO: 182) 4 GFTFSSY (SEQ ID MSSGGP (SEQ ID NO: 181 )NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AILMSGGSTYYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 183) (Chothia) ID NO: 164)C26 GFTFSSY (SEQ ID LMSGGS (SEQ ID NO: 184)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AISDSGGYRYYADSVKG YWPMSL (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 185) (Chothia) ID NO: 164)C13 GFTFSSY (SEQ ID SDSGGY (SEQ ID NO: 186)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AI LSSGGSTYYADSVKG YWPMDI (SEQ_0.6nM_ NO: 150) (Kabat); (SEQ ID NO: 187) (Chothia) ID NO: 155)C01 GFTFSSY (SEQ ID LSSGGS (SEQ ID NO: 188)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)A02_Rd4 SYAMN (SEQ ID AILDSGGSTYYADSVKG YWPMSP (SEQ _6nM_C0 NO: 150) (Kabat); (SEQ ID NO: 160) (Chothia) ID NO: 189) 8 GFTFSSY (SEQ ID LDSGGS (SEQ ID NO: 172)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)C01_Rd4 SYPMS (SEQ ID NO: AIGGSGGWSYYADSVKG YWPMDS (SEQ _6nM_C1 156) (Kabat); (SEQ ID NO: 190) (Chothia) ID NO: 161 ) 2 GFTFSSY (SEQ ID GGSGGW (SEQ ID NO:NO: 151 ) (Chothia); 191 ) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)C01_Rd4 SYPMS (SEQ ID NO: ATVGSGGSIGYADSVKG YWPMDS (SEQ _6nM_C0 156) (Kabat); (SEQ ID NO: 192) (Chothia) ID NO: 161 ) 9 GFTFSSY (SEQ ID VGSGGS (SEQ ID NO: 193)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYAMN (SEQ ID AISDSGGSRWYADSVKG YWPMDI (SEQ Rd4_0.6n NO: 150) (Kabat); (SEQ ID NO: 169) (Chothia) ID NO: 155) M_C22 GFTFSSY (SEQ ID SDSGGS (SEQ ID NO: 154)NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSIHYADSVKG YWPMDS (SEQ Rd4_0.6n 156) (Kabat); (SEQ ID NO: 194) (Chothia) ID NO: 161 ) M_C10 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AHIGSGGSTYYADSVKG YWPMDS (SEQ Rd4_0.6n 156) (Kabat); (SEQ ID NO: 195) (Chothia) ID NO: 161 ) M_C04 GFTFSSY (SEQ ID IGSGGS (SEQ ID NO: 196)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSTYYADSVKG YWPMDP (SEQ Rd4_0.6n 156) (Kabat); (SEQ ID NO: 162) (Chothia) ID NO: 197) M_C25 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSLPYADSVKG YWPMDS (SEQRd4_6nM 156) (Kabat); (SEQ ID NO: 158) (Chothia) ID NO: 161 ) _C21 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSLGYADSVKG YWPMDS (SEQ Rd4_6nM 156) (Kabat); (SEQ ID NO: 198) (Chothia) ID NO: 161 ) _C1 1 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIFASGGSTYYADSVKG YWPMDS (SEQ Rd4_6nM 156) (Kabat); (SEQ ID NO: 177) (Chothia) ID NO: 161 ) _C09 GFTFSSY (SEQ ID FASGGS (SEQ ID NO: 178)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGTWTYYADSVKG YWPMDS (SEQ Rd4_6nM 156) (Kabat); (SEQ ID NO: 199) (Chothia) ID NO: 161 ) _C08 GFTFSSY (SEQ ID GGSGTW (SEQ ID NO: 200)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: ALFGSGGSTYYADSVKG YWPMDS (SEQ Rd4_0.6n 156) (Kabat); (SEQ ID NO: 201) (Chothia) ID NO: 161 ) M_C23 GFTFSSY (SEQ ID FGSGGSNO: 151 ) (Chothia); (SEQ ID NO: 202) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AALGSGGSTYYADSVKG YWPMDS (SEQ Rd4_0.6n 156) (Kabat); (SEQ ID NO: 203) (Chothia) ID NO: 161) M_C12 GFTFSSY (SEQ ID LGSGGS (SEQ ID NO: 204)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYPMS (SEQ ID NO: AIGGSGGSLPYADSVKG YWPMAD (SEQ Rd4_6nM 156) (Kabat); (SEQ ID NO: 158) (Chothia) ID NO: 205) _C07 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)COMBO_ SYAMN (SEQ ID AISDSGGFVYYADSVKG YWPMDS (SEQ Rd4_6nM NO: 150) (Kabat); (SEQ ID NO: 206) (Chothia) ID NO: 161 ) _C02 GFTFSSY (SEQ ID SDSGGF (SEQ ID NO: 207 )NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)COMBO_ SYAMN (SEQ ID AIGGSGGSTYYADSVKG YWPMSL (SEQ Rd4_6nM NO: 150) (Kabat); (SEQ ID NO: 162) (Chothia) ID NO: 164) _C05 GFTFSSY (SEQ ID GGSGGS (SEQ ID NO: 159NO: 151 ) (Chothia); ) (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)COMBO_ SYAMN (SEQ ID ACLDSGGSTYYADSVKG YWPMDS (SEQRd4_6nM NO: 150) (Kabat); (SEQ ID NO: 208) (Chothia) ID NO: 161 )_C22 GFTFSSY (SEQ ID LDSGGS (SEQ ID NO: 172 )NO: 151 ) (Chothia); (Kabat)GFTFSSYAMN (SEQID NO: 152)(extended)COMBO_ SYPMS (SEQ ID NO: AALGSGGSTYYADSVKG YWPMSL (SEQRd4_6nM 156) (Kabat); (SEQ ID NO: 203) (Chothia) ID NO: 164)_C1 1 GFTFSSY (SEQ ID LGSGGS (SEQ ID NO: 204)NO: 151 ) (Chothia); (Kabat)GFTFSSYPMS (SEQID NO: 157)(extended)Heavy SYX1MX2, wherein AX1X2X3X4GX5X6X7X8YADX9 VSPIX1X2X3MDY, chain XT is A or P; and X2X-ioKG, wherein X-i is I, V, T, wherein X-i is A or consensu is T, N, or S (Kabat) H, L, A, or C; X2is S, D, G, Y; X2is A or S; s (SEQ ID NO: 301 ) T, I, L, F, M, or V; X3is G, Y, and X3is G, Q, L,GFTFX-iSY, wherein L, H, D, A, S, or M; X4is S, P, or E (SEQ IDXi is G or S (Chothia) Q, T, A, F, or W; X5is G or NO: 307)(SEQ ID NO: 302) T; X6is N, S, P, Y, W, or F; YWPMX^s,GFTFX1SYX2MX3, X7is S, T, I, L, A, R, V, K, G, wherein Xi is D, wherein X-i is G or S, or C; X8is F, Y, P, W, H, or S, T, or A; and X2X2is A or P; and X3G; X9is V, R, or L; and X0is is I, S, L, P, or D is T, N, or S (SEQ ID G or T (Chothia) (SEQ ID (SEQ ID NO: 308)NO: 303) (extended) NO: 305)X-iX2X3X4X5X6, wherein X-i isS, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M;X3is S, G, F, or W; X4is G orS; X5is G or T; and X6is N,S, P, Y, or W (Kabat) (SEQID NO: 306)P4G4 SYAMS (SEQ ID NO: SASGGS (SEQ ID NO: 368) LSWSGAFDN366) (Kabat); (Kabat) (SEQ ID NO: 370) GFTFSSY (SEQ ID AISASGGSTYYADSVKGNO: 151 ) (Chothia); (SEQ ID NO: 369 ) (Chothia)GFTFSSYAMS (SEQID NO: 367)(extended)P1A1 1 SYAMS (SEQ ID NO: SGSGGS (SEQ ID NO: 359) VGTSGAFGI366) (Kabat); (Kabat) (SEQ ID NO: 361 ) GFTFRSY (SEQ ID AISGSGGSTFYADSVKGNO: 371 ) (SEQ ID NO: 360) (Chothia)GFTFRSYAMS (SEQID NO: 372)Light ChainmAb CDRL1 CDRL2 CDRL3P6E01 RASQSVSSSYLA GASSRAT (SEQ ID NO: QHYGSPPSFT For the(SEQ ID NO: 209) 210) (SEQ ID NO: 21 1 ) followingmAbs:P6E01 / P6E01 ; andP6E01 / H3.AQ.L1.LGF / RASQSLGSFYLA GASSRAT (SEQ ID NO: KHYGWPPSFT L3.KW (SEQ ID NO: 212) 210) (SEQ ID NO: 213) For thefollowingmAbs:L1 .LGF / L3.KW / P6E01 I■ ,L1 .LGF / L3.KW / H3.AL,L1 .LGF / L3.KW / H3.AP; andL1 .LGF / L3.KW / H3.AQL1.LGF / RASQSLGSFYLA GASSRAT (SEQ ID NO: QHYNYPPSFTL3.NY (SEQ ID NO: 212) 210) (SEQ ID NO: 214)For thefollowingmAbs:L1 .LGF / L3.NY / P6E01 I■,L1 .LGF / L3.NY / H3.ALL1 .LGF / L3.NY / H3.AP; andL1 .LGF / L3.NY / H3AQL1.GDF / RASQSVGDFYLA GASSRAT (SEQ ID NO: QHYNYPPSFTL3.NY (SEQ ID NO: 215) 210) (SEQ ID NO: 214)For thefollowingmAbs:L1 .GDF / L3.NY / P6E01 ;L1 .GDF / L3.NY / H3.AI ■L,L1 .GDF / L3.NY / H3.AP; andL1 .GDF / L3.NY / H3.AQL1.LGF / RASQSLGSFYLA GASSRAT (SEQ ID NO: QHYPYPPSFTL3.PY (SEQ ID NO: 212) 210) (SEQ ID NO: 216)For thefollowingmAbs:L1 .LGF / L3.PY / H3.AP; andL1 .LGF / L3.PY / H3.AQL1.GDF RASQSVGDFYLA GASSRAT (SEQ ID NO: KHYGWPPSFT / L3.KW (SEQ ID NO: 215) 210) (SEQ ID NO: 213)For thefollowingmAbs:L1 .GDF / L3.KW / H3.AL;L1 .GDF / L3.KW / H3.AP; andL1 .GDF / L3.KW / H3.AQL1.GDF RASQSVGDFYLA GASSRAT (SEQ ID NO: QHYPYPPSFT / L3.PY / H (SEQ ID NO: 215) 210) (SEQ ID NO: 216)3.AQL3.KW / P RASQSVSSSYLA GASSRAT (SEQ ID NO: KHYGWPPSFT6E01 (SEQ ID NO: 209) 210) (SEQ ID NO: 213)L3.PY RASQSVSSSYLA GASSRAT (SEQ ID NO: QHYPYPPSFTFor the (SEQ ID NO: 209) 210) (SEQ ID NO: 216) followingmAbs:L3.PY / P6E01 ;L3.PY / H2.QR;L3.PY / H2.DY;L3.PY / H2.YQ;L3.PY / H2.LT;L3.PY / H2.HA;L3.PY / H2.QL;L3.PY / H3.YA;L3.PY / H3.AE;L3.PY / H3.AQ;L3.PY / H3.TAQL3.NY / P RASQSVSSSYLA GASSRAT (SEQ ID NO: QHYNYPPSFT6E01 (SEQ ID NO: 209) 210) (SEQ ID NO: 214)L3.PY / L RASQSVSSSYPS GASSRAT (SEQ ID NO: QHYPYPPSFT PS (SEQ ID NO: 217) 210) (SEQ ID NO: 216)For thefollowingmAbs:L3.PY / L1 .PS / P6E01 ;L3.PY / L1 .PS / H2.QRL3.PY / L1 .PS / H2.DY;L3.PY / L1.PS / H2.YQL3.PY / L1.PS / H2.LT;L3.PY / L1.PS / H2.HA;L3.PY / L1.PS / H2.QL;L3.PY / L1.PS / H3.YA;L3.PY / L1.PS / H3.AE;L3.PY / L1.PS / H3.AQL3.PY / L1.PS / H3.TAQL3.PY / L RASQSVSAHYLA GASSRAT (SEQ ID NO: QHYPYPPSFT1.AH (SEQ ID NO: 218 ) 210) (SEQ ID NO: 216)For thefollowingmAbs:L3.PY / L1.AH / P6E01L3.PY / L1.AH / H2.QRL3.PY / L1.AH / H2.DYL3.PY / L1.AH / H2.YQL3.PY / L1.AH / H2.LT;L3.PY / L1.AH / H2.HAL3.PY / L1.AH / H2.QL;L3.PY / L1.AH / H3.YA;L3.PY / L1.AH / H3.AE;L3.PY / L1.AH / H3.AQL3.PY / L1.AH / H3.TAQL3.PY / L RASQSVSSFFLA GASSRAT (SEQ ID NO: QHYPYPPSFT FF (SEQ ID NO: 219) 210) (SEQ ID NO: 216)For thefollowingmAbs:L3.PY / L1.FF / P6E01 ;L3.PY / L1.FF / H2.QR;L3.PY / L1.FF / H2.DY;L3.PY / L1.FF / H2.YQ;L3.PY / L1.FF / H2.LT;L3.PY / L1.FF / H2.HA;L3.PY / L1.FF / H2.QL;L3.PY / L1.FF / H3.YA;L3.PY / L1 .FF / H3.AE;L3.PY / L1 .FF / H3.AQ;andL3.PY / L1 .FF / H3.TAQL3.PY / L RASQSVSPHYLA GASSRAT (SEQ ID NO: QHYPYPPSFT1.PH (SEQ ID NO: 219) 210) (SEQ ID NO: 216)For thefollowingmAbs:L3.PY / L1 .PH / P6E01L3.PY / L1 .PH / H2.QRL3.PY / L1 .PH / H2.HAL3.PY / L1 .PH / H3.AE;L3.PY / L1 .PH / H3.AQ; andL3.PY / L1 .PH / H3.TAQL3.PY / L RASQSVSSSYLA GASSRAT (SEQ ID NO: KYYPYPPSFT 3.KY (SEQ ID NO: 209) 210) (SEQ ID NO: 220) For thefollowingmAbs:L3.PY / L3.KY / P6E01L3.PY / L3.KY / H2.QRL3.PY / L3.KY / H2.DYL3.PY / L3.KY / H2.YQ;L3.PY / L3.KY / H2.LTL3.PY / L3.KY / H2.HA;L3.PY / L3.KY / H2.QL;L3.PY / L3.KY / H3.YA; andL3.PY / L3.KY / H3.TAQL3.PY / L RASQSVSSSYLA GASSRAT (SEQ ID NO: KFYPYPPSFT (SEQ 3.KF (SEQ ID NO: 209) 210) ID NO: 220) For thefollowingmAbs:L3.PY / L3.KF / H2.DY;L3.PY / L3.KF / H2.YQ;L3.PY / L3.KF / H2.LT;L3.PY / L3.KF / H2.QL;L3.PY / L3.KF / H3.YA;L3.PY / L3.KF / H3.AE;L3.PY / L3.KF / H3.AQ;andL3.PY / L3.KF / H3.TAQP5A2_V RASQSVSSSYLA DAS I RAT QQYGSWPLT (SEQHVL (SEQ ID NO: 209) (SEQ ID NO: 221 ) ID NO: 222)A02_Rd RASQSVSVIYLA DAS I RAT QQYQRWPLT4_0.6nM (SEQ ID NO: 223) (SEQ ID NO: 221 ) (SEQ ID NO: 224) _C06A02_Rd RASQSVSSSYLA DAS I RAT QQYQSWPLT4_0.6nM (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 225) _C09;COMBO_Rd_0.6nM_C29; andCOMBO_Rd4_0.6nM_C21A02_Rd RASQSVSDIYLA DAS I RAT QQYQTWPLT (SEQ4_6nM_ (SEQ ID NO: 226) (SEQ ID NO: 221 ) ID NO: 227) C16A02_Rd RASQSVSNIYLA DAS I RAT QQYQGWPLT 4_6nM_ (SEQ ID NO: 228) (SEQ ID NO: 221 ) (SEQ ID NO: 229) C03A02_Rd RASQSVSAYYLA DAS I RAT QQYERWPLT 4_6nM_ (SEQ ID NO: 230) (SEQ ID NO: 221 ) (SEQ ID NO: 231 ) C01A02_Rd RASQSVSSIYLA DAS I RAT QQYQVWPLT 4_6nM_ (SEQ ID NO: 232) (SEQ ID NO: 221 ) (SEQ ID NO: 233) C26A02_Rd RASQSVSSSYLA DAS I RAT QQYLDWPLT 4_6nM_ (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 234) C25A02_Rd RASQSVSSSYLA DAS I RAT QQYQVWPLT 4_6nM_ (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 233) C22A02_Rd RASQSVSVIYLA DAS I RAT QQYLAWPLT 4_6nM_ (SEQ ID NO: 223) (SEQ ID NO: 221 ) (SEQ ID NO: 236) C19A02_Rd RASQSVSSSYLA DAS I RAT QQYFTWPLT4_0.6nM (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 237)_C03A02_Rd RASQSVSPYYLA DAS I RAT QQYERWPLT 4_6nM_ (SEQ ID NO: 238) (SEQ ID NO: 221 ) (SEQ ID NO: 231 ) C07A02_Rd RASQSVSVEYLA DAS I RAT QQYARWPLT 4_6nM_ (SEQ ID NO: 239 ) (SEQ ID NO: 221 ) (SEQ ID NO: 240 ) C23A02_Rd RASQSVSEIYLA DAS I RAT QQYFGWPLT4_0.6nM (SEQ ID NO: 241 ) (SEQ ID NO: 221 ) (SEQ ID NO: 242)_C18A02_Rd RASQSVEMSYLA DAS I RAT QQYAHWPLT 4_6nM_ (SEQ ID NO: 243) (SEQ ID NO: 221 ) (SEQ ID NO: 244) C10A02_Rd RASQSVSSSYLA DAS I RAT QQYQRWPLT 4_6nM_ (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 224) C05A02_Rd RASQSVSAQYLA DAS I RAT QQYQRWPLT4_0.6nM (SEQ ID NO: 245) (SEQ ID NO: 221 ) (SEQ ID NO: 224)_C10A02_Rd RASQSVSAIYLA DAS I RAT QQYQVWPLT 4_6nM_ (SEQ ID NO: 235) (SEQ ID NO: 221 ) (SEQ ID NO: 233) C04A02_Rd GPSQSVSSSYLA DAS I RAT QQYQSWPLT4_0.6nM (SEQ ID NO: 246) (SEQ ID NO: 221 ) (SEQ ID NO: 225)_C26A02_Rd RASQSVSSSYWA DAS I RAT QQYESWPLT4_0.6nM (SEQ ID NO: 247) (SEQ ID NO: 221 ) (SEQ ID NO: 248)_C13A02_Rd RGGQSVSSSYLA DAS I RAT QQYQSWPLT4_0.6nM (SEQ ID NO: 249) (SEQ ID NO: 221 ) (SEQ ID NO: 225)_C01A02_Rd RASQSVSFIYLA DAS I RAT QQYGSWPLT (SEQ 4_6nM_ (SEQ ID NO: 250) (SEQ ID NO: 221 ) ID NO: 222) C08P5C1_V RASQSVSSTYLA DASSRAP QQYSTSPLT HVL (SEQ ID NO: 251 ) (SEQ ID NO: 252) (SEQ ID NO: 253)C01_Rd RASQSVSPEYLA DASSRAP QQYSVWPLT 4_6nM_ (SEQ ID NO: 254) (SEQ ID NO: 252) (SEQ ID NO: 255) C24C01_Rd RASQSVSAIYLA DASSRAP QQYSAWPLT 4_6nM_ (SEQ ID NO: 235) (SEQ ID NO: 252) (SEQ ID NO: 256) C26C01_Rd RASQSVSSVYLA DASSRAP QQYSTWPLT 4_6nM_ (SEQ ID NO: 257) (SEQ ID NO: 252) (SEQ ID NO: 258) C10C01_Rd RASQSVSSTYLA DASSRAP QQYSRWPLT 4_0.6nM (SEQ ID NO: 251 ) (SEQ ID NO: 252) (SEQ ID NO: 259) _C27C01_Rd RASQSVSPIYLA DASSRAP QQYSAFPLT 4_6nM_ (SEQ ID NO: 260) (SEQ ID NO: 252) (SEQ ID NO: 261 ) C20C01_Rd WLSQSVSSTYLA DASSRAP QQYSEWPLT 4_6nM_ (SEQ ID NO: 262) (SEQ ID NO: 252) (SEQ ID NO: 263) C12C01_Rd RASQSVSSTYLA DASSRAP QQYSSWPLT 4_0.6nM (SEQ ID NO: 251 ) (SEQ ID NO: 252) (SEQ ID NO: 264) _C16C01_Rd RASQSVSSIFLA DASSRAP QQYSAWPLT 4_0.6nM (SEQ ID NO: 265) (SEQ ID NO: 252) (SEQ ID NO: 256) _C09C01_Rd ACSQSVSSTYLA DASSRAP QQYSAWPLT 4_6nM_ (SEQ ID NO: 266) (SEQ ID NO: 252) (SEQ ID NO: 256) C09C01_Rd RASCDVSSTYLA DASSRAP QQYMRSPLT 4_0.6nM (SEQ ID NO: 267) (SEQ ID NO: 252) (SEQ ID NO: 268) _C03C01_Rd RASEAVPSTYLA DASSRAP QQYSAFPLT 4_0.6nM (SEQ ID NO: 269) (SEQ ID NO: 252) (SEQ ID NO: 261 ) _C06C01_Rd CSSQSVSSTYLA DASSRAP QQYSAFPLT 4_0.6nM (SEQ ID NO: 270) (SEQ ID NO: 252) (SEQ ID NO: 261 ) _C04COMBO RASVRVSSTYLA DAS I RAT QQYMKWPLT_Rd4_0. (SEQ ID NO: 271 ) (SEQ ID NO: 221 ) (SEQ ID NO: 272)6nM_C22COMBO RASQSVSAAYLA DAS I RAT QQYMCWPLT_Rd4_6 (SEQ ID NO: 273) (SEQ ID NO: 221 ) (SEQ ID NO: 274) nM_C21COMBO RASQSVSSSYWG DAS I RAT QQYQCWPLT_Rd4_6 (SEQ ID NO: 275) (SEQ ID NO: 221 ) (SEQ ID NO: 276) nM_C10COMBO RASQSVSSTYLA DAS I RAT QQYQSWPLT_Rd4_0. (SEQ ID NO: 251 ) (SEQ ID NO: 221 ) (SEQ ID NO: 225) 6nM_C04COMBO RASQSVSSPYLA DAS I RAT QQYQSWPLT_Rd4_6 (SEQ ID NO: 277) (SEQ ID NO: 221 ) (SEQ ID NO: 225) nM_C25COMBO RASQSVSPIYLA DAS I RAT QQYKAWPLT_Rd4_6 (SEQ ID NO: 260) (SEQ ID NO: 221 ) (SEQ ID NO: 278) nM_C1 1COMBO RASQSVSYLYLA DAS I RAT QQYMEWPLT_Rd4_0. (SEQ ID NO: 279) (SEQ ID NO: 221 ) (SEQ ID NO: 280) 6nM_C20COMBO RASQSVSAQYLA DAS I RAT QQYQAWPLT_Rd4_6 (SEQ ID NO: 245) (SEQ ID NO: 221 ) (SEQ ID NO: 281 ) nM_C09COMBO RASQSVSSSYLA DAS I RAT QQYQKWPLT_Rd4_6 (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 282) nM_C08COMBO RASQSVSAVYLA DAS I RAT QQYRAWPLT_Rd4_0. (SEQ ID NO: 283) (SEQ ID NO: 221 ) (SEQ ID NO: 284) 6nM_C19COMBO RASIAVSSTYLA DAS I RAT QQYMVWPLT _Rd4_0. (SEQ ID NO: 285) (SEQ ID NO: 221 ) (SEQ ID NO: 286) 6nM_C02COMBO RPRQSVSSSYLA DAS I RAT QQYQDWPLT_Rd4_0. (SEQ ID NO: 287) (SEQ ID NO: 221 ) (SEQ ID NO: 288) 6nM_C23COMBO RASQSVSSTYLA DAS I RAT QQYQEWPLT_Rd4_0. (SEQ ID NO: 251 ) (SEQ ID NO: 221 ) (SEQ ID NO: 289) 6nM_C09COMBO RASQSVSASYLA DAS I RAT QQYMSWPLT_Rd4_6 (SEQ ID NO: 290) (SEQ ID NO: 221 ) (SEQ ID NO: 291 ) nM_C12COMBO RASQSVSYMYLA DAS I RAT QQYKSWPLT_Rd4_0. (SEQ ID NO: 292) (SEQ ID NO: 221 ) (SEQ ID NO: 293) 6nM_C30COMBO RASQSVSAIYLA DAS I RAT QQYYGWPLT_Rd4_0. (SEQ ID NO: 235) (SEQ ID NO: 221 ) (SEQ ID NO: 294) 6nM_C14COMBO RASQPISSSYLA DAS I RAT QQYQGWPLT_Rd4_6 (SEQ ID NO: 295) (SEQ ID NO: 221 ) (SEQ ID NO: 229) nM_C07COMBO RASQSVSSSYLA DAS I RAT QQYEFWPLT_Rd4_6 (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 296) nM_C02COMBO RASQSVSSTYLA DAS I RAT QQYMSWPLT_Rd4_0. (SEQ ID NO: 251 ) (SEQ ID NO: 221 ) (SEQ ID NO: 291 ) 6nM_C05COMBO RASQGISSTYLA DAS I RAT QQYAYWPLT_Rd4_0. (SEQ ID NO: 297) (SEQ ID NO: 221 ) (SEQ ID NO: 298) 6nM_C17COMBO RASQSVSSSYLA DAS I RAT QQYQGWPLT_Rd4_6 (SEQ ID NO: 209) (SEQ ID NO: 221 ) (SEQ ID NO: 229) nM_C22COMBO RASQSVSVRYLA DAS I RAT QQYGSWPIT_Rd4_0. (SEQ ID NO: 299) (SEQ ID NO: 221 ) (SEQ ID NO: 300) 6nM_C11Light Xl Χ2Χ3Χ4Χ5ΧβΧ7Χ8Χ9 X ASX2RAX3, wherein X X X2YX3X4PPSFT, chain X0XiiXi2, wherein X-i is G or D; X2is S or I; and wherein X-i is Q or K; consens is R, G, W, A, or C; X2X3is T or P (SEQ ID NO: X2is H or Y; X3is G, us is A, P, G, L, C, or S; 310) N, or P; and X4is S,X3is S, G, or R; X4is W, or Y (SEQ ID Q, C, E, V, or I; X5is NO: 31 1 ) S, P, G, A, R, or D; X6QQYX1X2X3PX4T, is V, G, I, or L; X7is S, wherein Xi is G, Q, E, D, P, or G; X8is S, E, L, F, A, S, M, K, P, F, A, M, E, V, N, D, R, or Y; X2is S, R, or Y; X9is I, T, V, E, F T, G, V, F, Y, D, A, S, A, M, Q, Y, H, or R; H, V, E, K, or C; X3X-io is Y or F; X-n is L, is W, F, or S; and X4W, or P; and X2is A, is L or I (SEQ ID S, or G (SEQ ID NO: NO: 312) 309)P4G4 RASQSVSSSYLA GASSRAY (SEQ ID NO: QHYGSPPLFT(SEQ ID NO: 209) 362) (SEQ ID NO: 499 )P1A1 1 RASQNVSSSYLA GASYRAT (SEQ ID NO: QHYGSPPSFT(SEQ ID NO: 500) 501) (SEQ ID NO: 21 1 )In some embodiments, the present invention provides an antibody that binds to BCMA and competes with the antibody as described herein, including P6E01 / P6E01 , P6E01 / H3.AQ, L1.LGF / L3.KW / P6E01 ; L1.LGF / L3.NY / P6E01 , L1.GDF / L3.NY / P6E01 , L1.LGF / L3.KW / H3.AL, L1.LGF / L3.KW / H3.AP, L1.LGF / L3.KW / H3.AQ, L1.LGF / L3.PY / H3.AP, L1.LGF / L3.PY / H3.AQ, L1.LGF / L3.NY / H3.AL,L1.LGF / L3.NY / H3.AP, L1.LGF / L3.NY / H3.AQ, L1.GDF / L3.KW / H3.AL,L1.GDF / L3.KW / H3.AP, L1.GDF / L3.KW / H3.AQ, L1.GDF / L3.PY / H3.AQ,L1.GDF / L3.NY / H3.AL, L1.GDF / L3.NY / H3.AP, L1.GDF / L3.NY / H3.AQ, L3.KW / P6E01 , L3.PY / P6E01 , L3.NY / P6E01 ,L3.PY / L1.PS / P6E01 , L3.PY / L1.AH / P6E01 , L3.PY / L1.FF / P6E01 , L3.PY / L1.PH / P6E01 , L3.PY / L3.KY / P6E01 , L3.PY / L3.KF / P6E01 , L3.PY / H2.QR, L3.PY / H2.DY, L3.PY / H2.YQ, L3.PY / H2.LT, L3.PY / H2.HA, L3.PY / H2.QL, L3.PY / H3.YA, L3.PY / H3.AE, L3.PY / H3.AQ, L3.PY / H3.TAQ, L3.PY / P6E01 , L3.PY / L1.PS / H2.QR, L3.PY / L1.PS / H2.DY, L3.PY / L1.PS / H2.YQ, L3.PY / L1.PS / H2.LT, L3.PY / L1.PS / H2.HA, L3.PY / L1.PS / H2.QL, L3.PY / L1.PS / H3.YA, L3.PY / L1.PS / H3.AE, L3.PY / L1.PS / H3.AQ, L3.PY / L1.PS / H3.TAQ, L3.PY / L1.AH / H2.QR, L3.PY / L1.AH / H2.DY, L3.PY / L1.AH / H2.YQ, L3.PY / L1.AH / H2.LT, L3.PY / L1.AH / H2.HA, L3.PY / L1.AH / H2.QL, L3.PY / L1.AH / H3.YA, L3.PY / L1.AH / H3.AE, L3.PY / L1.AH / H3.AQ, L3.PY / L1.AH / H3.TAQ, L3.PY / L1.FF / H2.QR, L3.PY / L1.FF / H2.DY, L3.PY / L1.FF / H2.YQ, L3.PY / L1.FF / H2.LT, L3.PY / L1.FF / H2.HA, L3.PY / L1.FF / H2.QL, L3.PY / L1.FF / H3.YA, L3.PY / L1.FF / H3.AE, L3.PY / L1.FF / H3.AQ, L3.PY / L1.FF / H3.TAQ, L3.PY / L1.PH / H2.QR, L3.PY / L1.PH / H2.HA, L3.PY / L1.PH / H3.AE, L3.PY / L1.PH / H3.AQ, L3.PY / L1.PH / H3.TAQ, L3.PY / L3.KY / H2.QR, L3. PY / L3. KY / H2. DY, L3.PY / L3.KY / H2.YQ L3.PY / L3.KY / H2.LT, L3.PY / L3.KY / H2.HA, L3.PY / L3.KY / H2.QL, L3.PY / L3.KY / H3.YA L3.PY / L3.KY / H3.TAQ, L3. PY / L3. KF / H 2. D Y, L3. PY / L3. KF / H2. YQ, L3.PY / L3.KF / H2.LT L3.PY / L3.KF / H2.QL, L3. PY / L3. KF / H3. YA, L3. PY / L3. KF / H3. AE, L3. PY / L3. KF / H3. AQ L3.PY / L3.KF / H3.TAQ, P5A2_VHVL, A02_Rd4_0.6nM_C06, A02_Rd4_0.6nM_C09 A02_Rd4_6nM_C16, A02_Rd4_6nM_C03, A02_Rd4_6nM_C01 , A02_Rd4_6nM_C26 A02_Rd4_6nM_C25, A02_Rd4_6nM_C22, A02_Rd4_6nM_C19, A02_Rd4_0.6nM_C03 A02_Rd4_6nM_C07, A02_Rd4_6nM_C23, A02_Rd4_0.6nM_C18, A02_Rd4_6nM_C10 A02_Rd4_6nM_C05, A02_Rd4_0.6nM_C10, A02_Rd4_6nM_C04,A02 Rd4 0.6nM C26A02_Rd4_0.6nM_C13, A02_Rd4_0.6nM_C01 , A02_Rd4_6nM_C08, P5C1_VHVL, C01_Rd4_6nM_C24, C01_Rd4_6nM_C26, C01_Rd4_6nM_C10, C01_Rd4_0.6nM_C27C01_Rd4_6nM_C20, C01_Rd4_6nM_C12, C01_Rd4_0.6nM_C16, C01 Rd4 0.6nM C09C01_Rd4_6nM_C09, C01_Rd4_0.6nM_C03, C01_Rd4_0.6nM_C06, C01_Rd4_6nM_C04COMBO_Rd4_0.6nM_C22, COMBO_Rd4_6nM_C21 , COMBO_Rd4_6nM_C10, COMBO_Rd4_0.6nM_C04, COMBO_Rd4_6nM_C25, COMBO_Rd4_0.6nM_C21 , CCOOMMBBOO_RRdd44_66nnMM_CC11 11 ,, COMBO_Rd4_0.6nM_C20, COMBO_Rd4_6nM_C09, COMBO_Rd4_6nM_C08, COMBO_Rd4_0.6nM_C19, COMBO_Rd4_0.6nM_C02, COMBO_Rd4_0.6nM_C23, COMBO_Rd4_0.6nM_C29, COMBO_Rd4_0.6nM_C09, COMBO_Rd4_6nM_C12, COMBO_Rd4_0.6nM_C30, COMBO_Rd4_0.6nM_C14,COMBO_Rd4_6nM_C07, COMBO_Rd4_6nM_C02, COMBO_Rd4_0.6nM_C05, COMBO_Rd4_0.6nM_C17, COMBO_Rd4_6nM_C22, COMBO_Rd4_0.6nM_C1 1 , COMBO_Rd4_0.6nM_C29, P4G4, or P1A1 1.In some embodiments, the present invention provides an antibody or an antigen binding fragment, which specifically binds to BCMA, wherein the antibody comprises a VH region comprising a sequence shown in SEQ ID NO: 1 12; and / or a VL region comprising a sequence shown in SEQ ID NO: 38. In some embodiments, the antibody comprises a light chain comprising the sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLMYDASIRATG IPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYQSWPLTFGQGTKVEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDST YSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC (SEQ ID NO: 357) and a heavy chain comprising the sequenceEVQLLESGGGLVQPGGSLRLSCAASGFTFSSYPMSWVRQAPGKGLEWVSAIGGSGG SLPYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARYWPMDIWGQGTLVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCP APELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAK TKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGS FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 358).In some embodiments, the present invention provides an antibody or an antigen binding fragment, which specifically bind to BCMA, wherein the antibody comprises a VH region comprising a sequence shown in SEQ ID NO: 2, 32, 42, or 78; and / or a VL region comprising a sequence shown in SEQ ID NO: 6, 16, 43, or 85, .In some embodiments, the invention also provides CDR portions of antibodies to BCMA antibodies based on CDR contact regions. CDR contact regions are regions of an antibody that imbue specificity to the antibody for an antigen. In general, CDR contact regions include the residue positions in the CDRs and Vernier zones which are constrained in order to maintain proper loop structure for the antibody to bind a specific antigen. See, e.g., Makabe et al., J. Biol. Chem., 283: 1 156-1166, 2007. Determination of CDR contact regions is well within the skill of the art.The binding affinity (KD) of the BCMA antibody as described herein to BCMA (such as human BCMA (e.g., (SEQ ID NO: 353) can be about 0.002 nM to about 6500 nM. In some embodiments, the binding affinity is about any of 6500 nm, 6000 nm, 5986 nm, 5567 nm, 5500 nm, 4500 nm, 4000 nm, 3500 nm, 3000 nm, 2500 nm, 2134 nm, 2000 nm, 1500 nm, 1000 nm, 750 nm, 500 nm, 400 nm, 300 nm, 250 nm, 200 nM, 193 nM, 100 nM, 90 nM, 50 nM, 45 nM, 40 nM, 35 nM, 30 nM, 25 nM, 20 nM, 19 nm, 18 nm, 17 nm, 16 nm, 15 nM, 10 nM, 8 nM, 7.5 nM, 7 nM, 6.5 nM, 6 nM, 5.5 nM, 5 nM, 4 nM, 3 nM, 2 nM, 1 nM, 0.5 nM, 0.3 nM, 0.1 nM, 0.01 nM, or 0.002 nM. In some embodiments, the binding affinity is less than about any of 6500 nm, 6000 nm, 5500 nm, 5000 nm, 4000 nm, 3000 nm, 2000 nm, 1000 nm, 900 nm, 800 nm, 250 nM, 200 nM, 100 nM, 50 nM, 30 nM, 20 nM, 10 nM, 7.5 nM, 7 nM, 6.5 nM, 6 nM, 5 nM, 4.5 nM, 4 nM, 3.5 nM, 3 nM, 2.5 nM, 2 nM, 1.5 nM, 1 nM, or 0.5 nM.In some embodiments, the invention encompasses compositions, including pharmaceutical compositions, comprising antibodies described herein or made by the methods and having the characteristics described herein. As used herein, compositions comprise one or more antibodies that bind to BCMA, and / or one or more polynucleotides comprising sequences encoding one or more these antibodies. These compositions may further comprise suitable excipients, such as pharmaceutically acceptable excipients including buffers, which are well known in the art.The invention also provides methods of making any of these antibodies. The antibodies of this invention can be made by procedures known in the art. The polypeptides can be produced by proteolytic or other degradation of the antibodies, by recombinant methods (i.e., single or fusion polypeptides) as described above or by chemical synthesis. Polypeptides of the antibodies, especially shorter polypeptides up to about 50 amino acids, are conveniently made by chemical synthesis. Methods of chemical synthesis are known in the art and are commercially available. For example, an antibody could be produced by an automated polypeptide synthesizer employing the solid phase method. See also, U.S. Pat. Nos. 5,807,715; 4,816,567; and 6,331 ,415.The invention also encompasses fusion proteins comprising one or more fragments or regions from the antibodies of this invention. In one embodiment, a fusion polypeptide is provided that comprises at least 10 contiguous amino acids of the variable light chain region shown in SEQ ID NOs: 1 , 4, 5, 6, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 34, 36, 38, 40, 41 , 43, 45, 47, 49, 51 , 53, 55, 57, 59, 61 , 63, 65, 67, 69, 71 , 73, 75, 77, 79, 317, 81 , 82, 84, 85, 86, 88, 89, 90, 91 , 93, 94, 96, 98, 100, 102, 103, 105, 107, 108, 109, 1 1 1 , 1 13, 1 15, 1 16, 1 17, 1 19, 121 , 123, 124, 126, 128, 80, 315, 36, or 364, and / or at least 10 amino acids of the variable heavy chain region shown in SEQ ID NOs: 2, 3, 7, 8, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 35, 37, 39, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 83, 87, 92, 95, 97, 99, 101 , 104, 106, 1 10, 1 12, 1 14, 1 18, 120, 122, 1 12, 125, 127, 313, 314, 363, or 365. In other embodiments, a fusion polypeptide is provided that comprises at least about 10, at least about 15, at least about 20, at least about 25, or at least about 30 contiguous amino acids of the variable light chain region and / or at least about 10, at least about 15, at least about 20, at least about 25, or at least about 30 contiguous amino acids of the variable heavy chain region. In another embodiment, the fusion polypeptide comprises a light chain variable region and / or a heavy chain variable region, as shown in any of the sequence pairs selected from among SEQ ID NOs: 1 and 2, 1 and 3, 4 and 2, 5 and 2, 6 and 2, 4 and 7, 4 and 8, 4 and 3, 9 and 8, 9 and 3, 10 and 7, 10 and 8, 10 and 3, 1 1 and 7, 1 1 and 8, 1 1 and 3, 12 and 3, 13 and 7, 13 and 8, 14 and 3, 15 and 2, 16 and 2, 17 and 2, 18 and 2, 19 and 2, 20 and 2, 21 and 2, 22 and 2, 23 and 2, 16 and 24, 16 and 25, 16 and 26, 16 and 27, 16 and 28, 16 and 29, 16 and 30, 16 and 31 , 16 and 3, 16 and 32, 16 and 2, 18 and 24, 18 and 25, 18 and 26, 18 and 27, 18 and 28, 18 and 29, 18 and 30, 18 and 31 , 18 and 3, 18 and 32, 19 and 24,19 and 25, 19 and 26, 19 and 27, 19 and 28, 19 and 29, 19 and 30, 19 and 31 , 19 and 3, 19 and 32, 20 and 24, 20 and 25, 20 and 26, 20 and 27, 20 and 28, 20 and 29, 20 and 30, 20 and 31 , 20 and 3, 20 and 32, 21 and 24, 21 and 28, 21 and 31 , 21 and 3, 21 and 32, 22 and 24, 22 and 25, 22 and 26, 22 and 27, 22 and 28, 22 and 29, 22 and 30, 22 and 32, 23 and 25, 23 and 26, 23 and 27, 23 and 29, 23 and 30, 23 and 31 , 23 and 3, 23 and 32, 34 and 33, 36 and 35, 38 and 37, 40 and 39, 41 and 33, 43 and 42, 45 and 44, 47 and 46, 49 and 48, 51 and 50, 53 and 52, 55 and 54, 57 and 56, 59 and 58, 61 and 60, 63 and 62, 65 and 64, 67 and 66, 69 and 68, 71 and 70, 73 and 72, 75 and 74, 77 and 76, 79 and 78, 317 and 78, 79 and 78, 81 and 78, 82 and 78, 84 and 83, 85 and 78, 86 and 78, 88 and 87, 89 and 78, 90 and 78, 91 and 78, 93 and 92, 94 and 78, 96 and 95, 98 and 97, 38 and 78, 102 and 101 , 103 and 78, 105 and 104, 107 and 106, 108 and 78, 109 and 78, 1 1 1 and 1 10, 38 and 1 12, 1 13 and 1 12, 1 15 and 1 14, 1 16 and 76, 1 17 and 1 12, 1 19 and 1 18, 121 and 120, 123 and 122, 124 and 1 12, 126 and 125, 128 and 127, 80 and 363, or 364 and 365. In another embodiment, the fusion polypeptide comprises one or more CDR(s). In still other embodiments, the fusion polypeptide comprises CDR H3 (VH CDR3) and / or CDR L3 (VL CDR3). For purposes of this invention, a fusion protein contains one or more antibodies and another amino acid sequence to which it is not attached in the native molecule, for example, a heterologous sequence or a homologous sequence from another region. Exemplary heterologous sequences include, but are not limited to a "tag" such as a FLAG tag or a 6His tag. Tags are well known in the art.The invention also provides isolated polynucleotides encoding the antibodies of the invention, and vectors and host cells comprising the polynucleotide.In one embodiment, a polynucleotide comprises a sequence encoding the heavy chain and / or the light chain variable regions of antibody P6E01 / P6E01 , P6E01 / H3.AQ, L1.LGF / L3.KW / P6E01 ; L1.LGF / L3.NY / P6E01 , L1.GDF / L3.NY / P6E01 ,L1.LGF / L3.KW / H3.AL, L1.LGF / L3.KW / H3.AP, L1.LGF / L3.KW / H3.AQ,L1.LGF / L3.PY / H3.AP, L1.LGF / L3.PY / H3.AQ, L1.LGF / L3.NY / H3.AL,L1.LGF / L3.NY / H3.AP, L1.LGF / L3.NY / H3.AQ, L1.GDF / L3.KW / H3.AL, L1.GDF / L3.KW / H3.AP, L1.GDF / L3.KW / H3.AQ, L1.GDF / L3.PY / H3.AQ,L1.GDF / L3.NY / H3.AL, L1.GDF / L3.NY / H3.AP, L1.GDF / L3.NY / H3.AQ, L3.KW / P6E01 , L3.PY / P6E01 , L3.NY / P6E01 ,L3.PY / L1.PS / P6E01 , L3.PY / L1.AH / P6E01 , L3.PY / L1.FF / P6E01 , L3.PY / L1.PH / P6E01 , L3.PY / L3.KY / P6E01 , L3.PY / L3.KF / P6E01 , L3.PY / H2.QR, L3.PY / H2.DY, L3.PY / H2.YQ, L3.PY / H2.LT, L3.PY / H2.HA, L3.PY / H2.QL, L3.PY / H3.YA, L3.PY / H3.AE, L3.PY / H3.AQ, L3.PY / H3.TAQ, L3.PY / P6E01 , L3.PY / L1.PS / H2.QR, L3.PY / L1.PS / H2.DY, L3.PY / L1.PS / H2.YQ, L3.PY / L1.PS / H2.LT, L3.PY / L1.PS / H2.HA, L3.PY / L1.PS / H2.QL, L3.PY / L1.PS / H3.YA, L3.PY / L1.PS / H3.AE, L3.PY / L1.PS / H3.AQ, L3.PY / L1.PS / H3.TAQ, L3.PY / L1.AH / H2.QR, L3.PY / L1.AH / H2.DY, L3.PY / L1.AH / H2.YQ, L3.PY / L1.AH / H2.LT, L3.PY / L1.AH / H2.HA, L3.PY / L1.AH / H2.QL, L3.PY / L1.ΑΗ / Η3.ΥΑ, L3.PY / L1.ΑΗ / Η3.ΑΕ, L3.PY / L1.AH / H3.AQ, L3.PY / L1.AH / H3.TAQ, L3.PY / L1.FF / H2.QR, L3.PY / L1.FF / H2.DY, L3.PY / L1.FF / H2.YQ, L3.PY / L1.FF / H2.LT, L3.PY / L1.FF / H2.HA, L3.PY / L1.FF / H2.QL, L3.PY / L1.FF / H3.YA, L3.PY / L1.FF / H3.AE, L3.PY / L1.FF / H3.AQ, L3.PY / L1.FF / H3.TAQ, L3.PY / L1.PH / H2.QR, L3.PY / L1.ΡΗ / Η2.ΗΑ, L3.PY / L1.ΡΗ / Η3.ΑΕ, L3.PY / L1.PH / H3.AQ, L3.PY / L1.PH / H3.TAQ, L3.PY / L3.KY / H2.QR, L3. PY / L3. ΚΥ / Η2. DY, L3.PY / L3.KY / H2.YQ L3.PY / L3.KY / H2.LT, L3.PY / L3.KY / H2.HA, L3.PY / L3.KY / H2.QL, L3.PY / L3.KY / H3.YA L3.PY / L3.KY / H3.TAQ, L3. PY / L3. KF / H 2. D Y, L3. PY / L3. KF / H2. YQ, L3.PY / L3.KF / H2.LT L3.PY / L3.KF / H2.QL, L3. PY / L3. KF / H3. YA, L3. PY / L3. KF / H3. AE, L3. PY / L3. KF / H3. AQ L3.PY / L3.KF / H3.TAQ, P5A2_VHVL, A02_Rd4_0.6nM_C06, A02_Rd4_0.6nM_C09 A02_Rd4_6nM_C16, A02_Rd4_6nM_C03, A02_Rd4_6nM_C01 , A02_Rd4_6nM_C26 A02_Rd4_6nM_C25, A02_Rd4_6nM_C22, A02_Rd4_6nM_C19, A02_Rd4_0.6nM_C03 A02_Rd4_6nM_C07, A02_Rd4_6nM_C23, A02_Rd4_0.6nM_C18, A02_Rd4_6nM_C10 A02_Rd4_6nM_C05, A02_Rd4_0.6nM_C10, A02_Rd4_6nM_C04,A02_Rd4_0.6nM_C26A02_Rd4_0.6nM_C13, A02_Rd4_0.6nM_C01 , A02_Rd4_6nM_C08, P5C1_VHVL, C01_Rd4_6nM_C24, C01_Rd4_6nM_C26, C01_Rd4_6nM_C10, C01_Rd4_0.6nM_C27C01_Rd4_6nM_C20, C01_Rd4_6nM_C12, C01_Rd4_0.6nM_C16, C01 Rd4 0.6nM C09C01_Rd4_6nM_C09, C01_Rd4_0.6nM_C03, C01_Rd4_0.6nM_C06,C01_Rd4_6nM_C04COMBO_Rd4_0.6nM_C22, COMBO_Rd4_6nM_C21 , COMBO_Rd4_6nM_C10,COMBO_Rd4_0.6nM_C04, COMBO_Rd4_6nM_C25, COMBO_Rd4_0.6nM_C21 ,COMBO_Rd4_6nM_C1 1 , COMBO_Rd4_0.6nM_C20, COMBO_Rd4_6nM_C09,COMBO_Rd4_6nM_C08, COMBO_Rd4_0.6nM_C19, COMBO_Rd4_0.6nM_C02,COMBO_Rd4_0.6nM_C23, COMBO_Rd4_0.6nM_C29, COMBO_Rd4_0.6nM_C09, COMBO_Rd4_6nM_C12, COMBO_Rd4_0.6nM_C30, COMBO_Rd4_0.6nM_C14, COMBO_Rd4_6nM_C07, COMBO_Rd4_6nM_C02, COMBO_Rd4_0.6nM_C05, COMBO_Rd4_0.6nM_C17, COMBO_Rd4_6nM_C22, COMBO_Rd4_0.6nM_C1 1 , COMBO_Rd4_0.6nM_C29, P4G4, or P1A1 1. The sequence encoding the antibody of interest may be maintained in a vector in a host cell and the host cell can then be expanded and frozen for future use. Vectors (including expression vectors) and host cells are further described herein.The invention also encompasses scFv of antibodies of this invention. Single chain variable region fragments are made by linking light and / or heavy chain variable regions by using a short linking peptide (Bird et al., Science 242:423-426, 1988). An example of a linking peptide is (GGGGS)3(SEQ ID NO: 498), which bridges approximately 3.5 nm between the carboxy terminus of one variable region and the amino terminus of the other variable region. Linkers of other sequences have been designed and used (Bird et al., 1988, supra). Linkers should be short, flexible polypeptides and preferably comprised of less than about 20 amino acid residues. Linkers can in turn be modified for additional functions, such as attachment of drugs or attachment to solid supports. The single chain variants can be produced either recombinantly or synthetically. For synthetic production of scFv, an automated synthesizer can be used. For recombinant production of scFv, a suitable plasmid containing polynucleotide that encodes the scFv can be introduced into a suitable host cell, either eukaryotic, such as yeast, plant, insect or mammalian cells, or prokaryotic, such as E. coli. Polynucleotides encoding the scFv of interest can be made by routine manipulations such as ligation of polynucleotides. The resultant scFv can be isolated using standard protein purification techniques known in the art.Other forms of single chain antibodies, such as diabodies or minibodies are also encompassed. Diabodies are bivalent, bispecific antibodies in which heavy chain variable (VH) and light chain variable (VL) domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see e.g., Holliger, P., et al., Proc. Natl. Acad Sci. USA 90:6444-6448, 1993; Poljak, R. J., et al., Structure 2:1 121 -1 123, 1994). Minibody includes the VL and VH domains of anative antibody fused to the hinge region and CH3 domain of the immunoglobulin molecule. See, e.g., US5,837,821.In another aspect, the invention provides compositions (such as a pharmaceutical compositions) comprising any of the polynucleotides of the invention. In some embodiments, the composition comprises an expression vector comprising a polynucleotide encoding any of the antibodies described herein. In still other embodiments, the composition comprises either or both of the polynucleotides shown inSEQ ID NO: 486 and SEQ ID NO: 485 below:COMBO_Rd4_0.6nM_C29 heavy chain variable regionGAAGTCCAACTCCTCGAATCCGGTGGCGGCCTTGTCCAGCCTGGAGGTTCCTTGCGCCTGTCATGTGCCGCCAGCGGATTCACCTTCTCGTCCTACCCGATGTCGTGGGTCCGCCAGGCTCCGGGAAAGGGCCTGGAATGGGTGTCAGCCATCGGAGGATCGGGGGGCTCCCTGCCCTACGCCGATATCGTGAAGGGAAGGTTCACCATTAGCCGGGACAACTCCAAGAACACTCTGTACCTCCAAATGAACAGCCTGAGAGCGGAGGACAC CGCAGTGTACTATTGCGCCCGGTACTGGCCAATGGACATCTGGGGCCAGGGGACTCTGGTCACCGTCTCCTCA (SEQ ID NO: 486)COMBO_Rd4_0.6nM_C29 light chain variable regionGAGATCGTGCTGACTCAGTCCCCTGGAACCCTGTCCCTGTCACCTGGCGAAAGAG CTACCTTGTCCTGTCGCGCATCACAATCCGTGTCGTCGAGCTATCTCGCGTGGTA CCAGCAGAAGCCCGGACAGGCCCCAAGGCTGCTTATGTACGACGCCTCCATCCG GGCCACTGGTATCCCCGACCGCTTCTCGGGCTCCGGAAGCGGCACCGACTTCAC CCTGACTATTTCCCGGCTCGAACCGGAGGATTTCGCCGTGTACTACTGCCAACAG TACCAGAGCTGGCCGCTGACGTTTGGGCAGGGGACCAAGGTCGAAATCAAA(SEQ ID NO: 485)In other embodiments, the composition comprises either or both of the polynucleotides shown in SEQ ID NO: 488 and SEQ ID NO: 487 below:L3.PY / H3TAQ heavy chain variable regionGAAGTGCAGCTGCTGGAATCTGGCGGAGGACTGGTGCAGCCTGGCGGCTCTCTG AGACTGTCTTGTGCCGCCAGCGGCTTCACCTTCGGCAGCTACGCTATGACCTGGG TGCGCCAGGCCCCTGGCAAAGGACTGGAATGGGTGTCCGCCATCTCTGGCAGCG GCGGCAATACCTTCTACGCCGAGAGCGTGAAGGGCCGGTTCACCATCAGCCGGG ACAACAGCAAGAACACCCTGTACCTGCAGATGAACAGCCTGCGGGCCGAGGACA CCGCCGTGTACTATTGTACACGGGTGTCCCCTATCGCCGCGCAGATGGATTATTGGGGCCAGGGCACTCTGGTCACCGTCTCCTCA(SEQ ID NO: 488)L3.PY / H3TAQ heavy chain variable regionGAGATCGTGCTGACACAGAGCCCTGGCACCCTGAGCCTGTCTCCAGGCGAAAGA GCCACCCTGTCCTGCAGAGCCAGCCAGAGCGTGTCCAGCAGCTACCTGGCCTGG TATCAGCAGAAGCCCGGCCAGGCTCCCCGGCTGCTGATCTATGGCGCCTCTTCTA GAGCCACCGGCATCCCCGATAGATTCAGCGGCTCTGGCAGCGGCACCGACTTCA CCCTGACCATCAGCAGACTGGAACCCGAGGACTTCGCCGTGTACTACTGCCAGCA CTACCCTTATCCCCCCAGCTTCACATTTGGCCAGGGCACCAAGGTGGAGATCAAA(SEQ ID NO: 487)In still other embodiments, the composition comprises either or both of the polynucleotides shown in SEQ ID NO: 490 and SEQ ID NO: 489 below:A02_Rd4_0.6nM_C01 heavy chain variable regionGAAGTTCAATTATTGGAATCTGGTGGAGGACTGGTGCAGCCTGGCGGCTCTCTGA GACTGTCTTGTGCCGCCAGCGGCTTCACCTTCAGCAGCTACGCCATGAACTGGGT GCGCCAGGCCCCTGGTAAAGGTTTGGAATGGGTTTCTGCTATTACTGCGTCTGGT GGTTCTACTTACTATGCCGATGTGGTTAAGGGTAGATTCACCATTTCTAGAGACAA CTCTAAGAACACCTTGTACTTGCAAATGAACTCCTTGAGAGCTGAAGATACTGCTG TTTATTACTGTGCTAGATACTGGCCAATGTCGTTGTGGGGTCAAGGTACTCTGGTC ACCGTCTCCTCA(SEQ ID NO: 490)A02_Rd4_0.6nM_C01 light chain variable regionGAGATCGTGCTGACACAGAGCCCTGGCACCCTGAGCCTGTCTCCTGGTGAAAGA GCTACTTTGTCTTGTAGAGCTTCTCAATCCGTTTCCGCGTATTATTTGGCTTGGTAT CAACAAAAACCAGGTCAAGCTCCAAGATTATTGATGTACGATGCTTCTATTAGAGC CACCGGTATTCCAGATAGATTTTCTGGTTCTGGTTCCGGTACTGATTTCACTTTGAC TATCTCTAGATTGGAACCAGAAGATTTCGCTGTTTACTACTGTCAACAATATGAGCG TTGGCCATTGACTTTTGGTCAAGGTACAAAGGTTGAAATCAAACGTGAG(SEQ ID NO: 489)In other embodiments, the composition comprises either or both of the polynucleotides shown in SEQ ID NO: 492 and SEQ ID NO: 491 below:A02_Rd4_0.6nM_C16 heavy chain variable regionGAAGTTCAATTATTGGAATCTGGTGGAGGACTGGTGCAGCCTGGCGGCTCTCTGA GACTGTCTTGTGCCGCCAGCGGCTTCACCTTCAGCAGCTACGCCATGAACTGGGT GCGCCAGGCCCCTGGTAAAGGTTTGGAATGGGTTTCTGCTATTTCTGATTTTGGTG GTTCTACTTACTATGCCGATATCGTTAAGGGTAGATTCACCATTTCTAGAGACAACT CTAAGAACACCTTGTACTTGCAAATGAACTCCTTGAGAGCTGAAGATACTGCTGTT TATTACTGTGCTAGATACTGGCCAATGGATATTTGGGGTCAAGGTACTCTGGTCAC CGTCTCCTCA(SEQ ID NO: 492)A02_Rd4_0.6nM_C16 light chain variable regionGAGATCGTGCTGACACAGAGCCCTGGCACCCTGAGCCTGTCTCCTGGTGAAAGA GCTACTTTGTCTTGTAGAGCTTCTCAATCCGTTTCCGATCTGTATTTGGCTTGGTAT CAACAAAAACCAGGTCAAGCTCCAAGATTATTGATGTACGATGCTTCTATTAGAGC CACCGGTATTCCAGATAGATTTTCTGGTTCTGGTTCCGGTACTGATTTCACTTTGAC TATCTCTAGATTGGAACCAGAAGATTTCGCTGTTTACTACTGTCAACAATATCAGAC TTGGCCATTGACTTTTGGTCAAGGTACAAAGGTTGAAATCAAACGTGAG(SEQ ID NO: 491 ).Expression vectors, and administration of polynucleotide compositions are further described herein.In another aspect, the invention provides a method of making any of the polynucleotides described herein.Polynucleotides complementary to any such sequences are also encompassed by the present invention. Polynucleotides may be single-stranded (coding or antisense) or double-stranded, and may be DNA (genomic, cDNA or synthetic) or RNA molecules. RNA molecules include HnRNA molecules, which contain introns and correspond to a DNA molecule in a one-to-one manner, and mRNA molecules, which do not contain introns. Additional coding or non-coding sequences may, but need not, be present within a polynucleotide of the present invention, and a polynucleotide may, but need not, be linked to other molecules and / or support materials.Polynucleotides may comprise a native sequence (i.e., an endogenous sequence that encodes an antibody or a portion thereof) or may comprise a variant of such a sequence. Polynucleotide variants contain one or more substitutions, additions, deletions and / or insertions such that the immunoreactivity of the encoded polypeptide is not diminished, relative to a native immunoreactive molecule. The effect on theimmunoreactivity of the encoded polypeptide may generally be assessed as described herein. Variants preferably exhibit at least about 70% identity, more preferably, at least about 80% identity, yet more preferably, at least about 90% identity, and most preferably, at least about 95% identity to a polynucleotide sequence that encodes a native antibody or a portion thereof.Two polynucleotide or polypeptide sequences are said to be "identical" if the sequence of nucleotides or amino acids in the two sequences is the same when aligned for maximum correspondence as described below. Comparisons between two sequences are typically performed by comparing the sequences over a comparison window to identify and compare local regions of sequence similarity. A "comparison window" as used herein, refers to a segment of at least about 20 contiguous positions, usually 30 to about 75, or 40 to about 50, in which a sequence may be compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned.Optimal alignment of sequences for comparison may be conducted using theMegalign program in the Lasergene suite of bioinformatics software (DNASTAR, Inc., Madison, Wl), using default parameters. This program embodies several alignment schemes described in the following references: Dayhoff, M.O., 1978, A model of evolutionary change in proteins - Matrices for detecting distant relationships. In Dayhoff, M.O. (ed.) Atlas of Protein Sequence and Structure, National Biomedical Research Foundation, Washington DC Vol. 5, Suppl. 3, pp. 345-358; Hein J., 1990, Unified Approach to Alignment and Phylogenes pp. 626-645 Methods in Enzymology vol. 183, Academic Press, Inc., San Diego, CA; Higgins, D.G. and Sharp, P.M., 1989, CABIOS 5: 151 -153; Myers, E.W. and Muller W., 1988, CABIOS 4: 1 1-17; Robinson, E.D., 1971 , Comb. Theor. 1 1 : 105; Santou, N., Nes, M., 1987, Mol. Biol. Evol. 4:406- 425; Sneath, P.H.A. and Sokal, R.R., 1973, Numerical Taxonomy the Principles and Practice of Numerical Taxonomy, Freeman Press, San Francisco, CA; Wilbur, W.J. and Lipman, D.J., 1983, Proc. Natl. Acad. Sci. USA 80:726-730.Preferably, the "percentage of sequence identity" is determined by comparing two optimally aligned sequences over a window of comparison of at least 20 positions, wherein the portion of the polynucleotide or polypeptide sequence in the comparison window may comprise additions or deletions (i.e., gaps) of 20 percent or less, usually 5 to 15 percent, or 10 to 12 percent, as compared to the reference sequences (whichdoes not comprise additions or deletions) for optimal alignment of the two sequences. The percentage is calculated by determining the number of positions at which the identical nucleic acid bases or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the reference sequence (i.e. the window size) and multiplying the results by 100 to yield the percentage of sequence identity.Variants may also, or alternatively, be substantially homologous to a native gene, or a portion or complement thereof. Such polynucleotide variants are capable of hybridizing under moderately stringent conditions to a naturally occurring DNA sequence encoding a native antibody (or a complementary sequence).Suitable "moderately stringent conditions" include prewashing in a solution of 5 X SSC, 0.5% SDS, 1.0 mM EDTA (pH 8.0); hybridizing at 50°C-65°C, 5 X SSC, overnight; followed by washing twice at 65°C for 20 minutes with each of 2X, 0.5X and 0.2X SSC containing 0.1 % SDS.As used herein, "highly stringent conditions" or "high stringency conditions" are those that: (1 ) employ low ionic strength and high temperature for washing, for example 0.015 M sodium chloride / 0.0015 M sodium citrate / 0.1 % sodium dodecyl sulfate at 50°C; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v / v) formamide with 0.1 % bovine serum albumin / 0.1 % Ficoll / 0.1 % polyvinylpyrrolidone / 50 mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42°C; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCI, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1 % sodium pyrophosphate, 5 x Denhardt's solution, sonicated salmon sperm DNA (50 pg / ml), 0.1 % SDS, and 10% dextran sulfate at 42°C, with washes at 42°C in 0.2 x SSC (sodium chloride / sodium citrate) and 50% formamide at 55°C, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55°C. The skilled artisan will recognize how to adjust the temperature, ionic strength, etc. as necessary to accommodate factors such as probe length and the like.It will be appreciated by those of ordinary skill in the art that, as a result of the degeneracy of the genetic code, there are many nucleotide sequences that encode a polypeptide as described herein. Some of these polynucleotides bear minimal homology to the nucleotide sequence of any native gene. Nonetheless, polynucleotides that vary due to differences in codon usage are specifically contemplated by the presentinvention. Further, alleles of the genes comprising the polynucleotide sequences provided herein are within the scope of the present invention. Alleles are endogenous genes that are altered as a result of one or more mutations, such as deletions, additions and / or substitutions of nucleotides. The resulting mRNA and protein may, but need not, have an altered structure or function. Alleles may be identified using standard techniques (such as hybridization, amplification and / or database sequence comparison).The polynucleotides of this invention can be obtained using chemical synthesis, recombinant methods, or PCR. Methods of chemical polynucleotide synthesis are well known in the art and need not be described in detail herein. One of skill in the art can use the sequences provided herein and a commercial DNA synthesizer to produce a desired DNA sequence.For preparing polynucleotides using recombinant methods, a polynucleotide comprising a desired sequence can be inserted into a suitable vector, and the vector in turn can be introduced into a suitable host cell for replication and amplification, as further discussed herein. Polynucleotides may be inserted into host cells by any means known in the art. Cells are transformed by introducing an exogenous polynucleotide by direct uptake, endocytosis, transfection, F-mating or electroporation. Once introduced, the exogenous polynucleotide can be maintained within the cell as a non-integrated vector (such as a plasmid) or integrated into the host cell genome. The polynucleotide so amplified can be isolated from the host cell by methods well known within the art. See, e.g., Sambrook et al., 1989.Alternatively, PCR allows reproduction of DNA sequences. PCR technology is well known in the art and is described in U.S. Patent Nos. 4,683, 195, 4,800,159, 4,754,065 and 4,683,202, as well as PCR: The Polymerase Chain Reaction, Mullis et al. eds., Birkauswer Press, Boston, 1994.RNA can be obtained by using the isolated DNA in an appropriate vector and inserting it into a suitable host cell. When the cell replicates and the DNA is transcribed into RNA, the RNA can then be isolated using methods well known to those of skill in the art, as set forth in Sambrook et al., 1989, supra, for example.Suitable cloning vectors may be constructed according to standard techniques, or may be selected from a large number of cloning vectors available in the art. While the cloning vector selected may vary according to the host cell intended to be used,useful cloning vectors will generally have the ability to self-replicate, may possess a single target for a particular restriction endonuclease, and / or may carry genes for a marker that can be used in selecting clones containing the vector. Suitable examples include plasmids and bacterial viruses, e.g., pUC18, pUC19, Bluescript (e.g., pBS SK+) and its derivatives, mp18, mp19, pBR322, pMB9, ColE1 , pCR1 , RP4, phage DNAs, and shuttle vectors such as pSA3 and pAT28. These and many other cloning vectors are available from commercial vendors such as BioRad, Strategene, and Invitrogen.Expression vectors generally are replicable polynucleotide constructs that contain a polynucleotide according to the invention. It is implied that an expression vector must be replicable in the host cells either as episomes or as an integral part of the chromosomal DNA. Suitable expression vectors include but are not limited to plasmids, viral vectors, including adenoviruses, adeno-associated viruses, retroviruses, cosmids, and expression vector(s) disclosed in PCT Publication No. WO 87 / 04462. Vector components may generally include, but are not limited to, one or more of the following: a signal sequence; an origin of replication; one or more marker genes; suitable transcriptional controlling elements (such as promoters, enhancers and terminator). For expression (i.e., translation), one or more translational controlling elements are also usually required, such as ribosome binding sites, translation initiation sites, and stop codons.The vectors containing the polynucleotides of interest can be introduced into the host cell by any of a number of appropriate means, including electroporation, transfection employing calcium chloride, rubidium chloride, calcium phosphate, DEAE- dextran, or other substances; microprojectile bombardment; lipofection; and infection (e.g., where the vector is an infectious agent such as vaccinia virus). The choice of introducing vectors or polynucleotides will often depend on features of the host cell.The invention also provides host cells comprising any of the polynucleotides described herein. Any host cells capable of over-expressing heterologous DNAs can be used for the purpose of isolating the genes encoding the antibody, polypeptide or protein of interest. Non-limiting examples of mammalian host cells include but not limited to COS, HeLa, and CHO cells. See also PCT Publication No. WO 87 / 04462. Suitable non-mammalian host cells include prokaryotes (such as E. coli or B. subtillis) and yeast (such as S. cerevisae, S. pombe; or K. lactis). Preferably, the host cells express the cDNAs at a level of about 5 fold higher, more preferably, 10 fold higher,even more preferably, 20 fold higher than that of the corresponding endogenous antibody or protein of interest, if present, in the host cells. Screening the host cells for a specific binding to BCMA or an BCMA domain (e.g., domains 1 -4) is effected by an immunoassay or FACS. A cell overexpressing the antibody or protein of interest can be identified.Representative materials of the present invention were deposited in the American Type Culture Collection (ATCC) on April 15, 2015. Vector having ATCC Accession No. PTA-122094 is a polynucleotide encoding a humanized BCMA antibody heavy chain variable region, and vector having ATCC Accession No. PTA-122093 is a polynucleotide encoding a humanized BCMA antibody light chain variable region. The deposits were made under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure and Regulations thereunder (Budapest Treaty). This assures maintenance of a viable culture of the deposit for 30 years from the date of deposit. The deposit will be made available by ATCC under the terms of the Budapest Treaty, and subject to an agreement between Pfizer, Inc. and ATCC, which assures permanent and unrestricted availability of the progeny of the culture of the deposit to the public upon issuance of the pertinent U.S. patent or upon laying open to the public of any U.S. or foreign patent application, whichever comes first, and assures availability of the progeny to one determined by the U.S. Commissioner of Patents and Trademarks to be entitled thereto according to 35 U.S.C. Section 122 and the Commissioner's rules pursuant thereto (including 37 C.F.R. Section 1.14 with particular reference to 886 OG 638).The assignee of the present application has agreed that if a culture of the materials on deposit should die or be lost or destroyed when cultivated under suitable conditions, the materials will be promptly replaced on notification with another of the same. Availability of the deposited material is not to be construed as a license to practice the invention in contravention of the rights granted under the authority of any government in accordance with its patent laws. BCMA Antibody ConjugatesThe present invention also provides a conjugate (or immunoconjugate) of the BCMA antibody as described herein, or of the antigen binding fragment thereof, wherein the antibody or the antigen binding fragment is conjugated to an agent (e.g., acytotoxic agent) for targeted immunotherapy (e.g., antibody-drug conjugates) either directly or indirectly via a linker. For example, a cytotoxic agent can be linked or conjugated to the BCMA antibody or the antigen binding fragment thereof as described herein for targeted local delivery of the cytotoxic agent moiety to tumors (e.g., BCMA expressing tumor).Methods for conjugating cytotoxic agent or other therapeutic agents to antibodies have been described in various publications. For example, chemical modification can be made in the antibodies either through lysine side chain amines or through cysteine sulfhydryl groups activated by reducing interchain disulfide bonds for the conjugation reaction to occur. See, e.g., Tanaka et al., FEBS Letters 579:2092-2096, 2005, and Gentle et al., Bioconjugate Chem. 15:658-663, 2004. Reactive cysteine residues engineered at specific sites of antibodies for specific drug conjugation with defined stoichiometry have also been described. See, e.g., Junutula et al., Nature Biotechnology, 26:925-932, 2008. Conjugation using an acyl donor glutamine- containing tag or an endogenous glutamine made reactive (i.e., the ability to form a covalent bond as an acyl donor) by polypeptide engineering in the presence of transglutaminase and an amine (e.g., a cytotoxic agent comprising or attached to a reactive amine) is also described in international applications WO2012 / 059882 and WO2015015448 .In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag engineered at a specific site of the antibody (e.g., a carboxyl terminus, an amino terminus, or at another site in the BCMA antibody). In some embodiments, the tag comprises an amino acid glutamine (Q) or an amino acid sequence LQG, LLQGG (SEQ ID NO:318), LLQG (SEQ ID NO:454), LSLSQG (SEQ ID NO: 455), GGGLLQGG (SEQ ID NO: 456), GLLQG (SEQ ID NO: 457), LLQ, GSPLAQSHGG (SEQ ID NO: 458), GLLQGGG (SEQ ID NO: 459), GLLQGG (SEQ ID NO: 460), GLLQ (SEQ ID NO: 461 ), LLQLLQGA (SEQ ID NO: 462), LLQGA (SEQ ID NO: 463), LLQYQGA (SEQ ID NO: 464), LLQGSG (SEQ ID NO: 465), LLQYQG (SEQ ID NO: 466), LLQLLQG (SEQ ID NO: 467), SLLQG (SEQ ID NO: 468), LLQLQ (SEQ ID NO: 469), LLQLLQ (SEQ ID NO: 470), LLQGR (SEQ ID NO: 471 ), LLQGPP (SEQ ID NO: 472), LLQGPA (SEQ ID NO: 473), GGLLQGPP (SEQ ID NO: 474), GGLLQGA (SEQ ID NO: 475), LLQGPGK (SEQ ID NO: 476), LLQGPG (SEQ ID NO: 477), LLQGP (SEQ ID NO: 478), LLQP (SEQ ID NO: 479), LLQPGK (SEQ ID NO:480), LLQAPGK (SEQ ID NO: 481 ), LLQGAPG (SEQ ID NO: 482), LLQGAP (SEQ ID NO: 483), and LLQLQG (SEQ ID NO: 484).In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag engineered at a specific site of the antibody, wherein the tag comprises an amino acid sequence GGLLQGPP (SEQ ID NO: 474) or GGLLQGA (SEQ ID NO: 475) engineered at the light chain carboxyl terminus of the BCMA antibody. In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag engineered at a specific site of the antibody, wherein the tag comprises an amino acid sequence LLQG (SEQ ID NO: 454) engineered after residue T135 in the heavy chain of the BCMA antibody. In other embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag engineered at a specific site of the antibody, wherein the tag comprises an amino acid sequence LLQGA (SEQ ID NO: 463) or LLQGPP (SEQ ID NO: 472) engineered at the heavy chain carboxyl terminus of the BCMA antibody and wherein the lysine residue at the heavy chain carboxyl terminus is deleted. In some embodiments, the BCMA antibody or the conjugate as described herein comprises an amino acid substitution at position 297 of the BCMA antibody (EU numbering scheme). For example, the amino acid asparagine (N) can be substituted with glutamine (Q) or alanine (A) at position 297 of the BCMA antibody.Also provided is an isolated antibody comprising an acyl donor glutamine- containing tag and an amino acid modification at position 222, 340, or 370 of the antibody (EU numbering scheme) wherein the modification is an amino acid deletion, insertion, substitution, mutation, or any combination thereof. Accordingly, in some embodiments, provided is the BCMA antibody or the conjugate as described herein comprising the acyl donor glutamine-containing tag (e.g., Q, LQG, LLQGG (SEQ ID NO:318), LLQG (SEQ ID NO:454), LSLSQG (SEQ ID NO: 455), GGGLLQGG (SEQ ID NO: 456), GLLQG (SEQ ID NO: 457), LLQ, GSPLAQSHGG (SEQ ID NO: 458), GLLQGGG (SEQ ID NO: 459), GLLQGG (SEQ ID NO: 460), GLLQ (SEQ ID NO: 461 ), LLQLLQGA (SEQ ID NO: 462), LLQGA (SEQ ID NO: 463), LLQYQGA (SEQ ID NO: 464), LLQGSG (SEQ ID NO: 465), LLQYQG (SEQ ID NO: 466), LLQLLQG (SEQ ID NO: 467), SLLQG (SEQ ID NO: 468), LLQLQ (SEQ ID NO: 469), LLQLLQ (SEQ ID NO: 470), LLQGR (SEQ ID NO: 471 ), LLQGPP (SEQ ID NO: 472), LLQGPA (SEQ ID NO:473), GGLLQGPP (SEQ ID NO: 474), GGLLQGA (SEQ ID NO: 475), LLQGPGK (SEQ ID NO: 476), LLQGPG (SEQ ID NO: 477), LLQGP (SEQ ID NO: 478), LLQP (SEQ ID NO: 479), LLQPGK (SEQ ID NO: 480), LLQAPGK (SEQ ID NO: 481 ), LLQGAPG (SEQ ID NO: 482), LLQGAP (SEQ ID NO: 483), and LLQLQG (SEQ ID NO: 484)) conjugated at a specific site (e.g., at a carboxyl terminus of the heavy or light chain, residue T135 in the antibody heavy chain, or at another site) of the BCMA antibody and an amino acid modification at position 222, 340, or 370 of the antibody (EU numbering scheme). In some embodiments, the amino acid modification is a substitution from lysine to arginine (e.g., K222R, K340R, or K370R).In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence GGLLQGPP (SEQ ID NO: 474) engineered at the C-terminus of the BCMA antibody light chain and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme). In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence GGLLQGA (SEQ ID NO: 475) engineered at the C-terminus of the BCMA antibody light chain and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme). In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence LLQGA (SEQ ID NO: 463) engineered at the C-terminus of the BCMA antibody heavy chain and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme), wherein the lysine residue at the heavy chain carboxyl terminus is deleted. In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence LLQG (SEQ ID NO: 454) engineered after residue T135 in the heavy chain of the BCMA antibody and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme).In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising a glutamine engineered at position 297 or an amino acid substitution at position 297 from asparagine (N) to another amino acid in the BCMA antibody and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme). For example, in someembodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence GGLLQGPP (SEQ ID NO: 474) engineered at the C-terminus of the BCMA antibody light chain, an amino acid substitution at position 297 of the BCMA antibody from asparagine (N) to glutamine (Q), and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme). In some embodiments, the BCMA antibody or the conjugate as described herein comprises an acyl donor glutamine-containing tag comprising the sequence LLQG (SEQ ID NO: 454) engineered after residue T135 in the heavy chain of the BCMA antibody, an amino acid substitution at position 297 of the BCMA antibody from asparagine (N) to alanine (A), and an amino acid substitution from lysine to arginine at position 222 of the antibody (EU numbering scheme).The agents that can be conjugated to the BCMA antibodies or the antigen binding fragments of the present invention include, but are not limited to, cytotoxic agents, immunomodulating agents, imaging agents, therapeutic proteins, biopolymers, or oligonucleotides.Examples of a cytotoxic agent include, but are not limited to, anthracycline, an auristatin, a dolastatin, a combretastatin, a duocarmycin, a pyrrolobenzodiazepine dimer, an indolino-benzodiazepine dimer, an enediyne, a geldanamycin, a maytansine, a puromycin, a taxane, a vinca alkaloid, a camptothecin, a tubulysin, a hemiasterlin, a spliceostatin, a pladienolide, and stereoisomers, isosteres, analogs, or derivatives thereof.The anthracyclines are derived from bacteria Strepomyces and have been used to treat a wide range of cancers, such as leukemias, lymphomas, breast, uterine, ovarian, and lung cancers. Exemplary anthracyclines include, but are not limited to, daunorubicin, doxorubicin (i.e., adriamycin), epirubicin, idarubicin, valrubicin, and mitoxantrone.Dolastatins and their peptidic analogs and derivatives, auristatins, are highly potent antimitotic agents that have been shown to have anticancer and antifungal activity. See, e.g., U.S. Pat. No. 5,663, 149 and Pettit et al., Antimicrob. AgentsChemother. 42:2961-2965, 1998. Exemplary dolastatins and auristatins include, but are not limited to, dolastatin 10, auristatin E, auristatin EB (AEB), auristatin EFP(AEFP), MMAD (Monomethyl Auristatin D or monomethyl dolastatin 10), MMAF(Monomethyl Auristatin F or N-methylvaline-valine-dolaisoleuine-dolaproine-phenylalanine), MMAE (Monomethyl Auristatin E or N-methylvaline-valine- dolaisoleuine-dolaproine-norephedrine), 5-benzoylvaleric acid-AE ester (AEVB), and other novel auristatins (such as the ones described in U.S. Publication No.2013 / 0129753). In some embodiments, the auristatin is 0101 (2-methylalanyl- / V- [(3 4S,5S)-3-methoxy-1-{(2S)-2-[(1 2 )-1 -methoxy-2-methyl-3-oxo-3-{[(1 S)-2- phenyl-1 -(1 ,3-thiazol-2-yl)ethyl]amino}propyl]pyrrolidin-1 -yl}-5-methyl-1 -oxoheptan-4-yl]- / V-methyl-L-valinamide) having the following structure:In some embodiments, the auristatin is 3377 (N,2-dimethylalanyl-N-{(1 S,2R)-4- {(2S)-2-[(1 R,2R)-3-{[(1 S)-1-carboxyl-2-phenylethyl]amino}-1-methoxy-2-methyl-3- oxopropyl]pyrrolidin-1 -yl}-2-methoxy-1-[(1 S)-1 -methylpropyl]-4-oxobutyl}-N-methyl-L- valinamide) having the following structure:In some embodiments, the auristatin is 0131-OMe (N,2-dimethylalanyl-N- [(3R,4S,5S)-3-methoxy-1-{(2S)-2-[(1 R,2R)-1 -methoxy-3-{[(2S)-1 -methoxy-1 -oxo-3- phenylpropan-2-yl]amino}-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}-5-methyl-1-oxoheptan- 4-yl]-N-methylL-valinamide) having the following structure:In other embodiments, the auristatin is 0131 (2-methyl-L-proly-N-[(3R,4S,5S)-1 - {(2S)-2-[(1 R,2R)-3-{[(1 S)-1-carboxy-2-phenylethyl]amino}-1 -methoxy-2-methyl-3- oxopropyl]pyrrolidin-1 -yl}-3-methoxy-5-methyl-1 -oxoheptan-4-yl]-N-methyl-L- valinamide) having the following structure:ln other embodiments, the auristatin is 0121 (2-methyl-L-proly-N-[(3R,4S,5S)-1 - {(2S)-2-[(1 R,2R)-3-{[(2S)-1-methoxy-1-oxo-3-phenylpropan-2-yl]amino}-1-methoxy-2- methyl-3-oxopropyl]pyrrolidin-1 -yl}-3-methoxy-5-methyl-1 -oxoheptan-4-yl]-N-methyl-L- valinamide) having the following structure:Camptothecin is a cytotoxic quinoline alkaloid which inhibits the enzyme topoisomerase I. Examples of camptothecin and its derivatives include, but are not limited to, topotecan and irinotecan, and their metabolites, such as SN-38.Combretastatins are natural phenols with vascular disruption properties in tumors. Exemplary combretastatins and their derivatives include, but are not limited to, combretastatin A-4 (CA-4) and ombrabulin.Duocarmycin and CC-1065 are DNA alkylating agents with cytotoxic potency. See Boger and Johnson, PNAS 92:3642-3649 (1995). Exemplary duocarmycin and CC-1065 include, but are not limited to, (+)-duocarmycin A and (+)-duocarmycin SA, (+)-CC-1065, and the compounds as disclosed in the international application PCT / IB2015 / 050280 including, but not limited to, N~2~-acetyl-L-lysyl-L-valyl-N~5~- carbamoyl-N-[4-({[(2-{[({(1 S)-1 -(chloromethyl)-3-[(5-{[(1 S)-1 -(chloromethyl)-5- (phosphonooxy)-1 ,2-dihydro-3H-benzo[e]indol-3-yl]carbonyl}thiophen-2-yl)carbonyl]- 2,3-di hydro-1 H-benzo[e]indol-5- yl}oxy)carbonyl](methyl)amino}ethyl)(methyl)carbamoyl]oxy}methyl)phenyl]-L- ornithinamide having the structure:N~2~-acetyl-L-lysyl-L-valyl-N~5~-carbamoyl-N-[4-({[(2-{[({(8S)-8-(chloromethyl)-6-[(3- {[(1 S)-1 -(chloromethyl)-8-methyl-5-(phosphonooxy)-1 ,6-dihydropyrrolo[3,2-e]indol- 3(2H)-yl]carbonyl}bicyclo[1.1.1 ]p ent-1 -yl)carbonyl]-1 -methyl-3,6,7,8- tetrahydropyrrolo[3,2-e]indol-4- yl}oxy)carbonyl](methyl)amino}ethyl)(methyl)carbamoyl]oxy}methyl)phenyl]-L- ornithinamide having the structure:N~2~-acetyl-L-lysyl-L-valyl-N~5~-carbamoyl-N-[4-({[(2-{[({(8S)-8-(chloromethyl)-6-[(4- {[(1 S)-1 -(chloromethyl)-8-methyl-5-(phosphonooxy)-1 ,6-dihydropyrrolo[3,2-e]indol- 3(2H)-yl]carbonyl}pentacyclo[4.2.0.0-2, 5~.0~3,8~.0~4,7~]oct-1-yl)carbonyl]-1-methyl- 3,6,7, 8-tetrahydropyrrolo[3,2-e]indol-4- yl}oxy)carbonyl](methyl)amino}ethyl)(methyl)carbamoyl]oxy}methyl)phenyl]-L- ornithinamide having the structure:Enediynes are a class of anti-tumor bacterial products characterized by either nine- and ten-membered rings or the presence of a cyclic system of conjugated triple- double-triple bonds. Exemplary enediynes include, but are not limited to, calicheamicin, esperamicin, uncialamicin, dynemicin, and their derivatives.Geldanamycins are benzoquinone ansamycin antibiotic that bind to Hsp90 (Heat Shock Protein 90) and have been used antitumor drugs. Exemplary geldanamycins include, but are not limited to, 17-AAG (17-N-Allylamino-17-Demethoxygeldanamycin) and 17-DMAG (17-Dimethylaminoethylamino-17-demethoxygeldanamycin).Hemiasterlin and its analogues (e.g., HTI-286) bind to the tubulin, disrupt normal microtubule dynamics, and, at stoichiometric amounts, depolymerize microtubules.Maytansines or their derivatives maytansinoids inhibit cell proliferation by inhibiting the microtubules formation during mitosis through inhibition of polymerization of tubulin. See Remillard et al., Science 189: 1002-1005, 1975. Exemplary maytansines and maytansinoids include, but are not limited to, mertansine (DM1 ) and its derivatives as well as ansamitocin.Pyrrolobenzodiazepine dimers (PBDs) and indolino-benzodiazepine dimers (IGNs) are anti-tumor agents that contain one or more immine functional groups, or their equivalents, that bind to duplex DNA. PBD and IGN molecules are based on the natural product athramycin, and interact with DNA in a sequence-selective manner, with a preference for purine-guanine-purine sequences. Exemplary PBDs and their analogs include, but are not limited to, SJG-136.Spliceostatins and pladienolides are anti-tumor compounds which inhibit splicing and interacts with spliceosome, SF3b. Examples of spliceostatins include, but are not limited to, spliceostatin A, FR901464, and (2S,3Z)-5-{[(2R,3R,5S,6S)-6-{(2E,4E)-5- [(3R,4R,5R,7S)-7-(2-hydrazinyl-2-oxoethyl)-4-hydroxy-1 ,6-dioxaspiro[2.5]oct-5-yl]-3- methylpenta-2,4-dien-1 -yl}-2,5-dimethyltetrahydro-2H-pyran-3-yl]amino}-5-oxopent-3- en-2-yl acetate having the structure ofExamples of pladienolides include, but are not limited to, Pladienolide B, Pladienolide D, or E7107.Taxanes are diterpenes that act as anti-tubulin agents or mitotic inhibitors. Exemplary taxanes include, but are not limited to, paclitaxel (e.g., TAXOL®) and docetaxel (TAXOTERE®).Tubulysins are natural products isolated from a strain of myxobacteria that has been shown to depolymerize microtubules and induce mitotic arrest. Exemplary tubulysins include, but are not limited to, tubulysin A, tubulysin B, and tubulysin D.Vinca alkyloids are also anti-tubulin agents. Exemplary vinca alkyloids include, but are not limited to, vincristine, vinblastine, vindesine, and vinorelbine.Accordingly, in some embodiments, the cytotoxic agent is selected from the group consisting of MMAD (Monomethyl Auristatin D), 0101 (2-methylalanyl- / V- [(3 4S,5S)-3-methoxy-1-{(2S)-2-[(1 2 )-1 -methoxy-2-methyl-3-oxo-3-{[(1 S)-2- phenyl-1 -(1 ,3-thiazol-2-yl)ethyl]amino}propyl]pyrrolidin-1 -yl}-5-methyl-1 -oxoheptan-4-yl]- / V-methyl-L-valinamide), 3377 (N,2-dimethylalanyl-N-{(1 S,2R)-4-{(2S)-2-[(1 R,2R)-3- {[(1 S)-1 -carboxyl-2-phenylethyl]amino}-1 -methoxy-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}- 2-methoxy-1 -[(1 S)-1 -methylpropyl]-4-oxobutyl}-N-methyl-L-valinamide), 0131 (2-methyl- L-proly-N-[(3R,4S,5S)-1 -{(2S)-2-[(1 R,2R)-3-{[(1 S)-1-carboxy-2-phenylethyl]amino}-1 - methoxy-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}-3-methoxy-5-methyl-1 -oxoheptan-4-yl]-N- methyl-L-valinamide), 0131 -OMe (N,2-dimethylalanyl-N-[(3R,4S,5S)-3-methoxy-1-{(2S)-2- [(1 R,2R)-1 -methoxy-3-{[(2S)-1 -methoxy-1 -oxo-3-phenylpropan-2-yl]amino}-2-methyl-3- oxopropyl]pyrrolidin-1-yl}-5-methyl-1 -oxoheptan-4-yl]-N-methylL-valinamide), 0121 (2- methyl-L-proly-N-[(3R,4S,5S)-1-{(2S)-2-[(1 R,2R)-3-{[(2S)-1 -methoxy-1 -oxo-3- phenylpropan-2-yl]amino}-1 -methoxy-2-methyl-3-oxopropyl]pyrrolidin-1 -yl}-3-methoxy-5-methyl-1 -oxoheptan-4-yl]-N-methyl-L-valinamide), and (2S,3Z)-5-{[(2R,3R,5S,6S)-6- {(2E,4E)-5-[(3R,4R,5R,7S)-7-(2-hydrazinyl-2-oxoethyl)-4-hydroxy-1 ,6- dioxaspiro[2.5]oct-5-yl]-3-methylpenta-2,4-dien-1 -yl}-2,5-dimethyltetrahydro-2H-pyran- 3-yl]amino}-5-oxopent-3-en-2-yl acetate.In some embodiments, the agent is an immunomodulating agent. Examples of an immunomodulating agent include, but are not limited to, gancyclovier, etanercept, tacrolimus, sirolimus, voclosporin, cyclosporine, rapamycin, cyclophosphamide, azathioprine, mycophenolgate mofetil, methotrextrate, glucocorticoid and its analogs, cytokines, stem cell growth factors, lymphotoxins, tumor necrosis factor (TNF), hematopoietic factors, interleukins (e.g., interleukin-1 (IL-1 ), IL-2, IL-3, IL-6, IL-10, IL-12, IL-18, and IL-21 ), colony stimulating factors (e.g., granulocyte-colony stimulating factor (G-CSF) and granulocyte macrophage-colony stimulating factor (GM-CSF)), interferons (e.g., interferons-a, -β and -γ), the stem cell growth factor designated "S 1 factor," erythropoietin and thrombopoietin, or a combination thereof.In some embodiments, the agent moiety is an imaging agent (e.g., a fluorophore or a chelator), such as fluorescein, rhodamine, lanthanide phosphors, and their derivatives thereof, or a radioisotope bound to a chelator. Examples of fluorophores include, but are not limited to, fluorescein isothiocyanate (FITC) (e.g., 5-FITC), fluorescein amidite (FAM) (e.g., 5-FAM), eosin, carboxyfluorescein, erythrosine, Alexa Fluor®(e.g., Alexa 350, 405, 430, 488, 500, 514, 532, 546, 555, 568, 594, 610, 633, 647, 660, 680, 700, or 750), carboxytetramethylrhodamine (TAMRA) (e.g., 5,-TAMRA), tetramethylrhodamine (TMR), and sulforhodamine (SR) (e.g., SR101 ). Examples of chelators include, but are not limited to, 1 ,4,7, 10-tetraazacyclododecane-N,N',N",N"'- tetraacetic acid (DOTA), 1 ,4,7-triazacyclononane-1 ,4,7-triacetic acid (NOTA), 1 ,4,7- triazacyclononane, 1 -glutaric acid-4,7-acetic acid (deferoxamine), diethylenetriaminepentaacetic acid (DTPA), and 1 ,2-bis(o-aminophenoxy)ethane- Ν,Ν,Ν',Ν'-tetraacetic acid) (BAPTA).Examples of fluorophores include, but are not limited to, fluorescein isothiocyanate (FITC) (e.g., 5-FITC), fluorescein amidite (FAM) (e.g., 5-FAM), eosin, carboxyfluorescein, erythrosine, Alexa Fluor®(e.g., Alexa 350, 405, 430, 488, 500, 514, 532, 546, 555, 568, 594, 610, 633, 647, 660, 680, 700, or 750), carboxytetramethylrhodamine (TAMRA) (e.g., 5,-TAMRA), tetramethylrhodamine (TMR), and sulforhodamine (SR) (e.g., SR101 ).ln some embodiments, therapeutic or diagnostic radioisotopes or other labels (e.g., PET or SPECT labels) can be incorporated in the agent for conjugation to the BCMA antibodies or the antigen binding fragments as described herein. Examples of a radioisotope or other labels include, but are not limited to,3H, C,3N,4C,5N,50,35S,8F,32P,33P,47Sc,5Cr,57Co,58Co,59Fe,62Cu,64Cu,67Cu,67Ga,68Ga,75Se,76Br,77Br,86Y,89Zr,90Y,94Tc,95Ru,97Ru,99Tc,03Ru,05Rh,05Ru,07Hg,09Pd, Ag, ln,113ln,121Te,122Te,123l,124l,125l,125Te,126l,131l,131ln,133l,142Pr,143Pr,153Pb,153Sm, 6 Tb,65Tm,66Dy,66H,67Tm,68Tm,69Yb,77Lu,86Re,88Re,89Re,97Pt,98Au,199Au,201TI,203Hg,211At,212Bi,212Pb,213Bi,223Ra,224Ac, or225Ac.In some embodiments, the agent is a therapeutic protein including, but is not limited to, a toxin, a hormone, an enzyme, and a growth factor.Examples of a toxin protein (or polypeptide) include, but are not limited to, dipththeria (e.g., diphtheria A chain), Pseudomonas exotoxin and endotoxin, ricin (e.g., ricin A chain), abrin (e.g., abrin A chain), modeccin (e.g., modeccin A chain), alpha- sarcin, Aleurites fordii proteins, dianthin proteins, ribonuclease (RNase), DNase I, Staphylococcal enterotoxin-A, pokeweed antiviral protein, gelonin, diphtherin toxin, Phytolaca americana proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, mitogellin, restrictocin, phenomycin, enomycin, tricothecenes, inhibitor cystine knot (ICK) peptides (e.g., ceratotoxins), and conotoxin (e.g., KIIIA or Smllla).In some embodiments, the agent is a biocompatible polymer. The BCMA antibodies or the antigen binding fragments as described herein can be conjugated to the biocompatible polymer to increase serum half-life and bioactivity, and / or to extend in vivo half-lives. Examples of biocompatible polymers include water-soluble polymer, such as polyethylene glycol (PEG) or its derivatives thereof and zwitterion-containing biocompatible polymers (e.g., a phosphorylcholine containing polymer).In some embodiments, the agent is an oligonucleotide, such as anti-sense oligonucleotides.In another aspect, the invention provides a conjugate of the antibody or the antigen binding fragment as described herein, wherein the conjugate comprises the formula: antibody-(acyl donor glutamine-containing tag)-(linker)-(cytotoxic agent), wherein the acyl donor glutamine-containing tag is engineered at a specific site of the antibody or the antigen binding fragment (e.g., at a carboxyl terminus of the heavy orlight chain, after residue T135 in the antibody heavy chain, or at an another site), wherein the tag is conjugated to a linker (e.g., a linker containing one or more reactive amines (e.g., primary amine NH2)), and wherein the linker is conjugated to a cytotoxic agent (e.g. , MMAD or other auristatins such as 0101 , 0131 , or 3377).Examples of a linker containing one or more reactive amines include, but are not limited to, Ac-Lys-Gly (acetyl-lysine-glycine), aminocaproic acid, Ac-Lys-p-Ala (acetyl- lysine-p-alanine), amino-PEG2 (polyethylene glycol)-C2, amino-PEG3-C2, amino- PEG6-C2 (or amino PEG6-propionyl), Ac-Lys-Val-Cit-PABC (acetyl-lysine-valine- citrulline-p-aminobenzyloxycarbonyl), amino-PEG6-C2-Val-Cit-PABC, aminocaproyl- Val-Cit-PABC, [(3R,5R)-1 -{3-[2-(2-aminoethoxy)ethoxy]propanoyl}piperidine-3,5- diyl]bis-Val-Cit-PABC, [(3S,5S)-1 -{3-[2-(2-aminoethoxy)ethoxy]propanoyl}piperidine-3,5- diyl]bis-Val-Cit-PABC, putrescine, or Ac-Lys-putrescine.In some embodiments, the conjugate is 1 ) antibody-GGLLQGPP (SEQ ID NO: 474)- AcLys-VC-PABC-0101 ; 2) antibody-AcLys-VC-PABC-0101 and comprises N297Q; 3) antibody-GGLLQGPP (SEQ ID NO: 474)-AcLys-VC-PABC-0101 and comprises N297Q; 4) antibody-LLQG (SEQ ID NO: 454)-amino-PEG6-C2-0131 and comprises N297A; 5) antibody-LLQG (SEQ ID NO: 454)-amino-PEG6-C2-3377 and comprises N297A; 6) antibody-GGLLQGA (SEQ ID NO: 475)-AcLys-VC-PABC-0101. In some embodiments, the acyl donor glutamine-containing tag comprising, e.g., GGLLQGPP (SEQ ID NO: 474) or GGLLQGA (SEQ ID NO: 475), is engineered at the C-terminus of the light chain of the antibody. In other embodiments, the acyl donor glutamine-containing tag (e.g., LLQGA (SEQ ID NO: 463) or LLQGPP (SEQ ID NO: 472)) is engineered at the C-terminus of the heavy chain of the antibody, wherein the lysine residue at the C-terminus is deleted. In some embodiments, the acyl donor glutamine-containing tag comprising, e.g., LLQG (SEQ ID NO: 454) is engineered after residue T135 in the antibody heavy chain or replaces amino acid residues E294-N297 in the antibody heavy chain. Examples of the antibody include, but are not limited to, P6E01 / P6E01 , P6E01 / H3.AQ, L1.LGF / L3.KW / P6E01 ; L1.LGF / L3.NY / P6E01 , L1.GDF / L3.NY / P6E01 , L1.LGF / L3.KW / H3.AL, L1.LGF / L3.KW / H3.AP, L1.LGF / L3.KW / H3.AQ, L1.LGF / L3.PY / H3.AP, L1. LGF / L3. PY / H3.AQ,L1.LGF / L3.NY / H3.AL, L1.LGF / L3.NY / H3.AP, L1.LGF / L3.NY / H3.AQ,L1.GDF / L3.KW / H3.AL, L1.GDF / L3.KW / H3.AP, L1.GDF / L3.KW / H3.AQ,L1.GDF / L3.PY / H3.AQ, L1.GDF / L3.NY / H3.AL, L1.GDF / L3.NY / H3.AP,L1.GDF / L3.NY / H3.AQ, L3.KW / P6E01 , L3.PY / P6E01 , L3.NY / P6E01 ,L3.PY / L1.PS / P6E01 , L3.PY / L1.AH / P6E01 , L3.PY / L1.FF / P6E01 , L3.PY / L1.PH / P6E01 , L3.PY / L3.KY / P6E01 , L3.PY / L3.KF / P6E01 , L3.PY / H2.QR, L3.PY / H2.DY, L3.PY / H2.YQ, L3.PY / H2.LT, L3.PY / H2.HA, L3.PY / H2.QL, L3.PY / H3.YA, L3.PY / H3.AE, L3.PY / H3.AQ, L3.PY / H3.TAQ, L3.PY / P6E01 , L3.PY / L1.PS / H2.QR, L3.PY / L1.PS / H2.DY, L3.PY / L1.PS / H2.YQ, L3.PY / L1.PS / H2.LT, L3.PY / L1.PS / H2.HA, L3.PY / L1.PS / H2.QL, L3.PY / L1.PS / H3.YA, L3.PY / L1.PS / H3.AE, L3.PY / L1.PS / H3.AQ, L3.PY / L1.PS / H3.TAQ, L3.PY / L1.AH / H2.QR, L3.PY / L1.AH / H2.DY, L3.PY / L1.AH / H2.YQ, L3.PY / L1.AH / H2.LT, L3.PY / L1.AH / H2.HA, L3.PY / L1.AH / H2.QL, L3.PY / L1.ΑΗ / Η3.ΥΑ, L3.PY / L1.ΑΗ / Η3.ΑΕ, L3.PY / L1.AH / H3.AQ, L3.PY / L1.AH / H3.TAQ, L3.PY / L1.FF / H2.QR, L3.PY / L1.FF / H2.DY, L3.PY / L1.FF / H2.YQ, L3.PY / L1.FF / H2.LT, L3.PY / L1.FF / H2.HA, L3.PY / L1.FF / H2.QL, L3.PY / L1.FF / H3.YA, L3.PY / L1.FF / H3.AE, L3.PY / L1.FF / H3.AQ, L3.PY / L1.FF / H3.TAQ, L3.PY / L1.PH / H2.QR, L3.PY / L1.ΡΗ / Η2.ΗΑ, L3.PY / L1.ΡΗ / Η3.ΑΕ, L3.PY / L1.PH / H3.AQ, L3.PY / L1.PH / H3.TAQ, L3.PY / L3.KY / H2.QR, L3. PY / L3. ΚΥ / Η2. DY, L3.PY / L3.KY / H2.YQ L3.PY / L3.KY / H2.LT, L3.PY / L3.KY / H2.HA, L3.PY / L3.KY / H2.QL, L3.PY / L3.KY / H3.YA L3.PY / L3.KY / H3.TAQ, L3. PY / L3. KF / H 2. D Y, L3. PY / L3. KF / H2. YQ, L3.PY / L3.KF / H2.LT L3.PY / L3.KF / H2.QL, L3. PY / L3. KF / H3. YA, L3. PY / L3. KF / H3. AE, L3. PY / L3. KF / H3. AQ L3.PY / L3.KF / H3.TAQ, P5A2_VHVL, A02_Rd4_0.6nM_C06, A02_Rd4_0.6nM_C09 A02_Rd4_6nM_C16, A02_Rd4_6nM_C03, A02_Rd4_6nM_C01 , A02_Rd4_6nM_C26 A02_Rd4_6nM_C25, A02_Rd4_6nM_C22, A02_Rd4_6nM_C19, A02_Rd4_0.6nM_C03 A02_Rd4_6nM_C07, A02_Rd4_6nM_C23, A02_Rd4_0.6nM_C18, A02_Rd4_6nM_C10 A02_Rd4_6nM_C05, A02_Rd4_0.6nM_C10, A02_Rd4_6nM_C04,A02_Rd4_0.6nM_C26A02_Rd4_0.6nM_C13, A02_Rd4_0.6nM_C01 , A02_Rd4_6nM_C08, P5C1_VHVL, C01_Rd4_6nM_C24, C01_Rd4_6nM_C26, C01_Rd4_6nM_C10,C01_Rd4_0.6nM_C27C01_Rd4_6nM_C20, C01_Rd4_6nM_C12, C01_Rd4_0.6nM_C16,C01_Rd4_0.6nM_C09C01_Rd4_6nM_C09, C01_Rd4_0.6nM_C03, C01_Rd4_0.6nM_C06,C01_Rd4_6nM_C04COMBO_Rd4_0.6nM_C22, COMBO_Rd4_6nM_C21 , COMBO_Rd4_6nM_C10, COMBO_Rd4_0.6nM_C04, COMBO_Rd4_6nM_C25, COMBO_Rd4_0.6nM_C21 ,COMBO_Rd4_6nM_C1 1 , COMBO_Rd4_0.6nM_C20, COMBO_Rd4_6nM_C09, COMBO_Rd4_6nM_C08, COMBO_Rd4_0.6nM_C19, COMBO_Rd4_0.6nM_C02, COMBO_Rd4_0.6nM_C23, COMBO_Rd4_0.6nM_C29, COMBO_Rd4_0.6nM_C09, COMBO_Rd4_6nM_C12, COMBO_Rd4_0.6nM_C30, COMBO_Rd4_0.6nM_C14, COMBO_Rd4_6nM_C07, COMBO_Rd4_6nM_C02, COMBO_Rd4_0.6nM_C05, COMBO_Rd4_0.6nM_C17, COMBO_Rd4_6nM_C22, COMBO_Rd4_0.6nM_C1 1 , COMBO_Rd4_0.6nM_C29, P4G4, or P1A1 1.In one variation, the conjugate further comprises an amino acid substitution from lysine to arginine at position 222. Accordingly, for example, the conjugate is 1 ) antibody-GGLLQGPP (SEQ ID NO: 474)- AcLys-VC-PABC-0101 and comprises K222R; 2) antibody-AcLys-VC-PABC-0101 and comprises N297Q and K222R; 3) antibody- GGLLQGPP (SEQ ID NO: 474)-AcLys-VC-PABC-0101 and comprises N297Q and K222R; 4) antibody-LLQG (SEQ ID NO: 454)-amino-PEG6-C2-0131 and comprises N297A and K222R; 5) antibody-LLQG (SEQ ID NO: 454)-amino-PEG6-C2- 3377 and comprises N297A and K222R; and 6) antibody-GGLLQGA (SEQ ID NO: 475)-AcLys-VC-PABC-0101 and comprises K222R. In some embodiments, the acyl donor glutamine-containing tag comprising, e.g., GGLLQGPP (SEQ ID NO: 474) or GGLLQGA (SEQ ID NO: 475) is engineered at the C-terminus of the light chain of the antibody. In other embodiments, the acyl donor glutamine-containing tag (e.g., LLQGA (SEQ ID NO: 473) or LLQGPP (SEQ ID NO: 472)) is engineered at the C-terminus of the heavy chain of the antibody, wherein the lysine residue at the C-terminus is deleted. In some embodiments, the acyl donor glutamine-containing tag comprising, e.g., LLQG (SEQ ID NO: 454) is engineered after residue T135 in the antibody heavy chain or replaces amino acid residues E294-N297 in the antibody heavy chain. Examples of the antibody include, but are not limited to, P6E01 / P6E01 , P6E01 / H3.AQ, L1.LGF / L3.KW / P6E01 ; L1.LGF / L3.NY / P6E01 , L1.GDF / L3.NY / P6E01 ,L1.LGF / L3.KW / H3.AL, L1.LGF / L3.KW / H3.AP, L1.LGF / L3.KW / H3.AQ,L1.LGF / L3.PY / H3.AP, L1.LGF / L3.PY / H3.AQ, L1.LGF / L3.NY / H3.AL,L1.LGF / L3.NY / H3.AP, L1.LGF / L3.NY / H3.AQ, L1.GDF / L3.KW / H3.AL, L1.GDF / L3.KW / H3.AP, L1.GDF / L3.KW / H3.AQ, L1.GDF / L3.PY / H3.AQ,L1.GDF / L3.NY / H3.AL, L1.GDF / L3.NY / H3.AP, L1.GDF / L3.NY / H3.AQ, L3.KW / P6E01 , L3.PY / P6E01 , L3.NY / P6E01 ,L3.PY / L1.PS / P6E01 , L3.PY / L1.AH / P6E01 , L3.PY / L1.FF / P6E01 , L3.PY / L1.PH / P6E01 , L3.PY / L3.KY / P6E01 , L3.PY / L3.KF / P6E01 , L3.PY / H2.QR, L3.PY / H2.DY, L3.PY / H2.YQ, L3.PY / H2.LT, L3.PY / H2.HA, L3.PY / H2.QL, L3.PY / H3.YA, L3.PY / H3.AE, L3.PY / H3.AQ, L3.PY / H3.TAQ, L3.PY / P6E01 , L3.PY / L1.PS / H2.QR, L3.PY / L1.PS / H2.DY, L3.PY / L1.PS / H2.YQ, L3.PY / L1.PS / H2.LT, L3.PY / L1.PS / H2.HA, L3.PY / L1.PS / H2.QL, L3.PY / L1.PS / H3.YA, L3.PY / L1.PS / H3.AE, L3.PY / L1.PS / H3.AQ, L3.PY / L1.PS / H3.TAQ, L3.PY / L1.AH / H2.QR, L3.PY / L1.AH / H2.DY, L3.PY / L1.AH / H2.YQ, L3.PY / L1.AH / H2.LT, L3.PY / L1.AH / H2.HA, L3.PY / L1.AH / H2.QL, L3.PY / L1.ΑΗ / Η3.ΥΑ, L3.PY / L1.ΑΗ / Η3.ΑΕ, L3.PY / L1.AH / H3.AQ, L3.PY / L1.AH / H3.TAQ, L3.PY / L1.FF / H2.QR, L3.PY / L1.FF / H2.DY, L3.PY / L1.FF / H2.YQ, L3.PY / L1.FF / H2.LT, L3.PY / L1.FF / H2.HA, L3.PY / L1.FF / H2.QL, L3.PY / L1.FF / H3.YA, L3.PY / L1.FF / H3.AE, L3.PY / L1.FF / H3.AQ, L3.PY / L1.FF / H3.TAQ, L3.PY / L1.PH / H2.QR, L3.PY / L1.ΡΗ / Η2.ΗΑ, L3.PY / L1.ΡΗ / Η3.ΑΕ, L3.PY / L1.PH / H3.AQ, L3.PY / L1.PH / H3.TAQ, L3.PY / L3.KY / H2.QR, L3. PY / L3. ΚΥ / Η2. DY, L3.PY / L3.KY / H2.YQ L3.PY / L3.KY / H2.LT, L3.PY / L3.KY / H2.HA, L3.PY / L3.KY / H2.QL, L3.PY / L3.KY / H3.YA L3.PY / L3.KY / H3.TAQ, L3. PY / L3. KF / H 2. D Y, L3. PY / L3. KF / H2. YQ, L3.PY / L3.KF / H2.LT L3.PY / L3.KF / H2.QL, L3. PY / L3. KF / H3. YA, L3. PY / L3. KF / H3. AE, L3. PY / L3. KF / H3. AQ L3.PY / L3.KF / H3.TAQ, P5A2_VHVL, A02_Rd4_0.6nM_C06, A02_Rd4_0.6nM_C09 A02_Rd4_6nM_C16, A02_Rd4_6nM_C03, A02_Rd4_6nM_C01 , A02_Rd4_6nM_C26 A02_Rd4_6nM_C25, A02_Rd4_6nM_C22, A02_Rd4_6nM_C19, A02_Rd4_0.6nM_C03 A02_Rd4_6nM_C07, A02_Rd4_6nM_C23, A02_Rd4_0.6nM_C18, A02_Rd4_6nM_C10 A02_Rd4_6nM_C05, A02_Rd4_0.6nM_C10, A02_Rd4_6nM_C04,A02_Rd4_0.6nM_C26A02_Rd4_0.6nM_C13, A02_Rd4_0.6nM_C01 , A02_Rd4_6nM_C08, P5C1_VHVL, C01_Rd4_6nM_C24, C01_Rd4_6nM_C26, C01_Rd4_6nM_C10, C01_Rd4_0.6nM_C27C01_Rd4_6nM_C20, C01_Rd4_6nM_C12, C01_Rd4_0.6nM_C16,C01_Rd4_0.6nM_C09C01_Rd4_6nM_C09, C01_Rd4_0.6nM_C03, C01_Rd4_0.6nM_C06,C01_Rd4_6nM_C04COMBO_Rd4_0.6nM_C22, COMBO_Rd4_6nM_C21 , COMBO_Rd4_6nM_C10,COMBO_Rd4_0.6nM_C04, COMBO_Rd4_6nM_C25, COMBO_Rd4_0.6nM_C21 , COMBO_Rd4_6nM_C1 1 , COMBO_Rd4_0.6nM_C20, COMBO_Rd4_6nM_C09, COMBO_Rd4_6nM_C08, COMBO_Rd4_0.6nM_C19, COMBO_Rd4_0.6nM_C02,COMBO_Rd4_0.6nM_C23, COMBO_Rd4_0.6nM_C29, COMBO_Rd4_0.6nM_C09,COMBO_Rd4_6nM_C12, COMBO_Rd4_0.6nM_C30, COMBO_Rd4_0.6nM_C14,COMBO_Rd4_6nM_C07, COMBO_Rd4_6nM_C02, COMBO_Rd4_0.6nM_C05,COMBO_Rd4_0.6nM_C17, COMBO_Rd4_6nM_C22, COMBO_Rd4_0.6nM_C1 1 , COMBO_Rd4_0.6nM_C29, or P4G4, or P1 A1 1 .CD3 Antibodies and Methods of Making ThereofThe present invention further provides an antibody that binds to CD3 (e.g., human CD3 (SEQ ID NO: 502; or accession number: NM_000733.3).In one aspect, provided is an isolated antibody, or an antigen binding fragment thereof, which specifically binds to CD3, wherein the antibody comprises a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399.In another aspect, provided is an isolated antibody, or an antigen binding fragment thereof, which specifically binds to CD3, wherein the VH region comprises (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 414, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453.In some embodiments, provided is an antibody having any one of partial light chain sequence as listed in Table 3 and / or any one of partial heavy chain sequence as listed in Table 3.Table 3mAb Light Chain Heavy Chainh2B4 DIVMTQSPDSLAVSLGERATINCT EVQLVESGGGLVQPGGSLRLSCASSQSLFNVRSRKNYLAWYQQKP ASGFTFSDYYMTWVRQAPGKGLEGQPPKLLISWASTRESGVPDRFS WVAFIRNRARGYTSDHNASVKGRGSGSGTDFTLTISSLQAEDVAVY FTISRDNAKNSLYLQMNSLRAEDT YCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 319) VTVSS(SEQ ID NO: 320)h2B4- DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCA VH-wt KSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLE VL_TK PGQPPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDHNASVKGRSGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDT YYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 321 ) VTVSS(SEQ ID NO: 322)h2B4- DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCAKSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLE VH-PGQPPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDHNPSVKGRhnps SGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDTYYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT VL_TK(SEQ ID NO: 323) VTVSS(SEQ ID NO: 324)h2B4- DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCAKSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLE VH-PGQPPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDYAESVKGRyaes SGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDTYYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT VL_TKVTVSS(SEQ ID NO: 325) (SEQ ID NO: 326)h2B4- DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCAKSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLE VH-PGQPPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDYADSVKGRyads SGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDTYYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT VL_TK(SEQ ID NO: 327) VTVSS(SEQ ID NO: 328)h2B4- DIVMTQSPDSLAVSLGERATINCT EVQLVESGGGLVQPGGSLRLSCASSQSLFNVRSRKNYLAWYQQKP ASGFTFSDYYMTWVRQAPGKGLE VH-GQPPKLLISWASTRESGVPDRFS WVAFIRNRARGYTSDYAPSVKGRyaps GSGSGTDFTLTISSLQAEDVAVY FTISRDNAKNSLYLQMNSLRAEDTYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT VL_TK(SEQ ID NO: 329) VTVSS(SEQ ID NO: 330)h2B4-DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCA VH- KSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLEPGQPPKLLIYWASTRESGVPDRF WVAFIRNRARGYTSDHNPSVKGRmAb Light Chain Heavy Chainhnps SGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDTYYCKQSYDLFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTTVL TK(SEQ ID NO: 344) VTVSS (SEQ ID NO: 345) -S55Yh2B4-DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCA VH- KSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLEPGQPPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDHNPSVKGRhnps SGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDT VL_TK YYCKQSYDLFTFGQGTKLEIK AVYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 346) VTVSS (SEQ ID NO: 347)S105Qh2B4-DIVMTQSPDSLAVSLGERATINC EVQLVESGGGLVQPGGSLRLSCA VH- KSSQSLFNVRSRKNYLAWYQQK ASGFTFSDYYMTWVRQAPGKGLEPGQPPKLLIYWASTRESGVPDRF WVAFIRNRARGYTSDHNPSVKGRhnpsSGSGSGTDFTLTISSLQAEDVAV FTISRDNAKNSLYLQMNSLRAEDT VL_TK YYCKQSYDLFTFGQGTKLEIK AVYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 348) VTVSS (SEQ ID NO: 349)S55Y / S105Q2B4DIVMSQSPPSLAVSVGDKVTMSC EVKLVESGGGLVQPGGSLRLSCA TSSQSLFNSRSRKNYLAWYQQK TFGFTFTDYYMTWVRQPPGKALESGQSPKLLISWASTRESGVPDRF WVAFIRNRARGYTSDHNASVKGRTGSGSGTDFTLTISSVQAEDLAV FTISRDNSQNILYLQMNTLRAEDS YYCKQSYDLFTFGSGTKLEIK ATYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 350) VTVSS (SEQ ID NO: 351 )h2B4-DIVMTQSPDSLAVSLGERATINCT EVQLVESGGGLVQPGGSLRLSCA1 1 SSQSLFNSRSRKNYLAWYQQKP ASGFTFSDYYMTWVRQAPGKGLEGQPPKLLISWASTRESGVPDRFS WVAFIRNRARGYTSDHNASVKGRGSGSGTDFTLTISSLQAEDVAVY FTISRDNAKNSLYLQMNSLRAEDT YCQQSYDTFTFGSGTKLEIK AVYYCARDRPSYYVLDYWGQGTT(SEQ ID NO: 445) VTVSS (SEQ ID NO: 444)1 C10DIVMSQSPSSLAVSAGEKVTMSC QVQLQQPGSELVRPGASVILSCKA KSSQSLLNSRTRKNYLAWYQQK SGYTFTSYWMHWVRQRPGQGLEPGQSPKLLIYWASTRESGVPDRF WIGNIYSGGDTINYDEKFKNKAILTTGSGSGTDFTLTIDSVQPEDLAV VDTSSSTAYMHLSSLTSEDSAVYY YYCTQSFILRTFGGGTKLEIK CTR D ATS RYF FD YWG Q GTTVTVS(SEQ ID NO: 352) S (SEQ ID NO: 354)1A4DIVMSQSPSSLAVSAGEKVTMSC QVQLQQSGPDLVKPGASVEISCK KSSQSLLNSRTRKNYLAWYQQK ASGYSFTTYYLHWVRQRPGQGLEPGQSPKLLIYWASTRASGVPDRF WIGWIFPGSDNTKYNEKFKGKATLmAb Light Chain Heavy ChainTGSGSGTDFTLTISSVQAEDLAIY TADTSSSTAYMQLSSLTSEDSAVY YCKQSFILRTFGGGTKLEIK (SEQ FCARNRDYYFDYWGQGTTVTVSS ID NO: 355) (SEQ ID NO: 356)7A3DIVVSQSPSSLAVSAGEKVIMSC EVQLQQSGAELVRPGALVKLSCK KSSQSLLNSRTRKNYLAWYQLK GSGFNIKDYYIHWVKQRPEQGLEPGQSPKLLIYSASTRESGVPDRF WIGWIDPENGNNKYDPKFQGKASITGSGSGTDFTLTISSVQTEDLAV TADTSSNIAYLQLSSLTSEDTAVYY YYCMQSFTLRTFGGGTKLEIK CARNDNYAFDYWGQGTTVTVSS(SEQ ID NO: 443) (SEQ ID NO: 442 )25A8 QAVVTQESALTTSPGEAVTLTCR EVQLVESGGGLVRPEGSLRLSCASSTGAVTTSNYANWVQEKPDHL ASGFTFNTYAMNWVRQAPGKGLE FTGLIGGTNTRAPGVPARFSGSLI WVG R I RSKI N N YATYYAESVKG R FGDKAALTITGAQTEDEAIYFCVL TLSRDDSLSMVYLQMNSLKNEDT WYNNYWVFGGGTKLTVL (SEQ AMYYCVRHETLRSGISWFASWGQID NO: 377) GTLVTVSS (SEQ ID NO: 378)16G7Q A VVTQ E S A LTTS P G ET VT LTC R EVQLVDSGGGLVQPKGSLKLSCA SSTGAVTTSNYANWVQEKPDHL ASGFTFNTYAMNWVRQAPGKGLE FTGLIGGTNNRAPGVPARFSGSL WVARIRSKSNNYATYYADSVKDRIGDKAALTITGAQTEDEAIYFCAL FTISRDDSQSRLYLQMNNLKTEDT WYSNHWVFGGGTKLTVL (SEQ AMYYCVRHETLRSGISWFANWGID NO: 379) QGTLVTVSS (SEQ ID NO: 380) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAB5SSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLE PRGLIGGTNTRAPGTPARFSGSL WVG R I RSKI N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYN N YWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 381 ) TLVTVSS (SEQ ID NO: 382) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAB8SSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLE PRGLIGGTNTRAPGTPARFSGSL WVG R I RSKI N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYNNHWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 383) TLVTVSS (SEQ ID NO: 384) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAB12ASTGAVTTSNYANWVQQKPGQ ASGFTFSTYAMNWVRQAPGKGLEAPRGLIGGTNTRAPGTPARFSGS WVG R I RSKI N N YATYYAESVKG R FLLGGKAALTLSGAQPEDEAEYYC TISRDDSKNTLYLQMNSLKTEDTA VLWYNNHWVFGGGTKLTVL VYYCVRHETLRSGISWFASWGQGmAb Light Chain Heavy Chain(SEQ ID NO: 385) TLVTVSS (SEQ ID NO: 386) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAB13TSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLEPRGLIGGTNTRAPGTPARFSGSL WVG R I RSKI N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYNNHWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 387) TLVTVSS (SEQ ID NO: 388) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAC5SSTGAVTTSNYANWVQQKPGQA ASGFTFNTYAMNWVRQAPGKGLE PRGLIGGTNTRAPGTPARFSGSL WVG R I RSKI N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYN N YWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 389) TLVTVSS (SEQ ID NO: 390) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAC8SSTGAVTTSNYANWVQQKPGQA ASGFTFNTYAMNWVRQAPGKGLE PRGLIGGTNTRAPGTPARFSGSL WVG R I RSKI N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYNNHWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 391 ) TLVTVSS (SEQ ID NO: 392) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAD13TSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLEPRGLIGGTNTRAPGTPARFSGSL WVG R I RSH I N N YATYYAESVKG R FLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTA LWYNNHWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 393) TLVTVSS (SEQ ID NO: 394) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAE13TSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLEPRGLIGGTNTRAPGTPARFSGSL WVGRIRSKYNNYATYYAESVKGRLGGKAALTLSGAQPEDEAEYYCV FTISRDDSKNTLYLQMNSLKTEDT LWYNNHWVFGGGTKLTVL (SEQ A VYYC V R H ET L RSG I SWF ASWG QID NO: 395) GTLVTVSS (SEQ ID NO: 396) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAF13TSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLEPRGLIGGTNTRAPGTPARFSGSL WVGRERSKINNYATYYAESVKGRLGGKAALTLSGAQPEDEAEYYCV FTISRDDSKNTLYLQMNSLKTEDT LWYNNHWVFGGGTKLTVL (SEQ A VYYC V R H ET L RSG I SWF ASWG QID NO: 397) GTLVTVSS (SEQ ID NO: 398) h25A8-Q A VVTQ E P S LTVS P G GTVT LTC R EVQLVESGGGLVKPGGSLRLSCAG13TSTGAVTTSNYANWVQQKPGQA ASGFTFSTYAMNWVRQAPGKGLEPRGLIGGTNTRAPGTPARFSGSL WVGRIRSKINNYKTYYAESVKGRFLGGKAALTLSGAQPEDEAEYYCV TISRDDSKNTLYLQMNSLKTEDTAmAb Light Chain Heavy ChainLWYNNHWVFGGGTKLTVL (SEQ VYYCVRHETLRSGISWFASWGQGID NO: 399) TLVTVSS (SEQ ID NO: 400)In Table 3, the underlined sequences are CDR sequences according to Kabat and in bold according to Chothia.The invention also provides CDR portions of antibodies to CD3 (including Chothia, Kabat CDRs, and CDR contact regions). Determination of CDR regions is well within the skill of the art. It is understood that in some embodiments, CDRs can be a combination of the Kabat and Chothia CDR (also termed "combined CRs" or "extended CDRs"). In some embodiments, the CDRs are the Kabat CDRs. In other embodiments, the CDRs are the Chothia CDRs. In other words, in embodiments with more than one CDR, the CDRs may be any of Kabat, Chothia, combination CDRs, or combinations thereof. Table 4 provides examples of CDR sequences provided herein. Table 4Heavy ChainmAb CDRH1 CDRH2 CDRH3h2B4 DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);(SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)GFTFSDY (SEQ ID FIRNRARGYTSDHNASVKGNO: 332)( Chothia);(SEQ ID NO: 334) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY VH-wt 331 ) (Kabat);(SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335) VL_TKGFTFSDY (SEQ ID FIRNRARGYTSDHNASVKGNO: 332)( Chothia);(SEQ ID NO: 334) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-hnps (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDHNPSVKGNO: 332)( Chothia);(SEQ ID NO: 336) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-yaes (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDYAESVKGNO: 332)( Chothia);(SEQ ID NO: 337) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-yads (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDYADSVKGNO: 332)( Chothia);(SEQ ID NO: 338) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-yaps (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDYAPSVKGNO: 332)( Chothia);(SEQ ID NO: 339) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-hnps (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDHNPSVKGNO: 332)( Chothia);(SEQ ID NO: 336) (Chothia)S55YGFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-hnps (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)GFTFSDY (SEQ IDVL_TK FIRNRARGYTSDHNPSVKGNO: 332)( Chothia);(SEQ ID NO: 336) (Chothia)S105QGFTFSDYYMT (SEQID NO: 333)(Extended) h2B4- DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);VH-hnps (SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)VL_TK GFTFSDY (SEQ ID FIRNRARGYTSDHNPSVKGNO: 332)( Chothia);(SEQ ID NO: 336) (Chothia)S55Y / S105Q GFTFSDYYMT (SEQID NO: 333)(Extended)2B4 DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);(SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)GFTFTDY (SEQ ID FIRNRARGYTSDHNASVKGNO: 415)( Chothia);(SEQ ID NO: 418) (Chothia)GFTFTDYYMT (SEQID NO: 416)(Extended) h2B4-1 1 DYYMT (SEQ ID NO: RNRARGYT DRPSYYVLDY331 ) (Kabat);(SEQ ID NO: 417) (Kabat) (SEQ ID NO: 335)GFTFSDY (SEQ ID FIRNRARGYTSDHNASVKGNO: 332)( Chothia);(SEQ ID NO: 418) (Chothia)GFTFSDYYMT (SEQID NO: 333)(Extended)1 C10 SYWMH (SEQ ID NO: YSGGDT DATSRYFFDY418 ) (Kabat)(SEQ ID NO: 421) (Kabat) (SEQ ID NO: 423)GYTFTSY (SEQ ID NIYSGGDTINYDEKFKNNO: 419) (Chothia)(SEQ ID NO: 422) (Chothia)GYTFTSYWMH (SEQID NO: 420)(Extended)1A4 TYYLH (SEQ ID NO: FPGSDN (SEQ ID NO: 427) NRDYYFDY 424) (Kabat)(Kabat) (SEQ ID NO: 429) GYSFTTYY (SEQ IDNO: 425) (Chothia) WIFPGSDNTKYNEKFKGGYSFTTYYLH (SEQ(SEQ ID NO: 428) (Chothia)ID NO: 426)(Extended)7A3 DYYIH (SEQ ID NO: DPENGN (SEQ ID NO: 449) NDNYAFDY446) (Kabat)(Kabat) (SEQ ID NO: 451 ) GFNIKDY(SEQ IDNO: 447) (Chothia) WIDPENGNNKYDPKFQGGFNIKDYYIH (SEQ(SEQ ID NO: 450) (Chothia)ID NO: 448)(Extended)25A8 TYAMN (SEQ ID NO: RSKINNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);404) (Kabat) S (SEQ ID NO:GFTFNTY (SEQ ID R I RS Kl N N YATYYAES VKG 406)NO: 402)( Chothia);(SEQ ID NO: 405) (Chothia)GFTFNTYAMN (SEQID NO: 403)(Extended)16G7 TYAMN (SEQ ID NO: RSKSNNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);404) (Kabat) N (SEQ ID NO:GFTFNTY (SEQ ID RIRSKSNNYATYYADSVKD 406)NO: 402)( Chothia);(SEQ ID NO: 405) (Chothia)GFTFNTYAMN (SEQID NO: 403)(Extended) h25A8- TYAMN (SEQ ID NO: RSKINNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);B5 404) (Kabat) S (SEQ ID NO:GFTFSTY (SEQ ID R I RS Kl N N YATYYAES VKG 406)NO: 407)( Chothia);(SEQ ID NO: 405) (Chothia)GFTFSTYAMN (SEQID NO: 408)(Extended) h25A8- TYAMN (SEQ ID NO: RSKINNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);B8 404) (Kabat) S (SEQ ID NO:GFTFSTY (SEQ ID R I RS Kl N N YATYYAES VKG 406)NO: 407)( Chothia);(SEQ ID NO: 410) (Chothia)GFTFSTYAMN (SEQID NO: 408)(Extended) h25A8- TYAMN (SEQ ID NO: RSKYNNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);E13 41 1) (Kabat) S (SEQ ID NO:GFTFSTY (SEQ ID RIRSKYNNYATYYAESVKG 406)NO: 407)( Chothia);(SEQ ID NO: 412) (Chothia)GFTFSTYAMN (SEQID NO: 408)(Extended) h25A8- TYAMN (SEQ ID NO: RSKINNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);F13 404) (Kabat) S (SEQ ID NO:GFTFSTY (SEQ ID RERSKINNYATYYAESVKG 406)NO: 407)( Chothia);(SEQ ID NO: 413) (Chothia)GFTFSTYAMN (SEQID NO: 408)(Extended) h25A8- TYAMN (SEQ ID NO: RSKINNYA (SEQ ID NO: HETLRSGISWFA401 ) (Kabat);G13 404) (Kabat) S (SEQ ID NO:GFTFSTY (SEQ ID RIRSKINNYKTYYAESVKG 406)NO: 407)( Chothia);(SEQ ID NO: 414) (Chothia)GFTFSTYAMN (SEQID NO: 408)(Extended)Light ChainmAb CDRH1 CDRH2 CDRH3h2B4 TSSQSLFNVRSRKN WASTRES KQSYDLFTYLA(SEQ ID NO: 341) (SEQ ID NO: 342)(SEQ ID NO: 340) h2B4- KSSQSLFNVRSRKN WASTRES KQSYDLFT VH-wt YLA(SEQ ID NO: 341) (SEQ ID NO: 342) VL TK (SEQ ID NO: 343)S105Qh2B4- KSSQSLFNVRSRKN WASTRES KQSYDLFTYLAVH-hnps (SEQ ID NO: 341) (SEQ ID NO: 342)(SEQ ID NO: 343)VL_TKS55Y / S105Q25A8 RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNYWV(SEQ ID NO: 435 )436) (SEQ ID NO: 437)16G7 RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: ALWYSNHWV(SEQ ID NO: 435 )436) (SEQ ID NO: 438) h25A8- RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNYWV B5 (SEQ ID NO: 435 )436) (SEQ ID NO: 437) h25A8- RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV B8 (SEQ ID NO: 435 )436) (SEQ ID NO: 439) h25A8- RASTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV B12 (SEQ ID NO: 440)436) (SEQ ID NO: 439) h25A8- RTSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV B13 (SEQ ID NO: 441 )436) (SEQ ID NO: 439) h25A8- RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNYWV C5 (SEQ ID NO: 435 )436) (SEQ ID NO: 437) h25A8- RSSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV C8 (SEQ ID NO: 435 )436) (SEQ ID NO: 439) h25A8- RTSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV D13 (SEQ ID NO: 441 )436) (SEQ ID NO: 439) h25A8- RTSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV E13 (SEQ ID NO: 441 )436) (SEQ ID NO: 439) h25A8- RTSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV F13 (SEQ ID NO: 441 )436) (SEQ ID NO: 439) h25A8- RTSTGAVTTSNYAN GTNTRAP (SEQ ID NO: VLWYNNHWV G13 (SEQ ID NO: 441 )436) (SEQ ID NO: 439)The invention also provides isolated polynucleotides encoding the antibodies of the invention, and vectors and host cells comprising the polynucleotide.ln one embodiment, a polynucleotide comprises a sequence encoding the heavy chain and / or the light chain variable regions of antibody h2B4, h2B4-VH-wt VL_TK, h2B4-VH-hnps VL_TK, h2B4-VH-yaes VL_TK, h2B4-VH-yads VL_TK, h2B4-VH-yaps VL_TK, h2B4-VH-hnps VL_TK-S55Y, h2B4-VH-hnps VL_TK-S105Q, h2B4— vH-hnps VL_TK-S55Y / S105Q, 2B4, h2B4-1 1 , 1 C10, 1A4, 7A3, 25A8, 16G7, h25A8-B5, h25A8- B8, h25A8-B12, h25A8-B13, h25A8-C5, h25A8-C8, h25A8-D13, h25A8-E13, h25A8- F13, or h25A8-G13. The sequence encoding the antibody of interest may be maintained in a vector in a host cell and the host cell can then be expanded and frozen for future use. Vectors (including expression vectors) and host cells are further described herein.The invention also encompasses fusion proteins comprising one or more fragments or regions from the antibodies of this invention. In one embodiment, a fusion polypeptide is provided that comprises at least 10 contiguous amino acids of the variable light chain region shown in SEQ ID NOs: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 445, 352, 355, 443, 377, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399, and / or at least 10 amino acids of the variable heavy chain region shown in SEQ ID NOs: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 354, 356, 444, 442, 378, 380, 382, 384, 386, 388, 390, 392, 394, 396, 398, or 400. In other embodiments, a fusion polypeptide is provided that comprises at least about 10, at least about 15, at least about 20, at least about 25, or at least about 30 contiguous amino acids of the variable light chain region and / or at least about 10, at least about 15, at least about 20, at least about 25, or at least about 30 contiguous amino acids of the variable heavy chain region. In another embodiment, the fusion polypeptide comprises a light chain variable region and / or a heavy chain variable region, as shown in any of the sequence pairs selected from among SEQ ID NOs: 319 and 320, 321 and 322, 323 and 324, 325 and 326, 327 and 328, 329 and 330, 344 and 345, 346 and 347, 348 and 349, 350 and 351 , 445 and 444, 352 and 354, 355 and 356, 443 and 442, 377 and 378, 379 and 380, 381 and 382, 383 and 384, 385 and 386, 387 and 388, 389 and 390, 391 and 392, 393 and 394, 395 and 396, 397 and 398, or 399 and 400. In another embodiment, the fusion polypeptide comprises one or more CDR(s). In still other embodiments, the fusion polypeptide comprises CDR H3 (VH CDR3) and / or CDR L3 (VL CDR3). For purposes of this invention, a fusion protein contains one or more antibodies and another amino acid sequence to which it is not attached in the native molecule, for example, aheterologous sequence or a homologous sequence from another region. Exemplary heterologous sequences include, but are not limited to a "tag" such as a FLAG tag or a 6His tag. Tags are well known in the art.A fusion polypeptide can be created by methods known in the art, for example, synthetically or recombinantly. Typically, the fusion proteins of this invention are made by preparing an expressing a polynucleotide encoding them using recombinant methods described herein, although they may also be prepared by other means known in the art, including, for example, chemical synthesis.Representative materials of the CD3 antibody in the present invention were deposited in the American Type Culture Collection (ATCC) on September 1 1 , 2015. Vector having ATCC Accession No. PTA-122513 is a polynucleotide encoding a humanized CD3 antibody heavy chain variable region, and vector having ATCC Accession No. PTA-122512 is a polynucleotide encoding a humanized CD3 antibody light chain variable region. The deposits were made under the provisions of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purpose of Patent Procedure and Regulations thereunder (Budapest Treaty). This assures maintenance of a viable culture of the deposit for 30 years from the date of deposit. The deposit will be made available by ATCC under the terms of the Budapest Treaty, and subject to an agreement between Pfizer, Inc. and ATCC, which assures permanent and unrestricted availability of the progeny of the culture of the deposit to the public upon issuance of the pertinent U.S. patent or upon laying open to the public of any U.S. or foreign patent application, whichever comes first, and assures availability of the progeny to one determined by the U.S. Commissioner of Patents and Trademarks to be entitled thereto according to 35 U.S.C. Section 122 and the Commissioner's rules pursuant thereto (including 37 C.F.R. Section 1.14 with particular reference to 886 OG 638).The assignee of the present application has agreed that if a culture of the materials on deposit should die or be lost or destroyed when cultivated under suitable conditions, the materials will be promptly replaced on notification with another of the same. Availability of the deposited material is not to be construed as a license to practice the invention in contravention of the rights granted under the authority of any government in accordance with its patent laws.Bispecific Antibodies and Methods of MakingBispecific antibodies, monoclonal antibodies that have binding specificities for at least two different antigens, can be prepared using the antibodies disclosed herein. Methods for making bispecific antibodies are known in the art (see, e.g., Suresh et al., Methods in Enzymology 121 :210, 1986). Traditionally, the recombinant production of bispecific antibodies was based on the coexpression of two immunoglobulin heavy chain-light chain pairs, with the two heavy chains having different specificities (Millstein and Cuello, Nature 305, 537-539, 1983).According to one approach to making bispecific antibodies, antibody variable domains with the desired binding specificities (antibody-antigen combining sites) are fused to immunoglobulin constant region sequences. The fusion preferably is with an immunoglobulin heavy chain constant region, comprising at least part of the hinge, CH2 and CH3 regions. It is preferred to have the first heavy chain constant region (CH1 ), containing the site necessary for light chain binding, present in at least one of the fusions. DNAs encoding the immunoglobulin heavy chain fusions and, if desired, the immunoglobulin light chain, are inserted into separate expression vectors, and are cotransfected into a suitable host organism. This provides for great flexibility in adjusting the mutual proportions of the three polypeptide fragments in embodiments when unequal ratios of the three polypeptide chains used in the construction provide the optimum yields. It is, however, possible to insert the coding sequences for two or all three polypeptide chains in one expression vector when the expression of at least two polypeptide chains in equal ratios results in high yields or when the ratios are of no particular significance.In one approach, the bispecific antibodies are composed of a hybrid immunoglobulin heavy chain with a first binding specificity in one arm, and a hybrid immunoglobulin heavy chain-light chain pair (providing a second binding specificity) in the other arm. This asymmetric structure, with an immunoglobulin light chain in only one half of the bispecific molecule, facilitates the separation of the desired bispecific compound from unwanted immunoglobulin chain combinations. This approach is described in PCT Publication No. WO 94 / 04690.In another approach, the bispecific antibodies are composed of amino acid modification in the first hinge region in one arm, and the substituted / replaced aminoacid in the first hinge region has an opposite charge to the corresponding amino acid in the second hinge region in another arm. This approach is described in International Patent Application No. PCT / US201 1 / 036419 (WO201 1 / 143545).In another approach, the formation of a desired heteromultimeric or heterodimeric protein (e.g., bispecific antibody) is enhanced by altering or engineering an interface between a first and a second immunoglobulin-like Fc region (e.g., a hinge region and / or a CH3 region). In this approach, the bispecific antibodies may be composed of a CH3 region, wherein the CH3 region comprises a first CH3 polypeptide and a second CH3 polypeptide which interact together to form a CH3 interface, wherein one or more amino acids within the CH3 interface destabilize homodimer formation and are not electrostatically unfavorable to homodimer formation. This approach is described in International Patent Application No. PCT / US201 1 / 036419 (WO201 1 / 143545).In another approach, the bispecific antibodies can be generated using a glutamine-containing peptide tag engineered to the antibody directed to an epitope (e.g., BCMA) in one arm and another peptide tag (e.g., a Lys-containing peptide tag or a reactive endogenous Lys) engineered to a second antibody directed to a second epitope in another arm in the presence of transglutaminase. This approach is described in International Patent Application No. PCT / IB201 1 / 054899 (WO2012 / 059882).In another aspect of the invention, the heterodimeric protein (e.g., bispecific antibody) as described herein comprises a full-length human antibody, wherein a first antibody variable domain of the heterodimeric protein is capable of recruiting the activity of a human immune effector cell by specifically binding to an effector antigen located on the human immune effector cell, and wherein a second antibody variable domain of the heterodimeric protein is capable of specifically binding to a target antigen. In some embodiments, the human antibody has an lgG1 , lgG2, lgG3, or lgG4 isotype. In some embodiments, the heterodimeric protein comprises an immunologically inert Fc region.The human immune effector cell can be any of a variety of immune effector cells known in the art. For example, the immune effector cell can be a member of the human lymphoid cell lineage, including, but not limited to, a T cell (e.g., a cytotoxic T cell), a B cell, and a natural killer (NK) cell. The immune effector cell can also be, for example without limitation, a member of the human myeloid lineage, including, but not limited to,a monocyte, a neutrophilic granulocyte, and a dendritic cell. Such immune effector cells may have either a cytotoxic or an apoptotic effect on a target cell or other desired effect upon activation by binding of an effector antigen.The effector antigen is an antigen (e.g., a protein or a polypeptide) that is expressed on the human immune effector cell. Examples of effector antigens that can be bound by the heterodimeric protein (e.g., a heterodimeric antibody or a bispecific antibody) include, but are not limited to, human CD3 (or CD3 (Cluster of Differentiation) complex), CD16, NKG2D, NKp46, CD2, CD28, CD25, CD64, and CD89.The target cell can be a cell that is native or foreign to humans. In a native target cell, the cell may have been transformed to be a malignant cell or pathologically modified (e.g., a native target cell infected with a virus, a Plasmodium, or a bacterium). In a foreign target cell, the cell is an invading pathogen, such as a bacterium, a Plasmodium, or a virus.The target antigen is expressed on a target cell in a diseased condition (e.g., an inflammatory disease, a proliferative disease (e.g., cancer), an immunological disorder, a neurological disease, a neurodegenerative disease, an autoimmune disease, an infectious disease (e.g., a viral infection or a parasitic infection), an allergic reaction, a graft-versus-host disease or a host-versus-graft disease). A target antigen is not effector antigen. Examples of the target antigens include, but are not limited to, BCMA, EpCAM (Epithelial Cell Adhesion Molecule), CCR5 (Chemokine Receptor type 5), CD19, HER (Human Epidermal Growth Factor Receptor)-2 / neu, HER-3, HER-4, EGFR (Epidermal Growth Factor Receptor), PSMA, CEA, MUC-1 (Mucin), MUC2, MUC3, MUC4, MUC5AC, MUC5B, MUC7, ClhCG, Lewis-Y, CD20, CD33, CD30, ganglioside GD3, 9-0-Acetyl-GD3, GM2, Globo H, fucosyl GM1 , Poly SA, GD2, Carboanhydrase IX (MN / CA IX), CD44v6, Shh (Sonic Hedgehog), Wue-1 , Plasma Cell Antigen, (membrane-bound) IgE, MCSP (Melanoma Chondroitin Sulfate Proteoglycan), CCR8, TNF-alpha precursor, STEAP, mesothelin, A33 Antigen, PSCA (Prostate Stem Cell Antigen), Ly-6; desmoglein 4, E-cadherin neoepitope, Fetal Acetylcholine Receptor, CD25, CA19-9 marker, CA-125 marker and MIS (Muellerian Inhibitory Substance) Receptor type II, sTn (sialylated Tn antigen; TAG-72), FAP (fibroblast activation antigen), endosialin, EGFRvlll, LG, SAS and CD63.In some embodiments, the heterodimeric protein (e.g., bispecific antibody) as described herein comprises a full-length human antibody, wherein a first antibodyvariable domain of the heterodimeric protein is capable of recruiting the activity of a human immune effector cell by specifically binding to an effector antigen (e.g., CD3 antigen) located on the human immune effector cell, wherein a second antibody variable domain of the heterodimeric protein is capable of specifically binding to a target antigen (e.g., CD20 antigen or EpCAM), wherein the first and second antibody variable domain of the heterodimeric protein comprise amino acid modifications at positions 223, 225, and 228 (e.g., (C223E or C223R), (E225R), and (P228E or P228R)) in the hinge region and at position 409 or 368 (e.g., K409R or L368E (EU numbering scheme)) in the CH3 region of human lgG2 (SEQ ID NO: 493).In some embodiments, the first and second antibody variable domains of the heterodimeric protein comprise amino acid modifications at positions 221 and 228 (e.g., (D221 R or D221 E) and (P228R or P228E)) in the hinge region and at position 409 or 368 (e.g., K409R or L368E (EU numbering scheme)) in the CH3 region of human lgG1 (SEQ ID NO: 494).In some embodiments, the first and second antibody variable domains of the heterodimeric protein comprise amino acid modifications at positions 228 (e.g., (P228E or P228R)) in the hinge region and at position 409 or 368 (e.g., R409 or L368E (EU numbering scheme)) in the CH3 region of human lgG4 (SEQ ID NO: 495).In another embodiment, the first antibody variable domain of the heterodimeric protein comprises a VH region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399, and the second antibody variable domain of the heterodimeric protein comprises VH region comprising the VH sequence shown in SEQ ID NO: 2, 3, 7, 8, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 35, 37, 39, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 83, 87, 92, 95, 97, 99, 101 , 104, 106, 1 10, 1 12, 1 14, 1 18, 120, 122, 125, 127, 313, 314, 363, or 365; and / or a VL region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 1 , 4, 5, 6, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 34, 36, 38, 40, 41 , 43, 45, 47, 49, 51 , 53, 55, 57, 59, 61 , 63, 65, 67, 69, 71 , 73, 75, 77, 79, 317, 81 , 82, 84, 85, 86, 88, 89, 90, 91 , 93, 94, 96, 98,100, 102, 103, 105, 107, 108, 109, 1 1 1 , 1 13, 1 15, 1 16, 1 17, 1 19, 121 , 123, 124, 126, 128, 315, or 364.In another embodiment, the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 324 or 388; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 323 or 387; and the second antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 1 12; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 38.The antibodies useful in the present invention can encompass monoclonal antibodies, polyclonal antibodies, antibody fragments (e.g., Fab, Fab', F(ab')2, Fv, Fc, etc.), chimeric antibodies, bispecific antibodies, heteroconjugate antibodies, single chain (ScFv), mutants thereof, fusion proteins comprising an antibody portion (e.g., a domain antibody), humanized antibodies, and any other modified configuration of the immunoglobulin molecule that comprises an antigen recognition site of the required specificity, including glycosylation variants of antibodies, amino acid sequence variants of antibodies, and covalently modified antibodies. The antibodies may be murine, rat, human, or any other origin (including chimeric or humanized antibodies).In some embodiments, the BCMA or CD3 antibody as described herein is a monoclonal antibody. For example, the BCMA or CD3 antibody is a humanized monoclonal antibody or a chimeric monoclonal antibody.In some embodiments, the antibody comprises a modified constant region, such as, for example without limitation, a constant region that has increased potential for provoking an immune response. For example, the constant region may be modified to have increased affinity to an Fc gamma receptor such as, e.g. , FcyRI, FcyRI IA, or FCYI I I .In some embodiments, the antibody comprises a modified constant region, such as a constant region that is immunologically inert, that is, having a reduced potential for provoking an immune response. In some embodiments, the constant region is modified as described in Eur. J. Immunol., 29:2613-2624, 1999; PCT Application No. PCT / GB99 / 01441 ; and / or UK Patent Application No. 98099518. The Fc can be humanlgG1 , human lgG2, human lgG3, or human lgG4. The Fc can be human lgG2 containing the mutation A330P331 to S330S331 (lgG2Aa), in which the amino acid residues are numbered with reference to the wild type lgG2 sequence. Eur. J. Immunol., 29:2613-2624, 1999. In some embodiments, the antibody comprises a constant region of lgG4comprising the following mutations (Armour et al., Molecular Immunology 40 585-593, 2003): E233F234L235 to P233V234A235 (lgG4Ac), in which the numbering is with reference to wild type lgG4. In yet another embodiment, the Fc is human lgG4 E233F234L235 to P233V234A235 with deletion G236 (lgG4Ab). In another embodiment, the Fc is any human lgG4 Fc (lgG4, lgG4Ab or lgG4Ac) containing hinge stabilizing mutation S228 to P228 (Aalberse et al., Immunology 105, 9- 19, 2002). In another embodiment, the Fc can be aglycosylated Fc.In some embodiments, the constant region is aglycosylated by mutating the oligosaccharide attachment residue (such as Asn297) and / or flanking residues that are part of the glycosylation recognition sequence in the constant region. In some embodiments, the constant region is aglycosylated for N-linked glycosylation enzymatically. The constant region may be aglycosylated for N-linked glycosylation enzymatically or by expression in a glycosylation deficient host cell.In some embodiments, the constant region has a modified constant region that removes or reduces Fc gamma receptor binding. For example, the Fc can be human lgG2 containing the mutation D265, in which the amino acid residues are numbered with reference to the wild type lgG2 sequence (SEQ ID NO: 493). Accordingly, in some embodiments, the constant region has a modified constant region having the sequence shown in SEQ ID NO: 496:ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCRVRCPRCPAPPVA GPSVFLFPPKPKDTLMISRTPEVTCVVVAVSHEDPEVQFNWYVDGVEVHNAKTKPRE EQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPSSIEKTISKTKGQPREPQVYTL PPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYS RLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK.In some embodiments, the constant region has a modified constant region having the sequence shown in SEQ ID NO: 497:ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSNFGTQTYTCNVDHKPSNTKVDKTVERKCEVECPECPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVAVSHEDPEVQFNWYVDGVEVHNAKTKPRE EQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPSSIEKTISKTKGQPREPQVYTL PPSREEMTKNQVSLTCEVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYS KLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK.One way of determining binding affinity of antibodies to BCMA or CD3 is by measuring binding affinity of monofunctional Fab fragments of the antibody. To obtain monofunctional Fab fragments, an antibody (for example, IgG) can be cleaved with papain or expressed recombinantly. The affinity of a BCMA Fab fragment of an antibody can be determined by surface plasmon resonance (Biacore™3000™ surface plasmon resonance (SPR) system, Biacore™, INC, Piscataway NJ) equipped with pre- immobilized streptavidin sensor chips (SA) or anti-mouse Fc or anti-human Fc using HBS-EP running buffer (0.01 M HEPES, pH 7.4, 0.15 NaCI, 3 mM EDTA, 0.005% v / v Surfactant P20). Biotinylated or Fc fusion human BCMA can be diluted into HBS-EP buffer to a concentration of less than 0.5 pg / mL and injected across the individual chip channels using variable contact times, to achieve two ranges of antigen density, either 50-200 response units (RU) for detailed kinetic studies or 800-1 ,000 RU for screening assays. Regeneration studies have shown that 25 mM NaOH in 25% v / v ethanol effectively removes the bound Fab while keeping the activity of BCMA on the chip for over 200 injections. Typically, serial dilutions (spanning concentrations of 0.1-1 Ox estimated KD) of purified Fab samples are injected for 1 min at 100 μΙ_Ληίηυίβ and dissociation times of up to 2 hours are allowed. The concentrations of the Fab proteins are determined by ELISA and / or SDS-PAGE electrophoresis using a Fab of known concentration (as determined by amino acid analysis) as a standard. Kinetic association rates (kon) and dissociation rates (k0fr) are obtained simultaneously by fitting the data globally to a 1 : 1 Langmuir binding model (Karlsson, R. Roos, H. Fagerstam, L. Petersson, B. (1994). Methods Enzymology 6. 99-1 10) using the BIAevaluation program. Equilibrium dissociation constant (KD) values are calculated as k0ff / kon. This protocol is suitable for use in determining binding affinity of an antibody to any BCMA, including human BCMA, BCMA of another mammal (such as mouse BCMA, rat BCMA, or primate BCMA), as well as different forms of BCMA (e.g., glycosylated BCMA). Binding affinity of an antibody is generally measured at 25°C, but can also be measured at 37°C.The antibodies as described herein may be made by any method known in the art. For the production of hybridoma cell lines, the route and schedule of immunization of the host animal are generally in keeping with established and conventional techniques for antibody stimulation and production, as further described herein. General techniques for production of human and mouse antibodies are known in the art and / or are described herein.It is contemplated that any mammalian subject including humans or antibody producing cells therefrom can be manipulated to serve as the basis for production of mammalian, including human and hybridoma cell lines. Typically, the host animal is inoculated intraperitoneal^, intramuscularly, orally, subcutaneously, intraplantar, and / or intradermally with an amount of immunogen, including as described herein.Hybridomas can be prepared from the lymphocytes and immortalized myeloma cells using the general somatic cell hybridization technique of Kohler, B. and Milstein, C, Nature 256:495-497, 1975 or as modified by Buck, D. W., et al., In Vitro, 18:377- 381 , 1982. Available myeloma lines, including but not limited to X63-Ag8.653 and those from the Salk Institute, Cell Distribution Center, San Diego, Calif., USA, may be used in the hybridization. Generally, the technique involves fusing myeloma cells and lymphoid cells using a fusogen such as polyethylene glycol, or by electrical means well known to those skilled in the art. After the fusion, the cells are separated from the fusion medium and grown in a selective growth medium, such as hypoxanthine- aminopterin-thymidine (HAT) medium, to eliminate unhybridized parent cells. Any of the media described herein, supplemented with or without serum, can be used for culturing hybridomas that secrete monoclonal antibodies. As another alternative to the cell fusion technique, EBV immortalized B cells may be used to produce the monoclonal antibodies of the subject invention. The hybridomas are expanded and subcloned, if desired, and supernatants are assayed for anti-immunogen activity by conventional immunoassay procedures (e.g., radioimmunoassay, enzyme immunoassay, or fluorescence immunoassay).Hybridomas that may be used as source of antibodies encompass all derivatives, progeny cells of the parent hybridomas that produce monoclonal antibodies specific for BCMA, CD3, or portions thereof.Hybridomas that produce such antibodies may be grown in vitro or in vivo using known procedures. The monoclonal antibodies may be isolated from the culture mediaor body fluids, by conventional immunoglobulin purification procedures such as ammonium sulfate precipitation, gel electrophoresis, dialysis, chromatography, and ultrafiltration, if desired. Undesired activity, if present, can be removed, for example, by running the preparation over adsorbents made of the immunogen attached to a solid phase and eluting or releasing the desired antibodies off the immunogen. Immunization of a host animal with a human BCMA or CD3, or a fragment containing the target amino acid sequence conjugated to a protein that is immunogenic in the species to be immunized, e.g., keyhole limpet hemocyanin, serum albumin, bovine thyroglobulin, or soybean trypsin inhibitor using a bifunctional or derivatizing agent, for example, maleimidobenzoyl sulfosuccinimide ester (conjugation through cysteine residues), N- hydroxysuccinimide (through lysine residues), glutaraldehyde, succinic anhydride, SOCI2, or R N=C=NR, where R and R are different alkyl groups, can yield a population of antibodies (e.g., monoclonal antibodies).If desired, the antibody (monoclonal or polyclonal) of interest may be sequenced and the polynucleotide sequence may then be cloned into a vector for expression or propagation. The sequence encoding the antibody of interest may be maintained in vector in a host cell and the host cell can then be expanded and frozen for future use. Production of recombinant monoclonal antibodies in cell culture can be carried out through cloning of antibody genes from B cells by means known in the art. See, e.g. Tiller et al., J. Immunol. Methods 329, 1 12, 2008; U.S. Pat. No. 7,314,622.In an alternative, the polynucleotide sequence may be used for genetic manipulation to "humanize" the antibody or to improve the affinity, or other characteristics of the antibody. For example, the constant region may be engineered to more nearly resemble human constant regions to avoid immune response if the antibody is used in clinical trials and treatments in humans. It may be desirable to genetically manipulate the antibody sequence to obtain greater affinity to BCMA or CD3 and greater efficacy in inhibiting BCMA.There are four general steps to humanize a monoclonal antibody. These are: (1 ) determining the nucleotide and predicted amino acid sequence of the starting antibody light and heavy variable domains (2) designing the humanized antibody, i.e., deciding which antibody framework region to use during the humanizing process (3) the actual humanizing methodologies / techniques and (4) the transfection and expression ofthe humanized antibody. See, for example, U.S. Pat. Nos. 4,816,567; 5,807,715; 5,866,692; 6,331 ,415; 5,530,101 ; 5,693,761 ; 5,693,762; 5,585,089; and 6, 180,370.A number of "humanized" antibody molecules comprising an antigen binding site derived from a non-human immunoglobulin have been described, including chimeric antibodies having rodent or modified rodent V regions and their associated CDRs fused to human constant regions. See, for example, Winter et al. Nature 349:293-299, 1991 , Lobuglio et al. Proc. Nat. Acad. Sci. USA 86:4220-4224, 1989, Shaw et al. J Immunol. 138:4534-4538, 1987, and Brown et al. Cancer Res. 47:3577-3583, 1987. Other references describe rodent CDRs grafted into a human supporting framework region (FR) prior to fusion with an appropriate human antibody constant region. See, for example, Riechmann et al. Nature 332:323-327, 1988, Verhoeyen et al. Science 239:1534-1536, 1988, and Jones et al. Nature 321 :522-525, 1986. Another reference describes rodent CDRs supported by recombinantly engineered rodent framework regions. See, for example, European Patent Publication No. 0519596. These "humanized" molecules are designed to minimize unwanted immunological response toward rodent anti-human antibody molecules which limits the duration and effectiveness of therapeutic applications of those moieties in human recipients. For example, the antibody constant region can be engineered such that it is immunologically inert (e.g., does not trigger complement lysis). See, e.g. PCT Publication No. PCT / GB99 / 01441 ; UK Patent Application No. 9809951.8. Other methods of humanizing antibodies that may also be utilized are disclosed by Daugherty et al., Nucl. Acids Res. 19:2471 -2476, 1991 , and in U.S. Pat. Nos. 6, 180,377; 6,054,297; 5,997,867; 5,866,692; 6,210,671 ; and 6,350,861 ; and in PCT Publication No. WO 01 / 27160.The general principles related to humanized antibodies discussed above are also applicable to customizing antibodies for use, for example, in dogs, cats, primate, equines and bovines. Further, one or more aspects of humanizing an antibody described herein may be combined, e.g., CDR grafting, framework mutation and CDR mutation.In one variation, fully human antibodies may be obtained by using commercially available mice that have been engineered to express specific human immunoglobulin proteins. Transgenic animals that are designed to produce a more desirable (e.g., fully human antibodies) or more robust immune response may also be used for generationof humanized or human antibodies. Examples of such technology are Xenomouse™ from Abgenix, Inc. (Fremont, CA) and HuMAb-Mouse® and TC Mouse™ from Medarex, Inc. (Princeton, NJ).In an alternative, antibodies may be made recombinantly and expressed using any method known in the art. In another alternative, antibodies may be made recombinantly by phage display technology. See, for example, U.S. Pat. Nos. 5,565,332; 5,580,717; 5,733,743; and 6,265, 150; and Winter et al., Annu. Rev. Immunol. 12:433-455, 1994. Alternatively, the phage display technology (McCafferty et al., Nature 348:552-553, 1990) can be used to produce human antibodies and antibody fragments in vitro, from immunoglobulin variable (V) domain gene repertoires from unimmunized donors. According to this technique, antibody V domain genes are cloned in-frame into either a major or minor coat protein gene of a filamentous bacteriophage, such as M13 or fd, and displayed as functional antibody fragments on the surface of the phage particle. Because the filamentous particle contains a single- stranded DNA copy of the phage genome, selections based on the functional properties of the antibody also result in selection of the gene encoding the antibody exhibiting those properties. Thus, the phage mimics some of the properties of the B cell. Phage display can be performed in a variety of formats; for review see, e.g., Johnson, Kevin S. and Chiswell, David J., Current Opinion in Structural Biology 3:564-571 , 1993. Several sources of V-gene segments can be used for phage display. Clackson et al., Nature 352:624-628, 1991 , isolated a diverse array of anti-oxazolone antibodies from a small random combinatorial library of V genes derived from the spleens of immunized mice. A repertoire of V genes from unimmunized human donors can be constructed and antibodies to a diverse array of antigens (including self-antigens) can be isolated essentially following the techniques described by Mark et al. , J. Mol. Biol. 222:581 -597, 1991 , or Griffith et al., EMBO J. 12:725-734, 1993. In a natural immune response, antibody genes accumulate mutations at a high rate (somatic hypermutation). Some of the changes introduced will confer higher affinity, and B cells displaying high-affinity surface immunoglobulin are preferentially replicated and differentiated during subsequent antigen challenge. This natural process can be mimicked by employing the technique known as "chain shuffling." (Marks et al., Bio / Technol. 10:779-783, 1992). In this method, the affinity of "primary" human antibodies obtained by phage display can be improved by sequentially replacing the heavy and light chain V region genes withrepertoires of naturally occurring variants (repertoires) of V domain genes obtained from unimmunized donors. This technique allows the production of antibodies and antibody fragments with affinities in the pM-nM range. A strategy for making very large phage antibody repertoires (also known as "the mother-of-all libraries") has been described by Waterhouse et al., Nucl. Acids Res. 21 :2265-2266, 1993. Gene shuffling can also be used to derive human antibodies from rodent antibodies, where the human antibody has similar affinities and specificities to the starting rodent antibody. According to this method, which is also referred to as "epitope imprinting", the heavy or light chain V domain gene of rodent antibodies obtained by phage display technique is replaced with a repertoire of human V domain genes, creating rodent-human chimeras. Selection on antigen results in isolation of human variable regions capable of restoring a functional antigen binding site, i.e., the epitope governs (imprints) the choice of partner. When the process is repeated in order to replace the remaining rodent V domain, a human antibody is obtained (see PCT Publication No. WO 93 / 06213). Unlike traditional humanization of rodent antibodies by CDR grafting, this technique provides completely human antibodies, which have no framework or CDR residues of rodent origin.Antibodies may be made recombinantly by first isolating the antibodies and antibody producing cells from host animals, obtaining the gene sequence, and using the gene sequence to express the antibody recombinantly in host cells (e.g., CHO cells). Another method which may be employed is to express the antibody sequence in plants (e.g., tobacco) or transgenic milk. Methods for expressing antibodies recombinantly in plants or milk have been disclosed. See, for example, Peeters, et al. Vaccine 19:2756, 2001 ; Lonberg, N. and D. Huszar Int. Rev. Immunol 13:65, 1995; and Pollock, et al., J Immunol Methods 231 :147, 1999. Methods for making derivatives of antibodies, e.g., humanized, single chain, etc. are known in the art.Immunoassays and flow cytometry sorting techniques such as fluorescence activated cell sorting (FACS) can also be employed to isolate antibodies that are specific for BCMA, CD3, or tumor antigens of interest.The antibodies as described herein can be bound to many different carriers. Carriers can be active and / or inert. Examples of well-known carriers include polypropylene, polystyrene, polyethylene, dextran, nylon, amylases, glass, natural and modified celluloses, polyacrylamides, agaroses, and magnetite. The nature of the carrier can be either soluble or insoluble for purposes of the invention. Those skilled inthe art will know of other suitable carriers for binding antibodies, or will be able to ascertain such, using routine experimentation. In some embodiments, the carrier comprises a moiety that targets the myocardium.DNA encoding the monoclonal antibodies is readily isolated and sequenced using conventional procedures (e.g., by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of the monoclonal antibodies). The hybridoma cells serve as a preferred source of such DNA. Once isolated, the DNA may be placed into expression vectors (such as expression vectors disclosed in PCT Publication No. WO 87 / 04462), which are then transfected into host cells such as E. coli cells, simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of monoclonal antibodies in the recombinant host cells. See, e.g., PCT Publication No. WO 87 / 04462. The DNA also may be modified, for example, by substituting the coding sequence for human heavy and light chain constant regions in place of the homologous murine sequences, Morrison et al., Proc. Nat. Acad. Sci. 81 :6851 , 1984, or by covalently joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. In that manner, "chimeric" or "hybrid" antibodies are prepared that have the binding specificity of a monoclonal antibody herein.The BCMA or tumor antigen of interest antibodies as described herein can be identified or characterized using methods known in the art, whereby reduction of BCMA or other tumor antigen expression levels are detected and / or measured. In some embodiments, a BCMA antibody is identified by incubating a candidate agent with BCMA and monitoring binding and / or attendant reduction of BCMA expression levels. The binding assay may be performed with purified BCMA polypeptide(s), or with cells naturally expressing, or transfected to express, BCMA polypeptide(s). In one embodiment, the binding assay is a competitive binding assay, where the ability of a candidate antibody to compete with a known BCMA antibody for BCMA binding is evaluated. The assay may be performed in various formats, including the ELISA format.Following initial identification, the activity of a candidate BCMA, CD3, or other tumor antigen antibody can be further confirmed and refined by bioassays, known to test the targeted biological activities. Alternatively, bioassays can be used to screencandidates directly. Some of the methods for identifying and characterizing antibodies are described in detail in the Examples.BCMA, CD3, or other tumor antigen antibodies may be characterized using methods well known in the art. For example, one method is to identify the epitope to which it binds, or "epitope mapping." There are many methods known in the art for mapping and characterizing the location of epitopes on proteins, including solving the crystal structure of an antibody-antigen complex, competition assays, gene fragment expression assays, and synthetic peptide-based assays, as described, for example, in Chapter 1 1 of Harlow and Lane, Using Antibodies, a Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1999. In an additional example, epitope mapping can be used to determine the sequence to which an antibody binds. Epitope mapping is commercially available from various sources, for example, Pepscan Systems (Edelhertweg 15, 8219 PH Lelystad, The Netherlands). The epitope can be a linear epitope, i.e., contained in a single stretch of amino acids, or a conformational epitope formed by a three-dimensional interaction of amino acids that may not necessarily be contained in a single stretch. Peptides of varying lengths (e.g., at least 4-6 amino acids long) can be isolated or synthesized (e.g., recombinantly) and used for binding assays with a BCMA, CD3, or other tumor antigen antibody. In another example, the epitope to which the BCMA, CD3, or other tumor antigen antibody binds can be determined in a systematic screening by using overlapping peptides derived from the BCMA, CD3, or other tumor antigen sequence and determining binding by the BCMA, CD3, or other tumor antigen antibody. According to the gene fragment expression assays, the open reading frame encoding BCMA, CD3, or other tumor antigen is fragmented either randomly or by specific genetic constructions and the reactivity of the expressed fragments of BCMA, CD3, or other tumor antigen with the antibody to be tested is determined. The gene fragments may, for example, be produced by PCR and then transcribed and translated into protein in vitro, in the presence of radioactive amino acids. The binding of the antibody to the radioactively labeled BCMA, CD3, or other tumor antigen fragments is then determined by immunoprecipitation and gel electrophoresis. Certain epitopes can also be identified by using large libraries of random peptide sequences displayed on the surface of phage particles (phage libraries). Alternatively, a defined library of overlapping peptide fragments can be tested for binding to the test antibody in simple binding assays. In anadditional example, mutagenesis of an antigen binding domain, domain swapping experiments and alanine scanning mutagenesis can be performed to identify residues required, sufficient, and / or necessary for epitope binding. For example, domain swapping experiments can be performed using a mutant BCMA, CD3, or other tumor antigen in which various fragments of the BCMA, CD3, or other tumor antigen protein have been replaced (swapped) with sequences from BCMA from another species (e.g., mouse), or a closely related, but antigenically distinct protein (e.g., Trop-1 ). By assessing binding of the antibody to the mutant BCMA, CD3, or other tumor antigen, the importance of the particular BCMA, CD3, or other tumor antigen fragment to antibody binding can be assessed.Yet another method which can be used to characterize a BCMA, CD3, or other tumor antigen antibody is to use competition assays with other antibodies known to bind to the same antigen, i.e., various fragments on BCMA, CD3, or other tumor antigen, to determine if the BCMA, CD3, or other tumor antigen antibody binds to the same epitope as other antibodies. Competition assays are well known to those of skill in the art.An expression vector can be used to direct expression of a BCMA, CD3, or other tumor antigen antibody. One skilled in the art is familiar with administration of expression vectors to obtain expression of an exogenous protein in vivo. See, e.g., U.S. Pat. Nos. 6,436,908; 6,413,942; and 6,376,471. Administration of expression vectors includes local or systemic administration, including injection, oral administration, particle gun or catheterized administration, and topical administration. In another embodiment, the expression vector is administered directly to the sympathetic trunk or ganglion, or into a coronary artery, atrium, ventrical, or pericardium.Targeted delivery of therapeutic compositions containing an expression vector, or subgenomic polynucleotides can also be used. Receptor-mediated DNA delivery techniques are described in, for example, Findeis et al., Trends Biotechnol., 1993, 1 1 :202; Chiou et al., Gene Therapeutics: Methods And Applications Of Direct Gene Transfer, J.A. Wolff, ed., 1994; Wu et al., J. Biol. Chem., 263:621 , 1988; Wu et al., J. Biol. Chem., 269:542, 1994; Zenke et al., Proc. Natl. Acad. Sci. USA, 87:3655, 1990; and Wu et al., J. Biol. Chem., 266:338, 1991. Therapeutic compositions containing a polynucleotide are administered in a range of about 100 ng to about 200 mg of DNA for local administration in a gene therapy protocol. Concentration ranges of about 500 ng to about 50 mg, about 1 μg to about 2 mg, about 5 μg to about 500 μg, and about 20 μgto about 100 μ9 of DNA can also be used during a gene therapy protocol. The therapeutic polynucleotides and polypeptides can be delivered using gene delivery vehicles. The gene delivery vehicle can be of viral or non-viral origin (see generally, Jolly, Cancer Gene Therapy, 1 :51 , 1994; Kimura, Human Gene Therapy, 5:845, 1994; Connelly, Human Gene Therapy, 1995, 1 :185; and Kaplitt, Nature Genetics, 6:148, 1994). Expression of such coding sequences can be induced using endogenous mammalian or heterologous promoters. Expression of the coding sequence can be either constitutive or regulated.Viral-based vectors for delivery of a desired polynucleotide and expression in a desired cell are well known in the art. Exemplary viral-based vehicles include, but are not limited to, recombinant retroviruses (see, e.g., PCT Publication Nos. WO 90 / 07936; WO 94 / 03622; WO 93 / 25698; WO 93 / 25234; WO 93 / 11230; WO 93 / 10218; WO 91 / 02805; U.S. Pat. Nos. 5, 219,740 and 4,777, 127; GB Pat. No. 2,200,651 ; and EP Pat. No. 0 345 242), alphavirus-based vectors (e.g., Sindbis virus vectors, Semliki forest virus (ATCC VR-67; ATCC VR-1247), Ross River virus (ATCC VR-373; ATCC VR-1246) and Venezuelan equine encephalitis virus (ATCC VR-923; ATCC VR-1250; ATCC VR 1249; ATCC VR-532)), and adeno-associated virus (AAV) vectors (see, e.g., PCT Publication Nos. WO 94 / 12649, WO 93 / 03769; WO 93 / 19191 ; WO 94 / 28938; WO 95 / 1 1984 and WO 95 / 00655). Administration of DNA linked to killed adenovirus as described in Curiel, Hum. Gene Then, 1992, 3: 147 can also be employed.Non-viral delivery vehicles and methods can also be employed, including, but not limited to, polycationic condensed DNA linked or unlinked to killed adenovirus alone (see, e.g., Curiel, Hum. Gene Then, 3:147, 1992); ligand-linked DNA (see, e.g., Wu, J. Biol. Chem., 264: 16985, 1989); eukaryotic cell delivery vehicles cells (see, e.g., U.S. Pat. No. 5,814,482; PCT Publication Nos. WO 95 / 07994; WO 96 / 17072; WO 95 / 30763; and WO 97 / 42338) and nucleic charge neutralization or fusion with cell membranes. Naked DNA can also be employed. Exemplary naked DNA introduction methods are described in PCT Publication No. WO 90 / 1 1092 and U.S. Pat. No. 5,580,859. Liposomes that can act as gene delivery vehicles are described in U.S. Pat. No. 5,422, 120; PCT Publication Nos. WO 95 / 13796; WO 94 / 23697; WO 91 / 14445; and EP 0524968. Additional approaches are described in Philip, Mol. Cell Biol., 14:241 1 , 1994 and in Woffendin, Proc. Natl. Acad. Sci., 91 :1581 , 1994.ln some embodiments, the invention encompasses compositions, including pharmaceutical compositions, comprising antibodies described herein or made by the methods and having the characteristics described herein. As used herein, compositions comprise one or more antibodies that bind to CD3 and a tumor antigen (e.g BCMA), and / or one or more polynucleotides comprising sequences encoding one or more these antibodies. These compositions may further comprise suitable excipients, such as pharmaceutically acceptable excipients including buffers, which are well known in the art.The invention also provides methods of making any of these antibodies. The antibodies of this invention can be made by procedures known in the art. The polypeptides can be produced by proteolytic or other degradation of the antibodies, by recombinant methods (i.e., single or fusion polypeptides) as described above or by chemical synthesis. Polypeptides of the antibodies, especially shorter polypeptides up to about 50 amino acids, are conveniently made by chemical synthesis. Methods of chemical synthesis are known in the art and are commercially available. For example, an antibody could be produced by an automated polypeptide synthesizer employing the solid phase method. See also, U.S. Pat. Nos. 5,807,715; 4,816,567; and 6,331 ,415.Heteroconjugate antibodies, comprising two covalently joined antibodies, are also within the scope of the invention. Such antibodies have been used to target immune system cells to unwanted cells (U.S. Pat. No. 4,676,980), and for treatment of HIV infection (PCT Publication Nos. WO 91 / 00360 and WO 92 / 200373; EP 03089). Heteroconjugate antibodies may be made using any convenient cross-linking methods. Suitable cross-linking agents and techniques are well known in the art, and are described in U.S. Pat. No. 4,676,980.Chimeric or hybrid antibodies also may be prepared in vitro using known methods of synthetic protein chemistry, including those involving cross-linking agents. For example, immunotoxins may be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate.In the recombinant humanized antibodies, the Fey portion can be modified to avoid interaction with Fey receptor and the complement and immune systems. The techniques for preparation of such antibodies are described in WO 99 / 58572. For example, the constant region may be engineered to more resemble human constantregions to avoid immune response if the antibody is used in clinical trials and treatments in humans. See, for example, U.S. Pat. Nos. 5,997,867 and 5,866,692.The invention encompasses modifications to the antibodies and polypeptides of the invention variants as described herein, including functionally equivalent antibodies which do not significantly affect their properties and variants which have enhanced or decreased activity and / or affinity. For example, the amino acid sequence may be mutated to obtain an antibody with the desired binding affinity to BCMA and / or CD3. Modification of polypeptides is routine practice in the art and need not be described in detail herein. Examples of modified polypeptides include polypeptides with conservative substitutions of amino acid residues, one or more deletions or additions of amino acids which do not significantly deleteriously change the functional activity, or which mature (enhance) the affinity of the polypeptide for its ligand, or use of chemical analogs.Amino acid sequence insertions include amino- and / or carboxyl-terminal fusions ranging in length from one residue to polypeptides containing a hundred or more residues, as well as intrasequence insertions of single or multiple amino acid residues. Examples of terminal insertions include an antibody with an N-terminal methionyl residue or the antibody fused to an epitope tag. Other insertional variants of the antibody molecule include the fusion to the N- or C-terminus of the antibody of an enzyme or a polypeptide which increases the half-life of the antibody in the blood circulation.Substitution variants have at least one amino acid residue in the antibody molecule removed and a different residue inserted in its place. The sites of greatest interest for substitutional mutagenesis include the hypervariable regions, but FR alterations are also contemplated. Conservative substitutions are shown in Table 5 under the heading of "conservative substitutions." If such substitutions result in a change in biological activity, then more substantial changes, denominated "exemplary substitutions" in Table 5, or as further described below in reference to amino acid classes, may be introduced and the products screened.Table 5: Amino Acid SubstitutionsSubstantial modifications in the biological properties of the antibody are accomplished by selecting substitutions that differ significantly in their effect on maintaining (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a sheet or helical conformation, (b) the charge or hydrophobicity of the molecule at the target site, or (c) the bulk of the side chain. Naturally occurring amino acid residues are divided into groups based on common side-chain properties:(1 ) Non-polar: Norleucine, Met, Ala, Val, Leu, He;(2) Polar without charge: Cys, Ser, Thr, Asn, Gin;(3) Acidic (negatively charged): Asp, Glu;(4) Basic (positively charged): Lys, Arg;(5) Residues that influence chain orientation: Gly, Pro; and(6) Aromatic: Trp, Tyr, Phe, His.Non-conservative substitutions are made by exchanging a member of one of these classes for another class.Any cysteine residue not involved in maintaining the proper conformation of the antibody also may be substituted, generally with serine, to improve the oxidative stability of the molecule and prevent aberrant cross-linking. Conversely, cysteine bond(s) may be added to the antibody to improve its stability, particularly where the antibody is an antibody fragment such as an Fv fragment.Amino acid modifications can range from changing or modifying one or more amino acids to complete redesign of a region, such as the variable region. Changes in the variable region can alter binding affinity and / or specificity. In some embodiments, no more than one to five conservative amino acid substitutions are made within a CDR domain. In other embodiments, no more than one to three conservative amino acid substitutions are made within a CDR domain. In still other embodiments, the CDR domain is CDR H3 and / or CDR L3.Modifications also include glycosylated and nonglycosylated polypeptides, as well as polypeptides with other post-translational modifications, such as, for example, glycosylation with different sugars, acetylation, and phosphorylation. Antibodies are glycosylated at conserved positions in their constant regions (Jefferis and Lund, Chem. Immunol. 65: 1 1 1 -128, 1997; Wright and Morrison, TibTECH 15:26-32, 1997). The oligosaccharide side chains of the immunoglobulins affect the protein's function (Boyd et al., Mol. Immunol. 32: 131 1 -1318, 1996; Wittwe and Howard, Biochem. 29:4175- 4180, 1990) and the intramolecular interaction between portions of the glycoprotein, which can affect the conformation and presented three-dimensional surface of the glycoprotein (Jefferis and Lund, supra; Wyss and Wagner, Current Opin. Biotech. 7:409-416, 1996). Oligosaccharides may also serve to target a given glycoprotein to certain molecules based upon specific recognition structures. Glycosylation of antibodies has also been reported to affect antibody-dependent cellular cytotoxicity (ADCC). In particular, CHO cells with tetracycline-regulated expression of β(1 ,4)-Ν- acetylglucosaminyltransferase III (GnTIII), a glycosyltransferase catalyzing formation ofbisecting GlcNAc, was reported to have improved ADCC activity (Umana et al., Mature Biotech. 17: 176-180, 1999).Glycosylation of antibodies is typically either N-linked or O-linked. N-linked refers to the attachment of the carbohydrate moiety to the side chain of an asparagine residue. The tripeptide sequences asparagine-X-serine, asparagine-X-threonine, and asparagine-X-cysteine, where X is any amino acid except proline, are the recognition sequences for enzymatic attachment of the carbohydrate moiety to the asparagine side chain. Thus, the presence of either of these tripeptide sequences in a polypeptide creates a potential glycosylation site. O-linked glycosylation refers to the attachment of one of the sugars N-acetylgalactosamine, galactose, or xylose to a hydroxyamino acid, most commonly serine or threonine, although 5-hydroxyproline or 5-hydroxylysine may also be used.Addition of glycosylation sites to the antibody is conveniently accomplished by altering the amino acid sequence such that it contains one or more of the above- described tripeptide sequences (for N-linked glycosylation sites). The alteration may also be made by the addition of, or substitution by, one or more serine or threonine residues to the sequence of the original antibody (for O-linked glycosylation sites).The glycosylation pattern of antibodies may also be altered without altering the underlying nucleotide sequence. Glycosylation largely depends on the host cell used to express the antibody. Since the cell type used for expression of recombinant glycoproteins, e.g. antibodies, as potential therapeutics is rarely the native cell, variations in the glycosylation pattern of the antibodies can be expected (see, e.g. Hse et al., J. Biol. Chem. 272:9062-9070, 1997).In addition to the choice of host cells, factors that affect glycosylation during recombinant production of antibodies include growth mode, media formulation, culture density, oxygenation, pH, purification schemes and the like. Various methods have been proposed to alter the glycosylation pattern achieved in a particular host organism including introducing or overexpressing certain enzymes involved in oligosaccharide production (U.S. Pat. Nos. 5,047,335; 5,510,261 and 5,278,299). Glycosylation, or certain types of glycosylation, can be enzymatically removed from the glycoprotein, for example, using endoglycosidase H (Endo H), N-glycosidase F, endoglycosidase F1 , endoglycosidase F2, endoglycosidase F3. In addition, the recombinant host cell can begenetically engineered to be defective in processing certain types of polysaccharides. These and similar techniques are well known in the art.Other methods of modification include using coupling techniques known in the art, including, but not limited to, enzymatic means, oxidative substitution and chelation. Modifications can be used, for example, for attachment of labels for immunoassay. Modified polypeptides are made using established procedures in the art and can be screened using standard assays known in the art, some of which are described below and in the Examples.In some embodiments of the invention, the antibody comprises a modified constant region, such as a constant region that has increased affinity to a human Fc gamma receptor, is immunologically inert or partially inert, e.g., does not trigger complement mediated lysis, does not stimulate antibody-dependent cell mediated cytotoxicity (ADCC), or does not activate macrophages; or has reduced activities (compared to the unmodified antibody) in any one or more of the following: triggering complement mediated lysis, stimulating antibody-dependent cell mediated cytotoxicity (ADCC), or activating microglia. Different modifications of the constant region may be used to achieve optimal level and / or combination of effector functions. See, for example, Morgan et al., Immunology 86:319-324, 1995; Lund et al., J. Immunology 157:4963-9 157:4963-4969, 1996; Idusogie et al., J. Immunology 164:4178-4184, 2000; Tao et al., J. Immunology 143: 2595-2601 , 1989; and Jefferis et al., Immunological Reviews 163:59-76, 1998. In some embodiments, the constant region is modified as described in Eur. J. Immunol., 1999, 29:2613-2624; PCT Application No. PCT / GB99 / 01441 ; and / or UK Patent Application No. 9809951.8. In other embodiments, the antibody comprises a human heavy chain lgG2 constant region comprising the following mutations: A330P331 to S330S331 (amino acid numbering with reference to the wild type lgG2 sequence). Eur. J. Immunol., 1999, 29:2613-2624. In still other embodiments, the constant region is aglycosylated for N-linked glycosylation. In some embodiments, the constant region is aglycosylated for N-linked glycosylation by mutating the glycosylated amino acid residue or flanking residues that are part of the N-glycosylation recognition sequence in the constant region. For example, N-glycosylation site N297 may be mutated to A, Q, K, or H. See, Tao et al., J. Immunology 143: 2595-2601 , 1989; and Jefferis et al., Immunological Reviews 163:59- 76, 1998. In some embodiments, the constant region is aglycosylated for N-linkedglycosylation. The constant region may be aglycosylated for N-linked glycosylation enzymatically (such as removing carbohydrate by enzyme PNGase), or by expression in a glycosylation deficient host cell.Other antibody modifications include antibodies that have been modified as described in PCT Publication No. WO 99 / 58572. These antibodies comprise, in addition to a binding domain directed at the target molecule, an effector domain having an amino acid sequence substantially homologous to all or part of a constant region of a human immunoglobulin heavy chain. These antibodies are capable of binding the target molecule without triggering significant complement dependent lysis, or cell- mediated destruction of the target. In some embodiments, the effector domain is capable of specifically binding FcRn and / or FcYRIIb. These are typically based on chimeric domains derived from two or more human immunoglobulin heavy chain CH2 domains. Antibodies modified in this manner are particularly suitable for use in chronic antibody therapy, to avoid inflammatory and other adverse reactions to conventional antibody therapy.The invention includes affinity matured embodiments. For example, affinity matured antibodies can be produced by procedures known in the art (Marks et al., Bio / Technology, 10:779-783, 1992; Barbas et al., Proc Nat. Acad. Sci, USA 91 :3809- 3813, 1994; Schier et al., Gene, 169: 147-155, 1995; Yelton et al., J. Immunol., 155:1994-2004, 1995; Jackson et al., J. Immunol., 154(7):3310-9, 1995, Hawkins et al. , J. Mol. Biol., 226:889-896, 1992; and PCT Publication No. WO2004 / 058184).The following methods may be used for adjusting the affinity of an antibody and for characterizing a CDR. One way of characterizing a CDR of an antibody and / or altering (such as improving) the binding affinity of a polypeptide, such as an antibody, termed "library scanning mutagenesis". Generally, library scanning mutagenesis works as follows. One or more amino acid positions in the CDR are replaced with two or more (such as 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, or 20) amino acids using art recognized methods. This generates small libraries of clones (in some embodiments, one for every amino acid position that is analyzed), each with a complexity of two or more members (if two or more amino acids are substituted at every position). Generally, the library also includes a clone comprising the native (unsubstituted) amino acid. A small number of clones, e.g., about 20-80 clones (depending on the complexity of the library), from each library are screened for bindingaffinity to the target polypeptide (or other binding target), and candidates with increased, the same, decreased, or no binding are identified. Methods for determining binding affinity are well-known in the art. Binding affinity may be determined using Biacore™ surface plasmon resonance analysis, which detects differences in binding affinity of about 2-fold or greater. Biacore™ is particularly useful when the starting antibody already binds with a relatively high affinity, for example a KDof about 10 nM or lower. Screening using Biacore™ surface plasmon resonance is described in the Examples, herein.Binding affinity may be determined using Kinexa Biocensor, scintillation proximity assays, ELISA, ORIGEN immunoassay (IGEN), fluorescence quenching, fluorescence transfer, and / or yeast display. Binding affinity may also be screened using a suitable bioassay.In some embodiments, every amino acid position in a CDR is replaced (in some embodiments, one at a time) with all 20 natural amino acids using art recognized mutagenesis methods (some of which are described herein). This generates small libraries of clones (in some embodiments, one for every amino acid position that is analyzed), each with a complexity of 20 members (if all 20 amino acids are substituted at every position).In some embodiments, the library to be screened comprises substitutions in two or more positions, which may be in the same CDR or in two or more CDRs. Thus, the library may comprise substitutions in two or more positions in one CDR. The library may comprise substitution in two or more positions in two or more CDRs. The library may comprise substitution in 3, 4, 5, or more positions, said positions found in two, three, four, five or six CDRs. The substitution may be prepared using low redundancy codons. See, e.g., Table 2 of Balint et al., Gene 137(1 ): 109-18, 1993.The CDR may be CDRH3 and / or CDRL3. The CDR may be one or more of CDRL1 , CDRL2, CDRL3, CDRH1 , CDRH2, and / or CDRH3. The CDR may be a Kabat CDR, a Chothia CDR, or an extended CDR.Candidates with improved binding may be sequenced, thereby identifying a CDR substitution mutant which results in improved affinity (also termed an "improved" substitution). Candidates that bind may also be sequenced, thereby identifying a CDR substitution which retains binding.Multiple rounds of screening may be conducted. For example, candidates (each comprising an amino acid substitution at one or more position of one or more CDR) with improved binding are also useful for the design of a second library containing at least the original and substituted amino acid at each improved CDR position (i.e., amino acid position in the CDR at which a substitution mutant showed improved binding). Preparation, and screening or selection of this library is discussed further below.Library scanning mutagenesis also provides a means for characterizing a CDR, in so far as the frequency of clones with improved binding, the same binding, decreased binding or no binding also provide information relating to the importance of each amino acid position for the stability of the antibody-antigen complex. For example, if a position of the CDR retains binding when changed to all 20 amino acids, that position is identified as a position that is unlikely to be required for antigen binding. Conversely, if a position of CDR retains binding in only a small percentage of substitutions, that position is identified as a position that is important to CDR function. Thus, the library scanning mutagenesis methods generate information regarding positions in the CDRs that can be changed to many different amino acids (including all 20 amino acids), and positions in the CDRs which cannot be changed or which can only be changed to a few amino acids.Candidates with improved affinity may be combined in a second library, which includes the improved amino acid, the original amino acid at that position, and may further include additional substitutions at that position, depending on the complexity of the library that is desired, or permitted using the desired screening or selection method. In addition, if desired, adjacent amino acid position can be randomized to at least two or more amino acids. Randomization of adjacent amino acids may permit additional conformational flexibility in the mutant CDR, which may in turn, permit or facilitate the introduction of a larger number of improving mutations. The library may also comprise substitution at positions that did not show improved affinity in the first round of screening.The second library is screened or selected for library members with improved and / or altered binding affinity using any method known in the art, including screening using Biacore™ surface plasmon resonance analysis, and selection using any method known in the art for selection, including phage display, yeast display, and ribosome display.This invention also provides compositions comprising antibodies conjugated (for example, linked) to an agent that facilitate coupling to a solid support (such as biotin or avidin). For simplicity, reference will be made generally to antibodies with the understanding that these methods apply to any of the BCMA antibody embodiments described herein. Conjugation generally refers to linking these components as described herein. The linking (which is generally fixing these components in proximate association at least for administration) can be achieved in any number of ways. For example, a direct reaction between an agent and an antibody is possible when each possesses a substituent capable of reacting with the other. For example, a nucleophilic group, such as an amino or sulfhydryl group, on one may be capable of reacting with a carbonyl-containing group, such as an anhydride or an acid halide, or with an alkyl group containing a good leaving group (e.g., a halide) on the other.In another aspect, the invention provides a method of making any of the polynucleotides described herein.Polynucleotides complementarity to any such sequences are also encompassed by the present invention. Polynucleotides may be single-stranded (coding or antisense) or double-stranded, and may be DNA (genomic, cDNA or synthetic) or RNA molecules. RNA molecules include HnRNA molecules, which contain introns and correspond to a D...

Claims

ClaimsIt is claimed:

1. An isolated antibody, or an antigen binding fragment thereof, which specifically binds to B-Cell Maturation Antigen (BCMA), wherein the antibody comprises(a) a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one (CDR1 ) comprising the sequence SYX1MX2, wherein Xi is A or P; and X2is T, N , or S (SEQ ID NO: 301 ), GFTFXT SY, wherein X is G or S (SEQ ID NO: 302), or GFTFXT SYXSMXS, wherein X is G or S, X2is A or P; and X3is T, N , or S (SEQ ID NO: 303); (ii) a VH CDR2 comprising the sequence AX.iX2X3X4GX5X6X7XeYADX9X.i0KG, wherein X-, is I, V, T, H, L, A, or C; X2is S, D, G, T, I, L, F, M, or V; X3is G, Y, L, H, D, A, S, or M; X4is S, Q, T, A, F, or W; X5is G or T;X6is N, S, P, Y, W, or F; X7is S, T, I, L, T, A, R, V, K, G, or C; X8is F, Y, P, W, H, or G; X9is V, R, or L; and X1 0is G or T (SEQ ID NO: 305), or X1X2X3X4X5X6,wherein X is S, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M; X3is S, G, F, or W; X4is G or S; X5is G or T; and X6is N, S, P, Y, or W (SEQ ID NO: 306); and iii) a VH CDR3 comprising the sequence VSPIXiX2X3X4, wherein X is A or Y; X2is A or S; and X3is G, Q, L, P, or E (SEQ ID NO: 307), or YWPMX^,wherein X-, is D, S, T, or A; and X2is I, S, L, P, or D (SEQ ID NO: 308); and / or(b) a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequenceis R, G, W, A, or C; X2is A, P, G, L, C, or S; X3is S, G, or R; X4is Q, C, E, V, or I; X5is S, P, G, A, R, or D; X6is V, G, I, or L; X7is S, E, D, P, or G; X8is S, P, F, A, M, E, V, N, D, or Y; X9is I, T, V, E, S, A, M, Q, Y, H, R, or F; X1 0is Y or F; Xn is L, W, or P; and X12is A, S, or G (SEQ ID NO: 309); (ii) a VL CDR2 comprising the sequence X ASX2RAX3, wherein X is G or D; X2is S or I; and X3is T or P (SEQ ID NO: 310); and (iii) a VL CDR3 comprising the sequence QQYX-|X2X3PX4T, wherein X-i is G, Q, E, L, F, A, S, M, K, R, or Y; X2is S, R, T, G, V, F, Y, D, A, H, V, E, K, or C; X3is W, F, or S; and X4is L or I (SEQ ID NO: 31 1 ), or QQYX1X2X3PX4, wherein Xi is G, Q, E, L, F, A, S, M, R, K, or Y; X2is S, R, T, G, R, V, D, A, H, E, K, C, F, or Y; X3is W, S, or F; and X4is L or I (SEQ ID NO: 312).

2. An isolated antibody, or an antigen binding fragment thereof, which specifically binds to BCMA, wherein the antibody comprises: a VH region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 2, 3, 7, 8, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 35, 37, 39, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76,78, 83, 87, 92, 95, 97, 99, 101 , 104, 106, 1 10, 1 12, 1 14, 1 18, 120, 122, 125, 127, 313, 314, 363, or 365; and / or a VL region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 1 , 4, 5, 6, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 34, 36, 38, 40, 41 , 43, 45, 47, 49, 51 , 53, 55, 57, 59, 61 , 63, 65, 67, 69,71 , 73, 75, 77, 79, 317, 80, 81 , 82, 84, 85, 86, 88, 89, 90, 91 , 93, 94, 96, 98, 100, 102, 103, 105, 107, 108, 109, 1 1 1 , 1 13, 1 15, 1 16, 1 17, 1 19, 121 , 123, 124, 126, 128, 315, 316, or 364.

3. The antibody or the antigen binding fragment of claim 2, wherein the VH region comprises (i) a VH CDR1 comprising SEQ ID NO: 150, 151 , 152, 156, or 157; (ii) a VH CDR2 comprising SEQ ID NO: 169, 154, 194, 159, 195, 196, 162, 158, 198, 177, 178, 199, 200, 201 , 202, 203, 204, 206, 207, 208, 172, 203, or 204 ; and (iii) a VH CDR3 comprising SEQ ID NO: 155, 161 , 197, 205, or 164; and / or wherein the VL region comprises (i) a VL CDR1 comprising SEQ ID NO: 209, 271 , 273, 275, 251 , 277, 260, 279, 245, 283, 285, 287, 290, 292, 235, 297, or 299; (ii) a VL CDR2 comprising SEQ ID NO: 221 ; and (iii) a VL CDR3 comprising SEQ ID NO: 225, 272, 274, 276, 278, 280, 281 , 282, 284, 286, 288, 289, 291 , 293, 294, 229, 296, 298, or 300.

4. The antibody or the antigen binding fragment of claim 3, wherein the VH region comprises (i) a VH CDR1 comprising SEQ ID NO: 151 , 156, or 157; (ii) a VH CDR2 comprising SEQ ID NO: 158 or 159; and (iii) a VH CDR3 comprising SEQ ID NO: 155; and / or wherein the VL region comprises (i) a VL CDR1 comprising SEQ ID NO: 209; (ii) a VL CDR2 comprising SEQ ID NO: 221 ; and (iii) a VL CDR3 comprising SEQ ID NO: 225.

5. The antibody or the antigen binding fragment of claim 4, wherein the VH region comprises the sequence shown in SEQ ID NO: 1 12 or a variant with one orseveral conservative amino acid substitutions in residues that are not within a CDR and / or the VL region comprises the amino acid sequence shown in SEQ ID NO: 38 or a variant thereof with one or several amino acid substitutions in amino acids that are not within a CDR.

6. The antibody or the antigen binding fragment of claim 5, wherein the antibody comprises a light chain comprising the sequence shown in SEQ ID NO: 357 and a heavy chain comprising the sequence shown in SEQ ID NO: 358.

7. The antibody or the antigen binding fragment of claim 3, wherein the antibody comprises a VH region produced by the expression vector with ATCC Accession No. PTA-122094.

8. The antibody or the antigen binding fragment of claim 4, wherein the antibody comprises a VL region produced by the expression vector with ATCC Accession No. PTA-122093.

9. An isolated antibody which specifically binds to BCMA and competes with the antibody of any one of claims 4-6.

10. A pharmaceutical composition comprising a therapeutically effective amount of the antibody or antigen binding fragment of any one of claims 1 -9 and a pharmaceutically acceptable carrier.

11. An isolated polynucleotide comprising a nucleotide sequence encoding the antibody of any one of claims 1 -9.

12. A vector comprising the polynucleotide of claim 1 1.

13. An isolated host cell that recombinantly produces the antibody or the antigen binding fragment of any one of claims 1 -9.

14. A method of producing an antibody, comprising culturing the host cell of claim 13 under conditions that result in production of the antibody, and isolating the antibody from the host cell or culture.

15. A method of treating a condition associated with cells expressing BCMA in a subject comprising administering to a subject in need thereof an effective amount of the pharmaceutical composition of claim 10.

16. The method of claim 15, wherein the condition is a cancer.

17. The method of claim 16, wherein the cancer is a B-cell related cancer selecting from the group consisting of multiple myeloma, malignant plasma cell neoplasm, Hodgkin's lymphoma, nodular lymphocyte predominant Hodgkin's lymphoma, Kahler's disease and Myelomatosis, plasma cell leukemia, plasmacytoma, B-cell prolymphocytic leukemia, hairy cell leukemia, B-cell non-Hodgkin's lymphoma (NHL), acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), follicular lymphoma, Burkitt's lymphoma, marginal zone lymphoma, mantle cell lymphoma, large cell lymphoma, precursor B-lymphoblastic lymphoma, myeloid leukemia, Waldenstrom's macroglobulienemia, diffuse large B cell lymphoma, follicular lymphoma, marginal zone lymphoma, mucosa-associated lymphatic tissue lymphoma, small cell lymphocytic lymphoma, mantle cell lymphoma, Burkitt lymphoma, primary mediastinal (thymic) large B-cell lymphoma, lymphoplasmactyic lymphoma, Waldenstrom macroglobulinemia, nodal marginal zone B cell lymphoma, splenic marginal zone lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, lymphomatoid granulomatosis, T cell / histiocyte-rich large B-cell lymphoma, primary central nervous system lymphoma, primary cutaneous diffuse large B-cell lymphoma (leg type), EBV positive diffuse large B-cell lymphoma of the elderly, diffuse large B-cell lymphoma associated with inflammation, intravascular large B-cell lymphoma, ALK-positive large B-cell lymphoma, plasmablastic lymphoma, large B-cell lymphoma arising in HHV8-associated multicentric Castleman disease, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and Burkitt lymphoma, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and classical Hodgkin lymphoma, and other B-cell related lymphoma.

18. A method of inhibiting tumor growth or progression in a subject who has malignant cells expressing BCMA, comprising administering to the subject in needthereof an effective amount of the pharmaceutical composition of claim 10 to the subject.

19. A method of inhibiting metastasis of malignant cells expressing BCMA in a subject, comprising administering to the subject in need thereof an effective amount of the pharmaceutical composition of claim 10 to the subject.

20. A method of inducing tumor regression in a subject who has malignant cells expressing BCMA, comprising administering to the subject in need thereof an effective amount of the pharmaceutical composition of claim 10 to the subject.

21. The method of claim 15, wherein the condition is an autoimmune disorder.

22. The method of claim 21 , wherein the autoimmune disorder is systemic lupus erythematosus or rheumatoid arthritis.

23. An isolated antibody, or an antigen binding fragment thereof, which specifically binds to CD3, wherein the antibody comprises a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399.

24. The antibody or the antigen binding fragment of claim 23, wherein the antibody comprises a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 324 or 388; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 323 or 387.

25. The antibody or the antigen binding fragment of claim 23, wherein the VH region comprises (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 4 4, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising thesequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453.

26. The antibody or the antigen binding fragment of claim 25, wherein the VH region comprises (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 407, or 408 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 336, 404, 405, or 417; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335 or 406; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 343 or 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342 or 439.

27. An isolated antibody which specifically binds to CD3 and competes with the antibody of claim 23.

28. A pharmaceutical composition comprising the antibody of any one of claims 23 to 26.

29. An isolated polynucleotide comprising a nucleotide sequence encoding the antibody of any one of claims 23 to 26.

30. A vector comprising the polynucleotide of claim 29.

31. An isolated host cell that recombinantly produces the antibody or the antigen binding fragment of any one of claims 23 to 26.

32. A method of producing an antibody, comprising culturing the host cell of claim 31 under conditions that result in production of the antibody, and isolating the antibody from the host cell or culture.

33. A bispecific antibody wherein the bispecific antibody is a full-length human antibody, comprising a first antibody variable domain of the bispecific antibody capable of recruiting the activity of a human immune effector cell by specifically binding to aneffector antigen located on the human immune effector cell, and comprising a second antibody variable domain of the bispecific antibody capable of specifically binding to a target antigen, wherein the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 320, 322, 324, 326, 328, 330, 345, 347, 349, 351 , 444, 354, 356, 378, 442, 380, 382, 384 386, 388, 390, 392, 394, 396, 398, or 400; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 319, 321 , 323, 325, 327, 329, 344, 346, 348, 350, 352, 355, 377, 443, 445, 379, 381 , 383, 385, 387, 389, 391 , 393, 395, 397, or 399.

34. The bispecific antibody of claim 33, wherein the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 414, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453.

35. The bispecific antibody of claim 34, wherein the first antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 324 or 388; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 323 or 387; and the second antibody variable domain comprises a heavy chain variable (VH) region comprising a VH CDR1 , VH CDR2, and VH CDR3 of the VH sequence shown in SEQ ID NO: 1 12; and / or a light chain variable (VL) region comprising VL CDR1 , VL CDR2, and VL CDR3 of the VL sequence shown in SEQ ID NO: 38.

36. A bispecific antibody wherein the bispecific antibody is a full-length human antibody, comprising a first antibody variable domain of the bispecific antibody capableof recruiting the activity of a human immune effector cell by specifically binding to an effector antigen located on the human immune effector cell, and comprising a second antibody variable domain of the bispecific antibody capable of specifically binding to a target antigen, wherein the first antibody variable domain comprisesa. a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one (CDR1 ) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 402, 403, 407, 408, 415, 416, 418, 419, 420, 424, 425, 426, 446, 447, or 448 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 334, 336, 337, 338, 339, 404, 405, 409, 410, 41 1 , 412, 413, 414, 417, 418, 421 , 422, 427, 428, 449, or 450; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335, 406, 423, 429, or 451 ; and / orb. a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 340, 343, 430, 431 , 435, or 440, 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 , 433, 452, or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342, 432, 434, 437, 438, 439, 446, or 453.

37. The bispecific antibody of claim 36, wherein the second antibody variable domain comprisesa. a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one (CDR1 ) comprising the sequence SYXiMX2, wherein X-, is A or P; and X2is T, N, or S (SEQ ID NO: 301 ), GFTFXT SY, wherein X is G or S (SEQ ID NO: 302), or GFTFXT SYXSMXS, wherein X is G or S, X2is A or P; and X3is T, N, or S (SEQ ID NO: 303); (ii) a VH CDR2 comprising the sequencewherein X-, is I, V, T, H, L, A, or C; X2is S, D, G, T, I, L, F, M, or V; X3is G, Y, L, H, D, A, S, or M; X4is S, Q, T, A, F, or W; X5is G or T;X6is N, S, P, Y, W, or F; X7is S, T, I, L, T, A, R, V, K, G, or C; X8is F, Y, P, W, H, or G; X9is V, R, or L; and X10is G or T (SEQ ID NO: 305), or X^XsX^sXe, wherein Xi is S, V, I, D, G, T, L, F, or M; X2is G, Y, L, H, D, A, S, or M; X3is S, G, F, or W; X4is G or S; X5is G or T; and X6is N, S, P, Y, or W (SEQ ID NO: 306); and iii) a VH CDR3 comprising the sequenceVSPIXiX2X3X4wherein is A or Y; X2is A or S; and X3is G, Q, L, P, or E (SEQ ID NO: 307), or YWPMX1X2, wherein Xi is D, S, T, or A; and X2is I, S, L, P, or D (SEQ ID NO: 308); and / orb. a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence XiX2X3X4X5X6X7X8X9XioXnXi2, wherein Xi is R, G, W, A, or C;X2is A, P, G, L, C, or S; X3is S, G, or R; X4is Q, C, E, V, or I; X5is S, L, P, G, A, R, or D; X6is V, G, or I; X7is S, E, D, or P; X8is S, P, F, A, M, E, V, N, D, or Y; X9is I, T, V, E, S, A, M, Q, Y, H, or R; X0is Y or F; Xn is L, W, or P; and X12is A, S, or G (SEQ ID NO: 309); (ii) a VL CDR2 comprising the sequence XiASX2RAX3, wherein Xi is G or D; X2is S or I; and X3is T or P (SEQ ID NO: 310); and (iii) a VL CDR3 comprising the sequence QQYX^XsPX^, wherein is G, Q, E, L, F, A, S, M, K, R, or Y; X2is S, R, T, G, V, F, Y, D, A, H, V, E, K, or C; X3is W, F, or S; and X4is L or I (SEQ ID NO: 31 1 ), or QQYX1X2X3PX4, wherein Χτ is G, Q, E, L, F, A, S, M, R, K, or Y; X2is S, R, T, G, R, V, D, A, H, E, K, C, F, or Y; X3isW, S, or F; and X4is L or I (SEQ ID NO: 312).

38. The bispecific antibody of claim 36, wherein the second antibody variable domain comprises a heavy chain variable (VH) region comprising (i) a VH CDR1 comprising the sequence shown in SEQ ID NO: 150, 151 , 152, 156, 157, 348, 349, 353, 354, or 355; (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 169, 154, 194, 159, 195, 196, 162, 158, 198, 177, 178, 199, 200, 201 , 202, 203, 204, 206, 207, 208, 172, 203, 204, 350, 351 , 356 or 357; and (iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 155, 161 , 197, 205,164, or 352, or 358; and / or wherein the light chain variable (VL) region comprises (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 209, 271 , 273, 275, 251 , 277, 260, 279, 245, 283, 285, 287, 290, 292, 235,297, 299, or 361 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 221 , 359 or 362; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 21 1 , 225, 272, 274, 276, 278, 280, 281 , 282, 284, 286, 288, 289, 291 , 293, 294, 229, 296,298, 300 or 360.

39. The bispecific antibody of claim 38, wherein thea. first antibody variable domain comprises a heavy chain variable (VH) region comprising (i) a VH complementarity determining region one(CDR1) comprising the sequence shown in SEQ ID NO: 331 , 332, 333, 401 , 407, or 408 (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 336, 417, 404, or 405; and iii) a VH CDR3 comprising the sequence shown in SEQ ID NO: 335 or 406; and / or a light chain variable (VL) region comprising (i) a VL CDR1 comprising the sequence shown inSEQ ID NO: 343 or 441 ; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 341 or 436; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 342 or 439; and theb. the second antibody variable domain comprises a heavy chain VH region comprising a heavy chain variable (VH) region comprising (i) a VH CDR1 comprising the sequence shown in SEQ ID NO: 151 , 156, or 157; (ii) a VH CDR2 comprising the sequence shown in SEQ ID NO: 158 OR 159; and (iii) a VH CDR3 comprising SEQ ID NO: 155; and / or wherein the light chain variable (VL) region comprises (i) a VL CDR1 comprising the sequence shown in SEQ ID NO: 209; (ii) a VL CDR2 comprising the sequence shown in SEQ ID NO: 221 ; and (iii) a VL CDR3 comprising the sequence shown in SEQ ID NO: 225.

40. The bispecific antibody of any one of claims 33-39, wherein both the first and the second antibody variable domains of the heterodimeric protein comprise amino acid modifications at positions 223, 225, and 228 in the hinge region and at position 409 or 368 (EU numbering scheme) in the CH3 region of a human lgG2 (SEQ ID NO: 493).

41. The bispecific antibody of claim 40, further comprising an amino acid modification at position 265 of the human lgG2.

42. A nucleic acid encoding the antibody of any one of claims 33-41.

43. A vector comprising the nucleic acid of claim 42.

44. A host cell comprising the nucleic acid of claim 42 or the vector of claim 43.

45. The bispecific antibody of any one of claims 33-41 for use as a medicament.

46. The bispecific antibody of claim 45, wherein the medicament is for use in treatment of a B-cell related cancer selecting from the group consisting of multiple myeloma, malignant plasma cell neoplasm, Hodgkin's lymphoma, nodular lymphocyte predominant Hodgkin's lymphoma, Kahler's disease and Myelomatosis, plasma cellleukemia, plasmacytoma, B-cell prolymphocyte leukemia, hairy cell leukemia, B-cell non-Hodgkin's lymphoma (NHL), acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), follicular lymphoma, Burkitt's lymphoma, marginal zone lymphoma, mantle cell lymphoma, large cell lymphoma, precursor B-lymphoblastic lymphoma, myeloid leukemia, Waldenstrom's macroglobulienemia, diffuse large B cell lymphoma, follicular lymphoma, marginal zone lymphoma, mucosa-associated lymphatic tissue lymphoma, small cell lymphocytic lymphoma, mantle cell lymphoma, Burkitt lymphoma, primary mediastinal (thymic) large B-cell lymphoma, lymphoplasmactyic lymphoma, Waldenstrom macroglobulinemia, nodal marginal zone B cell lymphoma, splenic marginal zone lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, lymphomatoid granulomatosis, T cell / histiocyte-rich large B-cell lymphoma, primary central nervous system lymphoma, primary cutaneous diffuse large B-cell lymphoma (leg type), EBV positive diffuse large B-cell lymphoma of the elderly, diffuse large B-cell lymphoma associated with inflammation, intravascular large B-cell lymphoma, ALK-positive large B-cell lymphoma, plasmablastic lymphoma, large B-cell lymphoma arising in HHV8-associated multicentric Castleman disease, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and Burkitt lymphoma, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and classical Hodgkin lymphoma, and other B-cell related lymphoma.

47. A method of treating a B-cell related cancer in a subject in need thereof comprising:a. providing the bispecific antibody according to any one of claims 33-41 ; andb. administering said bispecific antibody to said patient.

48. A pharmaceutical composition comprising the bispecific antibody of any one of claims 33-41.

49. A method of treating a condition associated with malignant cells expressing a tumor antigen in a subject comprising administering to the subject in need thereof an effective amount of the pharmaceutical composition of claim 48.

50. The method of claim 49, wherein the condition is a cancer.

51. The method of claim 50, wherein the cancer is a B-cell related cancer selecting from the group consisting of multiple myeloma, malignant plasma cell neoplasm, Hodgkin's lymphoma, nodular lymphocyte predominant Hodgkin's lymphoma, Kahler's disease and Myelomatosis, plasma cell leukemia, plasmacytoma, B-cell prolymphocytic leukemia, hairy cell leukemia, B-cell non-Hodgkin's lymphoma (NHL), acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), follicular lymphoma, Burkitt's lymphoma, marginal zone lymphoma, mantle cell lymphoma, large cell lymphoma, precursor B- lymphoblastic lymphoma, myeloid leukemia, Waldenstrom's macroglobulienemia, diffuse large B cell lymphoma, follicular lymphoma, marginal zone lymphoma, mucosa- associated lymphatic tissue lymphoma, small cell lymphocytic lymphoma, mantle cell lymphoma, Burkitt lymphoma, primary mediastinal (thymic) large B-cell lymphoma, lymphoplasmactyic lymphoma, Waldenstrom macroglobulinemia, nodal marginal zone B cell lymphoma, splenic marginal zone lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, lymphomatoid granulomatosis, T cell / histiocyte- rich large B-cell lymphoma, primary central nervous system lymphoma, primary cutaneous diffuse large B-cell lymphoma (leg type), EBV positive diffuse large B-cell lymphoma of the elderly, diffuse large B-cell lymphoma associated with inflammation, intravascular large B-cell lymphoma, ALK-positive large B-cell lymphoma, plasmablastic lymphoma, large B-cell lymphoma arising in HHV8-associated multicentric Castleman disease, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and Burkitt lymphoma, B-cell lymphoma unclassified with features intermediate between diffuse large B-cell lymphoma and classical Hodgkin lymphoma, and other B-cell related lymphoma.

52. A method of inhibiting tumor growth or progression in a subject who has malignant cells expressing BCMA, comprising administering to the subject in need thereof an effective amount of the pharmaceutical composition comprising the bispecific antibody of any one of claims 37-41 to the subject.

53. A method of inhibiting metastasis of malignant cells expressing BCMA in a subject, comprising administering to the subject in need thereof an effective amount ofthe pharmaceutical composition comprising the bispecific antibody of any one of claims 37-41 to the subject.

54. A method of inducing tumor regression in a subject who has malignant cells expressing BCMA, comprising administering to the subject in need thereof an effective amount of the pharmaceutical composition comprising the bispecific antibody of any one of claims 37-41 to the subject.

55. A method of treating multiple myeloma in a subject in need thereof, comprising administering to the subject an effective amount of the pharmaceutical composition comprising the bispecific antibody of any one of claims 37-41 to the subject and one or more other therapeutic agent selecting from the group consisting of bortezomib, lenalidomide, carfilzomib, and doxorubicin.

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