ES2632748T3 - Anticuerpos anti-C4.4a y usos de los mismos - Google Patents
Anticuerpos anti-C4.4a y usos de los mismos Download PDFInfo
- Publication number
- ES2632748T3 ES2632748T3 ES10798996.4T ES10798996T ES2632748T3 ES 2632748 T3 ES2632748 T3 ES 2632748T3 ES 10798996 T ES10798996 T ES 10798996T ES 2632748 T3 ES2632748 T3 ES 2632748T3
- Authority
- ES
- Spain
- Prior art keywords
- antibody
- antigen
- antibodies
- sequences
- binding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 230000027455 binding Effects 0.000 abstract description 70
- 239000000427 antigen Substances 0.000 abstract description 64
- 108091007433 antigens Proteins 0.000 abstract description 64
- 102000036639 antigens Human genes 0.000 abstract description 64
- 239000012634 fragment Substances 0.000 abstract description 39
- 101150086425 LYPD3 gene Proteins 0.000 abstract description 21
- 150000001413 amino acids Chemical class 0.000 abstract description 10
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 54
- 210000004027 cell Anatomy 0.000 description 27
- 238000000034 method Methods 0.000 description 19
- 108090000765 processed proteins & peptides Proteins 0.000 description 17
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 14
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 14
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 13
- 108020004414 DNA Proteins 0.000 description 13
- 229920001184 polypeptide Polymers 0.000 description 12
- 102000004196 processed proteins & peptides Human genes 0.000 description 12
- 125000003275 alpha amino acid group Chemical group 0.000 description 11
- 150000007523 nucleic acids Chemical class 0.000 description 10
- 101001038507 Homo sapiens Ly6/PLAUR domain-containing protein 3 Proteins 0.000 description 9
- 229940024606 amino acid Drugs 0.000 description 9
- 238000006467 substitution reaction Methods 0.000 description 9
- 102000050476 human LYPD3 Human genes 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- 108091035707 Consensus sequence Proteins 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 101100075702 Mus musculus Lypd3 gene Proteins 0.000 description 5
- 230000004663 cell proliferation Effects 0.000 description 5
- 239000003814 drug Substances 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 239000003053 toxin Substances 0.000 description 5
- 231100000765 toxin Toxicity 0.000 description 5
- 108700012359 toxins Proteins 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- RUDATBOHQWOJDD-UHFFFAOYSA-N (3beta,5beta,7alpha)-3,7-Dihydroxycholan-24-oic acid Natural products OC1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)CC2 RUDATBOHQWOJDD-UHFFFAOYSA-N 0.000 description 4
- 206010028980 Neoplasm Diseases 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000006143 cell culture medium Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 231100000433 cytotoxic Toxicity 0.000 description 3
- 229940127089 cytotoxic agent Drugs 0.000 description 3
- 231100000599 cytotoxic agent Toxicity 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 229940127121 immunoconjugate Drugs 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 108091033319 polynucleotide Proteins 0.000 description 3
- 102000040430 polynucleotide Human genes 0.000 description 3
- 239000002157 polynucleotide Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 102220093101 rs150016894 Human genes 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 102220491520 Acid ceramidase_V97G_mutation Human genes 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 101000699762 Homo sapiens RNA 3'-terminal phosphate cyclase Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 102100029143 RNA 3'-terminal phosphate cyclase Human genes 0.000 description 2
- IWUCXVSUMQZMFG-AFCXAGJDSA-N Ribavirin Chemical compound N1=C(C(=O)N)N=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](CO)O1 IWUCXVSUMQZMFG-AFCXAGJDSA-N 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 239000002254 cytotoxic agent Substances 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 210000004602 germ cell Anatomy 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
- 102220123611 rs886043449 Human genes 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- PKYCWFICOKSIHZ-UHFFFAOYSA-N 1-(3,7-dihydroxyphenoxazin-10-yl)ethanone Chemical compound OC1=CC=C2N(C(=O)C)C3=CC=C(O)C=C3OC2=C1 PKYCWFICOKSIHZ-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- YRNWIFYIFSBPAU-UHFFFAOYSA-N 4-[4-(dimethylamino)phenyl]-n,n-dimethylaniline Chemical compound C1=CC(N(C)C)=CC=C1C1=CC=C(N(C)C)C=C1 YRNWIFYIFSBPAU-UHFFFAOYSA-N 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 230000004568 DNA-binding Effects 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102220473545 ELAV-like protein 1_A90R_mutation Human genes 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000009490 IgG Receptors Human genes 0.000 description 1
- 108010073807 IgG Receptors Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 231100000742 Plant toxin Toxicity 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 101710183280 Topoisomerase Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108090000704 Tubulin Proteins 0.000 description 1
- 102000004243 Tubulin Human genes 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- QTQAWLPCGQOSGP-VKNBREQOSA-N [(3r,5r,6s,7r,8e,10r,11r,12z,14e)-6-hydroxy-5,11,21-trimethoxy-3,7,9,15-tetramethyl-16,20,22-trioxo-17-azabicyclo[16.3.1]docosa-1(21),8,12,14,18-pentaen-10-yl] carbamate Chemical compound N1C(=O)\C(C)=C\C=C/[C@@H](OC)[C@H](OC(N)=O)\C(C)=C\[C@@H](C)[C@H](O)[C@H](OC)C[C@H](C)CC2=C(OC)C(=O)C=C1C2=O QTQAWLPCGQOSGP-VKNBREQOSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000611 antibody drug conjugate Substances 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 229940049595 antibody-drug conjugate Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 125000003712 glycosamine group Chemical group 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003966 growth inhibitor Substances 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 238000002847 impedance measurement Methods 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000007154 intracellular accumulation Effects 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 229940043515 other immunoglobulins in atc Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000003123 plant toxin Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 231100000654 protein toxin Toxicity 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 102220011343 rs267606538 Human genes 0.000 description 1
- 102200070542 rs786205436 Human genes 0.000 description 1
- 102220075010 rs796053096 Human genes 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- -1 that is Substances 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000036326 tumor accumulation Effects 0.000 description 1
- 238000000870 ultraviolet spectroscopy Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/39558—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against tumor tissues, cells, antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/30—Macromolecular organic or inorganic compounds, e.g. inorganic polyphosphates
- A61K47/42—Proteins; Polypeptides; Degradation products thereof; Derivatives thereof, e.g. albumin, gelatin or zein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K49/00—Preparations for testing in vivo
- A61K49/06—Nuclear magnetic resonance [NMR] contrast preparations; Magnetic resonance imaging [MRI] contrast preparations
- A61K49/08—Nuclear magnetic resonance [NMR] contrast preparations; Magnetic resonance imaging [MRI] contrast preparations characterised by the carrier
- A61K49/10—Organic compounds
- A61K49/14—Peptides, e.g. proteins
- A61K49/16—Antibodies; Immunoglobulins; Fragments thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/04—Antineoplastic agents specific for metastasis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/77—Internalization into the cell
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Cell Biology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Oncology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Inorganic Chemistry (AREA)
- Radiology & Medical Imaging (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP09178474 | 2009-12-09 | ||
| EP09178474 | 2009-12-09 | ||
| EP10170797 | 2010-07-26 | ||
| EP10170797 | 2010-07-26 | ||
| PCT/EP2010/069216 WO2011070088A1 (en) | 2009-12-09 | 2010-12-08 | Anti-c4.4a antibodies and uses thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2632748T3 true ES2632748T3 (es) | 2017-09-15 |
Family
ID=43629588
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES10798996.4T Active ES2632748T3 (es) | 2009-12-09 | 2010-12-08 | Anticuerpos anti-C4.4a y usos de los mismos |
Country Status (27)
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5881604B2 (ja) * | 2010-06-15 | 2016-03-09 | 国立大学法人大阪大学 | 癌予後判定可能な抗体、および癌予後判定方法 |
| JP2014515753A (ja) * | 2011-04-21 | 2014-07-03 | バイエル・インテレクチュアル・プロパティ・ゲゼルシャフト・ミット・ベシュレンクテル・ハフツング | 新規な結合剤−薬物複合体（ａｄｃ）およびそれらの使用 |
| JP2014117191A (ja) * | 2012-12-13 | 2014-06-30 | Fisheries Research Agency | リン酸化中性スフィンゴミエリナーゼ１、抗リン酸化中性スフィンゴミエリナーゼ１抗体、中性スフィンゴミエリナーゼ１変異体、及びそれらの用途 |
| JP2017534251A (ja) * | 2014-09-09 | 2017-11-24 | ボード・オブ・リージエンツ，ザ・ユニバーシテイ・オブ・テキサス・システム | Ａｇｒ２およびその受容体ｃ４．４ａに対する遮断モノクローナル抗体 |
| JP6720208B2 (ja) * | 2015-04-17 | 2020-07-08 | スプリング バイオサイエンス コーポレーション | Ｃ４．４ａを検出するための抗体、組成物、及び免疫組織化学法 |
| BR112018011270A2 (pt) * | 2015-12-04 | 2018-11-21 | Univ California | anticorpo isolado, composição farmacêutica, e, métodos para tratamento ou redução da taxa de recorrência de um câncer em um paciente e para detecção de células tronco do câncer. |
| WO2017156280A1 (en) * | 2016-03-09 | 2017-09-14 | Viba Therapeutics, Inc. | Methods of treating cancer using monoclonal antibodies to agr2 and c4.4a |
| JP7617603B2 (ja) | 2017-01-11 | 2025-01-20 | ザ ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティー | Ｒ－スポンジン（ｒｓｐｏ）サロゲート分子 |
| CA3050133A1 (en) | 2017-01-26 | 2018-08-02 | Surrozen, Inc. | Tissue-specific wnt signal enhancing molecules and uses thereof |
| JP7052389B2 (ja) * | 2018-02-07 | 2022-04-12 | 株式会社三洋物産 | 遊技機 |
| WO2020014271A1 (en) | 2018-07-09 | 2020-01-16 | Surrozen, Inc. | Tissue-specific wnt signal enhancing molecules and uses |
| JP2021530238A (ja) * | 2018-07-20 | 2021-11-11 | デューク ユニバーシティ | がんの処置のための抗ｌｙｐｄ３ ｃａｒ ｔ細胞療法 |
| US20210324434A1 (en) * | 2018-11-08 | 2021-10-21 | National University Corporation Kagawa University | Method for producing rare sugar-containing composition and rare sugar-containing composition |
| CN111349164B (zh) * | 2018-12-21 | 2023-05-26 | 艾比玛特医药科技（上海）有限公司 | 糖基磷脂酰肌醇锚定糖蛋白（c4.4a）的单克隆抗体及其应用 |
| AU2020298326A1 (en) * | 2019-06-21 | 2022-01-27 | Children's National Medical Center | Methods and composition for a binding molecule targeting cancer cells expressing SSX2 peptide 41-49 in HLA-A*0201 context |
| EP4054602A4 (en) | 2019-11-08 | 2023-12-06 | Mayo Foundation for Medical Education and Research | EPHA3 TARGETED CAR-T CELLS FOR TREATING TUMORS |
| JP2023549854A (ja) | 2020-11-16 | 2023-11-29 | スロゼン オペレーティング， インコーポレイテッド | 肝臓特異的Ｗｎｔシグナル増強分子およびその使用 |
| KR20250021299A (ko) | 2022-03-16 | 2025-02-12 | 펜틱사팜 아게 | Lypd3에 대한 항체 |
| CA3258344A1 (en) | 2022-06-07 | 2023-12-14 | Actinium Pharmaceuticals, Inc. | CHELETARIANS AND BIFUNCTIONAL CONJUGATES |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4657760A (en) | 1979-03-20 | 1987-04-14 | Ortho Pharmaceutical Corporation | Methods and compositions using monoclonal antibody to human T cells |
| US5179017A (en) | 1980-02-25 | 1993-01-12 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4634665A (en) | 1980-02-25 | 1987-01-06 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4510245A (en) | 1982-11-18 | 1985-04-09 | Chiron Corporation | Adenovirus promoter system |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US5206344A (en) | 1985-06-26 | 1993-04-27 | Cetus Oncology Corporation | Interleukin-2 muteins and polymer conjugation thereof |
| US4968615A (en) | 1985-12-18 | 1990-11-06 | Ciba-Geigy Corporation | Deoxyribonucleic acid segment from a virus |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| US5225212A (en) | 1989-10-20 | 1993-07-06 | Liposome Technology, Inc. | Microreservoir liposome composition and method |
| DK0590058T3 (da) | 1991-06-14 | 2004-03-29 | Genentech Inc | Humaniseret heregulin-antistof |
| EP0859841B1 (en) | 1995-08-18 | 2002-06-19 | MorphoSys AG | Protein/(poly)peptide libraries |
| JP4318752B2 (ja) * | 1996-05-31 | 2009-08-26 | ヘルス・リサーチ・インコーポレーテッド | 抗エンドグリンモノクローナル抗体および抗血管新生治療におけるその使用 |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| IL138608A0 (en) | 1998-04-02 | 2001-10-31 | Genentech Inc | Antibody variants and fragments thereof |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| EP1220919A2 (en) * | 1999-09-29 | 2002-07-10 | Deutsches Krebsforschungszentrum Stiftung des öffentlichen Rechts | Metastasis-associated antigen c4.4a |
| AU2002314495A1 (en) * | 2001-06-20 | 2003-01-02 | Prochon Biotech Ltd. | Antibodies that block receptor protein tyrosine kinase activation, methods of screening for and uses thereof |
| RU2404810C9 (ru) * | 2004-06-01 | 2015-06-20 | Дженентек, Инк. | Конъюгаты антитело-лекарственное средство и способы |
| US8105602B2 (en) * | 2006-12-08 | 2012-01-31 | Tactic Pharma, Llc | Urokinase-type plasminogen activator receptor epitope, monoclonal antibodies derived therefrom and methods of use thereof |
| JP2014515753A (ja) * | 2011-04-21 | 2014-07-03 | バイエル・インテレクチュアル・プロパティ・ゲゼルシャフト・ミット・ベシュレンクテル・ハフツング | 新規な結合剤−薬物複合体（ａｄｃ）およびそれらの使用 |
-
2010
- 2010-12-08 AU AU2010329904A patent/AU2010329904B2/en not_active Ceased
- 2010-12-08 LT LTEP10798996.4T patent/LT2510012T/lt unknown
- 2010-12-08 WO PCT/EP2010/069216 patent/WO2011070088A1/en not_active Ceased
- 2010-12-08 HR HRP20170973TT patent/HRP20170973T1/hr unknown
- 2010-12-08 CN CN201080063444.XA patent/CN102812047B/zh not_active Expired - Fee Related
- 2010-12-08 DK DK10798996.4T patent/DK2510012T3/en active
- 2010-12-08 RU RU2012128343/10A patent/RU2577977C2/ru not_active IP Right Cessation
- 2010-12-08 KR KR1020127017608A patent/KR101931820B1/ko not_active Expired - Fee Related
- 2010-12-08 ES ES10798996.4T patent/ES2632748T3/es active Active
- 2010-12-08 NZ NZ600470A patent/NZ600470A/en not_active IP Right Cessation
- 2010-12-08 HU HUE10798996A patent/HUE034847T2/en unknown
- 2010-12-08 BR BR112012013915A patent/BR112012013915A8/pt not_active Application Discontinuation
- 2010-12-08 PT PT107989964T patent/PT2510012T/pt unknown
- 2010-12-08 TW TW099142735A patent/TWI488642B/zh not_active IP Right Cessation
- 2010-12-08 US US13/514,789 patent/US20120321619A1/en not_active Abandoned
- 2010-12-08 EP EP10798996.4A patent/EP2510012B1/en active Active
- 2010-12-08 CA CA2783338A patent/CA2783338A1/en not_active Abandoned
- 2010-12-08 PL PL10798996T patent/PL2510012T3/pl unknown
- 2010-12-08 RS RS20170650A patent/RS56161B1/sr unknown
- 2010-12-08 SI SI201031493T patent/SI2510012T1/sl unknown
- 2010-12-08 EP EP16191498.1A patent/EP3144323A3/en not_active Withdrawn
- 2010-12-08 MX MX2012006593A patent/MX2012006593A/es active IP Right Grant
- 2010-12-08 JP JP2012542543A patent/JP5989544B2/ja not_active Expired - Fee Related
- 2010-12-08 IN IN5175DEN2012 patent/IN2012DN05175A/en unknown
- 2010-12-09 AR ARP100104549A patent/AR079340A1/es unknown
-
2012
- 2012-05-14 ZA ZA2012/03498A patent/ZA201203498B/en unknown
- 2012-05-15 IL IL219801A patent/IL219801A/en not_active IP Right Cessation
-
2016
- 2016-03-03 JP JP2016040961A patent/JP6240696B2/ja not_active Expired - Fee Related
-
2017
- 2017-02-06 US US15/425,397 patent/US20170158775A1/en not_active Abandoned
- 2017-07-04 CY CY20171100712T patent/CY1119051T1/el unknown
- 2017-11-02 JP JP2017212592A patent/JP2018019721A/ja active Pending
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2632748T3 (es) | Anticuerpos anti-C4.4a y usos de los mismos | |
| JP7592022B2 (ja) | 抗クローディン１８．２抗体及びその用途 | |
| ES2645272T3 (es) | Moduladores de DLL3 y procedimientos de utilización | |
| CN104136610B (zh) | 人源化抗上皮调节蛋白抗体和含有该抗体作为有效成分的癌症治疗药 | |
| KR102046435B1 (ko) | 항-gcc 항체 분자 및 gcc-표적화 치료법에 대한 감수성을 평가하기 위한 그 용도 | |
| JP6006640B2 (ja) | 高い内在化能力を有する抗ｃｄｈ３抗体 | |
| CN111936515A (zh) | Cd47结合剂 | |
| WO2020022475A1 (ja) | 抗体－薬物コンジュゲートの薬物部位を認識する蛋白質 | |
| WO2021227307A1 (zh) | 抗cd73抗体及其用途 | |
| KR20170052648A (ko) | 대음세포작용 인간 항-cd46 항체 및 표적화된 암 치료제 | |
| JP2016538318A (ja) | 新規ｓｅｚ６モジュレーターおよび使用方法 | |
| CN109575136A (zh) | 新型抗dpep3抗体和使用方法 | |
| CN113330036B (zh) | 结合pd-l1和ox40的双特异性抗体 | |
| JP7419238B2 (ja) | Ｐｄ１結合剤 | |
| CA3193584A1 (en) | Nectin-4 antibodies and uses thereof | |
| WO2019062877A1 (zh) | 结合至纤维连接蛋白b结构域的蛋白 | |
| KR20230154020A (ko) | 클라우딘-6에 대한 항체 및 이의 용도 | |
| JP2022539344A (ja) | 抗ｃｅａ抗体及びその応用 | |
| CN105517571A (zh) | 含有人源化抗上皮调节蛋白抗体作为有效成分的腺癌以外的非小细胞肺癌的治疗药 | |
| ES2778100T3 (es) | Anticuerpos monoclonales anti-gpc-1 y usos de los mismos | |
| CN111788229A (zh) | Csf1r结合剂 | |
| CN114181301A (zh) | 针对SARS-CoV-2的无ADE效应的中和抗体 | |
| US20190194319A1 (en) | Anti-ascl1 antibodies and methods of use | |
| RU2822550C2 (ru) | Антитело против клаудина 18.2 и его применение | |
| WO2025228407A1 (zh) | 结合ly6g6d的分子及其用途 |