VANHOOREN VALERIE (ES)
DE FRIAS SÁNCHEZ MERCÈ (ES)
MORANCHO ARMISEN BEATRIZ (ES)
GUARDIOLA BAGÁN SALVADOR (ES)
GEOFFREY HALE (GB)
WILKINSON IAN (GB)
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CLAIMS 1. An isolated antibody that binds to CD36, which comprises a light chain CDR1 region, a light chain CDR2 region, a light chain CDR3 region, a heavy chain CDR1 region, a heavy chain CDR2 region, and a heavy chain CDR3 region, wherein: the heavy chain CDR1 region comprises a sequence selected from the group consisting of SEQ ID NOs: 85-105; the heavy chain CDR2 region comprises a sequence selected from the group consisting of SEQ ID NOs: 106-132, or 248; the heavy chain CDR3 region comprises a sequence selected from the group consisting of SEQ ID NOs: 133-158; the light chain CDR1 region comprises a sequence selected from the group consisting of SEQ ID NOs: 159-172; the light chain CDR2 region comprises a sequence selected from the group consisting of SEQ ID NOs: 173-185, or 246; and the light chain CDR3 region comprises a sequence selected from the group consisting of SEQ ID NOs: 186-206, or 247. 2. The isolated antibody of claim 1, wherein the antibody is a chimeric antibody. 3. The isolated antibody of claim 1, wherein the antibody is a humanized antibody. 4. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 85, the heavy chain CDR2 region comprises SEQ ID NO: 106, the heavy chain CDR3 region comprises SEQ ID NO: 133, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 186. 5. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 86, the heavy chain CDR2 region comprises SEQ ID NO: 107, the heavy chain CDR3 region comprises SEQ ID NO: 134, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 6. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 86, the heavy chain CDR2 region comprises SEQ ID NO: 108, the heavy chain CDR3 region comprises SEQ ID NO: 135, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 188. 7. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 87, the heavy chain CDR2 region comprises SEQ ID NO: 109, the heavy chain CDR3 region comprises SEQ ID NO: 136, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 8. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 88, the heavy chain CDR2 region comprises SEQ ID NO: 110, the heavy chain CDR3 region comprises SEQ ID NO: 137, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 9. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 89, the heavy chain CDR2 region comprises SEQ ID NO: 111, the heavy chain CDR3 region comprises SEQ ID NO: 138, the light chain CDR1 region comprises SEQ ID NO: 161, the light chain CDR2 region comprises SEQ ID NO: 175, and the light chain CDR3 region comprises SEQ ID NO: 189. 10. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 112, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 11. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 91, the heavy chain CDR2 region comprises SEQ ID NO: 113, the heavy chain CDR3 region comprises SEQ ID NO: 140, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 12. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 92, the heavy chain CDR2 region comprises SEQ ID NO: 114, the heavy chain CDR3 region comprises SEQ ID NO: 141, the light chain CDR1 region comprises SEQ ID NO: 162, the light chain CDR2 region comprises SEQ ID NO: 176, and the light chain CDR3 region comprises SEQ ID NO: 191. 13. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 93, the heavy chain CDR2 region comprises SEQ ID NO: 115, the heavy chain CDR3 region comprises SEQ ID NO: 142, the light chain CDR1 region comprises SEQ ID NO: 163, the light chain CDR2 region comprises SEQ ID NO: 177, and the light chain CDR3 region comprises SEQ ID NO: 192. 14. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 94, the heavy chain CDR2 region comprises SEQ ID NO: 116, the heavy chain CDR3 region comprises SEQ ID NO: 143, the light chain CDR1 region comprises SEQ ID NO: 164, the light chain CDR2 region comprises SEQ ID NO: 175, and the light chain CDR3 region comprises SEQ ID NO: 193. 15. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 117, the heavy chain CDR3 region comprises SEQ ID NO: 144, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 16. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 118, the heavy chain CDR3 region comprises SEQ ID NO: 145, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 17. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 119, the heavy chain CDR3 region comprises SEQ ID NO: 146, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 18. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 194. 19. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 148, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 20. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 186. 21. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 196. 22. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 23. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 97, the heavy chain CDR2 region comprises SEQ ID NO: 122, the heavy chain CDR3 region comprises SEQ ID NO: 149, the light chain CDR1 region comprises SEQ ID NO: 165, the light chain CDR2 region comprises SEQ ID NO: 178, and the light chain CDR3 region comprises SEQ ID NO: 197. 24. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 97, the heavy chain CDR2 region comprises SEQ ID NO: 123, the heavy chain CDR3 region comprises SEQ ID NO: 150, the light chain CDR1 region comprises SEQ ID NO: 165, the light chain CDR2 region comprises SEQ ID NO: 178, and the light chain CDR3 region comprises SEQ ID NO: 197. 25. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 98, the heavy chain CDR2 region comprises SEQ ID NO: 124, the heavy chain CDR3 region comprises SEQ ID NO: 151, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 198. 26. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 27. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 91, the heavy chain CDR2 region comprises SEQ ID NO: 125, the heavy chain CDR3 region comprises SEQ ID NO: 152, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 28. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 99, the heavy chain CDR2 region comprises SEQ ID NO: 126, the heavy chain CDR3 region comprises SEQ ID NO: 133, the light chain CDR1 region comprises SEQ ID NO: 162, the light chain CDR2 region comprises SEQ ID NO: 176, and the light chain CDR3 region comprises SEQ ID NO: 199. 29. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 100, the heavy chain CDR2 region comprises SEQ ID NO: 127, the heavy chain CDR3 region comprises SEQ ID NO: 153, the light chain CDR1 region comprises SEQ ID NO: 166, the light chain CDR2 region comprises SEQ ID NO: 179, and the light chain CDR3 region comprises SEQ ID NO: 200. 30. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 101, the heavy chain CDR2 region comprises SEQ ID NO: 128, the heavy chain CDR3 region comprises SEQ ID NO: 154, the light chain CDR1 region comprises SEQ ID NO: 167, the light chain CDR2 region comprises SEQ ID NO: 180, and the light chain CDR3 region comprises SEQ ID NO: 201. 31. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 101, the heavy chain CDR2 region comprises SEQ ID NO: 128, the heavy chain CDR3 region comprises SEQ ID NO: 154, the light chain CDR1 region comprises SEQ ID NO: 168, the light chain CDR2 region comprises SEQ ID NO: 181, and the light chain CDR3 region comprises SEQ ID NO: 202. 32. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 102, the heavy chain CDR2 region comprises SEQ ID NO: 129, the heavy chain CDR3 region comprises SEQ ID NO: 155, the light chain CDR1 region comprises SEQ ID NO: 169, the light chain CDR2 region comprises SEQ ID NO: 182, and the light chain CDR3 region comprises SEQ ID NO: 203. 33. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 103, the heavy chain CDR2 region comprises SEQ ID NO: 130, the heavy chain CDR3 region comprises SEQ ID NO: 156, the light chain CDR1 region comprises SEQ ID NO: 170, the light chain CDR2 region comprises SEQ ID NO: 183, and the light chain CDR3 region comprises SEQ ID NO: 204. 34. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 104, the heavy chain CDR2 region comprises SEQ ID NO: 131, the heavy chain CDR3 region comprises SEQ ID NO: 157, the light chain CDR1 region comprises SEQ ID NO: 171, the light chain CDR2 region comprises SEQ ID NO: 184, and the light chain CDR3 region comprises SEQ ID NO: 205. 35. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 105, the heavy chain CDR2 region comprises SEQ ID NO: 132, the heavy chain CDR3 region comprises SEQ ID NO: 158, the light chain CDR1 region comprises SEQ ID NO: 172, the light chain CDR2 region comprises SEQ ID NO: 185, and the light chain CDR3 region comprises SEQ ID NO: 206. 36. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 248, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO:160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 247. 37. The antibody of any one of claims 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 248, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO:160, the light chain CDR2 region comprises SEQ ID NO: 246, and the light chain CDR3 region comprises SEQ ID NO: 247. 38. The antibody of claim 1 or claim 2, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region has at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the amino acid sequence of at least one of SEQ ID NOs: 13-44, 241, or 243; and wherein the light chain variable region has at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the amino acid sequence of at least one of SEQ ID NOs: 45-78, 240, 242, 244, or 245. 39. The antibody of claim 38, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises a sequence selected from the group consisting of SEQ ID NOs: 13-44, 241, and 243; and wherein the light chain variable region comprises a sequence selected from the group consisting of SEQ ID NOs: 45-78, 240, 242, 244, and 245. 40. The antibody of claim 39, wherein: v. the heavy chain variable region comprises SEQ ID NO: 13 and the light chain variable region comprises SEQ ID NO: 45; vi. the heavy chain variable region comprises SEQ ID NO: 14 and the light chain variable region comprises SEQ ID NO: 46; vii. the heavy chain variable region comprises SEQ ID NO: 15 and the light chain variable region comprises SEQ ID NO: 47; viii. the heavy chain variable region comprises SEQ ID NO: 16 and the light chain variable region comprises SEQ ID NO: 48; ix. the heavy chain variable region comprises SEQ ID NO: 17 and the light chain variable region comprises SEQ ID NO: 49; x. the heavy chain variable region comprises SEQ ID NO: 18 and the light chain variable region comprises SEQ ID NO: 50; xi. the heavy chain variable region comprises SEQ ID NO: 19 and the light chain variable region comprises SEQ ID NO: 51; xii. the heavy chain variable region comprises SEQ ID NO: 20 and the light chain variable region comprises SEQ ID NO: 52; xiii. the heavy chain variable region comprises SEQ ID NO: 21 and the light chain variable region comprises SEQ ID NO: 53; xiv. the heavy chain variable region comprises SEQ ID NO: 22 and the light chain variable region comprises SEQ ID NO: 54; xv. the heavy chain variable region comprises SEQ ID NO: 23 and the light chain variable region comprises SEQ ID NO: 55; xvi. the heavy chain variable region comprises SEQ ID NO: 24 and the light chain variable region comprises SEQ ID NO: 56; xvii. the heavy chain variable region comprises SEQ ID NO: 25 and the light chain variable region comprises SEQ ID NO: 57; xviii. the heavy chain variable region comprises SEQ ID NO: 26 and the light chain variable region comprises SEQ ID NO: 58; xix. the heavy chain variable region comprises SEQ ID NO: 26 and the light chain variable region comprises SEQ ID NO: 59; xx. the heavy chain variable region comprises SEQ ID NO: 27 and the light chain variable region comprises SEQ ID NO: 60; xxi. the heavy chain variable region comprises SEQ ID NO: 28 and the light chain variable region comprises SEQ ID NO: 61; xxii. the heavy chain variable region comprises SEQ ID NO: 29 and the light chain variable region comprises SEQ ID NO: 62; xxiii. the heavy chain variable region comprises SEQ ID NO: 30 and the light chain variable region comprises SEQ ID NO: 63; xxiv. the heavy chain variable region comprises SEQ ID NO: 31 and the light chain variable region comprises SEQ ID NO: 64; xxv. the heavy chain variable region comprises SEQ ID NO: 32 and the light chain variable region comprises SEQ ID NO: 65; xxvi. the heavy chain variable region comprises SEQ ID NO: 33 and the light chain variable region comprises SEQ ID NO: 66; xxvii. the heavy chain variable region comprises SEQ ID NO: 34 and the light chain variable region comprises SEQ ID NO: 67; xxviii. the heavy chain variable region comprises SEQ ID NO: 35 and the light chain variable region comprises SEQ ID NO: 68; xxix. the heavy chain variable region comprises SEQ ID NO: 36 and the light chain variable region comprises SEQ ID NO: 69; xxx. the heavy chain variable region comprises SEQ ID NO: 37 and the light chain variable region comprises SEQ ID NO: 70; xxxi. the heavy chain variable region comprises SEQ ID NO: 38 and the light chain variable region comprises SEQ ID NO: 71; xxxii. the heavy chain variable region comprises SEQ ID NO: 39 and the light chain variable region comprises SEQ ID NO: 72; xxxiii. the heavy chain variable region comprises SEQ ID NO: 40 and the light chain variable region comprises SEQ ID NO: 73; xxxiv. the heavy chain variable region comprises SEQ ID NO: 40 and the light chain variable region comprises SEQ ID NO: 74; xxxv. the heavy chain variable region comprises SEQ ID NO: 41 and the light chain variable region comprises SEQ ID NO: 75; xxxvi. the heavy chain variable region comprises SEQ ID NO: 42 and the light chain variable region comprises SEQ ID NO: 76; xxxvii. the heavy chain variable region comprises SEQ ID NO: 43 and the light chain variable region comprises SEQ ID NO: 77; xxxviii. the heavy chain variable region comprises SEQ ID NO: 44 and the light chain variable region comprises SEQ ID NO: 78; xxxix. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 240; xl. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 240; xli. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 242; xlii. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 242; xliii. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 244; xliv. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 244; xlv. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 245; or xlvi. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 245. 41. The antibody of any one of claims 1 to 40, wherein the antibody binds to human CD36. 42. The antibody of claim 41, wherein the antibody specifically binds to human CD36. 43. The antibody of claim 41, wherein the antibody has cross-reactivity to human CD36 and non-human CD36. 44. The antibody of claim 43, wherein the antibody has cross-reactivity to human CD36 and non-human primate CD36. 45. The antibody of claim 44, wherein the non-human primate CD36 is cynomomolgus CD36 or rhesus macaque CD36. 46. The antibody of claim 44, wherein the antibody has cross-reactivity to human CD36, non- human primate CD36, and rodent CD36. 47. The antibody of claim 46, wherein the rodent CD36 is mouse CD36 or rat CD36. 48. The antibody of claim 41, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 145A, 146S, 147H, 148I, 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q, 156M, 157I, 158L, 159N, 160S, 185P, 186F, 187L, 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T, 197T, 198V, 199G, 398K, 399I, 400Q, 401V, 402L, 403K, 404N, 405L, 406K, 407R, 408N, 409Y, 410I, 411V, 412P, 413I, and 414L. 49. The antibody of claim 48, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q, 156M,188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T, 400Q, 401V, 402L, 403K. 50. The antibody of claim 49, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 152Q, 192Y, and 406K. 51. The antibody of claim 48, wherein the antibody binds to an epitope comprising 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q and 156M. 52. The antibody of claim 48, wherein the antibody binds to an epitope comprising 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T. 53. The antibody of claim 48, wherein the antibody binds to an epitope comprising 400Q, 401V, 402L, and 403K . 54. The antibody of claim 41, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 280E, 281S, 282D, 283V, 284N, 285L, 286K, 287G, 288I, 289P, 290V, 291Y, 292R, 293F, 294V, 295L, 296P, 297S, 298K, 341I, 342S, 343L, 344P, 345H, 346F, 347L, 348Y, 349A, 350S, 351P, 352D, 353V, 354S, 355E, 356P, 357I, 358D, 359G, 360L, 361N, 362P, 363n, 364E, 365E. 55. The antibody of claim 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 286K, 287G, 288I, 289P, 290V, 291Y, and 292R. 56. The antibody of claim 55, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 288I, 289P, 290V, 402D, 403V, and 404S. 57. The antibody of claim 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 286K, 287G, 288I, 289P, 290V, 292Y, and 292R. 58. The antibody of claim 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of399A, 400S, 401P, 402D, 403V, 404S, 405E, 406P, and 407I. 59. The antibody of any one of claims 1 to 58, wherein the antibody binds to human CD36 with a KD of less than 20 nM, as measured using surface plasmon resonance with a bivalent model 60. The antibody of claim 59, wherein the antibody binds to human CD36 with a KD of less than 10 nM, as measured using surface plasmon resonance with a bivalent model. 61. The antibody of any one of claims 1 to 60, which further comprises a heavy chain constant region. 62. The antibody of claim 61, wherein the heavy chain constant region is selected from the group consisting of human immunoglobulin IgA1, IgA2, IgG1, IgG2, IgG3, or IgG4 heavy chain constant regions. 63. The antibody of claim 62, which comprises an IgG1 heavy chain constant region. 64. The antibody of embodiment 62, wherein the heavy chain constant region comprises an IgG constant region containing at least one amino acid substitution, wherein the at least one amino acid substitution results in reduced binding to at least one Fcγ receptor and reduced or dampened Fc effector function. 65. The antibody of embodiment 64, wherein the at least one Fc silencing mutation includes the amino acid substitutions L234A and L235A ("LALA"). 66. The antibody of embodiment 64, wherein the at least one Fc silencing mutation includes a set of amino acid substitutions selected from the group consisting of L234G, L235S, and G236R; L234S, L235T, and G236R; L234S, L235V, and G236R; L234T, L235Q, and G236R; L234T, L235T, and G236R; L234A and L235A; and L234A, L235A, and P329G. 67. The antibody of claim 62, which comprises an IgG4 heavy chain constant region. 68. The antibody of claim 66, wherein the heavy chain constant region comprises an IgG constant region containing the amino acid substitution S228P. 69. The antibody of any one of claims 1 to 68, wherein the antibody further comprises a light chain constant region. 70. The antibody of claim 69, wherein the light chain constant region is selected from the group consisting of human immunoglobulins κ and λ light chain constant regions. 71. The antibody of any one of claims 1 to 70, wherein the antibody further comprises a heavy chain constant region and a light chain constant region, wherein the heavy chain constant region is a human IgG1 heavy chain constant region, and wherein the light chain constant region is a human κ light chain constant region. 72. The antibody of any one of claims 1 to 71, wherein the antibody is a bispecific antibody. 73. The antibody of claim 72, comprising a first antigen-binding region that specifically binds to CD36. 74. The antibody of claim 73, comprising a second antigen-binding region that specifically binds to an immune cell antigen. 75. The antibody of claim 74, wherein the immune cell antigen is selected from the group consisting of PD-1, PD-L1, CTLA4, CD3, LAG3, OX40, CD28, CD33, B7H3, CD47, TIM3, ICOS, LGR5, 4-1BB, CD40, CD40-L, and TIGIT. 76. The antibody of claim 73, comprising a second antigen-binding region that specifically binds to a tumor-specific antigen. 77. The antibody of claim 76, wherein the tumor-specific antigen is selected from the group consisting of HER2, HER3, EGFR, VEGF, IGF-1, IGF-2, ANG2, DLL1, IGF-1R, cMET, DLL4, FAP, DR5, IL15, IL15Ra, CD3, CEA, EPCAM, HER3, PSMA, PMEL, and GPC3. 78. The antibody of claim 75 or 76, wherein the immune cell antigen or tumor-specific antigen is CD3. 79. The antibody of claim 73, wherein the antibody is a biparatopic antibody. 80. The antibody of claim 79, comprising two antigen-binding regions, wherein each antigen- binding region specifically binds to a unique, non-overlapping CD36 epitope. 81. The antibody of claim 80, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04. 82. The antibody of claim 81, further comprising a second antigen-binding domain, which comprises an antigen-binding domain of an antibody selected from the group consisting of 10G04, 11G04, 19G04, 20G04, and 30G04. 83. The antibody of any one of claims 80-82, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04, and a second antigen-binding domain, which comprises an antigen-binding domain of 11G04. 84. The antibody of any one of claims 1-71, which is an antigen binding fragment. 85. The antigen binding fragment of claim 84, wherein the antigen binding fragment comprises a Fab, Fab', F(ab')2, single chain Fv (scFv), disulfide linked Fv, V-NAR domain, IgNar, intrabody, IgGΔCH2, minibody, F(ab')3, tetrabody, triabody, diabody, single-domain antibody, DVD-Ig, Fcab, mAb2, (scFv)2, or scFv-Fc. 86. A pharmaceutical composition comprising the antibody of any one of claims 1 to 85 and a pharmaceutically acceptable excipient. 87. The pharmaceutical composition of claim 86, wherein at least 95% of the antibodies in the composition are afucosylated. 88. The pharmaceutical composition of claim 86 or claim 87, which further comprises a PD-1 inhibitor. 89. The pharmaceutical composition of claim 88, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 90. The pharmaceutical composition of claim 89, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 91. The pharmaceutical composition of any one of claims 86 to 90, which further comprises a PD-L1 inhibitor. 92. The pharmaceutical composition of claim 91, wherein the PD-L1 inhibitor is an anti-PD- L1 antibody. 93. The pharmaceutical composition of claim 92, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 94. The pharmaceutical composition of any one of claims 86 to 93, which further comprises a CTLA-4 inhibitor. 95. The pharmaceutical composition of claim 94, wherein the CTLA-4 inhibitor is an anti- CTLA-4 antibody. 96. The pharmaceutical composition of claim 95, wherein the anti-CTLA-4 antibody is ipilimumab. 97. The pharmaceutical composition of any one of claims 86-96, wherein the composition further comprises a chemotherapeutic agent. 98. The pharmaceutical composition of claim 87, wherein the chemotherapeutic agent is cisplatin. 99. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 100. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the anti- CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 101. The method of claim 99 or claim 100, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma melanoma, leukemia, or lymphoma. 102. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 103. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 104. The method of any one of claims 99 to 103, wherein the anti-CD36 antibody is the antibody of any one of claims 1 to 85. 105. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of claims 1 to 72, or a therapeutically effective amount of the pharmaceutical composition of any one of claims 86 to 98. 106. The method of claim 105, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma, melanoma, leukemia, or lymphoma. 107. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of claims 1 to 85, or a therapeutically effective amount of the pharmaceutical composition of any one of claims 86 to 98. 108. The method of claim 102 or claim 107, wherein the metastatic tumors are metastatic oral squamous cell carcinoma, metastatic head and neck cancer, metastatic esophageal cancer, metastatic gastric cancer, metastatic ovarian cancer, metastatic cervical cancer, metastatic lung cancer, metastatic breast cancer, metastatic colon cancer, metastatic renal cancer, metastatic prostate cancer, metastatic sarcoma, metastatic liposarcoma, metastatic melanoma, metastatic leukemia, or metastatic lymphoma. 109. The method of any one of claims 99 to 108, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 110. The method of any one of claims 99 to 109, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 111. The method of any one of claims 99 to 110, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL, while blocking less than 50% of CD36’s binding to TSP-1 as measured by surface plasmon resonance. 112. The method of any one of claims 99 to 111, wherein the patient is a human patient. 113. The method of any one of claims 99 to 112, wherein the anti-CD36 antibody is a full length antibody, a single chain antibody, a scFv, a Fab fragment, or a F(ab')2 fragment. 114. The method of any one of claims 99 to 113, wherein the anti-CD36 antibody is a full length antibody. 115. The method of claim 114, wherein the anti-CD36 antibody comprises the antibody of any one of claims 38 to 40. 116. The method of any one of claims 99-115, wherein the method further comprises administering a second therapy. 117. The method of claim 116, wherein the second therapy is an immunotherapy. 118. The method of claim 117, wherein the immunotherapy is a PD-1 inhibitor. 119. The method of claim 118, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 120. The method of claim 119, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 121. The method of claim 117, wherein the immunotherapy is a PD-L1 inhibitor. 122. The method of claim 121, wherein the PD-L1 inhibitor is an anti-PD-L1 antibody. 123. The method of claim 122, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 124. The method of claim 117, wherein the immunotherapy is a CTLA-4 inhibitor. 125. The method of claim 124, wherein the CTLA-4 inhibitor is an anti-CTLA-4 antibody. 126. The method of claim 125, wherein the anti-CTLA-4 antibody is ipilimumab. 127. The method claim 116, wherein the second therapy is a chemotherapeutic agent. 128. The method of claim 127, wherein the chemotherapeutic agent is cisplatin. 129. The method of any one of claims 99-128, wherein metastasis is reduced or inhibited in the subject. 130. The method of any one of claims 116-129, wherein the two therapies are administered sequentially. 131. The method of any one of claims 116-129, wherein the two therapies are administered simultaneously. 132. The antibody of any one of claims 1 to 85, for use in a method of treating a subject having a cancer that expresses CD36, the method comprising administering to the subject a therapeutically effective amount of the anti-CD36 antibody according to the invention. 133. The antibody for use of claim 132, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma, melanoma, leukemia, or lymphoma. 134. The antibody for use of claim 132 or claim 133, wherein the cancer is a metastatic cancer. 135. The antibody for use of any one of claims 132 to 134, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 136. The antibody for use of any one of claims 132 to 135, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 137. The antibody for use of any one of claims 132 to 136, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while having little to no effect on CD36's binding to TSP-1. 138. The antibody for use of any one of claims 132-137, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 139. The antibody for use of any one of claims 132-138, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 140. The antibody for use of any one of claims 132 to 139, wherein the use is in combination with a second therapy. 141. The antibody for use of claim 140, wherein the second therapy is an immunotherapy. 142. The antibody for use of claim 141, wherein the immunotherapy is an anti-PD-1 antibody, an anti-PL-L1 antibody, or an anti-CTLA-4 antibody. 143. The antibody for use of claim 140, wherein the second therapy is a chemotherapeutic agent. 144. The antibody for use of claim 143, wherein the chemotherapeutic agent is cisplatin. 145. Use of the antibody of any one of claims 1 to 85 in the manufacture of a medicament for treating a subject having a cancer that expresses CD36. 146. The use of the antibody according to claim 145, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma, melanoma, leukemia, or lymphoma. 147. The use of the antibody according to claim 145 or claim 146, wherein the cancer is a metastatic cancer. 148. The use of the antibody according to any one of claims 145 to 148, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 149. The use of the antibody according to any one of claims 145 to 148, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 150. The use of the antibody according to any one of claims 145 to 149, wherein the anti- CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while having little to no effect on CD36's binding to TSP-1. 151. The use of the antibody according to any one of claims 145-150, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 152. The use of the antibody according to any one of claims 145-151, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti- CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 153. The use of the antibody according to any one of claims 145 to 152, wherein the use is in combination with a second therapy. 154. The use of the antibody according to claim 153, wherein the second therapy is an immunotherapy. 155. The use of the antibody according to claim 154, wherein the immunotherapy is an anti- PD-1 antibody, an anti-PL-L1 antibody, or an anti-CTLA-4 antibody. 156. The use of the antibody according to claim 153, wherein the second therapy is a chemotherapeutic agent. 157. The use of the antibody according to claim 156, wherein the chemotherapeutic agent is cisplatin. 158. An isolated polynucleotide that encodes the antibody of any one of claims 1 to 85. 159. The isolated polynucleotide of claim 158, which encodes the light chain variable region and the heavy chain variable region of claim 40. 160. The isolated polynucleotide of claim 158 or 159, which comprises at least one polynucleotide encoding a heavy chain selected from the group consisting of SEQ ID NOs: 226, 228, 230, 232, 234, 236, and 253-256. 161. The isolated polynucleotide of any one of claims 158 to 160, which comprises at least one polynucleotide encoding a light chain selected from the group consisting of SEQ ID NOs: 227, 229, 231, 233, 235, 237, 257, and 258. 162. The isolated polynucleotide of any one of claims 158 to 161, wherein the isolated polynucleotide comprises SEQ ID NOs: 226 and 227, SEQ ID NOs: 228 and 229, SEQ ID NOs: 230 and 231, SEQ ID NOs: 232 and 233, SEQ ID NOs: 234 and 235, SEQ ID NOs: 236 and 237, SEQ ID NOs: 253 and 257, SEQ ID NOs: 253 and 258, SEQ ID NOs: 254 and 257, SEQ ID NOs: 254 and 258, SEQ ID NOs: 255 and 257, SEQ ID NOs: 255 and 258, SEQ ID NOs: 256 and 257, or SEQ ID NOs: 256 and 258. 163. A vector comprising the isolated polynucleotide of any one of claims 158 to 162. 164. A cell comprising the isolated polynucleotide of any one of claims 158 to 162 or the vector of claim 163. 165. The cell of claim 164, which is selected from the group consisting of E. coli, Pseudomonas, Bacillus, Streptomyces, yeast, CHO, YB/20, NS0, PER-C6, HEK 293, HEK 293T, NIH 3T3, HeLa, BHK, Hep G2, SP2/0, R1.1, B-W, L-M, COS 1, COS 7, BSC1, BSC40, BMT10 cell, plant cell, insect cell, and human cell in tissue culture. 166. The cell of claim 164 or 165, wherein the cell lacks a functional alpha-1,6- fucosyltransferase gene (FUT8) gene. 167. A method of making an antibody that is capable of specifically binding CD36, comprising culturing the cell of any one of claims 165 to 166 under conditions suitable for expression of the antibody and isolating the antibody expressed therein. 168. A method of claim 167, wherein the the antibody is secreted from the cell and isolated from media in which the cell has been cultured. 169. The use of an antibody of any one of claims 1 to 85, for the manufacture of a pharmaceutical composition. 170. The use of an antibody of any one of claims 1 to 85 and a pharmaceutically acceptable excipient or carrier for the manufacture of a pharmaceutical composition. 171. The method of any one of claims 99 to 131, wherein the metastatic tumors are present in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 172. The antibody for use of any one of claims 132 to 144, wherein the metastatic cancer comprises metastatic tumors in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 173. The use of the antibody of any one of claims 144-157, wherein the metastatic cancer comprises metastatic tumors in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 174. A method of treating both a primary tumor and metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of claims 1 to 85 or a therapeutically effective amount of the pharmaceutical composition of any one of claims 86 to 98. 175. The method of claim 174, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma, melanoma, leukemia, or lymphoma. 176. The method of claim 174 or 175, wherein the metastatic tumors are metastatic oral squamous cell carcinoma, metastatic head and neck cancer, metastatic esophageal cancer, metastatic gastric cancer, metastatic ovarian cancer, metastatic cervical cancer, metastatic lung cancer, metastatic breast cancer, metastatic colon cancer, metastatic renal cancer, metastatic prostate cancer, metastatic sarcoma, metastatic liposarcoma, metastatic melanoma, metastatic leukemia, or metastatic lymphoma. 177. The method of any one of claims 174 to 176, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 178. The method of any one of claims 174 to 177 wherein the treatment reduces the size of a primary tumor. 179. The method of any one of claims 174 to 178, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 180. The method of any one of claims 174 to 179, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while blocking less than 50% of CD36’s binding to TSP-1 as measured by surface plasmon resonance. 181. The method of any one of claims 174-180, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 182. The method of any one of claims 174-181, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 183. The method of any one of claims 174 to 182, wherein the patient is a human patient. 184. The method of any one of claims 174 to 183, wherein the anti-CD36 antibody is a full length antibody, a single chain antibody, a scFv, a Fab fragment, or a F(ab')2 fragment. 185. The method of any one of claims 174 to 184, wherein the anti-CD36 antibody is a full length antibody. 186. The method of claim 185, wherein the anti-CD36 antibody comprises the antibody of any one of claims 38 to 40. 187. The method of any one of claims 174 to 186, wherein the method further comprises administering a second therapy. 188. The method of claim 187, wherein the second therapy is an immunotherapy. 189. The method of claim 188, wherein the immunotherapy is a PD-1 inhibitor. 190. The method of claim 189, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 191. The method of claim 190, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 192. The method of claim 188, wherein the immunotherapy is a PD-L1 inhibitor. 193. The method of claim 192, wherein the PD-L1 inhibitor is an anti-PD-L1 antibody. 194. The method of claim 193, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 195. The method of claim 188, wherein the immunotherapy is a CTLA-4 inhibitor. 196. The method of claim 195, wherein the CTLA-4 inhibitor is an anti-CTLA-4 antibody. 197. The method of claim 196, wherein the anti-CTLA-4 antibody is ipilimumab. 198. The method claim 187, wherein the second therapy is a chemotherapeutic agent. 199. The method of claim 198, wherein the chemotherapeutic agent is cisplatin. 200. The method of any one of claims 174 to 199, wherein metastasis is reduced or inhibited in the subject. 201. The method of any one of claims 187-200, wherein the two therapies are administered sequentially. 202. The method of any one of claims 187-200, wherein the two therapies are administered simultaneously. |
[0259] In some embodiments, the present invention provides methods of treating cancer in a mammal using a combination of an anti-CD36 antibody and an anti-PD-1 antibody. In some embodiments, the cancer is selected from the group consisting of oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma , e.g., liposarcoma, melanoma, leukemia, and lymphoma. In some embodiments, the cancer is oral squamous cell carcinoma. In some embodiments, the cancer is ovarian cancer. In other embodiments, the cancer is melanoma. In a further embodiment, the cancer is any other cancer disclosed herein. In one embodiment, the cancer is metastatic cancer. In some embodiments, the cancer is both a primary tumor and a metastatic cancer. In some embodiments, the anti-CD36 antibody is a full length antibody, a single chain antibody, or a scFv, Fab or F(ab') 2 fragment. In one embodiment, the anti-CD36 antibody is a full length antibody. In an embodiment, the anti-CD36 antibody is a humanized antibody. In certain embodiments, the anti-CD36 antibody is an antibody disclosed herein. In certain embodiments, the anti-CD36 antibody is a commercial anti-CD36 antibody such as the antibody JC63.1. In one embodiment, the anti-PD-1 antibody is pembrolizumab (KEYTRUDA; MK-3475), pidilizumab (CT-011), or nivolumab (OPDIVO; BMS-936558). [0260] Examples of cancers and/or malignant tumors that may be treated using the methods of the invention, include liver cancer, hepatocellular carcinoma (HCC), bone cancer, pancreatic cancer, skin cancer, oral cancer, cancer of the head or neck, breast cancer, lung cancer, small cell lung cancer, NSCLC, cutaneous or intraocular malignant melanoma, Merkel cell carcinoma (MCC), cutaneous squamous cell carcinoma (cSCC), renal cancer, uterine cancer, ovarian cancer, colorectal cancer, colon cancer, rectal cancer, cancer of the anal region, stomach cancer, testicular cancer, uterine cancer, carcinoma of the fallopian tubes, carcinoma of the endometrium, carcinoma of the cervix, carcinoma of the vagina, carcinoma of the vulva, squamous cell carcinoma of the head and neck (SCCHN), non-Hodgkin's lymphoma, cancer of the esophagus, cancer of the small intestine, cancer of the endocrine system, cancer of the thyroid gland, cancer of the parathyroid gland, cancer of the adrenal gland, sarcoma of soft tissue (e.g., liposarcoma), cancer of the urethra, cancer of the penis, solid tumors of childhood, lymphocytic lymphoma, cancer of the bladder, urothelial carcinoma, cancer of the kidney or ureter, carcinoma of the renal pelvis, neoplasm of the central nervous system (CNS), primary CNS lymphoma, tumor angiogenesis, spinal axis tumor, brain stem glioma, pituitary adenoma, Kaposi's sarcoma, epidermoid cancer, squamous cell cancer, environmentally induced cancers including those induced by asbestos, hematologic malignancies including, for example, multiple myeloma, B-cell lymphoma, Hodgkin lymphoma/primary mediastinal B-cell lymphoma, non-Hodgkin's lymphomas, acute myeloid lymphoma, chronic myelogenous leukemia, chronic lymphoid leukemia, follicular lymphoma, diffuse large B-cell lymphoma, Burkitt's lymphoma, immunoblastic large cell lymphoma, precursor B-lymphoblastic lymphoma, mantle cell lymphoma, acute lymphoblastic leukemia, mycosis fungoides, anaplastic large cell lymphoma, T-cell lymphoma, and precursor T-lymphoblastic lymphoma, and any combinations of said cancers. The present invention is also applicable to treatment of metastatic cancers. In embodiments, the cancer is oral squamous cell carcinoma. In some embodiments, the cancer is ovarian cancer. In other embodiments, the cancer is melanoma. [0261] In particular embodiments, the methods disclosed herein reduce the size of a primary tumor within a treated patient. Methods that may be used to measure the size of a primary tumor include physical measurement (e.g., of diameter, weight, or number of cells), IVIS imaging, and H&E staining as part of immunohistochemical analysis. In some embodiments, the methods reduce the size of the primary tumor by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90% in size. [0262] In particular embodiments, the methods disclosed herein reduce the size of at least one metastatic tumor within a treated patient. Methods that may be used to measure the size of a metastatic tumor include physical measurement (e.g., of diameter, weight, or number of cells), IVIS imaging, and H&E staining as part of immunohistochemical analysis. In some embodiments, the methods reduce the size of the one or more metastatic tumors by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90% in size. [0263] In particular embodiments, the methods disclosed herein prevent the growth in size of a primary tumor within treated patients, relative to patients administered a control treatment. Methods that may be used to measure the size of a primary tumor include physical measurement (e.g., of diameter, weight, or number of cells), IVIS imaging, and H&E staining as part of immunohistochemical analysis. In some embodiments, the methods prevent the growth in size of the primary tumor by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90%, relative to tumors in patients administered a control treatment. [0264] In particular embodiments, the methods disclosed herein prevent the growth in size of one or more metastatic tumors within treated patients, relative to patients administered a control treatment. Methods that may be used to measure the size of a metastatic tumor include physical measurement (e.g., of diameter, weight, or number of cells), IVIS imaging, and H&E staining as part of immunohistochemical analysis. In some embodiments, the methods prevent the growth in size of the one or more metastatic tumors by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90%, relative to metastatic tumors in patients administered a control treatment. In some embodiments, the methods increase the percentage of metastatic tumors that are limited in size to only a few cells, relative to the percentage of metastatic tumors that are limited in size to only a few cells in patients administered a control treatment. In some embodiments, the methods increase the percentage of metastatic tumors that are limited in size to only a few cells by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90%, relative to the percentage of metastatic tumors that are limited in size to only a few cells in patients administered a control treatment. In some embodiments, the methods reduce the percentage of metastatic tumors that are large (i.e., diameter > 5 mm) or medium (i.e., diameter between 1 and 2 mm), relative to the percentage of metastatic tumors that are large or medium in patients administered a control treatment. In some embodiments, the methods reduce the percentage of metastatic tumors that are large or medium by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90%, relative to the percentage of metastatic tumors that are large or medium in patients administered a control treatment. [0265] In particular embodiments, the methods disclosed herein reduce the number of metastatic tumors within treated patients, relative to patients administered a control treatment. Methods that may be used to measure the number of a metastatic tumor include physical examination (e.g., counting the number of tumors), IVIS imaging, and H&E staining as part of immunohistochemical analysis. In some embodiments, the methods reduce the number of metastatic tumors by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, or at least about 90%, relative to tumors in patients administered a control treatment. [0266] In embodiments, the antibodies can be administered systemically, for instance, intraperitoneally, and can be in the form of an appropriate suspension, for instance an aqueous suspension, in water or another appropriate liquid such as saline solution. [0267] For administration of the antibodies, the dosage ranges from about 0.0001 to 100 mg/kg, and more usually 0.01 to 5 mg/kg, of the host body weight. For example dosages can be 0.3 mg/kg body weight, 1 mg/kg body weight, 3 mg/kg body weight, 5 mg/kg body weight or 10 mg/kg body weight or within the range of 1-10 mg/kg. An exemplary treatment regime entails administration once per week, once every two weeks, once every three weeks, once every four weeks, once a month, once every 3 months or once every three to 6 months. In certain embodiments, the antibodies are administered at a flat or fixed dose. In embodiments, the antibodies are administered at any dosage described for the antibody in the art. Anti-PD-1 and Anti-PD-L1 Antibodies [0268] As used herein, the terms "Programmed Death 1," "Programmed Cell Death 1," "Protein PD-1," "PD-1," "PD1," "PDCD1," "hPD-1" and "hPD-I" are used interchangeably, and include variants, isoforms, species homologs of human PD-1, and analogs having at least one common epitope with PD-1. The complete PD-1 sequence can be found under GenBank Accession No. U64863. [0269] Programmed Cell Death 1 (PD-1) is a cell surface signaling receptor that plays a critical role in the regulation of T cell activation and tolerance (Keir M.E., et al., Annu. Rev. Immunol.2008; 26:677-704). It is a type I transmembrane protein and together with BTLA, CTLA-4, ICOS and CD28, comprise the CD28 family of T cell co-stimulatory receptors. PD-1 is primarily expressed on activated T cells, B cells, and myeloid cells (Dong H., et al., Nat. Med.1999; 5:1365-1369; Agata et al., supra; Okazaki et al. (2002) Curr. Opin. Immunol.14: 391779-82; Bennett et al. (2003) J Immunol 170:711-8). It is also expressed on natural killer (NK) cells (Terme M., et al., Cancer Res.2011; 71:5393- 5399). Binding of PD-1 by its ligands, PD-L1 and PD-L2, results in phosphorylation of the tyrosine residue in the proximal intracellular immune receptor tyrosine inhibitory domain, followed by recruitment of the phosphatase SHP-2, eventually resulting in down- regulation of T cell activation. One important role of PD-1 is to limit the activity of T cells in peripheral tissues at the time of an inflammatory response to infection, thus limiting the development of autoimmunity (Pardoll D.M., Nat. Rev. Cancer 2012; 12:252- 264). Evidence of this negative regulatory role comes from the finding that PD-1- deficient mice develop lupus-like autoimmune diseases including arthritis and nephritis, along with cardiomyopathy (Nishimura H., et al., Immunity, 1999; 11:141-151; and Nishimura H., et al., Science, 2001; 291:319-322). In the tumor setting, the consequence is the development of immune resistance within the tumor microenvironment. PD-1 is highly expressed on tumor-infiltrating lymphocytes, and its ligands are up-regulated on the cell surface of many different tumors (Dong H., et al., Nat. Med.2002; 8:793-800). Multiple murine cancer models have demonstrated that binding of ligand to PD-1 results in immune evasion. In addition, blockade of this interaction results in anti-tumor activity (Topalian S.L., et al. NEJM 2012; 366(26):2443-2454; Hamid O., et al., NEJM 2013; 369:134-144). Moreover, it has been shown that inhibition of the PD-1/PD-L1 interaction mediates potent antitumor activity in preclinical models (U.S. Pat. Nos.8,008,449 and 7,943,743). [0270] The initial members of the PD-1 family, CD28 and ICOS, were discovered by functional effects on augmenting T cell proliferation following the addition of monoclonal antibodies (Hutloff et al. Nature (1999); 397:263-266; Hansen et al. Immunogenics (1980); 10:247-260). PD-1 was discovered through screening for differential expression in apoptotic cells (Ishida et al. EMBO J (1992); 11:3887-95). The other members of the family, CTLA-4 and BTLA, were discovered through screening for differential expression in cytotoxic T lymphocytes and TH1 cells, respectively. CD28, ICOS and CTLA-4 all have an unpaired cysteine residue allowing for homodimerization. In contrast, PD-1 is suggested to exist as a monomer, lacking the unpaired cysteine residue characteristic in other CD28 family members. [0271] The PD-1 gene is a 55 kDa type I transmembrane protein that is part of the Ig gene superfamily (Agata et al. (1996) Int Immunol 8:765-72). PD-1 contains a membrane proximal immunoreceptor tyrosine inhibitory motif (ITIM) and a membrane distal tyrosine-based switch motif (ITSM) (Thomas, M. L. (1995) J Exp Med 181:1953-6; Vivier, E and Daeron, M (1997) Immunol Today 18:286-91). Although structurally similar to CTLA-4, PD-1 lacks the MYPPPY motif (SEQ ID NO: 239) that is critical for B7-1 and B7-2 binding. Two ligands for PD-1 have been identified, PD-L1 and PD-L2, that have been shown to downregulate T cell activation upon binding to PD-1 (Freeman et al. (2000) J Exp Med 192:1027-34; Latchman et al. (2001) Nat Immunol 2:261-8; Carter et al. (2002) Eur J Immunol 32:634-43). Both PD-L1 and PD-L2 are B7 homologs that bind to PD-1, but do not bind to other CD28 family members. PD-L1 is abundant in a variety of human cancers (Dong et al. (2002) Nat. Med.8:787-9). The interaction between PD-1 and PD-L1 results in a decrease in tumor infiltrating lymphocytes, a decrease in T-cell receptor mediated proliferation, and immune evasion by the cancerous cells (Dong et al. (2003) J. Mol. Med.81:281-7; Blank et al. (2005) Cancer Immunol. Immunother.54:307-314; Konishi et al. (2004) Clin. Cancer Res.10:5094-100). Immune suppression can be reversed by inhibiting the local interaction of PD-1 with PD-L1, and the effect is additive when the interaction of PD-1 with PD-L2 is blocked as well (Iwai et al. (2002) Proc. Nat'l. Acad. Sci. USA 99:12293-7; Brown et al. (2003) J. Immunol. 170:1257-66). [0272] Consistent with PD-1 being an inhibitory member of the CD28 family, PD-1 deficient animals develop various autoimmune phenotypes, including autoimmune cardiomyopathy and a lupus-like syndrome with arthritis and nephritis (Nishimura et al. (1999) Immunity 11:141-51; Nishimura et al. (2001) Science 291:319-22). Additionally, PD-1 has been found to play a role in autoimmune encephalomyelitis, systemic lupus erythematosus, graft-versus-host disease (GVHD), type I diabetes, and rheumatoid arthritis (Salama et al. (2003) J Exp Med 198:71-78; Prokunina and Alarcon-Riquelme (2004) Hum Mol Genet 13:R143; Nielsen et al. (2004) Lupus 13:510). In a murine B cell tumor line, the ITSM of PD-1 was shown to be essential to block BCR-mediated Ca 2+ - flux and tyrosine phosphorylation of downstream effector molecules (Okazaki et al. (2001) PNAS 98:13866-71). [0273] "Programmed Death Ligand-1 (PD-L1)" is one of two cell surface glycoprotein ligands for PD-1 (the other being PD-L2) that down-regulate T cell activation and cytokine secretion upon binding to PD-1. The term "PD-L1" as used herein includes human PD-L1 (hPD-L1), variants, isoforms, and species homologs of hPD-L1, and analogs having at least one common epitope with hPD-L1. The complete hPD-L1 sequence can be found under GenBank Accession No. Q9NZQ7. [0274] Some embodiments of the invention include an anti-PD-1 antibody, or an anti-PD- L1 antibody, in combination with an anti-CD36 antibody. PD-1 is a key immune checkpoint receptor expressed by activated T and B cells and mediates immunosuppression. PD-1 is a member of the CD28 family of receptors, which includes CD28, CTLA-4, ICOS, PD-1, and BTLA. Two cell surface glycoprotein ligands for PD-1 have been identified, Programmed Death Ligand-1 (PD-L1) and Programmed Death Ligand-2 (PD-L2), that are expressed on antigen-presenting cells as well as many human cancers and have been shown to down regulate T cell activation and cytokine secretion upon binding to PD-1. Inhibition of the PD-1/PD-L1 interaction mediates potent antitumor activity in preclinical models. [0275] Human monoclonal antibodies (HuMAbs) that bind specifically to PD-1 with high affinity have been disclosed in U.S. Patent Nos.8,008,449 and 8,779,105. Other anti-PD- 1 mAbs have been described in, for example, U.S. Patent Nos.6,808,710, 7,488,802, 8,168,757 and 8,354,509, and PCT Publication Nos. WO2012/145493 and WO2016/168716. Each of the anti-PD-1 HuMAbs disclosed in U.S. Patent No.8,008,449 has been demonstrated to exhibit one or more of the following characteristics: (a) binds to human PD-1 with a KD of 1 x 10 -7 M or less, as determined by surface plasmon resonance using a Biacore biosensor system; (b) does not substantially bind to human CD28, CTLA- 4 or ICOS; (c) increases T-cell proliferation in a Mixed Lymphocyte Reaction (MLR) assay; (d) increases interferon-γ production in an MLR assay; (e) increases IL-2 secretion in an MLR assay; (f) binds to human PD-1 and cynomolgus monkey PD-1; (g) inhibits the binding of PD-L1 and/or PD-L2 to PD-1; (h) stimulates antigen-specific memory responses; (i) stimulates Ab responses; and (j) inhibits tumor cell growth in vivo. Anti- PD-1 antibodies useful for the present invention include mAbs that bind specifically to human PD-1 and exhibit at least one, preferably at least five, of the preceding characteristics. [0276] Anti-human-PD-1 antibodies (or VH and/or VL domains derived therefrom) suitable for use in the invention can be generated using methods well known in the art. Alternatively, art recognized anti-PD-1 antibodies can be used. For example, monoclonal antibodies 5C4 (referred to herein as Nivolumab or BMS-936558), 17D8, 2D3, 4H1, 4A11, 7D3, and 5F4, described in WO 2006/121168, the teachings of which are hereby incorporated by reference, can be used. Other known PD-1 antibodies include lambrolizumab (MK-3475) described in WO 2008/156712, and AMP-514 described in WO 2012/145493. Further known anti-PD-1 antibodies and other PD-1 inhibitors include those described in WO 2009/014708, WO 03/099196, WO 2009/114335 and WO 2011/161699. Another known anti-PD-1 antibody is pidilizumab (CT-011). Antibodies that compete with any of these antibodies or inhibitors for binding to PD-1 also can be used. [0277] In one embodiment, the anti-PD-1 antibody is nivolumab. Nivolumab (also known as "OPDIVO®"; BMS-936558; formerly designated 5C4, BMS-936558, MDX-1106, or ONO-4538) is a fully human IgG4 (S228P) PD-1 immune checkpoint inhibitor antibody that selectively prevents interaction with PD-1 ligands (PD-L1 and PD-L2), thereby blocking the down-regulation of antitumor T-cell functions (U.S. Patent No.8,008,449; Wang et al., 2014 Cancer Immunol Res.2(9):846-56). In another embodiment, the anti- PD-1 antibody or fragment thereof cross-competes with nivolumab. In other embodiments, the anti-PD-1 antibody or fragment thereof binds to the same epitope as nivolumab. In certain embodiments, the anti-PD-1 antibody has the same CDRs as nivolumab. [0278] In another embodiment, the anti-PD-1 antibody is pembrolizumab. Pembrolizumab is a humanized monoclonal IgG4 (S228P) antibody directed against human cell surface receptor PD-1 (programmed death-1 or programmed cell death-1). Pembrolizumab is described, for example, in U.S. Patent Nos.8,354,509 and 8,900,587. [0279] In another embodiment, the anti-PD-1 antibody cross-competes with pembrolizumab. In some embodiments, the anti-PD-1 antibody binds to the same epitope as pembrolizumab. In certain embodiments, the anti-PD-1 antibody has the same CDRs as pembrolizumab. In another embodiment, the anti-PD-1 antibody is pembrolizumab. Pembrolizumab (also known as "KEYTRUDA®", lambrolizumab, and MK-3475) is a humanized monoclonal IgG4 antibody directed against human cell surface receptor PD-1 (programmed death-1 or programmed cell death-1). Pembrolizumab is described, for example, in U.S. Patent Nos.8,354,509 and 8,900,587 (incorporated herein by reference in their entirety); see also http://www.cancer.gov/drugdictionary?cdrid=695789 (last accessed: May 25, 2017). Pembrolizumab has been approved by the FDA for the treatment of relapsed or refractory melanoma. [0280] In other embodiments, the anti-PD-1 antibody thereof cross-competes with MEDI0608. In still other embodiments, the anti-PD-1 antibody binds to the same epitope as MEDI0608. In certain embodiments, the anti-PD-1 antibody has the same CDRs as MEDI0608. In other embodiments, the anti-PD-1 antibody is MEDI0608 (formerly AMP- 514), which is a monoclonal antibody. MEDI0608 is described, for example, in U.S. Patent No.8,609,089 or in http://www.cancer.gov/drugdictionary?cdrid=756047 (last accessed May 25, 2017). [0281] In other embodiments, the anti-PD-1 antibody cross-competes with BGB-A317. In some embodiments, the anti-PD-1 antibody binds the same epitope as BGB-A317. In certain embodiments, the anti-PD-1 antibody has the same CDRs as BGB-A317. In certain embodiments, the anti-PD-1 antibody is BGB-A317, which is a humanized monoclonal antibody. BGB-A317 is described in U.S. Publ. No.2015/0079109. [0282] Anti-PD-1 antibodies useful for the disclosed compositions also include isolated antibodies that bind specifically to human PD-1 and cross-compete for binding to human PD-1 with nivolumab (see, e.g., U.S. Patent Nos.8,008,449 and 8,779,105; Int'l Pub. No. WO 2013/173223). The ability of antibodies to cross-compete for binding to an antigen indicates that these antibodies bind to the same epitope region of the antigen and sterically hinder the binding of other cross-competing antibodies to that particular epitope region. These cross-competing antibodies are expected to have functional properties very similar to those of nivolumab by virtue of their binding to the same epitope region of PD- 1. Cross-competing antibodies can be readily identified based on their ability to cross- compete with nivolumab in standard PD-1 binding assays such as Biacore analysis, ELISA assays or flow cytometry (see, e.g., Int'l Pub. No. WO 2013/173223). [0283] In certain embodiments, antibodies that cross-compete for binding to human PD-1 with, or bind to the same epitope region of human PD-1 as, nivolumab are mAbs. For administration to human subjects, these cross-competing antibodies can be chimeric antibodies, or humanized or human antibodies. Such chimeric, humanized or human mAbs can be prepared and isolated by methods well known in the art. [0284] Anti-PD-1 antibodies useful for the compositions of the disclosed invention also include antigen-binding portions of the above antibodies. It has been amply demonstrated that the antigen-binding function of an antibody can be performed by fragments of a full length antibody. Examples of binding fragments encompassed within the term "antigen- binding portion" of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CH1 domains; (ii) a F(ab') 2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) a Fd fragment consisting of the VH and CH1 domains; and (iv) a Fv fragment consisting of the VL and VH domains of a single arm of an antibody. [0285] Anti-PD-1 antibodies suitable for use in the disclosed compositions are antibodies that bind to PD-1 with high specificity and affinity, block the binding of PD-L1 and or PD-L2, and inhibit the immunosuppressive effect of the PD-1 signaling pathway. In any of the compositions or methods disclosed herein, an anti-PD-1 "antibody" includes an antigen-binding portion or fragment that binds to the PD-1 receptor and exhibits the functional properties similar to those of whole antibodies in inhibiting ligand binding and upregulating the immune system. In certain embodiments, the anti-PD-1 antibody cross- competes with nivolumab for binding to human PD-1. In other embodiments, the anti-PD- 1 antibody is a chimeric, humanized or human monoclonal antibody or a portion thereof. In certain embodiments, the antibody is a humanized antibody. In other embodiments, the antibody is a human antibody. Antibodies of an IgG1, IgG2, IgG3 or IgG4 isotype can be used. [0286] In certain embodiments, the anti-PD-1 antibody comprises a heavy chain constant region which is of a human IgG1 or IgG4 isotype. In certain other embodiments, the sequence of the IgG4 heavy chain constant region of the anti-PD-1 antibody contains an S228P mutation which replaces a serine residue in the hinge region with the proline residue normally found at the corresponding position in IgG1 isotype antibodies. This mutation, which is present in nivolumab, prevents Fab arm exchange with endogenous IgG4 antibodies, while retaining the low affinity for activating Fc receptors associated with wild-type IgG4 antibodies (Wang et al., 2014). In yet other embodiments, the antibody comprises a light chain constant region which is a human kappa or lambda constant region. In other embodiments, the anti-PD-1 antibody is a mAb or an antigen- binding portion thereof. In certain embodiments of any of the therapeutic methods described herein comprising administration of an anti-PD-1 antibody, the anti-PD-1 antibody is nivolumab. In other embodiments, the anti-PD-1 antibody is pembrolizumab. In other embodiments, the anti-PD-1 antibody is chosen from the human antibodies 17D8, 2D3, 4H1, 4A11, 7D3 and 5F4 described in U.S. Patent No.8,008,449. In still other embodiments, the anti-PD-1 antibody is MEDI0608 (formerly AMP-514), AMP-224, or Pidilizumab (CT-011). Other known PD-1 antibodies include lambrolizumab (MK-3475) described in, for example, WO 2008/156712, and AMP-514 described in, for example, WO 2012/145493. Further known anti-PD-1 antibodies and other PD-1 inhibitors include those described in, for example, WO 2009/014708, WO 03/099196, WO 2009/114335 and WO 2011/161699. In one embodiment, the anti-PD-1 antibody is REGN2810. In one embodiment, the anti-PD-1 antibody is PDR001. Another known anti-PD-1 antibody is pidilizumab (CT-011). Each of the above references are incorporated by reference. Antibodies that compete with any of these antibodies or inhibitors for binding to PD-1 also can be used. [0287] Other anti-PD-1 monoclonal antibodies have been described in, for example, U.S. Patent Nos.6,808,710, 7,488,802, 8,168,757 and 8,354,509, US Publication No. 2016/0272708, and PCT Publication Nos. WO 2012/145493, WO 2008/156712, WO 2015/112900, WO 2012/145493, WO 2015/112800, WO 2014/206107, WO 2015/35606, WO 2015/085847, WO 2014/179664, WO 2017/020291, WO 2017/020858, WO 2016/197367, WO 2017/024515, WO 2017/025051, WO 2017/123557, WO 2016/106159, WO 2014/194302, WO 2017/040790, WO 2017/133540, WO 2017/132827, WO 2017/024465, WO 2017/025016, WO 2017/106061, WO 2017/19846, WO 2017/024465, WO 2017/025016, WO 2017/132825, and WO 2017/133540, each of which are herein incorporated by reference. [0288] In some embodiments, the anti-PD-1 antibody is selected from the group consisting of nivolumab (also known as OPDIVO®, 5C4, BMS-936558, MDX-1106, and ONO-4538), pembrolizumab (Merck; also known as KEYTRUDA®, lambrolizumab, and MK-3475; see WO2008/156712), PDR001 (Novartis; see WO 2015/112900), MEDI- 0680 (AstraZeneca; also known as AMP-514; see WO 2012/145493), cemiplimab (Regeneron; also known as REGN-2810; see WO 2015/112800), JS001 (TAIZHOU JUNSHI PHARMA; see Si-Yang Liu et al., J. Hematol. Oncol.10:136 (2017)), BGB- A317 (Beigene; see WO 2015/35606 and US 2015/0079109), INCSHR1210 (Jiangsu Hengrui Medicine; also known as SHR-1210; see WO 2015/085847; Si-Yang Liu et al., J. Hematol. Oncol.10:136 (2017)), TSR-042 (Tesaro Biopharmaceutical; also known as ANB011; see WO2014/179664), GLS-010 (Wuxi/Harbin Gloria Pharmaceuticals; also known as WBP3055; see Si-Yang Liu et al., J. Hematol. Oncol.10:136 (2017)), AM- 0001 (Armo), STI-1110 (Sorrento Therapeutics; see WO 2014/194302), AGEN2034 (Agenus; see WO 2017/040790), MGA012 (Macrogenics, see WO 2017/19846), and IBI308 (Innovent; see WO 2017/024465, WO 2017/025016, WO 2017/132825, and WO 2017/133540). Each of the above references are herein incorporated by reference. [0289] In embodiments, the anti-PD-1 antibody is a bispecific antibody. In embodiments, the second therapy is a PD-1 inhibitor. In embodiments, the PD-1 inhibitor is a small molecule. [0290] Because anti-PD-1 antibodies and anti-PD-L1 antibodies target the same signaling pathway and have been shown in clinical trials to exhibit similar levels of efficacy in a variety of cancers, an anti-PD-L1 antibody can be substituted for an anti-PD-1 antibody in any of the therapeutic methods or compositions disclosed herein. [0291] Anti-human-PD-L1 antibodies (or VH and/or VL domains derived therefrom) suitable for use in the invention can be generated using methods well known in the art. Alternatively, art recognized anti-PD-L1 antibodies can be used. For example, human anti-PD-L1 antibodies disclosed in U.S. Pat. No.7,943,743, the contents of which are hereby incorporated by reference, can be used. Such anti-PD-L1 antibodies include 3G10, 12A4 (also referred to as BMS-936559), 10A5, 5F8, 10H10, 1B12, 7H1, 11E6, 12B7, and 13G4. Other art recognized anti-PD-L1 antibodies which can be used include those described in, for example, U.S. Pat. Nos.7,635,757 and 8,217,149, U.S. Publication No. 2009/0317368, and PCT Publication Nos. WO 2011/066389 and WO 2012/145493, each of which are herein incorporated by reference. Other examples of an anti-PD-L1 antibody include atezolizumab (TECENTRIQ; RG7446), or durvalumab (IMFINZI; MEDI4736). Antibodies that compete with any of these art-recognized antibodies or inhibitors for binding to PD-L1 also can be used. [0292] Examples of anti-PD-L1 antibodies useful in the methods of the present disclosure include the antibodies disclosed in US Patent No.9,580,507, which is herein incorporated by reference. Anti-PD-L1 human monoclonal antibodies disclosed in U.S. Patent No. 9,580,507 have been demonstrated to exhibit one or more of the following characteristics: (a) bind to human PD-L1 with a K D of 1 x 10 -7 M or less, as determined by surface plasmon resonance using a Biacore biosensor system; (b) increase T-cell proliferation in a Mixed Lymphocyte Reaction (MLR) assay; (c) increase interferon-γ production in an MLR assay; (d) increase IL-2 secretion in an MLR assay; (e) stimulate antibody responses; and (f) reverse the effect of T regulatory cells on T cell effector cells and/or dendritic cells. Anti-PD-L1 antibodies usable in the present invention include monoclonal antibodies that bind specifically to human PD-L1 and exhibit at least one, in some embodiments, at least five, of the preceding characteristics. [0293] In certain embodiments, the anti-PD-L1 antibody is BMS-936559 (formerly 12A4 or MDX-1105) (see, e.g., U.S. Patent No.7,943,743; WO 2013/173223). In other embodiments, the anti-PD-L1 antibody is MPDL3280A (also known as RG7446 and atezolizumab) (see, e.g., Herbst et al.2013 J Clin Oncol 31(suppl):3000; U.S. Patent No. 8,217,149), MEDI4736 (Khleif, 2013, In: Proceedings from the European Cancer Congress 2013; September 27-October 1, 2013; Amsterdam, The Netherlands. Abstract 802), or MSB0010718C (also called Avelumab; see US 2014/0341917). In certain embodiments, antibodies that cross-compete for binding to human PD-L1 with, or bind to the same epitope region of human PD-L1 as the above-references PD-L1 antibodies are mAbs. For administration to human subjects, these cross-competing antibodies can be chimeric antibodies, or can be humanized or human antibodies. Such chimeric, humanized or human mAbs can be prepared and isolated by methods well known in the art. In certain embodiments, the anti-PD-L1 antibody is selected from the group consisting of BMS-936559 (also known as 12A4, MDX-1105; see, e.g., U.S. Patent No. 7,943,743 and WO 2013/173223), atezolizumab (Roche; also known as TECENTRIQ®; MPDL3280A, RG7446; see US 8,217,149; see, also, Herbst et al. (2013) J Clin Oncol 31(suppl):3000), durvalumab (AstraZeneca; also known as IMFINZI™, MEDI-4736; see, e.g., WO 2011/066389), avelumab (Pfizer; also known as BAVENCIO®, MSB- 0010718C; see , e.g., WO 2013/079174), STI-1014 (Sorrento; see, e.g., WO2013/181634), CX-072 (Cytomx; see, e.g., WO2016/149201), KN035 (3D Med/Alphamab; see Zhang et al., Cell Discov.7:3 (March 2017), LY3300054 (Eli Lilly Co.; see, e.g., WO 2017/034916), and CK-301 (Checkpoint Therapeutics; see Gorelik et al., AACR:Abstract 4606 (Apr 2016)). The above references are herein incorporated by reference. [0294] In certain embodiments, the PD-L1 antibody is atezolizumab (TECENTRIQ®). Atezolizumab is a fully humanized IgG1 monoclonal anti-PD-L1 antibody. [0295] In certain embodiments, the PD-L1 antibody is durvalumab (IMFINZI™). Durvalumab is a human IgG1 kappa monoclonal anti-PD-L1 antibody. [0296] In certain embodiments, the PD-L1 antibody is avelumab (BAVENCIO®). Avelumab is a human IgG1 lambda monoclonal anti-PD-L1 antibody. [0297] In other embodiments, the anti-PD-L1 monoclonal antibody is selected from the group consisting of 28-8, 28-1, 28-12, 29-8, 5H1, and any combination thereof. [0298] Anti-PD-L1 antibodies usable in the disclosed methods also include isolated antibodies that bind specifically to human PD-L1 and cross-compete for binding to human PD-L1 with any anti-PD-L1 antibody disclosed herein, e.g., atezolizumab, durvalumab, and/or avelumab. In some embodiments, the anti-PD-L1 antibody binds the same epitope as any of the anti-PD-L1 antibodies described herein, e.g., atezolizumab, durvalumab, and/or avelumab. The ability of antibodies to cross-compete for binding to an antigen indicates that these antibodies bind to the same epitope region of the antigen and sterically hinder the binding of other cross-competing antibodies to that particular epitope region. These cross-competing antibodies are expected to have functional properties very similar those of the reference antibody, e.g., atezolizumab and/or avelumab, by virtue of their binding to the same epitope region of PD-L1. Cross- competing antibodies can be readily identified based on their ability to cross-compete with atezolizumab and/or avelumab in standard PD-L1 binding assays such as Biacore analysis, ELISA assays or flow cytometry (see, e.g., WO 2013/173223). [0299] In certain embodiments, the antibodies that cross-compete for binding to human PD-L1 with, or bind to the same epitope region of human PD-L1 antibody as, atezolizumab, durvalumab, and/or avelumab, are monoclonal antibodies. For administration to human subjects, these cross-competing antibodies are chimeric antibodies, engineered antibodies, or humanized or human antibodies. Such chimeric, engineered, humanized or human monoclonal antibodies can be prepared and isolated by methods well known in the art. [0300] Anti-PD-L1 antibodies usable in the methods of the disclosed invention also include antigen-binding portions of the above antibodies. It has been amply demonstrated that the antigen-binding function of an antibody can be performed by fragments of a full length antibody. [0301] Anti-PD-L1 antibodies suitable for use in the disclosed methods or compositions are antibodies that bind to PD-L1 with high specificity and affinity, block the binding of PD-1, and inhibit the immunosuppressive effect of the PD-1 signaling pathway. In any of the compositions or methods disclosed herein, an anti-PD-L1 "antibody" includes an antigen-binding portion or fragment that binds to PD-L1 and exhibits the functional properties similar to those of whole antibodies in inhibiting receptor binding and up- regulating the immune system. In certain embodiments, the anti-PD-L1 antibody cross- competes with atezolizumab, durvalumab, and/or avelumab for binding to human PD-L1. Anti-CTLA-4 Antibodies [0302] In certain embodiments, an embodiment encompasses use of an anti-CTLA-4 antibody. In one embodiment, the anti-CTLA-4 antibody binds to and inhibits CTLA-4. In some embodiments, the anti-CTLA-4 antibody is ipilimumab (YERVOY), tremelimumab (ticilimumab; CP-675,206), AGEN-1884, or ATOR-1015. FURTHER EMBODIMENTS 1. An isolated antibody that binds to CD36, which comprises a light chain CDR1 region, a light chain CDR2 region, a light chain CDR3 region, a heavy chain CDR1 region, a heavy chain CDR2 region, and a heavy chain CDR3 region, wherein: the heavy chain CDR1 region comprises a sequence selected from the group consisting of SEQ ID NOs: 85-105; the heavy chain CDR2 region comprises a sequence selected from the group consisting of SEQ ID NOs: 106-132, or 248; the heavy chain CDR3 region comprises a sequence selected from the group consisting of SEQ ID NOs: 133-158; the light chain CDR1 region comprises a sequence selected from the group consisting of SEQ ID NOs: 159-172; the light chain CDR2 region comprises a sequence selected from the group consisting of SEQ ID NOs: 173-185, or 246; and the light chain CDR3 region comprises a sequence selected from the group consisting of SEQ ID NOs: 186-206, or 247. 2. The isolated antibody of embodiment 1, wherein the antibody is a chimeric antibody. 3. The isolated antibody of embodiment 1, wherein the antibody is a humanized antibody. 4. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 85, the heavy chain CDR2 region comprises SEQ ID NO: 106, the heavy chain CDR3 region comprises SEQ ID NO: 133, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 186. 5. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 86, the heavy chain CDR2 region comprises SEQ ID NO: 107, the heavy chain CDR3 region comprises SEQ ID NO: 134, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 6. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 86, the heavy chain CDR2 region comprises SEQ ID NO: 108, the heavy chain CDR3 region comprises SEQ ID NO: 135, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 188. 7. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 87, the heavy chain CDR2 region comprises SEQ ID NO: 109, the heavy chain CDR3 region comprises SEQ ID NO: 136, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 8. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 88, the heavy chain CDR2 region comprises SEQ ID NO: 110, the heavy chain CDR3 region comprises SEQ ID NO: 137, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 9. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 89, the heavy chain CDR2 region comprises SEQ ID NO: 111, the heavy chain CDR3 region comprises SEQ ID NO: 138, the light chain CDR1 region comprises SEQ ID NO: 161, the light chain CDR2 region comprises SEQ ID NO: 175, and the light chain CDR3 region comprises SEQ ID NO: 189. 10. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 112, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 11. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 91, the heavy chain CDR2 region comprises SEQ ID NO: 113, the heavy chain CDR3 region comprises SEQ ID NO: 140, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 12. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 92, the heavy chain CDR2 region comprises SEQ ID NO: 114, the heavy chain CDR3 region comprises SEQ ID NO: 141, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 191. 13. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 93, the heavy chain CDR2 region comprises SEQ ID NO: 115, the heavy chain CDR3 region comprises SEQ ID NO: 142, the light chain CDR1 region comprises SEQ ID NO: 163, the light chain CDR2 region comprises SEQ ID NO: 177, and the light chain CDR3 region comprises SEQ ID NO: 192. 14. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 94, the heavy chain CDR2 region comprises SEQ ID NO: 116, the heavy chain CDR3 region comprises SEQ ID NO: 143, the light chain CDR1 region comprises SEQ ID NO: 164, the light chain CDR2 region comprises SEQ ID NO: 175, and the light chain CDR3 region comprises SEQ ID NO: 193. 15. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 117, the heavy chain CDR3 region comprises SEQ ID NO: 144, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 16. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 118, the heavy chain CDR3 region comprises SEQ ID NO: 145, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 187. 17. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 95, the heavy chain CDR2 region comprises SEQ ID NO: 119, the heavy chain CDR3 region comprises SEQ ID NO: 146, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 18. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 194. 19. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 148, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 20. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 186. 21. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 196. 22. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 121, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 23. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 97, the heavy chain CDR2 region comprises SEQ ID NO: 122, the heavy chain CDR3 region comprises SEQ ID NO: 149, the light chain CDR1 region comprises SEQ ID NO: 165, the light chain CDR2 region comprises SEQ ID NO: 178, and the light chain CDR3 region comprises SEQ ID NO: 197. 24. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 97, the heavy chain CDR2 region comprises SEQ ID NO: 123, the heavy chain CDR3 region comprises SEQ ID NO: 150, the light chain CDR1 region comprises SEQ ID NO: 165, the light chain CDR2 region comprises SEQ ID NO: 178, and the light chain CDR3 region comprises SEQ ID NO: 197. 25. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 98, the heavy chain CDR2 region comprises SEQ ID NO: 124, the heavy chain CDR3 region comprises SEQ ID NO: 151, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 198. 26. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 96, the heavy chain CDR2 region comprises SEQ ID NO: 120, the heavy chain CDR3 region comprises SEQ ID NO: 147, the light chain CDR1 region comprises SEQ ID NO: 159, the light chain CDR2 region comprises SEQ ID NO: 173, and the light chain CDR3 region comprises SEQ ID NO: 195. 27. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 91, the heavy chain CDR2 region comprises SEQ ID NO: 125, the heavy chain CDR3 region comprises SEQ ID NO: 152, the light chain CDR1 region comprises SEQ ID NO: 160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 190. 28. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 99, the heavy chain CDR2 region comprises SEQ ID NO: 126, the heavy chain CDR3 region comprises SEQ ID NO: 133, the light chain CDR1 region comprises SEQ ID NO: 162, the light chain CDR2 region comprises SEQ ID NO: 176, and the light chain CDR3 region comprises SEQ ID NO: 199. 29. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 100, the heavy chain CDR2 region comprises SEQ ID NO: 127, the heavy chain CDR3 region comprises SEQ ID NO: 153, the light chain CDR1 region comprises SEQ ID NO: 166, the light chain CDR2 region comprises SEQ ID NO: 179, and the light chain CDR3 region comprises SEQ ID NO: 200. 30. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 101, the heavy chain CDR2 region comprises SEQ ID NO: 128, the heavy chain CDR3 region comprises SEQ ID NO: 154, the light chain CDR1 region comprises SEQ ID NO: 167, the light chain CDR2 region comprises SEQ ID NO: 180, and the light chain CDR3 region comprises SEQ ID NO: 201. 31. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 101, the heavy chain CDR2 region comprises SEQ ID NO: 128, the heavy chain CDR3 region comprises SEQ ID NO: 154, the light chain CDR1 region comprises SEQ ID NO: 168, the light chain CDR2 region comprises SEQ ID NO: 181, and the light chain CDR3 region comprises SEQ ID NO: 202. 32. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 102, the heavy chain CDR2 region comprises SEQ ID NO: 129, the heavy chain CDR3 region comprises SEQ ID NO: 155, the light chain CDR1 region comprises SEQ ID NO: 169, the light chain CDR2 region comprises SEQ ID NO: 182, and the light chain CDR3 region comprises SEQ ID NO: 203. 33. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 103, the heavy chain CDR2 region comprises SEQ ID NO: 130, the heavy chain CDR3 region comprises SEQ ID NO: 156, the light chain CDR1 region comprises SEQ ID NO: 170, the light chain CDR2 region comprises SEQ ID NO: 183, and the light chain CDR3 region comprises SEQ ID NO: 204. 34. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 104, the heavy chain CDR2 region comprises SEQ ID NO: 131, the heavy chain CDR3 region comprises SEQ ID NO: 157, the light chain CDR1 region comprises SEQ ID NO: 171, the light chain CDR2 region comprises SEQ ID NO: 184, and the light chain CDR3 region comprises SEQ ID NO: 205. 35. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 105, the heavy chain CDR2 region comprises SEQ ID NO: 132, the heavy chain CDR3 region comprises SEQ ID NO: 158, the light chain CDR1 region comprises SEQ ID NO: 172, the light chain CDR2 region comprises SEQ ID NO: 185, and the light chain CDR3 region comprises SEQ ID NO: 206. 36. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 248, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO:160, the light chain CDR2 region comprises SEQ ID NO: 174, and the light chain CDR3 region comprises SEQ ID NO: 247. 37. The antibody of any one of embodiments 1-3, wherein the heavy chain CDR1 region comprises SEQ ID NO: 90, the heavy chain CDR2 region comprises SEQ ID NO: 248, the heavy chain CDR3 region comprises SEQ ID NO: 139, the light chain CDR1 region comprises SEQ ID NO:160, the light chain CDR2 region comprises SEQ ID NO: 246, and the light chain CDR3 region comprises SEQ ID NO: 247. 38. The antibody of embodiment 1 or embodiment 2, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region has at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the amino acid sequence of at least one of SEQ ID NOs: 13-44, 241, or 243; and wherein the light chain variable region has at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity with the amino acid sequence of at least one of SEQ ID NOs: 45-78, 240, 242, 244, or 245. 39. The antibody of embodiment 38, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises a sequence selected from the group consisting of SEQ ID NOs: 13-44, 241 and 243 and wherein the light chain variable region comprises a sequence selected from the group consisting of SEQ ID NOs: 45-78, 240, 242, 244, and 245. 40. The antibody of embodiment 39, wherein: i. the heavy chain variable region comprises SEQ ID NO: 13 and the light chain variable region comprises SEQ ID NO: 45; ii. the heavy chain variable region comprises SEQ ID NO: 14 and the light chain variable region comprises SEQ ID NO: 46; iii. the heavy chain variable region comprises SEQ ID NO: 15 and the light chain variable region comprises SEQ ID NO: 47; iv. the heavy chain variable region comprises SEQ ID NO: 16 and the light chain variable region comprises SEQ ID NO: 48; v. the heavy chain variable region comprises SEQ ID NO: 17 and the light chain variable region comprises SEQ ID NO: 49; vi. the heavy chain variable region comprises SEQ ID NO: 18 and the light chain variable region comprises SEQ ID NO: 50; vii. the heavy chain variable region comprises SEQ ID NO: 19 and the light chain variable region comprises SEQ ID NO: 51; viii. the heavy chain variable region comprises SEQ ID NO: 20 and the light chain variable region comprises SEQ ID NO: 52; ix. the heavy chain variable region comprises SEQ ID NO: 21 and the light chain variable region comprises SEQ ID NO: 53; x. the heavy chain variable region comprises SEQ ID NO: 22 and the light chain variable region comprises SEQ ID NO: 54; xi. the heavy chain variable region comprises SEQ ID NO: 23 and the light chain variable region comprises SEQ ID NO: 55; xii. the heavy chain variable region comprises SEQ ID NO: 24 and the light chain variable region comprises SEQ ID NO: 56; xiii. the heavy chain variable region comprises SEQ ID NO: 25 and the light chain variable region comprises SEQ ID NO: 57; xiv. the heavy chain variable region comprises SEQ ID NO: 26 and the light chain variable region comprises SEQ ID NO: 58; xv. the heavy chain variable region comprises SEQ ID NO: 26 and the light chain variable region comprises SEQ ID NO: 59; xvi. the heavy chain variable region comprises SEQ ID NO: 27 and the light chain variable region comprises SEQ ID NO: 60; xvii. the heavy chain variable region comprises SEQ ID NO: 28 and the light chain variable region comprises SEQ ID NO: 61; xviii. the heavy chain variable region comprises SEQ ID NO: 29 and the light chain variable region comprises SEQ ID NO: 62; xix. the heavy chain variable region comprises SEQ ID NO: 30 and the light chain variable region comprises SEQ ID NO: 63; xx. the heavy chain variable region comprises SEQ ID NO: 31 and the light chain variable region comprises SEQ ID NO: 64; xxi. the heavy chain variable region comprises SEQ ID NO: 32 and the light chain variable region comprises SEQ ID NO: 65; xxii. the heavy chain variable region comprises SEQ ID NO: 33 and the light chain variable region comprises SEQ ID NO: 66; xxiii. the heavy chain variable region comprises SEQ ID NO: 34 and the light chain variable region comprises SEQ ID NO: 67; xxiv. the heavy chain variable region comprises SEQ ID NO: 35 and the light chain variable region comprises SEQ ID NO: 68; xxv. the heavy chain variable region comprises SEQ ID NO: 36 and the light chain variable region comprises SEQ ID NO: 69; xxvi. the heavy chain variable region comprises SEQ ID NO: 37 and the light chain variable region comprises SEQ ID NO: 70; xxvii. the heavy chain variable region comprises SEQ ID NO: 38 and the light chain variable region comprises SEQ ID NO: 71; xxviii. the heavy chain variable region comprises SEQ ID NO: 39 and the light chain variable region comprises SEQ ID NO: 72; xxix. the heavy chain variable region comprises SEQ ID NO: 40 and the light chain variable region comprises SEQ ID NO: 73; xxx. the heavy chain variable region comprises SEQ ID NO: 40 and the light chain variable region comprises SEQ ID NO: 74; xxxi. the heavy chain variable region comprises SEQ ID NO: 41 and the light chain variable region comprises SEQ ID NO: 75; xxxii. the heavy chain variable region comprises SEQ ID NO: 42 and the light chain variable region comprises SEQ ID NO: 76; xxxiii. the heavy chain variable region comprises SEQ ID NO: 43 and the light chain variable region comprises SEQ ID NO: 77; xxxiv. the heavy chain variable region comprises SEQ ID NO: 44 and the light chain variable region comprises SEQ ID NO: 78; xxxv. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 240; xxxvi. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 240; xxxvii. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 242; xxxviii. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 242; xxxix. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 244; xl. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 244; xli. the heavy chain variable region comprises SEQ NO: 241 and the light chain variable region comprises SEQ ID NO: 245; or xlii. the heavy chain variable region comprises SEQ NO: 243 and the light chain variable region comprises SEQ ID NO: 245. 41. The antibody of any one of embodiments 1 to 40, wherein the antibody binds to human CD36. 42. The antibody of embodiment 41, wherein the antibody specifically binds to human CD36. 43. The antibody of embodiment 41, wherein the antibody has cross-reactivity to human CD36 and non-human CD36. 44. The antibody of embodiment 43, wherein the antibody has cross-reactivity to human CD36 and non-human primate CD36. 45. The antibody of embodiment 44, wherein the non-human primate CD36 is cynomomolgus CD36 or rhesus macaque CD36. 46. The antibody of embodiment 44, wherein the antibody has cross-reactivity to human CD36, non-human primate CD36, and rodent CD36. 47. The antibody of embodiment 46, wherein the rodent CD36 is mouse CD36 or rat CD36. 48. The antibody of embodiment 41, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 145A, 146S, 147H, 148I, 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q, 156M, 157I, 158L, 159N, 160S, 185P, 186F, 187L, 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T, 197T, 198V, 199G, 398K, 399I, 400Q, 401V, 402L, 403K, 404N, 405L, 406K, 407R, 408N, 409Y, 410I, 411V, 412P, 413I, and 414L. 49. The antibody of embodiment 48, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q, 156M, 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T, 400Q, 401V, 402L, and 403K. 50. The antibody of embodiment 49, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 152Q, 192Y, and 406K. 51. The antibody of embodiment 49, wherein the antibody binds to an epitope comprising 149Y, 150Q, 151N, 152Q, 153F, 154V, and 155Q and 156M. 52. The antibody of embodiment 48, wherein the antibody binds to an epitope comprising 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T. 53. The antibody of embodiment 48, wherein the antibody binds to an epitope comprising 400Q, 401V, 402L, and 403K. 54. The antibody of embodiment 41, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 280E, 281S, 282D, 283V, 284N, 285L, 286K, 287G, 288I, 289P, 290V, 291Y, 292R, 293F, 294V, 295L, 296P, 297S, 298K, 341I, 342S, 343L, 344P, 345H, 346F, 347L, 348Y, 349A, 350S, 351P, 352D, 353V, 354S, 355E, 356P, 357I, 358D, 359G, 360L, 361N, 362P, 363N, 364E, and 365E. 55. The antibody of embodiment 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 286K, 287G, 288I, 289P, 290V, 291Y, 292R, 341I, 342S, 343L, 344P, 345H, 346F, 347L, 348Y, 349A, and 350S. 56. The antibody of embodiment 55, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 288I, 289P, 290V, 402D, 403V, and 404S. 57. The antibody of embodiment 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of 286K, 287G, 288I, 289P, 290V, 291Y, and 292R. 58. The antibody of embodiment 54, wherein the antibody binds to an epitope in human CD36 comprising at least one amino acid selected from the group consisting of: 400S, 401P, 402D, and 403V. 59. The antibody of any one of embodiments 1 to 58, wherein the antibody binds to human CD36 with a KD of less than 20 nM, as measured using surface plasmon resonance with a bivalent model. 60. The antibody of embodiment 59, wherein the antibody binds to human CD36 with a K D of less than 10 nM, as measured using surface plasmon resonance with a bivalent model. 61. The antibody of any one of embodiments 1 to 60, which further comprises a heavy chain constant region. 62. The antibody of embodiment 61, wherein the heavy chain constant region is selected from the group consisting of human immunoglobulin IgA1, IgA2, IgG1, IgG2, IgG3, or IgG4 heavy chain constant regions. 63. The antibody of embodiment 62, which comprises an IgG1 heavy chain constant region. 64. The antibody of embodiment 63, wherein the heavy chain constant region comprises an IgG constant region containing at least one amino acid substitution, wherein the at least one amino acid substitution results in reduced Fc binding to at least one Fcgamma receptor and reduced Fc effector function. 65. The antibody of embodiment 64, wherein the at least one Fc silencing mutation includes the amino acid substitutions L234A and L235A ("LALA"). 66. The antibody of embodiment 64, wherein the at least one Fc silencing mutation includes a set of amino acid substitutions selected from the group consisting of L234G, L235S, and G236R; L234S, L235T, and G236R; L234S, L235V, and G236R; L234T, L235Q, and G236R; L234T, L235T, and G236R; L234A, L235S, and G236R; L234Q, L235S, and G236R; L234S, L235G, and G236R; L234T, L235S, and G236R; L234Q, L235S, and G236R; L234A and L235A; and L234A, L235A, and P329G. 67. The antibody of embodiment 62, which comprises an IgG4 heavy chain constant region. 68. The antibody of embodiment 66, wherein the heavy chain constant region comprises an IgG constant region containing the amino acid substitution S228P. 69. The antibody of any one of embodiments 1 to 68, wherein the antibody further comprises a light chain constant region. 70. The antibody of embodiment 69, wherein the light chain constant region is selected from the group consisting of human immunoglobulins κ and λ light chain constant regions. 71. The antibody of any one of embodiments 1 to 70, wherein the antibody further comprises a heavy chain constant region and a light chain constant region, wherein the heavy chain constant region is a human IgG1 heavy chain constant region, and wherein the light chain constant region is a human κ light chain constant region. 72. The antibody of any one of embodiments 1 to 71, wherein the antibody is a bispecific antibody. 73. The antibody of embodiment 72, comprising a first antigen-binding region that specifically binds to CD36. 74. The antibody of embodiment 73, comprising a second antigen-binding region that specifically binds to an immune cell antigen. 75. The antibody of embodiment 74, wherein the immune cell antigen is selected from the group consisting of PD-1, PD-L1, CTLA4, CD3, LAG3, OX40, CD28, CD33, B7H3, CD47, TIM3, ICOS, LGR5, 4-1BB, CD40, CD40-L, and TIGIT. 76. The antibody of embodiment 73, comprising a second antigen-binding region that specifically binds to a tumor-specific antigen. 77. The antibody of embodiment 76, wherein the tumor-specific antigen is selected from the group consisting of HER2, HER3, EGFR, VEGF, IGF-1, IGF-2, ANG2, DLL1, IGF-1R, cMET, DLL4, FAP, DR5, IL15, IL15Ra, CD3, CEA, EPCAM, HER3, PSMA, PMEL, and GPC3. 78. The antibody of embodiment 74 to 76, wherein the immune cell antigen or tumor-specific antigen is CD3. 79. The antibody of embodiment 73, wherein the antibody is a biparatopic antibody. 80. The antibody of embodiment 79, comprising two antigen-binding regions, wherein each antigen-binding region specifically binds to a unique, non-overlapping CD36 epitope. 81. The antibody of embodiment 80, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04. 82. The antibody of embodiment 81, further comprising a second antigen-binding domain, which comprises an antigen-binding domain of an antibody selected from the group consisting of 10G04, 11G04, 19G04, 20G04, and 30G04. 83. The antibody of any of embodiments 80-82, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04, and a second antigen-binding domain, which comprises an antigen-binding domain of 11G04. 84. The antibody of any one of embodiments 1-71, which is an antigen binding fragment. 85. The antigen binding fragment of embodiment 84, wherein the antigen binding fragment comprises a Fab, Fab', F(ab') 2 , single chain Fv (scFv), disulfide linked Fv, V-NAR domain, IgNar, intrabody, IgGΔCH2, minibody, F(ab') 3 , tetrabody, triabody, diabody, single-domain antibody, DVD-Ig, Fcab, mAb2, (scFv) 2 , or scFv-Fc. 86. A pharmaceutical composition comprising the antibody of any one of embodiments 1 to 87 and a pharmaceutically acceptable excipient. 87. The pharmaceutical composition of embodiment 86, wherein at least 95% of the antibodies in the composition are afucosylated. 88. The pharmaceutical composition of embodiment 86 or embodiment 87, which further comprises a PD-1 inhibitor. 89. The pharmaceutical composition of embodiment 88, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 90. The pharmaceutical composition of embodiment 89, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 91. The pharmaceutical composition of any one of embodiments 86 to 90, which further comprises a PD-L1 inhibitor 92. The pharmaceutical composition of embodiment 91, wherein the PD-L1 inhibitor is an anti-PD-L1 antibody. 93. The pharmaceutical composition of embodiment 92, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 94. The pharmaceutical composition of any one of embodiments 86 to 93, which further comprises a CTLA-4 inhibitor. 95. The pharmaceutical composition of embodiment 94, wherein the CTLA-4 inhibitor is an anti-CTLA-4 antibody. 96. The pharmaceutical composition of embodiment 95, wherein the anti-CTLA-4 antibody is ipilimumab. 97. The pharmaceutical composition of any one of embodiments 86 to 96, wherein the composition further comprises a chemotherapeutic agent. 98. The pharmaceutical composition of embodiment 87, wherein the chemotherapeutic agent is cisplatin. 99. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 100. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the anti- CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 101. The method of embodiment 99 or embodiment 100, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, melanoma, leukemia, or lymphoma. 102. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 103. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of an anti-CD36 antibody, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 104. The method of any one of embodiments 99 to 103, wherein the anti-CD36 antibody is the antibody of any one of embodiments 1 to 85. 105. A method of treating cancer in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of embodiments 1 to 85, or a therapeutically effective amount of the pharmaceutical composition of any one of embodiments 86 to 98. 106. The method of embodiment 105, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, liposarcoma, melanoma, leukemia, or lymphoma. 107. A method of treating one or more metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of embodiments 1 to 85, or a therapeutically effective amount of the pharmaceutical composition of any one of embodiments 86 to 98. 108. The method of embodiment 102 or embodiment 107, wherein the metastatic tumors are metastatic oral squamous cell carcinoma, metastatic head and neck cancer, metastatic esophageal cancer, metastatic gastric cancer, metastatic ovarian cancer, metastatic cervical cancer, metastatic lung cancer, metastatic breast cancer, metastatic colon cancer, metastatic renal cancer, metastatic prostate cancer, metastatic sarcoma, metastatic melanoma, metastatic leukemia, or metastatic lymphoma. 109. The method of any one of embodiments 99 to 108, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 110. The method of any one of embodiments 99 to 109, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 111. The method of any one of embodiments 99 to110, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL, while blocking less than 50% of CD36’s binding to TSP-1 as measured by surface plasmon resonance. 112. The method of any one of embodiments 99 to 111, wherein the patient is a human patient. 113. The method of any one of embodiments 99 to 112, wherein the anti-CD36 antibody is a full length antibody, a single chain antibody, a scFv, a Fab fragment, or a F(ab') 2 fragment. 114. The method of any one of embodiments 99 to 113, wherein the anti-CD36 antibody is a full length antibody. 115. The method of embodiment 114, wherein the anti-CD36 antibody comprises the antibody of any one of embodiments 38 to 40. 116. The method of any one of embodiments 99-115, wherein the method further comprises administering a second therapy. 117. The method of embodiment 116, wherein the second therapy is an immunotherapy. 118. The method of embodiment 117, wherein the immunotherapy is a PD-1 inhibitor. 119. The method of embodiment 118, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 120. The method of embodiment 119, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 121. The method of embodiment 117, wherein the immunotherapy is a PD-L1 inhibitor. 122. The method of embodiment 121, wherein the PD-L1 inhibitor is an anti-PD-L1 antibody. 123. The method of embodiment 122, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 124. The method of embodiment 117, wherein the immunotherapy is a CTLA-4 inhibitor. 125. The method of embodiment 124, wherein the CTLA-4 inhibitor is an anti-CTLA-4 antibody. 126. The method of embodiment 125, wherein the anti-CTLA-4 antibody is ipilimumab. 127. The method embodiment 116, wherein the second therapy is a chemotherapeutic agent. 128. The method of embodiment 127, wherein the chemotherapeutic agent is cisplatin. 129. The method of any one of embodiments 99-128, wherein metastasis is reduced or inhibited in the subject. 130. The method of any one of embodiments 116-129, wherein the two therapies are administered sequentially. 131. The method of any one of embodiments 116-129, wherein the two therapies are administered simultaneously. 132. The antibody of any one of embodiments 1 to 85, for use in a method of treating a subject having a cancer that expresses CD36, the method comprising administering to the subject a therapeutically effective amount of the anti-CD36 antibody according to the invention. 133. The antibody for use of embodiment 132, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, melanoma, leukemia, or lymphoma. 134. The antibody for use of embodiment 132 or embodiment 133, wherein the cancer is a metastatic cancer. 135. The antibody for use of any one of embodiments 132 to 134, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 136. The antibody for use of any one of embodiments 132 to 135, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 137. The antibody for use of any one of embodiments 132 to 136, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while having little to no effect on CD36's binding to TSP-1. 138. The antibody for use of any one of embodiments 132-137, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC 50 of less than 20 nM, as measured by FACS assay. 139. The antibody for use of any one of embodiments 132-138, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC 50 of less than 10 nM, as measured by the anti- CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 140. The antibody for use of any one of embodiments 132 to 139, wherein the use is in combination with a second therapy. 141. The antibody for use of embodiment 140, wherein the second therapy is an immunotherapy. 142. The antibody for use of embodiment 141, wherein the immunotherapy is an anti-PD-1 antibody, an anti-PL-L1 antibody, or an anti-CTLA-4 antibody. 143. The antibody for use of embodiment 140, wherein the second therapy is a chemotherapeutic agent. 144. The antibody for use of embodiment 143, wherein the chemotherapeutic agent is cisplatin. 145. Use of the antibody of any one of embodiments 1 to 85 in the manufacture of a medicament for treating a subject having a cancer that expresses CD36. 146. The use of the antibody according to embodiment 145, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, melanoma, leukemia, or lymphoma. 147. The use of the antibody according to embodiment 145 or embodiment 146, wherein the cancer is a metastatic cancer. 148. The use of the antibody according to any one of embodiments 145 to 147, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 149. The use of the antibody according to any one of embodiments 145 to 148, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 150. The use of the antibody according to any one of embodiments 145 to 149, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while having little to no effect on CD36's binding to TSP-1. 151. The use of the antibody according to any one of embodiments 145-150, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC50 of less than 20 nM, as measured by FACS assay. 152. The use of the antibody according to any one of embodiments 145-151, wherein the anti- CD36 antibody inhibits oxLDL uptake with an IC 50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 153. The use of the antibody according to any one of embodiments 145 to 152, wherein the use is in combination with a second therapy. 154. The use of the antibody according to embodiment 153, wherein the second therapy is an immunotherapy. 155. The use of the antibody according to embodiment 154, wherein the immunotherapy is an anti-PD-1 antibody, an anti-PL-L1 antibody, or an anti-CTLA-4 antibody. 156. The use of the antibody according to embodiment 153, wherein the second therapy is a chemotherapeutic agent. 157. The use of the antibody according to embodiment 156, wherein the chemotherapeutic agent is cisplatin. 158. An isolated polynucleotide that encodes the antibody of any one of embodiments 1 to 85. 159. The isolated polynucleotide of embodiment 158, which encodes the light chain variable region and the heavy chain variable region of embodiment 40. 160. The isolated polynucleotide of embodiment 158 or 159, which comprises at least one polynucleotide encoding a heavy chain selected from the group consisting of SEQ ID NOs: 226, 228, 230, 232, 234, 236, 257, and 258. 161. The isolated polynucleotide of any one of embodiments 158 to 160, which comprises at least one polynucleotide encoding a light chain selected from the group consisting of SEQ ID NOs: 227, 229, 231, 233, 235, 237, and 253-256. 162. The isolated polynucleotide of any one of embodiments 158 to 161, wherein the isolated polynucleotide comprises SEQ ID NOs: 226 and 227, SEQ ID NOs: 228 and 229, SEQ ID NOs: 230 and 231, SEQ ID NOs: 232 and 233, SEQ ID NOs: 234 and 235, SEQ ID NOs: 236 and 237, SEQ ID NOs: 253 and 257, SEQ ID NOs: 253 and 258, SEQ ID NOs: 254 and 257, SEQ ID NOs: 254 and 258, SEQ ID NOs: 255 and 257, SEQ ID NOs: 255 and 258, SEQ ID NOs: 256 and 257, or SEQ ID NOs: 256 and 258. 163. A vector comprising the isolated polynucleotide of any one of embodiments 158 to 162. 164. A cell comprising the isolated polynucleotide of any one of embodiments 158 to 162 or the vector of embodiment 163. 165. The cell of embodiment 164, which is selected from the group consisting of E. coli, Pseudomonas, Bacillus, Streptomyces, yeast, CHO, YB/20, NS0, PER-C6, HEK 293, HEK 293T, NIH 3T3, HeLa, BHK, Hep G2, SP2/0, R1.1, B-W, L-M, COS 1, COS 7, BSC1, BSC40, BMT10 cell, plant cell, insect cell, and human cell in tissue culture. 166. The cell of embodiment 164 or 165, wherein the cell lacks a functional alpha-1,6- fucosyltransferase gene (FUT8) gene. 167. A method of making an antibody that is capable of specifically binding CD36, comprising culturing the cell of any one of embodiments 164 to 166 under conditions suitable for expression of the antibody and isolating the antibody expressed therein. 168. A method of embodiment 167, wherein the the antibody is secreted from the cell and isolated from media in which the cell has been cultured. 169. The use of an antibody of any one of embodiments 1 to 85, for the manufacture of a pharmaceutical composition. 170. The use of an antibody of any one of embodiments 1 to 85 and a pharmaceutically acceptable excipient or carrier for the manufacture of a pharmaceutical composition. 171. The method of any one of embodiments 99 to 131, wherein the metastatic tumors are present in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 172. The antibody for use of any one of embodiments 132 to 144, wherein the metastatic cancer comprises metastatic tumors in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 173. The use of the antibody of any one of embodiments 145-157, wherein the metastatic cancer comprises metastatic tumors in one or more of the liver, lung, spleen, kidney, cervical lymph nodes, or peritoneal wall. 174. A method of treating both a primary tumor and metastatic tumors in a patient comprising administering to a subject in need thereof a therapeutically effective amount of the antibody of any one of embodiments 1 to 85 or a therapeutically effective amount of the pharmaceutical composition of any one of embodiments 86 to 98. 175. The method of embodiment 174, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, melanoma, leukemia, or lymphoma. 176. The method of embodiment 174 or 175, wherein the metastatic tumors are metastatic oral squamous cell carcinoma, metastatic head and neck cancer, metastatic esophageal cancer, metastatic gastric cancer, metastatic ovarian cancer, metastatic cervical cancer, metastatic lung cancer, metastatic breast cancer, metastatic colon cancer, metastatic renal cancer, metastatic prostate cancer, metastatic sarcoma, metastatic melanoma, metastatic leukemia, or metastatic lymphoma. 177. The method of any one of embodiments 174 to 176, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 178. The method of any one of embodiments 174 to 177wherein the treatment reduces the size of a primary tumor. 179. The method of any one of embodiments 174 to 178, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. 180. The method of any one of embodiments 174 to 179, wherein the anti-CD36 antibody blocks the CD36-mediated uptake of fatty acids and/or oxLDL while blocking less than 50% of CD36’s binding to TSP-1 as measured by surface plasmon resonance. 181. The method of any one of embodiments 174-180, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC 50 of less than 20 nM, as measured by FACS assay. 182. The method of any one of embodiments 174-181, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC 50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 183. The method of any one of embodiments 174 to 182, wherein the patient is a human patient. 184. The method of any one of embodiments 174 to 183, wherein the anti-CD36 antibody is a full length antibody, a single chain antibody, a scFv, a Fab fragment, or a F(ab') 2 fragment. 185. The method of any one of embodiments 174 to 184, wherein the anti-CD36 antibody is a full length antibody. 186. The method of embodiment 185, wherein the anti-CD36 antibody comprises the antibody of any one of embodiments 38 to 40. 187. The method of any one of embodiments 174 to 186, wherein the method further comprises administering a second therapy. 188. The method of embodiment 187, wherein the second therapy is an immunotherapy. 189. The method of embodiment 188, wherein the immunotherapy is a PD-1 inhibitor. 190. The method of embodiment 189, wherein the PD-1 inhibitor is an anti-PD-1 antibody. 191. The method of embodiment 190, wherein the anti-PD-1 antibody is pembrolizumab, pidilizumab, or nivolumab. 192. The method of embodiment 188, wherein the immunotherapy is a PD-L1 inhibitor. 193. The method of embodiment 192, wherein the PD-L1 inhibitor is an anti-PD-L1 antibody. 194. The method of embodiment 193, wherein the anti-PD-L1 antibody is atezolizumab, durvalumab, avelumab, or BMS-936559. 195. The method of embodiment 188, wherein the immunotherapy is a CTLA-4 inhibitor. 196. The method of embodiment 195, wherein the CTLA-4 inhibitor is an anti-CTLA-4 antibody. 197. The method of embodiment 196, wherein the anti-CTLA-4 antibody is ipilimumab. 198. The method embodiment 187, wherein the second therapy is a chemotherapeutic agent. 199. The method of embodiment 198, wherein the chemotherapeutic agent is cisplatin. 200. The method of any one of embodiments 174 to 199, wherein metastasis is reduced or inhibited in the subject. 201. The method of any one of embodiments 187-200, wherein the two therapies are administered sequentially. 202. The method of any one of embodiments 187-200, wherein the two therapies are administered simultaneously. 203. An antibody that binds to human CD36, wherein the epitope comprises or consists of amino acid residues 149-156 and/or amino acid residues 188-196 and/or amino acid residues 400-403 within human CD36 defined by SEQ ID NO: 1; preferably all, more preferably wherein determination of the epitope is conducted by hydrogen-deuterium exchange mass spectrometry. 204. The antibody of embodiment 203, wherein the epitope comprises or consists of amino acid residues 145-160 and/or amino acid residues 185-199 and/or amino acid residues 398-414 within human CD36 defined by SEQ ID NO: 1, preferably the epitope comprises or consists of all said amino acid residues. 205. An antibody that specifically binds to human CD36, that binds to the same epitope on human CD36 as antibody 1G04 or competes with antibody 1G04 for binding to human CD36. 206. The antibody of any of embodiments 203 to 205, wherein said antibody is not 1G04 or wherein said antibody is 1G06. 207. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 136 or an HCDR3 with at least a 70% identity thereto with at least a 70% identity thereto. 208. The antibody according to embodiment 207, wherein said antibody is selected from the group consisting of: a) an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 87, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 109, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 136, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 187; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 16 and the light chain variable region comprises or consists of SEQ ID NO: 48; more preferably wherein said antibody is 7G04; b) an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 88, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 110, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 137, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 187; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 17 and the light chain variable region comprises or consists of SEQ ID NO: 49; more preferably wherein said antibody is 09G04. 209. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 142 or an HCDR3 with at least a 70% identity thereto. 210. The antibody according to embodiment 209, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 93, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 115, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 142, the light chain CDR1 region comprises or consists of SEQ ID NO: 163, the light chain CDR2 region comprises or consists of SEQ ID NO: 177, and the light chain CDR3 region comprises or consists of SEQ ID NO: 192; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 22 and the light chain variable region comprises or consists of SEQ ID NO: 54; more preferably wherein said antibody is 14G04. 211. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:133 or an HCDR3 with at least a 70% identity thereto. 212. The antibody according to embodiment 211, wherein said antibody is selected from the group consisting of: i. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 85, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 106, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 133, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 186; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 13 and the light chain variable region comprises or consists of SEQ ID NO: 45; more preferably wherein said antibody is 04G04 ii. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 99, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 126, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 133, the light chain CDR1 region comprises or consists of SEQ ID NO: 162, the light chain CDR2 region comprises or consists of SEQ ID NO: 176, and the light chain CDR3 region comprises or consists of SEQ ID NO: 199; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 38 and the light chain variable region comprises or consists of SEQ ID NO: 71; more preferably wherein said antibody is 31G04. 213. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 141 or an HCDR3 with at least a 70% identity thereto. 214. The antibody according to embodiment 213, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 92, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 114, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 141, the light chain CDR1 region comprises or consists of SEQ ID NO: 162, the light chain CDR2 region comprises or consists of SEQ ID NO: 176, and the light chain CDR3 region comprises or consists of SEQ ID NO: 191; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 21 and the light chain variable region comprises or consists of SEQ ID NO: 53; more preferably, wherein said antibody is 13G04. 215. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:147 or an HCDR3 with at least a 70% identity thereto. 216. The antibody according to embodiment 215, wherein said antibody is selected from the group consisting of: a. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 120, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 147, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 194; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 28 and the light chain variable region comprises or consists of SEQ ID NO: 61; more preferably wherein said antibody is 21G04; b. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 121, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 148, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 195; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 29 and the light chain variable region comprises or consists of SEQ ID NO: 62; preferably wherein said antibody is 22G04; c. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 120, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 147, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 186; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 30 and the light chain variable region comprises or consists of SEQ ID NO: 63; more preferably wherein said antibody is 23G04; d. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 121, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 147, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 196; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 31 and the light chain variable region comprises or consists of SEQ ID NO: 64; more preferably wherein said antibody is 24G04; e. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 121, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 147, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 195; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 32 and the light chain variable region comprises or consists of SEQ ID NO: 65; more preferably wherein said antibody is 25G04; f. an antib`ody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 96, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 120, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 147, the light chain CDR1 region comprises or consists of SEQ ID NO: 159, the light chain CDR2 region comprises or consists of SEQ ID NO: 173, and the light chain CDR3 region comprises or consists of SEQ ID NO: 195; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 36 and the light chain variable region comprises or consists of SEQ ID NO: 69; more preferably wherein said antibody is 29G04. 217. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 143 or an HCDR3 with at least a 70% identity thereto. 218. The antibody according to embodiment 217, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 94, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 116, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 143, the light chain CDR1 region comprises or consists of SEQ ID NO: 164, the light chain CDR2 region comprises or consists of SEQ ID NO: 175, and the light chain CDR3 region comprises or consists of SEQ ID NO: 193; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 23 and the light chain variable region comprises or consists of SEQ ID NO: 55; more preferably wherein said antibody is 15G04. 219. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 150 or an HCDR3 with at least a 70% identity thereto. 220. The antibody according to embodiment 219, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 97, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 123, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 150, the light chain CDR1 region comprises or consists of SEQ ID NO: 165, the light chain CDR2 region comprises or consists of SEQ ID NO: 178, and the light chain CDR3 region comprises or consists of SEQ ID NO: 197; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 34 and the light chain variable region comprises or consists of SEQ ID NO: 67; more preferably wherein said antibody is 27G04. 221. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 149 or an HCDR3 with at least a 70% identity thereto. 222. The antibody according to the embodiment 221, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 97, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 122, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 149, the light chain CDR1 region comprises or consists of SEQ ID NO: 165, the light chain CDR2 region comprises or consists of SEQ ID NO: 178, and the light chain CDR3 region comprises or consists of SEQ ID NO: 197; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 33 and the light chain variable region comprises or consists of SEQ ID NO: 66; more preferably wherein said antibody is 26G04. 223. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 151 or an HCDR3 with at least a 70% identity thereto. 224. The antibody according to the embodiment 223, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 98, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 124, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 151, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 198; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 35 and the light chain variable region comprises or consists of SEQ ID NO: 68; more preferably wherein said antibody is 28G04. 225. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 146 or with an HCDR3 at least a 70% identity thereto. 226. The antibody according to the embodiment 225, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 95, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 119, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 146, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 26 and the light chain variable region comprises or consists of SEQ ID NO: 58; more preferably wherein said antibody is 18G04. 227. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:144 or an HCDR3 with at least a 70% identity thereto. 228. The antibody according to the embodiment 227, wherein said antibody is selected from the group consisting of: a. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 95, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 117, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 144, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 24 and the light chain variable region comprises or consists of SEQ ID NO: 56; more preferably where said antibody is 16G04; b. an an`tibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 95, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 118, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 145, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 187preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 25 and the light chain variable region comprises or consists of SEQ ID NO: 57; more preferably wherein said antibody is 17G04. 229. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:134 or an HCDR3 with at least a 70% identity thereto. 230. The antibody according to embodiment 229, wherein said antibody is selected from the group consisting of: a. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 86, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 107, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 134, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 187; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 14 and the light chain variable region comprises or consists of SEQ ID NO: 4; more preferably wherein said antibody is 05G04; b. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 86, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 108, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 135, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 188; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 15 and the light chain variable region comprises or consists of SEQ ID NO: 47; more preferably wherein said antibody is 06G04. 231. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 140 or an HCDR3 with at least a 70% identity thereto. 232. The antibody according to embodiment 231, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 91, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 113, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 140, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 187; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 20 and the light chain variable region comprises or consists of SEQ ID NO: 52; more preferably wherein said antibody is 12G04. 233. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 152 or an HCDR3 with at least a 70% identity thereto. 234. The antibody according to embodiment 233, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 91, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 125, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 152, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably the heavy chain variable region comprises or consists of SEQ ID NO: 37 and the light chain variable region comprises or consists of SEQ ID NO: 70; more preferably wherein said antibody is 30G04. 235. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 153 or an HCDR3 with at least a 70% identity thereto. 236. The antibody according to embodiment 235, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 100, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 127, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 153, the light chain CDR1 region comprises or consists of SEQ ID NO: 166, the light chain CDR2 region comprises or consists of SEQ ID NO: 179, and the light chain CDR3 region comprises or consists of SEQ ID NO: 200; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 39 and the light chain variable region comprises or consists of SEQ ID NO: 72; more preferably wherein said antibody is 32G04. 237. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:154 or an HCDR3 with at least a 70% identity thereto. 238. The antibody according to embodiment 237, preferably wherein said antibody is selected from the group consisting of: a. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 101, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 128, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 154, the light chain CDR1 region comprises or consists of SEQ ID NO: 167, the light chain CDR2 region comprises or consists of SEQ ID NO: 180, and the light chain CDR3 region comprises or consists of SEQ ID NO: 201; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 40 and the light chain variable region comprises or consists of SEQ ID NO: 73; more preferably wherein said antibody is 33G04; b. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 101, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 128, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 154, the light chain CDR1 region comprises or consists of SEQ ID NO: 168, the light chain CDR2 region comprises or consists of SEQ ID NO: 181, and the light chain CDR3 region comprises or consists of SEQ ID NO: 202; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 40 and the light chain variable region comprises or consists of SEQ ID NO: 74; more preferably wherein said antibody is 34G04. 239. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:155 or an HCDR3 with at least a 70% identity thereto. 240. The antibody according to embodiment 239, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 102, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 129, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 155, the light chain CDR1 region comprises or consists of SEQ ID NO: 169, the light chain CDR2 region comprises or consists of SEQ ID NO: 182, and the light chain CDR3 region comprises or consists of SEQ ID NO: 203; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 41 and the light chain variable region comprises or consists of SEQ ID NO: 75; more preferably wherein said antibody is 35G04. 241. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:156 or an HCDR3 with at least a 70% identity thereto. 242. The antibody according to embodiment 241, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 103, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 130, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 156, the light chain CDR1 region comprises or consists of SEQ ID NO: 170, the light chain CDR2 region comprises or consists of SEQ ID NO: 183, and the light chain CDR3 region comprises or consists of SEQ ID NO: 204; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 42 and the light chain variable region comprises or consists of SEQ ID NO: 76; more preferably wherein said antibody is 36G04. 243. The antibody according to any of the embodiments 203 to 206, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO:157 or an HCDR3 with at least a 70% identity thereto. 244. The antibody according to embodiment 243, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 104, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 131, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 157, the light chain CDR1 region comprises or consists of SEQ ID NO: 171, the light chain CDR2 region comprises or consists of SEQ ID NO: 184, and the light chain CDR3 region comprises or consists of SEQ ID NO: 205; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 43 and the light chain variable region comprises or consists of SEQ ID NO: 77; more preferably wherein said antibody is 37G04. 245. An antibody that binds to human CD36, wherein the epitope comprises or consists of or consists of amino acid residues 286-292 and/or amino acid residues 341-350 within human CD36 defined by SEQ ID NO: 1, preferably all the residues; more preferably wherein determination of the epitope is conducted by hydrogen-deuterium exchange mass spectrometry. 246. The antibody of embodiment 245, wherein the epitope comprises or consists of amino acid residues 280-298 and/or amino acid residues 341-365 within human CD36 defined by SEQ ID NO: 1, preferably comprises or consists of all the residues. 247. An antibody that specifically binds to human CD36, that binds to the same epitope on human CD36 as antibody 11G04 or competes with antibody 11G04 for binding to human CD36. 248. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 146 or an HCDR3 with at least a 70% identity thereto. 249. The antibody according to embodiment 248, wherein the heavy chain CDR1 region comprises or consists of or consists of SEQ ID NO: 95, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 119, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 146, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein said antibody is selected from the group consisting of: a) an antibody wherein the heavy chain variable region comprises or consists of SEQ ID NO: 26 and the light chain variable region comprises or consists of SEQ ID NO: 58; more preferably wherein said antibody is 18G04; b) an antibody wherein the heavy chain variable region comprises or consists of SEQ ID NO: 26 and the light chain variable region comprises or consists of SEQ ID NO: 59; more preferably wherein said antibody is 19G04; c) an antibody wherein the heavy chain variable region comprises or consists of SEQ ID NO: 27 and the light chain variable region comprises or consists of SEQ ID NO: 60; more preferably wherein said antibody is 20G04. 250. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 144 or an HCDR3 with at least a 70% identity thereto. 251. The antibody according to embodiment 250, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 95, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 117, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 144, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 24 and the light chain variable region comprises or consists of SEQ ID NO: 56; more preferably wherein said antibody is 16G04. 252. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 152 or an HCDR3 with at least a 70% identity thereto. 253. The antibody according to embodiment 252, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 91, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 125, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 152, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 37 and the light chain variable region comprises or consists of SEQ ID NO: 70; more preferably wherein said antibody is 30G04. 254. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 154 or an HCDR3 with at least a 70% identity thereto. 255. The antibody according to embodiment 254, wherein said antibody is selected from the group consisting of: a. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 101, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 128, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 154, the light chain CDR1 region comprises or consists of SEQ ID NO: 167, the light chain CDR2 region comprises or consists of SEQ ID NO: 180, and the light chain CDR3 region comprises or consists of SEQ ID NO: 201; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 40 and the light chain variable region comprises or consists of SEQ ID NO: 73; more preferably wherein said antibody is 33G04; b. an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 101, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 128, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 154, the light chain CDR1 region comprises or consists of SEQ ID NO: 168, the light chain CDR2 region comprises or consists of SEQ ID NO: 181, and the light chain CDR3 region comprises or consists of SEQ ID NO: 202; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 40 and the light chain variable region comprises or consists of SEQ ID NO: 74; more preferably wherein said antibody is 34G04. 256. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 155 or an HCDR3 with at least a 70% identity thereto. 257. The antibody according to embodiment 256, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 102, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 129, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 155, the light chain CDR1 region comprises or consists of SEQ ID NO: 169, the light chain CDR2 region comprises or consists of SEQ ID NO: 182, and the light chain CDR3 region comprises or consists of SEQ ID NO: 203; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 41 and the light chain variable region comprises or consists of SEQ ID NO: 75; more preferably wherein said antibody is 35G04. 258. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 156 or an HCDR3 with at least a 70% identity thereto. 259. The antibody according to embodiment 258, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 103, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 130, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 156, the light chain CDR1 region comprises or consists of SEQ ID NO: 170, the light chain CDR2 region comprises or consists of SEQ ID NO: 183, and the light chain CDR3 region comprises or consists of SEQ ID NO: 204; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 42 and the light chain variable region comprises or consists of SEQ ID NO: 76; more preferably wherein said antibody is 36G04. 260. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 157 or an HCDR3 with at least a 70% identity thereto. 261. The antibody according to embodiment 260, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 104, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 131, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 157, the light chain CDR1 region comprises or consists of SEQ ID NO: 171, the light chain CDR2 region comprises or consists of SEQ ID NO: 184, and the light chain CDR3 region comprises or consists of SEQ ID NO: 205; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 43 and the light chain variable region comprises or consists of SEQ ID NO: 77; more preferably wherein said antibody is 37G04. 262. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 158 or an HCDR3 with at least a 70% identity thereto. 263. The antibody according to embodiment 262, wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 105, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 132, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 158, the light chain CDR1 region comprises or consists of SEQ ID NO: 172, the light chain CDR2 region comprises or consists of SEQ ID NO: 185, and the light chain CDR3 region comprises or consists of SEQ ID NO: 206; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 44 and the light chain variable region comprises or consists of SEQ ID NO: 78; more preferably wherein said antibody is 38G04. 264. The antibody according to any of embodiments 245-247, wherein said antibody is an antibody having the HCDR3 of SEQ ID NO: 139 or an HCDR3 with at least a 70% identity thereto. 265. The antibody according to embodiment 262, wherein said antibody is selected from the group consisting of: a) an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 90, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 112, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 139, the light chain CDR1 region comprises or consists of SEQ ID NO: 160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 190; preferably wherein the heavy chain variable region comprises or consists of SEQ ID NO: 19 and the light chain variable region comprises or consists of SEQ ID NO: 51; more preferably wherein said antibody is 11G04 or 11G06; b) an antibody wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 90, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 248, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 139, the light chain CDR1 region comprises or consists of SEQ ID NO:160, the light chain CDR2 region comprises or consists of SEQ ID NO: 174, and the light chain CDR3 region comprises or consists of SEQ ID NO: 247; preferably wherein said antibody is selected from the group consisting of: i. an antibody wherein the heavy chain variable region comprises or consists of SEQ NO: 241 and the light chain variable region comprises or consists of SEQ ID NO: 240; preferably wherein said antibody is 73G06; ii. an antibody wherein the heavy chain variable region comprises or consists of SEQ NO: 243 and the light chain variable region comprises or consists of SEQ ID NO: 240; preferably wherein said antibody is 74G06; iii. an antibody wherein the heavy chain variable region comprises or consists of SEQ NO: 241 and the light chain variable region comprises or consists of SEQ ID NO: 242; preferably wherein said antibody is 75G06; and iv. an antibody wherein the heavy chain variable region comprises or consists of SEQ NO: 243 and the light chain variable region comprises or consists of SEQ ID NO: 242; preferably wherein said antibody is 76G06; c) wherein the heavy chain CDR1 region comprises or consists of SEQ ID NO: 90, the heavy chain CDR2 region comprises or consists of SEQ ID NO: 248, the heavy chain CDR3 region comprises or consists of SEQ ID NO: 139, the light chain CDR1 region comprises or consists of SEQ ID NO:160, the light chain CDR2 region comprises or consists of SEQ ID NO: 246, and the light chain CDR3 region comprises or consists of SEQ ID NO: 247; preferably wherein said antibody is selected from the group consisting of: i. the heavy chain variable region comprises or consists of SEQ NO: 241 and the light chain variable region comprises or consists of SEQ ID NO: 244; preferably wherein said antibody is 77G06; ii. the heavy chain variable region comprises or consists of SEQ NO: 243 and the light chain variable region comprises or consists of SEQ ID NO: 244; preferably wherein said antibody is 78G06; iii. the heavy chain variable region comprises or consists of SEQ NO: 241 and the light chain variable region comprises or consists of SEQ ID NO: 245; preferably wherein said antibody is 79G06; and iv. the heavy chain variable region comprises or consists of SEQ NO: 243 and the light chain variable region comprises or consists of SEQ ID NO: 245; preferably wherein said antibody is 80G06. 266. The antibody of any one of the preceding embodiments, wherein the antibody specifically binds to human CD36. 267. The antibody of embodiment 266, wherein the antibody has cross-reactivity to human CD36 and non-human CD36. 268. The antibody of embodiment 267, wherein the antibody has cross-reactivity to human CD36 and non-human primate CD36. 269. The antibody of embodiment 268, wherein the non-human primate CD36 is cynomomolgus CD36 or rhesus macaque CD36. 270. The antibody of embodiment 267, wherein the antibody has cross-reactivity to human CD36, non-human primate CD36, and rodent CD36. 271. The antibody of embodiment 270, wherein the rodent CD36 is mouse CD36 or rat CD36. 272. The antibody of any one of the preceding embodiments, wherein the antibody binds to human CD36 with a KD of less than 20 nM, as measured using surface plasmon resonance with a bivalent model. 273. The antibody of embodiment 272, wherein the antibody binds to human CD36 with a KD of less than 10 nM, as measured using surface plasmon resonance with a bivalent model. 274. The antibody of any of the preceding embodiments, wherein the antibody inhibits fatty acid uptake in HEK 293 cells expressing CD36 with an IC 50 of less than 20 nM, as measured by FACS assay. 275. The antibody of any of the preceding embodiments, wherein the anti-CD36 antibody inhibits oxLDL uptake with an IC 50 of less than 10 nM, as measured by the anti-CD36 antibody’s ability to inhibit uptake of oxLDL linked to a fluorophore into SCC cells stably expressing human CD36. 276. The antibody of any one of the preceding embodiments, which comprises a heavy chain constant region. 277. The antibody of embodiment 276, wherein the heavy chain constant region is selected from the group consisting of human immunoglobulin IgA1, IgA2, IgG1, IgG2, IgG3, or IgG4 heavy chain constant regions. 278. The antibody of embodiment 277, which comprises an IgG1 heavy chain constant region. 279. The antibody of embodiment 277 or 278, wherein the heavy chain constant region comprises an IgG constant region containing at least one amino acid substitution, wherein the at least one amino acid substitution results in reduced Fc binding to at least one Fcgamma receptor and reduced Fc effector function. 280. The antibody of embodiment 277 or 278, wherein the at least one Fc silencing mutation includes the amino acid substitutions L234A and L235A ("LALA"). 281. The antibody of embodiment 279, wherein the at least one Fc silencing mutation includes a set of amino acid substitutions selected from the group consisting of L234G, L235S, and G236R; L234S, L235T, and G236R; L234S, L235V, and G236R; L234T, L235Q, and G236R; L234T, L235T, and G236R; L234A, L235S, and G236R; L234Q, L235S, and G236R; L234S, L235G, and G236R; L234T, L235S, and G236R; L234Q, L235S, and G236R; L234A and L235A; and L234A, L235A, and P329G. 282. The antibody of embodiment 277, which comprises an IgG4 heavy chain constant region. 283. The antibody of any of embodiments 281 or 282, wherein the heavy chain constant region comprises an IgG constant region containing the amino acid substitution S228P; preferably wherein said heavy chain constant region is a human IgG4 constant region containing the amino acid substitutions S228P and L235E. 284. The antibody of any one of the preceding embodiments, wherein the antibody comprises a light chain constant region. 285. The antibody of embodiment 284, wherein the light chain constant region is selected from the group consisting of human immunoglobulins κ and λ light chain constant regions. 286. The antibody of any one of the preceding embodiments, wherein the antibody further comprises a heavy chain constant region and a light chain constant region, wherein the heavy chain constant region is a human IgG1 heavy chain constant region, and wherein the light chain constant region is a human κ light chain constant region. 287. The antibody of any one of the preceding embodiments, wherein the antibody is a bispecific antibody. 288. The antibody of embodiment 287, comprising a first antigen-binding region that specifically binds to CD36. 289. The antibody of embodiment 288, comprising a second antigen-binding region that specifically binds to an immune cell antigen. 290. The antibody of embodiment 289, wherein the immune cell antigen is selected from the group consisting of PD-1, PD-L1, CTLA4, CD3, LAG3, OX40, CD28, CD33, B7H3, CD47, TIM3, ICOS, LGR5, 4-1BB, CD40, CD40-L, and TIGIT. 291. The antibody of embodiment 288, comprising a second antigen-binding region that specifically binds to a tumor-specific antigen. 292. The antibody of embodiment 291, wherein the tumor-specific antigen is selected from the group consisting of HER2, HER3, EGFR, VEGF, IGF-1, IGF-2, ANG2, DLL1, IGF-1R, cMET, DLL4, FAP, DR5, IL15, IL15Ra, CD3, CEA, EPCAM, HER3, PSMA, PMEL, and GPC3. 293. The antibody of embodiment 289 to 292, wherein the immune cell antigen or tumor- specific antigen is CD3. 294. The antibody of embodiment 288, wherein the antibody is a biparatopic antibody. 295. The antibody of embodiment 294, comprising two antigen-binding regions, wherein each antigen-binding region specifically binds to a unique, non-overlapping CD36 epitope. 296. The antibody of embodiment 295, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04. 297. The antibody of embodiment 296, further comprising a second antigen-binding domain, which comprises an antigen-binding domain of an antibody selected from the group consisting of 10G04, 11G04, 19G04, 20G04, and 30G04. 298. The antibody of any of embodiments 294 to 297, comprising a first antigen-binding domain, which comprises the antigen-binding domain of 1G04, and a second antigen- binding domain, which comprises an antigen-binding domain of 11G04. 299. The antibody of any one of the preceding embodiments, which is an antigen binding fragment. 300. The antigen binding fragment of embodiment 299, wherein the antigen binding fragment comprises a Fab, Fab', F(ab') 2 , single chain Fv (scFv), disulfide linked Fv, V-NAR domain, IgNar, intrabody, IgGΔCH2, minibody, F(ab') 3 , tetrabody, triabody, diabody, single-domain antibody, DVD-Ig, Fcab, mAb2, (scFv) 2 , or scFv-Fc. 301. A pharmaceutical composition comprising the antibody of any one of the preceding embodiments and a pharmaceutically acceptable excipient. 302. The pharmaceutical composition of embodiment 301, wherein at least 95% of the antibodies in the composition are afucosylated. 303. An antibody or pharmaceutical composition as described in any one of the preceding embodiments for use as a medicament. 304. An antibody or pharmaceutical composition as described in any one of the preceding embodiments for use in a method of treating cancer as described in the present application, optionally in a combination treatment as described herein. 305. An antibody or pharmaceutical composition according to embodiment 304, wherein the cancer is oral squamous cell carcinoma, head and neck cancer, esophageal cancer, gastric cancer, ovarian cancer, cervical cancer, lung cancer, breast cancer, colon cancer, renal cancer, prostate cancer, sarcoma, melanoma, leukemia, or lymphoma. 306. An antibody or pharmaceutical composition according to embodiment 304, wherein the treatment reduces the size of metastatic tumors, as measured by IVIS imaging or H&E staining. 307. An antibody or pharmaceutical composition according to embodiment 302, wherein the treatment inhibits the formation or development of metastatic tumors, as measured by IVIS imaging or H&E staining. EXAMPLES Example 1: Animal studies materials and methods [0303] Unless otherwise indicated, the animal studies disclosed in the Examples below were carried out using the following materials and methodologies. [0304] NOD scid gamma (NSG) (NOD.Cg-Prkdc scid II2rg tm1Wjl /SzJ) mice were purchased from Charles River and crossed in-house. All mice were housed under a regimen of 12h light / 12h dark cycles and SPF conditions, and all procedures were evaluated and approved by the CEEA (Ethical Committee for Animal Experimentation) from the Government of Catalunya. SCC intra-tongue injection was performed as previously described (Oskarsson et al., 2014; Nieman et al., 2011). Briefly, mice were anesthetized by intraperitoneal injection with a mixture of 50 mg per kg of ketamine and 0.5 mg per kg of medetomidin, and SCC cells resuspended in 30 μl PBS were injected into each mouse tongue with a BD ultra-fine 6 mm needle. Mice were monitored for the luciferase bioluminescent signal immediately after injection (T0) and once weekly thereafter with a Xenogen IVIS Imaging System-100 (Caliper Life Sciences). Briefly, animals were injected by retro-orbital injection with 50 μl of D-luciferin (Promega) diluted in 1×PBS at 5 mg ml −1 . Continuous administration of isofluorane gas was provided to ensure anesthetizing animals during imaging. Data was quantified with the Living Image software version 4.4 (Caliper Life Sciences). Quantifications were calculated with unsaturated pixels. Color scale minimum and maximum values are shown in pictures. [0305] To treat mice in vivo with neutralizing anti-CD36 antibodies, mice were injected intraperitoneally with 100 μl of physiological serum containing 5 μg, 10 μg or 20 μg of the neutralizing monoclonal anti-CD36 antibody JC63.1 (CAYMAN, CAY-10009893- 500); 5 μg, 10 μg or 20 μg of neutralizing monoclonal anti-CD36 ONA-0-v1 (either IgA or IgG isotype); or 5 μg, 10 μg or 20 μg of the corresponding control IgA (mouse IgA, kappa [S107], Abcam, ab37322) or IgG antibody. These doses corresponded to 0.25, 0.5, and 1 mg/kg, respectively. All antibodies were azide-free with no added preservative compound. [0306] For each experiment, mice were sacrificed at the same time, once an experimental group reached the humane endpoint according to the approved CEEA protocol (4-6 weeks after the orthotopic injection as soon as mice started to lose weight due to the growth of the oral lesion), and subsequent cell analysis was performed. [0307] Total blood samples from mice were collected from the inferior vena cava and then processed in the Experimental Toxicology and Ecotoxicology Unit (PCB) following standard procedures. [0308] Animal tissue was collected and fixed with 4% paraformaldehyde (PFA) for overnight at room temperature (RT) and then either embedded in OCT and frozen at −80 °C or dehydrated and embedded in paraffin. Toxicological study was performed at the Histopathology Facility according to standard procedures. [0309] Histological Analysis. For analysis, cryo- or de-paraffinized antigen retrieved sections (10 min in boiling 0.01M citric acid, pH 6.0) of 8 μm were permeabilized for 25 min in 0.25% Triton X-100/PBS and blocked for 90 min in 0.25% gelatin/PBS. Hematoxilin and eosin (H&E) staining was done according to the standard protocol. Images were acquired using a Nikon E600+Olympus DP72, Leica SPE and a Leica TCS SP5 confocal microscope. Representative pictures were selected in each case. [0310] For all the experiments, adequate sample size was determined based on results of pilot studies. No statistical method was used to determine sample size. All the animals that fulfilled proper experimental conditions during the experimental procedures were included in the analysis. Based on results of pilot studies, homogeneous groups of males and females between 8 and 12 weeks and their control littermates were used for the experimental studies. Animals were randomized at day 7 post-injection based on luminescence intensity of the primary tumours or of the cervical lymph nodes metastasis. Data are generally shown as the mean±s.e.m. Statistical significance was analyzed using Prism 6 software (GraphPad) by using a two-tailed t-test, Mann-Whitney U test, Fisher exact test or hypergeometric test. Significance was considered at P< or equal 0.05. Example 2: Treatment of cancer using an anti-CD36 antibody, with or without cisplatin, in a mouse model of oral cancer [0311] Studies of the effects of an anti-CD36 antibody, both with and without cisplatin, were performed in NSG mice (immuno-deficient). An experimental overview of these studies is provided in Figure 1A. The studies included only male mice, though similar trends (data not reported) were observed using female mice. All mice were inoculated with commercially available Detroit 562 (ATCC) cancer cells, transduced with a retroviral vector expressing luciferase and the green fluorescent protein (Luc-GFP). Detroit 562 cells were derived from the metastatic site of a pharyngeal carcinoma (i.e., from an oral cancer). Prior to inoculation, the Detroit 562 cells were cultured in a humidified incubator at 37° C. with 5% CO 2 , and were grown in EMEM (LONZA) supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0312] For each mouse, 50,000 Detroit 562 cells were inoculated via orthotopic injection. Previous testing revealed that, in untreated NSG mice, 100% of mice inoculated with Detroit 562 cells formed a large primary tumor and 81% of inoculated mice were observed to develop lymph node metastases within one week of inoculation. [0313] Treatment of the inoculated mice began nine days after inoculation with the cancer cells. Inoculated mice were divided into four distinct treatment groups. As can be seen in Figure 1B, the treatment groups were: Group 1: IgA isotype control (n = 9 on days 1 through 23; n = 6 on day 29); Group 2: IgA isotype control plus cisplatin (n = 5); Group 3: commercial anti-CD36 antibody (JC63.1) (n = 6 on days 1 through 23; n = 4 on day 29); Group 4: commercial anti-CD36 antibody (JC63.1) plus cisplatin (n = 5). [0314] Antibody treatments were administered via intraperitoneal (i.p.) injection daily at a dose of 1 mg/kg. Cisplatin was administered twice weekly at a dose of 2 mg/kg (Groups 2 and 4). Mice that did not receive cisplatin (Groups 1 and 3) instead received a volume equivalent injection of PBS. During the course of treatment, mice were observed once weekly using an in vivo imaging system (IVIS). Further, mouse body weight was measured twice weekly to update appropriate dosage amounts. Mice were sacrificed either when their bodyweight dropped under the ethical approved guidelines or at the end of the treatment period. Upon sacrifice, organs and tissues were collected for performance of immunohistochemistry analysis. [0315] As can be seen in Figures 2A-2C, the tested anti-CD36 Ab treatment has at least additive anti-tumor activity with cisplatin on suppressing the growth of a primary tumor in oral cancer. Figure 2A shows that mice treated with both anti-CD36 antibody and cisplatin were better able to suppress tumor growth than mice treated with control antibody (IgA) and cisplatin, as measured by the relative intensity of luciferase-induced luminescence in treated mice relative to control mice. Figure 2B shows a representative image of a primary tumor developed in the tongue after orthotopic injection of the Detroit 562 cells. Figure 2C shows that mice treated with both anti-CD36 antibody or with control antibody (IgA) and cisplatin had primary tumors with reduced tumor surface area. [0316] Figure 3 shows representative images of lung metastases present in mice inoculated with Detroit 562 cancer cells and treated as described above. These images illustrate that mice treated with cisplatin (top right), a commercial anti-CD36 antibody (JC63.1; bottom left), or cisplatin and JC63.1 (bottom right) have fewer and smaller metastases than control treated mice (top left). Further, the quantitation of the number (Figure 4A) and size (Figure 4B) of lung metastases shows that mice treated with JC63.1 alone had smaller and fewer metastases than control-treated mice. Mice treated with cisplatin alone had similar numbers of metastases to control cells, though cisplatin did reduce the size of the metastatic tumors. Treatment with both JC63.1 and cisplatin resulted in mice with similar numbers of metastases as treatment with JC63.1 alone. However, treatment with both JC63.1 and cisplatin resulted in reduction of metastatic tumor size to a greater extent than either JC63.1 or cisplatin alone. For example, anti- CD36 antibody treatment alone, and cisplatin in combination with an isotype control antibody, inhibited limited the size of metastatic tumors such that 25-40% of the metastatic tumors were only a few cells, as measured using immunohistochemistry analysis. Treatment with anti-CD36 antibody in combination with cisplatin limited the size of metastatic tumors such that over 80% of the metastatic tumors were only a few cells, as measured using immunohistochemistry analysis. Example 3: Treatment of cancer using the ONA-0-v1 anti-CD36 antibody, with or without cisplatin, in a mouse model of oral cancer [0317] Studies on the combination of the effects of the ONA-0-v1 anti-CD36 antibody, both with and without cisplatin, were performed in NSG mice (immuno-deficient). An experimental overview of these studies is provided in Figure 5A. The studies included both male and female mice. All mice were inoculated with commercially available FaDu (ATCC) cancer cells, transduced with a retroviral vector expressing luciferase and the green fluorescent protein (Luc-GFP). FaDu cells were derived from a squamous cell carcinoma (i.e., from an oral cancer). Prior to inoculation, the FaDu cells were cultured in a humidified incubator at 37° C. with 5% CO2, and were grown in EMEM (LONZA) supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0318] For each mouse, 100,000 FaDu cells were inoculated via orthotopic injection. Previous testing revealed that, in untreated NSG mice, 100% of mice inoculated with FaDu cells formed a large primary tumor and 91% of inoculated mice were observed to develop lymph node metastases within one week of inoculation. [0319] Treatment of the inoculated mice began nine days after inoculation with the cancer cells. Inoculated mice were divided into four distinct treatment groups. As can be seen in Figure 5B, the treatment groups were: Group 1: IgA isotype control (n = 7); Group 2: IgA isotype control plus cisplatin (n = 8); Group 3: anti-CD36 antibody ONA-0-v1 (n = 8); Group 4: anti-CD36 antibody ONA-0-v1 plus cisplatin (n = 8). [0320] Antibody treatments were administered via intraperitoneal (i.p.) injection daily at a dose of 1 mg/kg. Cisplatin was administered twice weekly at a dose of 2 mg/kg (Groups 2 and 4). Mice that did not receive cisplatin (Groups 1 and 3) instead received a volume equivalent injection of PBS. During the course of treatment, mice were observed once weekly using an in vivo imaging system (IVIS). Further, mouse body weight was measured twice weekly to update appropriate dosage amounts. At the end of the treatment period, the mice were sacrificed, and organs and tissues were collected for performance of immunohistochemistry analysis. [0321] As can be seen in Figures 6A and 6B, treating with the anti-CD36 antibody ONA- 0-v1 in combination with cisplatin had similar effects to treating with cisplatin alone as measured by IVIS imaging and H&E staining of the primary tumor. Treatment with ONA-0-v1 alone at a 1 mg/kg dose in this model did not have a statistically significant effect on the primary tumor relative to treatment with an isotype control antibody. In contrast, Figures 7A and 7B show that treatment with ONA-0-v1 alone was able to inhibit growth of lymph node metastases, as measured by relative intensity in IVIS imaging. Moreover, treatment with ONA-0-v1 in combination with cisplatin resulted in almost complete inhibition of lymph node metastasis growth, as measured by relative intensity in IVIS imaging. [0322] Treatment with the ONA-0-v1 antibody inhibited growth of lymph node metastases. Figure 8 shows a representative IVIS image of an inoculated NSG mouse on day 7 post-orthotopic injection of FaDu cells, immediately prior to the start of treatment. The lymph node metastasis in that mouse is indicated by the circled area, with the intensity of the luciferase signalling indicated by the heat map. Figure 8 also shows the quantitation of the lymph node metastases present in all groups of mice on day 7. That initial intensity was the same in all groups. Further IVIS imaging was performed at the end-point of treatment, As shown in Figure 9 (left panel), treatment with ONA-0-v1 antibody inhibited metastatic tumor growth by greater than 50% relative to the IgA isotype control, as measured by the ratio of IVIS imaging intensity between the ending and starting points of treatment. Further, also as shown in Figure 9 (right panel), addition of ONA-0-v1 to cisplatin enhanced cisplatin's ability to inhibit metastatic tumor growth. The ONA-0-v1 and cisplatin combination resulted in almost complete inhibition of tumor growth in lymph node metastases. [0323] Treatment with the ONA-0-v1 antibody also inhibited penetrance of metastases into lymph nodes, as shown in Figure 10. All control mice presented with lymph node metastases. Treatment with either cisplatin or ONA-0-v1 prevented metastasis into the lymph nodes in one of the eight tested mice in each respective treatment group (i.e., 12.5%). Moreover, ONA-0-v1's inhibition of penetrance was synergistic with that of cisplatin, as the combination of cisplatin and ONA-0-v1 prevented any metastasis in five of the eight tested mice (i.e., 62.5%). [0324] Treatment with the ONA-0-v1 antibody was well-tolerated by NSG mice over the course of treatment. As shown in Figure 11A and Figure 11B, ONA-0-v1 treatment alone did not have any effects on mouse body weight or platelet count relative to isotype control-treated mice. ONA-0-v1 treatment also did not significantly enhance cisplatin- mediated weight loss or the cisplatin-mediated decrease in platelet count. Example 4: Antitumor efficacy of anti-CD36 antibodies in combination with PD1 inhibition in C57Bl6/J mice bearing YUMM1.7 cells-derived melanoma tumors [0325] 250,000 YUMM1.7 cells are suspended in PBS and are injected subcutaneously in the flank of 8-12 week-old C57Bl6/J mice. When tumors reach a mean volume of 50-100 mm 3 , mice are randomized and the treatment is started. [0326] The experimental groups are as shown in Table 6 below. TABLE 6 – Treatment Groups for Treating with anti-CD36 and anti-PD-1 Antibodies [0327] All antibodies are injected IP at the concentration of 10 mg/kg, 3 times/week. Mice are monitored three times per week for body weight and tumour volume and daily for behaviour and survival. When tumour reaches a maximum volume of 1.500 mm 3 , mice are euthanized and tissues collected. Primary tumours are weighted and measured again with a caliper. Lung and liver are embedded in paraffin for H&E staining and a blinded analysis for metastatic lesions. Results of the study will show that anti-CD36 antibodies (e.g., 1G04) and anti-PD-1 antibodies have additive or synergistic effects in treating cancer in the YUMM1.7 mouse model of melanoma. Example 5: Treatment of ovarian cancer using the ONA-0-v1 anti-CD36 antibody [0328] Studies of the effects of the ONA-0-v1 anti-CD36 antibody on ovarian cancer were performed in NSG mice (immuno-deficient). An experimental overview of these studies is provided in Figure 12A. The studies included only female mice. All mice were inoculated with commercially available OVCAR-3 (ATCC) cancer cells. OVCAR-3 cells were derived from a human progressive adenocarcinoma of the ovary (i.e., from an ovarian cancer). Prior to inoculation, the OVCAR-3 cells were cultured in a humidified incubator at 37 °C with 5% CO2, and were grown in RPMI-1640 supplemented with 5 μg ml −1 penicillin/streptomycin, 0.01 mg/ml bovine insulin and 20% FBS (GIBCO). [0329] For each mouse, a piece of an OVCAR-3 xenograft was implanted orthotopically. As shown in Figure 12B, NSG mice implanted with OVCAR-3 cells form a large primary tumor. Mice implanted with OVCAR-3 also develop metastases in both the peritoneal wall and liver. Exemplary metastases from inoculated mice are shown in Figures 13A and 13B. [0330] Treatment of the implanted mice began 23 days after implantation with the OVCAR-3 tumor pieces. Inoculated mice were divided into one of two treatment groups: vehicle injection control (n = 9) or ONA-0-v1 treatment (n = 9). Antibody treatments were administered via intraperitoneal (i.p.) injection daily at a dose of 3 mg/kg, while control mice received an equal volume of vehicle on the same schedule. Mice were sacrificed at the end of the treatment period. Upon sacrifice, organs and tissues were collected for performance of immunohistochemistry analysis. [0331] As can be seen in Figures 12B and 12C, treatment with ONA-0-v1 results in smaller tumors in the OVCAR-3 mouse model of ovarian cancer. The quantification of this effect in Figure 12C shows that treatment with OVCAR-3 reduced tumor weight from an average of 1.844 g to an average of 1.058 g, a decrease of 43% percent. These data indicate that ONA-0-v1 inhibited tumor growth and/or promoted tumor cell destruction during the treatment period. [0332] Histological analysis of the primary tumors in vehicle-treated and ONA-0-v1– treated mice was also performed. First, the tumors were analyzed to determine percent necrosis by visual inspection and quantification of a pathologist. The results of this analysis are shown in Figure 12D, which shows that ONA-0-v1 increased necrosis from approximately 24.4% to approximately 40.71% (* = p value of 0.0287). This increase indicates that treated tumors present higher cell death. The primary tumors of treated and ONA-0-v1–treated mice were also analyzed to determine the percent of collagenous and fibrotic areas by Sirius red staining. The results of this analysis are shown in Figure 12E, which shows that ONA-0-v1 increased the SR positive area from 16.9% to 22.5% (*= p value of 0.0457). This increase indicates that treatment with ONA-0-v1 increases fibrosis and, together with the increased necrosis, indicates that the treated tumors are not only smaller, but also they are composed of fewer tumoral cells. [0333] Figures 14A, 14B, and 14C show the results of quantifying metastatic tumors in ONA-0-v1 treated mice. Figure 14A shows that the total number of metastases decreased by over 50% in the ONA-0-v1–treated mice relative to vehicle-treated mice. The total number of metastases was determined by visual inspection of the organs. Figure 14B and Figure 14C show the results of macroscopic analysis of the size of metastases in the peritoneal wall and liver, respectively. The size of the metastases was measured by visual inspection. In the vehicle-treated group, 48% of the animals had large metastasis (>5mm), 41% small metastasis (1-2mm), and 11% no metastasis in the peritoneal wall. In the ONA-0-v1 treated animals, no large metastasis were detected, 38% of the animals had small metastasis, and 63% presented no metastasis. In the liver, the percentage of mice without metastasis increased from 22% in the vehicle group to 50% in the treated group. Among the animals with liver metastasis, the number of large ones was reduced from 16% to 6% and small ones from 62% to 44%. Treating with ONA-0-v1 shifted the size of peritoneal wall metastases such that large metastases disappeared entirely, and more mice did not have peritoneal metastases at all (Figure 14B). Similarly, treating with ONA-0-v1 shifted the size of liver metastases such that fewer large metastases were found, and more mice did not have liver metastases at all (Figure 14C). Collectively, Figures 14A, 14B, and 14C show that ONA-0-v1 is effective at reducing the formation and growth of metastases from ovarian cancer. Example 6: Treatment of ovarian cancer using the ONA-0-v1 and 1G04 anti-CD36 antibodies [0334] Studies of the effects of the ONA-0-v1 and 1G04 anti-CD36 antibodies on ovarian cancer were performed in NSG mice (immuno-deficient). An experimental overview of these studies is provided in Figure 15A. The studies included only female mice. All mice were inoculated with commercially available OVCAR-3 (ATCC) cancer cells. OVCAR-3 cells were derived from a human progressive adenocarcinoma of the ovary (i.e., from an ovarian cancer). For each mouse, a piece of an OVCAR-3 xenograft was implanted orthotopically. Prior to inoculation, the OVCAR-3 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 , and were grown in RPMI-1640 supplemented with 5 μg ml −1 penicillin/streptomycin, 0.01 mg/ml bovine insulin and 20% FBS (GIBCO). [0335] Treatment of the implanted mice began 7 days after implantation with the OVCAR-3 tumor pieces. Inoculated mice were divided into one of three treatment groups: vehicle injection control (n = 9), ONA-0-v1 treatment (n = 9), or 1G04 treatment (n = 9). ONA-0-v1 antibody treatments were administered via intraperitoneal (i.p.) injection daily at a dose of 3 mg/kg.1G04 antibody treatments were administered via i.p. injection TIW (three-times weekly) at a dose of 10 mg/kg. Control mice received an equal volume of vehicle daily. As can be seen in Figure 15B, the weight of mice in all three treatment groups remained the same throughout the treatment period. Mice were sacrificed at the end of the treatment period. Upon sacrifice, organs and tissues were collected for performance of necropsy and histopathology analysis. [0336] Figures 15C-15G show the results of quantifying metastatic tumors in treated mice. Figure 15C shows the total number of metastases for each treatment condition. The total number of metastases was determined by visual inspection of the organs. This analysis revealed that the number of metastases decreased by approximately 45% in the ONA-0-v1–treated mice, relative to vehicle-treated mice (52 metastasis counted in vehicle and 29 in treated group). The total number of metastases also decreased by approximately 35% in the 1G04–treated mice, relative to vehicle-treated mice (52 metastasis counted in vehicle and 34 in treated group). [0337] Figure 15D and Figure 15E show the results of macroscopic analysis of the size of metastases in the peritoneal wall and liver, respectively. The size of the metastases was measured by visual inspection. Treating with either ONA-0-v1 or 1G04 reduced the observed size of metastases such that fewer large (>5mm) and medium (1-2mm) sized metastases were observed. Vehicle-treated animals presented with 26% of the mice having >5mm metastasis, 39% having 2-5 mm metastasis, and 13% having 1-2 mm metastasis in the peritoneal wall. ONA-0-v1 treated animals presented with 19% of mice having >5mm metastasis, 19% having 2-5 mm metastasis, and 19% having 1-2 mm metastasis in the peritoneal wall.1G04-treated animals presented with 7% of mice having >5mm metastasis, 11% with 2-5 mm metastasis, and 49% with 1-2 mm metastasis in the peritoneal wall. In addition, the livers of treated mice showed an analogous pattern. Vehicle-treated animals presented with 5% of the mice having 2-5 mm metastasis, 25% having 1-2 mm metastasis, and 25% having <1 mm metastasis in the liver. ONA-0-v1 treated animals presented with 6% of the mice having 2-5 mm metastasis, 17% having 1- 2 mm metastasis, and none having <1mm metastasis in the liver.1G04-treated none with 2-5 mm metastasis, 11% with 1-2 mm metastasis and none with <1mm metastasis. Moreover, treatment with either ONA-0-v1 or 1G04 increased the percentage of animals that were free of metastases in the peritoneal wall and liver.22% of the vehicle-treated mice, 44% of the ONA-0-v1–treated mice, and 33% of the 1G04-treated mice were metastasis-free in the peritoneal wall.44% of vehicle-treated mice, 78% of the ONA-0- v1–treated mice, and 89% of the 1G04-treated mice were free of metastasis in the liver. [0338] Figure 15F shows the results of microscopic analysis of the penetrance of metastases in the lung. As with the peritoneal wall and liver, treatment with either ONA- 0-v1 or 1G04 increased the percentage of animals that were free of metastases in the lung (from 33% in vehicle to 44% and 66% in ONA-0-v1 and 1G04 groups respectively). Moreover, as quantified in Figure 15G, treatment with either ONA-0-v1 or 1G04 reduced the number of metastases in the lungs per mouse (mean metastasis number 3.6 in vehicle- treated, 1.6 in ONA-0-v1 and 1.2 in 1G04 groups). [0339] Collectively, Figures 15C-15G show that both ONA-0-v1 (a murine IgA antibody) and 1G04 (a chimeric IgG1 antibody) are effective at reducing the formation and growth of metastases from ovarian cancer. Example 7: Treatment of colon cancer using the 1G04 anti-CD36 antibody [0340] Studies of the effects of the 1G04 anti-CD36 antibody on colon cancer were performed in BALB/c nude mice (immuno-deficient). An experimental overview of these studies is provided in Figure 16A. The studies included only female mice. All mice were inoculated with commercially available HCT-116 (ATCC) cancer cells, transduced with a retroviral vector expressing luciferase. HCT-116 cells were derived from a human colorectal carcinoma (i.e., from a colon cancer). Prior to inoculation, the HCT-116 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 , and were grown in McCoy’s 5A medium supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0341] For each mouse, 2x10 6 HCT-116 cells were inoculated via orthotopic injection. Each mouse was imaged after inoculation and one week later and liver metastasis were confirmed by ex vivo luminescence prior to start of treatment. Treatment began 12 days after inoculation with the HCT-116 cells. Inoculated mice were divided into one of two treatment groups: vehicle injection control (n = 10) or 1G04 treatment (n = 10). Antibody treatments were administered via intraperitoneal (i.p.) injection at a dose of 10 mg/kg three times per week, while control mice received an equal volume of vehicle on the same schedule. One day prior to the start of treatment, and at 7, 14, and 21 days after the start of treatment, all mice were imaged via IVIS. Mice were sacrificed at the end of the treatment period (day 25). Upon sacrifice, organs and tissues were collected for performance of necropsy, ex-vivo IVIS, and histopathology. [0342] As can be seen in Figure 16B, mice treated with 1G04 were better able to maintain weight during the course of treatment. Figure 16C shows the results of whole-animal bioluminescence imaging over time, which is a readout for the growth of luciferase- containing tumor cells in the mouse. The bioluminescence imaging showed that 1G04 decreased whole animal luminescence, and thus slowed the growth of the injected HCT- 116 tumor cells in vivo. [0343] Figures 16D, 16E, 16F, and 16G show the results of quantifying metastatic tumors in the 1G04 and vehicle treated mice. After the organs to be examined were removed from the mice, the luminescence of the metastatic tumors in the liver (Figure 16D), lung (Figure 16E), spleen (Figure 16F), and kidney (Figure 16G) was quantified by ex vivo luminescence using IVIS. In each organ, 1G04 treatment decreases the luminescence, reflecting a reduction in the size and/or number of metastases. The observed mean luminiscence values for liver, lung, spleen and kidney of vehicle-treated mice were 1.69*10 8 , 5.38*10 6 , 2.66*10 8 , and 4.11*10 7 , respectively. The observed mean luminiscence values for liver, lung, spleen and kidney of 1G04-treated mice were 1.07*10 8 , 1.68*10 6 , 1.83*10 7 , and 1.46*10 7 , respectively. These data indicate that 1G04 is a potent inhibitor of metastasis spread and growth in colon cancer. [0344] Collectively, Figures 16D-16G show that 1G04 is effective at reducing the formation and growth of metastases from colon cancer. Example 8: Treatment of lung cancer using the 1G04 anti-CD36 antibody [0345] Studies of the effects of the 1G04 anti-CD36 antibody on lung cancer were performed in NSG mice (immuno-deficient). An experimental overview of these studies is provided in Figure 17A. The studies included only female mice. All mice were inoculated with commercially available A549-luc2 (ATCC) cancer cells, a modified version of A549 cells generated by stable transduction with a lentiviral vector expressing luciferase. A549 cells are cells derived from a lung carcinoma (i.e. from a lung cancer), and therefore were used as part of a mouse model of lung cancer. Prior to inoculation, the A549 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 , and were grown in F-12K medium supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0346] For each mouse, 1x10 6 A549 cells were inoculated intravenously via tail vein injection. Each mouse was imaged after inoculation and one week later and lung metastasis was confirmed by luminescence prior to start of treatment. Treatment began 8 days after inoculation with the A549 cells. As detailed in Figure 17B, inoculated mice were divided into one of two treatment groups: vehicle injection control (n = 11) or 1G04 treatment (n = 11). Antibody treatments were administered via intraperitoneal (i.p.) injection at a dose of 10 mg/kg three times per week, while control mice received an equal volume of vehicle on the same schedule. One day prior to the start of treatment, and once weekly after the start of treatment, all mice were imaged via IVIS. Mice were sacrificed at the end of the treatment period (day 61). Upon sacrifice, organs and tissues were collected for performance of necropsy and ex-vivo IVIS. [0347] Figure 17C shows the results of imaging whole-animal bioluminescence over time, with decreased fluorescence observed in 1G04 treated mice. This indicates that 1G04 treatment reduced the growth of the injected A549 tumor cells in vivo (** = p value of p=0,0002). At endpoint, lungs of mice treated with 1G04 antibody were smaller than lungs from control vehicle-treated mice (Figure 17D), indicating that less tumor growth occurred. The observed mean lung weight was 0.90g in vehicle-treated mice and 0.72g in 1G04-treated mice (20% reduction). Animals treated with 1G04 also presented less luminescence in the lung at endpoint (2.11*10 8 to 1.39*10 8 ) as presented in Figure 17E. These results indicate that 1G04 inhibits metastasis growth in lung cancer. Example 9: Treatment of colon cancer using the 1G04 anti-CD36 antibody [0348] Studies of the effects of the 1G04 anti-CD36 antibody on colon cancer were performed in C57BL/6 mice (immuno-competent). An experimental overview of these studies is provided in Figure 18A. The studies included only female mice. All mice were inoculated with commercially available MC-38 cancer cells, transduced with a vector expressing luciferase. MC-38 cells are cells derived from a mouse colon adenocarcinoma (i.e. from a colon cancer). Prior to inoculation, MC-38 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 and were grown in DMEM medium supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0349] For each mouse, 1x10 6 MC-38 cells were inoculated intrasplenically. Each mouse was imaged 4 days later, and liver metastasis was confirmed by ex vivo luminescence prior to start of treatment on day 5 after inoculation. As detailed in Figure 18B, inoculated mice were divided into one of two treatment groups: vehicle injection control (n = 13) or 1G04 treatment (n = 10). Antibody treatments were administered via intraperitoneal (i.p.) injection at a dose of 10 mg/kg three times per week, while control mice received an equal volume of vehicle on the same schedule. One day prior to the start of treatment, and twice weekly after the start of treatment, all mice were imaged via IVIS. Mice were sacrificed at the end of the treatment period (day 60). Upon sacrifice, organs and tissues were collected for performance of necropsy and ex-vivo IVIS. [0350] Whole-animal bioluminescence imaging during the study showed that 1G04- treatment decreases luminescence, indicating a reduction in tumoral growth (*= p value of 0.003, Figure 18C). Ex vivo analysis of luminescence showed that mice treated with 1G04 present lower luminescence in both liver (1.41*10 9 to 6.67*10 4 ; i.e., greater than 99.99% reduction) and lungs (7.23*10 6 to 6.78*10 4 ; i.e., greater than 99% reduction) (Figures 18D and 18E, respectively). In conclusion, 1G04 showed efficacy decreasing metastasis size in colon cancer. Example 10: Treatment of breast cancer using the 1G04 anti-CD36 antibody [0351] Studies of the effects of the 1G04 anti-CD36 antibody on breast cancer were performed in BALB/c mice (immuno-competent). An experimental overview of these studies is provided in Figure 19A. The studies included only female mice. All mice were inoculated with commercially available 4T1 cancer cells (ATCC), transduced with a vector expressing luciferase.4T1 cells were derived from murine mammary gland tissue (i.e. from a breast cancer). Prior to inoculation, 4T1 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 , and were grown in RPMI medium supplemented with 5 μg ml −1 penicillin/streptomycin, 2mM L-Glutamine and 10% FBS (GIBCO). [0352] For each mouse, 4x10 4 4T1 cells were inoculated orthotopically in the mammary fat pad. Treatment began 5 days after inoculation with 4T1 cells. Mice were divided into one of two treatment groups: vehicle injection control (n = 10) or 1G04 treatment (n = 10). Antibody treatments were administered via intraperitoneal (i.p.) injection at a dose of 10 mg/kg three times per week, while control mice received an equal volume of vehicle on the same schedule (Figure 19B). Mice were sacrificed at the end of the treatment period (day 22). Upon sacrifice, organs and tissues were collected for performance of necropsy and ex-vivo IVIS. [0353] Luminescence in the lungs was reduced in 1G04-treated mice compared to vehicle-treated ones (2.49*10 5 to 5.96*10 4 , Figure 19C), indicating that anti-CD36 treatment reduces the size of metastasis and/or metastatic spread to distant organs. Example 11: Characterization of anti-CD36 antibodies [0354] Novel anti-CD36 antibodies were generated via immunization of mice or chickens with recombinant human CD36. Mice were immunized with five injections of human CD36 protein, followed by a sixth injection of human-CD36-overexpressing CHO cells. Other mice were immunized with four injections of human-CD36-overexpressing CHO cells. Chickens were immunized with four injections of human CD36 protein. These immunization resulted in generation of Fab fragments, and the variable regions from these Fab fragments were then grafted onto a human IgG scaffold with the LALA alteration to form chimeric antibodies. The murine immunization process resulted in generation of the 4G04, 5G04, 6G04, 7G04, 9G04, 10G04, 11G04, 12G04, 13G04, 14G04, 15G04, 16G04, 17G04, 18G04, 19G04, 20G04, 21G04, 22G04, 23G04, 24G04, 25G04, 26G04, 27G04, 28G04, 29G04, 30G04, 31G04, and 32G04 chimeric antibodies. The chicken immunization process resulted in generation of the 33G04, 34G04, 35G04, 36G04, 37G04, and 38G04 chimeric antibodies. Humanization of 11G04 resulted in the generation of, 73G06, 74G06, 75G06, 76G06, 77G06, 78G06, 79G06, or 80G06. Amino acid sequences relating to these antibodies are provided in Table 2 and Table 3. [0355] The murine-derived chimeric antibodies were screened for their ability to bind to HEK 293 cells transiently overexpressing human CD36 (SEQ ID NO: 1), nonhuman primate CD36 (SEQ ID NO: 2), or mouse CD36 (SEQ ID NO: 3). After transiently transfecting the HEK 293 cells with a CD36 expression construct, cells were treated with three-fold serial dilution of each candidate antibody (10 dilutions starting at 500 nM). The antibody 1G04 (SEQ ID NOs: 9 and 10; see PCT/IB2021/051881, which is herein incorporated by reference) was used as a positive control. After incubation with the cells, an anti-human fluorescently labelled antibody was added to the cell media, allowed to incubate further, and the unbound antibody was washed off of the cells. Subsequently, the cells were subjected to FACS analysis to determine antibody binding to the cells. The results were fitted to a sigmoidal titration curve. Using a nonlinear regression model, the EC 50 values for each antibody were calculated from the GeoMFI and MFI values using the log(agonist) versus response (four parameters) fitting on the data transformed according to X=Log[X] in GraphPad PRISM. The results of this analysis are provided in Table 7 below as the EC50 of each antibody’s ability to bind human CD36, non-human primate CD36 (cynomolgus), and mouse CD36 on the HEK 293 cells. All antibodies bound human CD36, but some were classified as not determined (N.D.) because they did not present a proper titration curve that fits the nonlinear regression model used to calculate EC50. Most of the antibodies were measured to have a similar EC50 as 1G04 against human CD36. Two antibodies (31G04 and 4G04) showed low affinity for the three CD36 species tested, and these antibodies’ EC 50 value could not be unambiguously calculated by nonlinear regression. Two antibodies (26G04 and 31G04) did not bind nonhuman primate CD36, while one antibody (4G04) bound to nonhuman primate CD36 with significantly less affinity than the other antibodies. Eleven antibodies did not bind mouse CD36 or bound to it with significantly less affinity than the other antibodies. TABLE 7 – Antibody Binding to HEK 293 Cells Overexpressing CD36 [0356] A subset of humanized antibodies were also screened for their ability to bind to HEK 293 cells transiently overexpressing human CD36 (SEQ ID NO: 1). After transiently transfecting the HEK 293 cells with a CD36 expression construct, cells were treated with three-fold serial dilution of each candidate antibody (10 dilutions starting at 500 nM). The antibodies 11G04 (SEQ ID NOs: 19 and 51) and 11G06 (SEQ ID NOs: 16 and 51) were used as a positive control. Antibody binding to cells was measured by FACS as above. The results of this analysis are provided in Table 8 below as the EC 50 of each antibody’s ability to bind human CD36. All tested antibodies bound human CD36 and have a similar EC50 as 11G04 and 11G06 against human CD36. TABLE 8 – Humanized Antibody Binding to HEK293 Cells Overexpressing CD36 [0357] A subset of the murine-derived chimeric antibodies were also screened for their ability to bind to SCC25 cells stably overexpressing human CD36 (SEQ ID NO: 1). Using the same FACS-based titration assay as used for the HEK 293 cells, the tested antibodies all had similar EC50’s with SCC25 cells as they did with HEK 293 cells. These results are shown in Table 9 below. TABLE 9 – Antibody Binding to SCC25 Cells Overexpressing CD36 [0358] The binding affinity of the reported antibodies for human CD36 was also measured by surface plasmon resonance (SPR) using a Biacore T200. The anti-histidine antibody provided in His Capture Kit (Cytiva # 28-9950-56) was diluted to 50 μg/ml in immobilization buffer and covalently coupled to a CM5 Sensor Chip by standard amine coupling to a level of approximately 13,000 RU. For each single-cycle experiment, human CD36 (His-tagged) was captured at low density (approximately 40 RU) and a titration of five antibody concentrations (diluted in running buffer) were injected over the captured antigen and then the dissociation of the complex was measured. A double referencing method was employed in which data from the reference surfaces where no antigen was captured (fc 1) were subtracted from the antigen bound capture surface (fc 2). Blank injections of buffer were run for every antibody titration cycle and then subtracted from analyte injection cycles, to correct for small changes in the capture surface density. Surface regeneration between cycles was performed by injecting Glycine pH 1.5 for 60 s. All analysis was performed at 20 °C in HBS-P running buffer (flow 30 μL/min), and the sample rack was kept at 6 °C during experimental runs. Data was fitted to a bivalent analyte model from which the kinetic and thermodynamic binding constants were derived. Data from this analysis is provided in Table 10 below. TABLE 10 – Mean Kinetic Data for the SPR-Measured Interaction with CD36 (Bivalent Model) [0359] To further assess properties of the anti-CD36 antibodies, the melting temperature of the antibodies was measured. Each tested antibody was mixed with a dye that strongly fluoresces when it binds to hydrophobic regions of a protein (Sypro orange), and slowly heated to 100 °C. The melting temperature was identified as the point of maximum slope in a plot of the fluorescence over time, representing when the protein unfolds and exposes its hydrophobic regions to the dye. The results of this assay are shown in Table 11 below. TABLE 11 – Melting Temperature of Anti-CD36 Antibodies [0360] A set of anti-CD36 antibodies were evaluated for their ability to compete with either the 1G04 antibody, the FA6-152 anti-CD36 antibody (Abcam), and/or the 11G04 antibody for binding to human CD36. This was done using the AlphaScreen® bead-based microplate assay. The reference antibody (1G04, FA6-152, or 11G04) (20 μg/mL) was conjugated to AlphaLISA® acceptor beads and incubated with purified biotin-tagged human CD36 (12.5 nM) and the test anti-CD36 antibody (two-fold serial dilutions from 500 to 0.10 nM). AlphaLISA® Streptavidin Donor Beads were then added and the mix incubated for 30 min at 25ºC in the dark. The donor bead contains a photosensitizer, which upon excitation by light at 680 nm, converts oxygen (O2) into an excited form, singlet oxygen. Singlet oxygen molecules have a reduced lifetime (4 microseconds half- life) and can diffuse approximately 200 nm in solution before falling back to ground state. In the absence of acceptor beads, the singlet oxygen molecules fall back to ground state without producing any light signal. In case an acceptor bead is within 200 nm, energy is transferred from the singlet oxygens to the bead, resulting in light production at 615 nm. Accordingly, the degree of binding between the reference antibody and CD36 was measured as the degree of fluorescence at 615 nm observed in the presence of a test anti- CD36 antibody, with decreased fluorescence relative to controls expected if the antibody is capable of disrupting the bead-to-bead interaction by competing for binding to the bound CD36. The results of the competition assay are summarized in Table 12 below. Most of the tested antibodies compete solely with 1G04 (05G04, 17G04, 21G04, 22G04, 23G04, 32G04, 12G04, 7G04, 9G04, 28G04 and 14G04), or with both 1G04 and 11G04 (16G04, 18G04, 30G04, 33G04, 34G04, 35G04, 36G04, 37G04, and 38G04). The 19G04 and 20G04 antibodies were observed to compete solely with 11G04. The 4G04, 6G04, 13G04, 15G04, 24G04, 25G04, 26G04, 27G04, 29G04, and 31G04 antibodies were observed to compete with both 1G04 and FA6-152. The 10G04 and 11G04 and 19G04 antibodies did not compete with either 1G04 or FA6-152. TABLE 12 – Anti-CD36 Antibody Competition Example 12: Testing Effects of Anti-CD36 Antibodies on CD36’s interaction with its ligands [0361] The ability of anti-CD36 antibodies to affect CD36-mediated fatty acid uptake was measured using a cell-based assay adapted from prior publications. See Feng, W. et al., Cell Reports 29(11):3405-3420 (2019); Henkin, A. et al., ACS Chem. Biol. 7(11):1884-91 (2012). Briefly, SCC25 cells were engineered to overexpress both luciferase and human CD36 and plated in a 96-well plate. Palmitic acid coupled to luciferin was then added to the cell media, and incubated to allow CD36-mediated uptake and the generation of luminescence by reaction of luciferase with its substrate luciferin. The resultant luminescence was measured after incubation either with a control isotype antibody or an anti-CD36 antibody present in the cell media. As shown in Figure 20, each anti-CD36 antibody tested inhibited fatty acid uptake relative to the uptake observed after treatment with an isotype control antibody. The mean percent inhibition of fatty acid uptake observed is also shown in Table 13. TABLE 13 - Anti-CD36 Antibody Inhibition of Fatty Acid Uptake [0362] The ability of anti-CD36 antibodies to inhibit CD36-mediated fatty acid uptake was also measured by their ability to inhibit uptake of palmitic acid linked to a fluorophore (BODIPY FL C16). The basic experimental protocol is provided in Figure 21A. HEK 293 cells were stably transfected with a vector to overexpress human CD36 to generate a stable cell line (HEK hCD36 cl48), which enhanced fatty acid uptake. Both control untransfected HEK 293 cells and the HEK hCD36 cl48 cells were used in each assay as reference controls (Figures 21B-21J). Either an anti-CD36 antibody or an isotype control were then added to the cell media of a well containing HEK hCD36 cl48 cells, and incubated for 30 minutes at 37 °C. Bodipy-labelled palmitic acid was then added and incubated with the cells for 20 minutes at 37 °C, at which point FACS analysis was performed to detect intracellular fluorescence. Each antibody was titrated to test its effects at a range of concentrations from 0.125 nM to 1000 nM. The results of this assay are plotted in Figures 21B-21J. Each of 6G04 (Figure 21D), 7G04 (Figure 21E), 9G04 (Figure 21F), 11G04 (Figure 21G), 13G04 (Figure 21H), 14G04 (Figure 21I), and 28G04 (Figure 21J) inhibited palmitic acid uptake into HEK 293 cells, relative to treatment with isotype control antibody (Figure 21B). In addition, each of 6G04, 7G04, 9G04, 11G04, 13G04, 14G04, and 28G04 inhibited palmitic acid uptake more effectively than 1G04 (Figure 21C). The IC50 for inhibition of fatty acid uptake for each tested antibody is provided in Table 14. TABLE 14 Anti-CD36 inhibition (IC 50 calculation) of fatty acid uptake [0363] In addition to facilitating fatty acid uptake, CD36 facilitates internalization of oxidized LDL (“oxLDL”). The ability of anti-CD36 antibodies to inhibit CD36-mediated oxLDL uptake was measured by their ability to inhibit uptake of oxLDL linked to a fluorophore (DiI). The basic experimental protocol is provided in Figure 22A. SCC25 cells stably expressing human CD36 were plated and treated with either an anti-CD36 antibody or an isotype control in the cell media and incubated for 60 minutes at 37 °C. DiI-labelled oxLDL was then added and incubated with the cells for 120 minutes at 37 °C, at which point FACS analysis was performed to detect intracellular fluorescence. Each antibody was titrated to test its effects at a range of concentrations from 335 nM to 0.00067 nM. The results of this assay are plotted in Figure 22B. Each of 1G04, 6G04, 7G04, 11G04, 13G04, 14G04, and 28G04 inhibited oxLDL uptake into SCC25 cells, relative to treatment with isotype control antibody. The IC50 for inhibition of oxLDL uptake for each tested antibody is provided in Table 15. TABLE 15. Anti-CD36 inhibition of oxLDL uptake [0364] To evaluate if the binding of the Abs to CD36 interferes with the CD36’s interaction with TSP1, anti-CD36 antibodies were tested in an SPR competition experiment. After immobilizing CD36 on the SPR surface, 20 nM anti-CD36 antibody was injected to reach binding saturation on CD36. After binding saturation is reached (approximately 250 seconds), a short pulse of 200 nM TSP1 was injected. An exemplary plot of the data obtained using 1G04, with the protocol steps annotated, is provides in Figure 23A. To determine whether anti-CD36 antibody interferes with TSP-1 interaction, the change in response units (RUs) after TSP-1 injection was compared for injections containing anti-CD36 antibody and injections containing buffer only (see Figure 23A). As shown in Figure 23B, none of the tested antibodies reduced the TSP-1/CD36 interaction by more than 50%. Example 13 – Engineering the Fc region of anti-CD36 antibodies [0365] The variable regions of the 1G04 anti-CD36 antibody were cloned to be attached to different constant regions, each of which contained a different Fc silencing alteration. The constant regions tested were: (1) the human IgG1 wild type sequence; (2) human IgG1 with the L234A and L235A ("LALA") alteration; (3) human IgG1 with the amino acid mutations L234A, L235A and P329G ("P329G LALA"); human IgG1 with the amino acid mutations L234S, L235T, and G236R ("STR"); and human IgG4 with the amino acid mutations S228P and L235E (“SPLE”). The antibodies generated in this way were the 1G03 antibody (WT IgG1), the 1G05 antibody (IgG1 with P329G LALA); the 1G06 antibody (IgG1 with STR); and the 1G07 antibody (IgG4 with SPLE). [0366] Each of the resultant chimeric antibodies derived from 1G04 was then tested for its ability to bind to human CD36 and mouse CD36. Binding was first tested using an ELISA assay in which 96-well ELISA plates were coated with human CD36 (Sino Biological) or mouse CD36 protein. As shown in Figure 24A (binding to human CD36) and Figure 24B (binding to mouse CD36), no binding differences were observed for the different Fc-formatted antibodies. [0367] The different Fc-formatted anti-CD36 antibodies were also tested for their ability to bind to SCC25 cells stably expressing human CD36 (SEQ ID NO: 1). SCC25 cells were treated with 10-fold serial dilution of each antibody (5 dilutions starting at 100 nM). After incubation with the cells, an anti-human fluorescently labelled antibody was added to the cell media, allowed to incubate further, and the unbound antibody was washed off of the cells. Subsequently, the cells were subjected to FACS analysis to determine antibody binding to the cells. The results were fitted to a sigmoidal titration curve. Using a nonlinear regression model, the EC 50 values for each antibody were calculated from the GeoMFI and MFI values using the log(agonist) versus response (four parameters) fitting on the data transformed according to X=Log[X] in GraphPad PRISM. The results of this analysis are provided in Table 16 below, and plotted in Figure 24C. These data further confirm that Fc engineering does not affect binding to CD36. TABLE 16 – Antibody Binding to SCC25 Cells Overexpressing CD36 [0368] The ability of the different Fc-formatted anti-CD36 antibodies to affect CD36- mediated fatty acid uptake was measured using a cell-based assay adapted from prior publications. See Feng et al., Cell Reports 2019; Henkin et al., ACS Chem. Biol.2012. Briefly, SCC25 cells were engineered to overexpress both luciferase and human CD36 and plated in a 96-well plate. Palmitic acid coupled to luciferin was then added to the cell media, and incubated to allow CD36-mediated uptake and the generation of luminescence by reaction of luciferase with its substrate luciferin. The resultant luminescence was measured after incubation either with a control isotype antibody or an anti-CD36 antibody present in the cell media. As shown in Figure 24D, each of the different Fc variants inhibited fatty acid uptake at similar levels, which showed that Fc engineering does not affect CD36-mediated fatty acid uptake inhibition by anti-CD36 antibodies. [0369] The binding of the different Fc-formatted anti-CD36 antibodies to FcγRs and FcRn was measured by SPR by immobilizing the antibodies through their light chains. The setup for these assays orients the antibody such that the Fc domain is solvent- exposed, allowing quantification of the interaction with soluble receptor proteins. Antibodies with well-defined binding properties were included as positive/negative controls in all the assays. As shown in Figure 25A, each of the tested Fc alterations reduced interaction with human and cynomolgus FcγRs. Antibodies containing the LALAPG (1G05) and STR alterations were the most inactive toward human and cynomolgus FcγRs. In contrast, none of the alterations altered the affinity of the interaction (KD) with human FcRn at pH 5.8—as shown in Figure 26. This indicates that all Fc variants maintain FcRn affinity at endosomal pH, while dissociation at neutral pH is fast, thus ensuring an efficient Fc-mediated cellular recycling of the Ab in vivo. [0370] The different Fc-formatted anti-CD36 antibodies were also tested using Promega’s ADCC, ADCP, and CDC Reporter Bioassays according to the manufacturer’s instructions. As shown in Figure 25B, the FcγRIIIa-mediated ADCC response is completed abrogated (i.e., undetectable) in cells exposed to 1G04, 1G05, 1G06, and 1G07 antibodies. Similarly, as shown in Figure 25C, the FcγRIIa-mediated ADCP response is completely abrogated (i.e., undetectable) in cells exposed to 1G04, 1G05, 1G06, and 1G07 antibodies. And finally, as shown in Figure 25D, the CDC complement response is undetectable in cells exposed to 1G04, 1G05, 1G06, and 1G07 antibodies. In each of these assays, a significant response was observed after exposure to the 1G03 antibody, which contains an unmodified IgG1 Fc region. [0371] Binding to complement C1q protein was also measured, using a standard ELISA assay in which 96-well ELISA plates were coated with the tested antibodies and C1q human protein was added (2.5-fold serial dilution starting at 250 μg/mL). As shown in Figure 27, no binding was observed for any of the Fc-engineered samples, while the wild type Fc antibodies showed binding to C1q human protein. [0372] The different Fc formatted anti-CD36 antibodies were also tested in an in vitro antibody-induced platelet aggregation assay. Platelet aggregation responses were measured by light transmission aggregometry (LTA) as an increase in light transmission through the sample using a specialised aggregometer, AggRAM (Helena Biosciences), in platelet rich plasma (PRP) prepared from whole blood samples from six healthy volunteers. Antibodies were tested in the presence and absence of the platelet agonist adenosine diphosphate (ADP). ADP was titrated to produce a partial aggregation response in PRP from all volunteers (thereby confirming the viability of the PRP samples). An anti-CD226/DNAM-1 (LeoA1) antibody with a known effect on platelets via FcγRIIa receptor was included as a positive control. Possible direct and potentiation effects of the test antibodies were also assessed in the presence of a blocking anti-CD32 antibody (IV.3) to confirm if any observed effects were mediated via the FcγRIIa receptor. Each anti-CD36 antibody was tested at a 500 nM concentration (with n=6). As shown in Figure 28A and 28B, each of the Fc alterations eliminated antibody-induced platelet aggregation, even in the presence of a platelet aggregation agonist (ADP). Example 14 – Epitope analysis of the 1G04 and 11G04 anti-CD36 antibodies [0373] For deuterium labeling, the 1G04 and 11G04 antibodies were each incubated with recombinant human CD36 at an optimal stoichiometric ratio of 1:1.5 in D 2 O-labeling solution and concentrated to 10 mg/mL via membrane filtration. All samples were buffer exchanged in PBS pH 7.4 and incubated for various time points at room temperature. The deuteration was quenched by transferring 30 μL of the sample to 30 μL of prechilled 1 M tris(2-carboxyethyl)phosphine (TCEP) in 8 M guanidine chloride, pH 2.5 (quench buffer), and the mixed sample was incubated at 1.0 °C for 2 min. The quenched sample was then subjected to online digestion using an immobilized pepsin/protease column. The digested peptides were trapped onto a C18 precolumn at 0 °C and eluted to an analytical C18 column for chromatographic separation using a 9 min gradient separation of 3–40% 5 (mobile phase A: 0.1% formic acid in water; mobile phase B: 0.1% formic acid in acetonitrile). For identification of CD36 peptides, LC/MSE data from an undeuterated sample were processed and searched against a database including human CD36. The deuterium uptake of each peptide in CD36 alone and CD36 with mAb was calculated based on centroid mass value at each time point with aligned retention time and high mass accuracy (<10 ppm) from triplicates. Any region of CD36 with significant protection upon mAb binding was defined as a component of the mAb’s epitope. Figure 30 shows the deuterium uptake for each CD36 peptide from 1G04 alone and with mAb. Figure 31C shows the deuterium uptake for each CD36 peptide from 11G04 alone and with mAb. [0374] The residues that were identified as constituting the main 1G04 binding epitope are shown underlined in bold in the human CD36 sequence (SEQ ID NO: 1) in Figure 29A. A combined ribbon and space filling model of CD36 is shown in Figure 29B. Residues identified by hydrogen-deuterium exchange experiments to constitute the main binding epitope for 1G04 are highlighted in bold (145A, 146S, 147H, 148I, 149Y, 150Q, 151N, 152Q, 153F, 154V, 155Q, 156M, 157I, 158L, 159N, 160S, 185P, 186F, 187L, 188S, 189L, 190V, 191P, 192Y, 193P, 194V, 195T, 196T, 197T, 198V, 199G, 398K, 399I, 400Q, 401V, 402L, 403K, 404N, 405L, 406K, 407R, 408N, 409Y, 410I, 411V, 412P, 413I, and 414L). [0375] The residues that were identified as constituting the main 11G04 binding epitope are shown underlined in bold in the human CD36 sequence (SEQ ID NO: 1) in Figure 31A. A combined ribbon and space filling model of CD36 is shown in Figure 31B. Residues identified by hydrogen-deuterium exchange experiments to constitute the main binding epitope for 11G04 are highlighted in bold (280E, 281S, 282D, 283V, 284N, 285L, 286K, 287G, 288I, 289P, 290V, 291Y, 292R, 293F, 294V, 295L, 296P, 297S, 298K, 341I, 342S, 343L, 344P, 345H, 346F, 347L, 348Y, 349A, 350S, 351P, 352D, 353V, 354S, 355E, 356P, 357I, 358D, 359G, 360L 361N, 362D, 363N, 364E, 365E). Example 15: Treatment of colon cancer using anti-CD36 antibodies [0376] Studies of the effects of the anti-CD36 antibodies on colon cancer were performed in BALB/c nude mice (immuno-deficient). An experimental overview of these studies is provided in Figure 32A. The studies included only female mice. All mice were inoculated with commercially available HCT-116 (ATCC) cancer cells, transduced with a retroviral vector expressing luciferase. HCT-116 cells were derived from a human colorectal carcinoma (i.e., from a colon cancer). Prior to inoculation, the HCT-116 cells were cultured in a humidified incubator at 37 °C with 5% CO 2 , and were grown in McCoy’s 5A medium supplemented with 5 μg ml −1 penicillin/streptomycin and 10% FBS (GIBCO). [0377] For each mouse, 2x10 6 HCT-116 cells were inoculated via orthotopic injection. Each mouse was imaged after inoculation and one week later and liver metastasis were confirmed by ex vivo luminescence prior to start of treatment. Treatment began 13 days after inoculation with the HCT-116 cells. Inoculated mice were divided into one of seven treatment groups: vehicle injection control (n = 8), 1G04 treatment (n = 8), 11G04 treatment (n = 9), 13G04 treatment (n = 6), 14G04 treatment (n = 7), 28G04 treatment (n = 9) and 6G04 treatment (n = 8). Antibody treatments were administered via intraperitoneal (i.p.) injection at a dose of 10 mg/kg three times per week, while control mice received an equal volume of vehicle on the same schedule. One day prior to the start of treatment, and at 6, 13, and 21 days after the start of treatment, all mice were imaged via IVIS. Mice were sacrificed at the end of the treatment period (day 23). Upon sacrifice, organs and tissues were collected for performance of necropsy and ex-vivo IVIS. [0378] Figure 32B shows the results of whole-animal bioluminescence imaging over time, which is a readout for the growth of luciferase-containing tumor cells in the mouse. The bioluminescence imaging showed that all anti-CD36 antibodies decreased whole animal luminescence, and thus slowed the growth of the injected HCT-116 tumor cells in vivo. [0379] After the liver was removed from the mice, the luminescence of the metastatic tumors in the liver (Figure 32C) was quantified by ex vivo luminescence using IVIS. The observed mean luminescence values for vehicle-treated mice were 1.60*10 8 . The observed mean luminescence values for the groups of mice treated with anti-CD36 antibodies were 3.61*10 7 (1G04), 6.85*10 7 (11G04), 8.99*10 7 (13G04), 6.38*10 7 (14G04), 4.76*10 7 (28G04) and 5.84*10 7 (6G04). Thus, anti-CD36 treatment decreases the luminescence, reflecting a reduction in the size and/or number of metastases. These data indicate that all tested antibodies were potent inhibitors of metastasis spread and growth in colon cancer. [0380] Collectively, Figures 32B and 32C show that the tested anti-CD36 antibodies are effective at reducing the formation and growth of metastases from colon cancer. Example 16: Antibody clustering according to similarity of HCDR3 [0381] HCDR3 clustering of some of the anti-CD36 antibodies was performed based on the mutual similarity in the amino acid sequence across HCDR3, which constitutes the main hypervariable loop in the paratope. [0382] The results are shown in Table 17 below: Table 17 – HCDR3 clustering