ES2594493T3 - Anticuerpos anti-c-Met - Google Patents
Anticuerpos anti-c-Met Download PDFInfo
- Publication number
- ES2594493T3 ES2594493T3 ES11778618.6T ES11778618T ES2594493T3 ES 2594493 T3 ES2594493 T3 ES 2594493T3 ES 11778618 T ES11778618 T ES 11778618T ES 2594493 T3 ES2594493 T3 ES 2594493T3
- Authority
- ES
- Spain
- Prior art keywords
- sequence
- antibody
- seq
- met
- human
- 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
- 241000282414 Homo sapiens Species 0.000 claims abstract description 400
- 230000027455 binding Effects 0.000 claims abstract description 213
- 239000000427 antigen Substances 0.000 claims abstract description 144
- 108091007433 antigens Proteins 0.000 claims abstract description 144
- 102000036639 antigens Human genes 0.000 claims abstract description 144
- 239000012634 fragment Substances 0.000 claims abstract description 95
- 108010089836 Proto-Oncogene Proteins c-met Proteins 0.000 claims abstract description 64
- 102000008022 Proto-Oncogene Proteins c-met Human genes 0.000 claims abstract description 64
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 claims abstract description 45
- 101000737793 Homo sapiens Cerebellar degeneration-related antigen 1 Proteins 0.000 claims abstract description 40
- 210000004027 cell Anatomy 0.000 claims description 168
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 128
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 56
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 44
- 229920001184 polypeptide Polymers 0.000 claims description 43
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 claims description 33
- 230000001404 mediated effect Effects 0.000 claims description 30
- 206010028980 Neoplasm Diseases 0.000 claims description 26
- 238000000034 method Methods 0.000 claims description 25
- 239000012636 effector Substances 0.000 claims description 23
- 230000014509 gene expression Effects 0.000 claims description 22
- 230000006870 function Effects 0.000 claims description 21
- 108091033319 polynucleotide Proteins 0.000 claims description 19
- 102000040430 polynucleotide Human genes 0.000 claims description 19
- 239000002157 polynucleotide Substances 0.000 claims description 19
- 230000001965 increasing effect Effects 0.000 claims description 18
- 238000011282 treatment Methods 0.000 claims description 18
- 230000001419 dependent effect Effects 0.000 claims description 16
- 239000013604 expression vector Substances 0.000 claims description 10
- 201000011510 cancer Diseases 0.000 claims description 9
- 230000004540 complement-dependent cytotoxicity Effects 0.000 claims description 7
- 239000008194 pharmaceutical composition Substances 0.000 claims description 5
- 229940127089 cytotoxic agent Drugs 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 3
- 206010057249 Phagocytosis Diseases 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 239000002254 cytotoxic agent Substances 0.000 claims description 2
- 231100000599 cytotoxic agent Toxicity 0.000 claims description 2
- 229940127121 immunoconjugate Drugs 0.000 claims description 2
- 230000008782 phagocytosis Effects 0.000 claims description 2
- 230000001105 regulatory effect Effects 0.000 claims description 2
- 239000003053 toxin Substances 0.000 claims description 2
- 231100000765 toxin Toxicity 0.000 claims description 2
- 239000000824 cytostatic agent Substances 0.000 claims 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 252
- 102000003745 Hepatocyte Growth Factor Human genes 0.000 description 153
- 108090000100 Hepatocyte Growth Factor Proteins 0.000 description 153
- 235000001014 amino acid Nutrition 0.000 description 113
- 150000001413 amino acids Chemical class 0.000 description 103
- 229940024606 amino acid Drugs 0.000 description 96
- 210000004602 germ cell Anatomy 0.000 description 78
- 230000000694 effects Effects 0.000 description 59
- 230000004913 activation Effects 0.000 description 50
- 108020004414 DNA Proteins 0.000 description 46
- 239000005557 antagonist Substances 0.000 description 45
- 125000000539 amino acid group Chemical group 0.000 description 38
- 102000005962 receptors Human genes 0.000 description 36
- 108020003175 receptors Proteins 0.000 description 36
- 238000006467 substitution reaction Methods 0.000 description 34
- 239000000556 agonist Substances 0.000 description 32
- 108090000623 proteins and genes Proteins 0.000 description 32
- 238000003556 assay Methods 0.000 description 31
- 235000018102 proteins Nutrition 0.000 description 26
- 102000004169 proteins and genes Human genes 0.000 description 26
- 230000003828 downregulation Effects 0.000 description 25
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 24
- 230000005764 inhibitory process Effects 0.000 description 20
- 108060003951 Immunoglobulin Proteins 0.000 description 17
- 102000018358 immunoglobulin Human genes 0.000 description 17
- 238000003566 phosphorylation assay Methods 0.000 description 17
- 241000282832 Camelidae Species 0.000 description 16
- 241000894007 species Species 0.000 description 16
- 102000009203 Sema domains Human genes 0.000 description 15
- 108050000099 Sema domains Proteins 0.000 description 15
- 230000026731 phosphorylation Effects 0.000 description 15
- 238000006366 phosphorylation reaction Methods 0.000 description 15
- 238000005406 washing Methods 0.000 description 15
- 235000002198 Annona diversifolia Nutrition 0.000 description 14
- 238000002965 ELISA Methods 0.000 description 14
- 230000004048 modification Effects 0.000 description 14
- 238000012986 modification Methods 0.000 description 14
- 230000000903 blocking effect Effects 0.000 description 13
- 238000010494 dissociation reaction Methods 0.000 description 13
- 230000005593 dissociations Effects 0.000 description 13
- 230000035772 mutation Effects 0.000 description 13
- 241000282842 Lama glama Species 0.000 description 12
- 230000013595 glycosylation Effects 0.000 description 12
- 238000006206 glycosylation reaction Methods 0.000 description 12
- 241000699666 Mus <mouse, genus> Species 0.000 description 11
- 238000007792 addition Methods 0.000 description 11
- 230000035578 autophosphorylation Effects 0.000 description 11
- 150000001875 compounds Chemical class 0.000 description 11
- 239000006185 dispersion Substances 0.000 description 11
- 230000003053 immunization Effects 0.000 description 11
- 238000002649 immunization Methods 0.000 description 11
- 239000003446 ligand Substances 0.000 description 11
- 238000012360 testing method Methods 0.000 description 11
- 241000282412 Homo Species 0.000 description 10
- 230000009089 cytolysis Effects 0.000 description 10
- 238000012217 deletion Methods 0.000 description 10
- 230000037430 deletion Effects 0.000 description 10
- 238000006471 dimerization reaction Methods 0.000 description 10
- 230000003389 potentiating effect Effects 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 9
- 102000018697 Membrane Proteins Human genes 0.000 description 9
- 108010052285 Membrane Proteins Proteins 0.000 description 9
- 230000000875 corresponding effect Effects 0.000 description 9
- 210000005260 human cell Anatomy 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 229910052757 nitrogen Inorganic materials 0.000 description 9
- 102000039446 nucleic acids Human genes 0.000 description 9
- 108020004707 nucleic acids Proteins 0.000 description 9
- 150000007523 nucleic acids Chemical class 0.000 description 9
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 9
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 8
- 241000283707 Capra Species 0.000 description 8
- 241000282838 Lama Species 0.000 description 8
- 230000008485 antagonism Effects 0.000 description 8
- 239000005018 casein Substances 0.000 description 8
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 8
- 235000021240 caseins Nutrition 0.000 description 8
- 230000000670 limiting effect Effects 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 230000001225 therapeutic effect Effects 0.000 description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 7
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 7
- 241001529936 Murinae Species 0.000 description 7
- 230000028993 immune response Effects 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 239000013642 negative control Substances 0.000 description 7
- 208000002154 non-small cell lung carcinoma Diseases 0.000 description 7
- 239000013641 positive control Substances 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 210000004881 tumor cell Anatomy 0.000 description 7
- 241000699670 Mus sp. Species 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 230000008484 agonism Effects 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 238000000684 flow cytometry Methods 0.000 description 6
- 238000005734 heterodimerization reaction Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
- 230000035755 proliferation Effects 0.000 description 6
- 230000011664 signaling Effects 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- 101000737796 Homo sapiens Cerebellar degeneration-related protein 2 Proteins 0.000 description 5
- 230000003042 antagnostic effect Effects 0.000 description 5
- 230000003305 autocrine Effects 0.000 description 5
- 230000002860 competitive effect Effects 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- 230000009260 cross reactivity Effects 0.000 description 5
- 230000007423 decrease Effects 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 230000001747 exhibiting effect Effects 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 230000001900 immune effect Effects 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 230000002018 overexpression Effects 0.000 description 5
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 230000004614 tumor growth Effects 0.000 description 5
- 229910052727 yttrium Inorganic materials 0.000 description 5
- 101000746783 Homo sapiens Cytochrome b-c1 complex subunit 6, mitochondrial Proteins 0.000 description 4
- 101000654674 Homo sapiens Semaphorin-6A Proteins 0.000 description 4
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 4
- 102100032795 Semaphorin-6A Human genes 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 230000004663 cell proliferation Effects 0.000 description 4
- 238000001516 cell proliferation assay Methods 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- 230000002496 gastric effect Effects 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 102000048638 human UQCRH Human genes 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 230000001976 improved effect Effects 0.000 description 4
- 230000006872 improvement Effects 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 210000003734 kidney Anatomy 0.000 description 4
- 210000003292 kidney cell Anatomy 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 4
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 3
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 3
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 3
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 241001416177 Vicugna pacos Species 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 239000012148 binding buffer Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000000481 breast Anatomy 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 230000008030 elimination Effects 0.000 description 3
- 238000003379 elimination reaction Methods 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 206010017758 gastric cancer Diseases 0.000 description 3
- 208000010749 gastric carcinoma Diseases 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 229940072221 immunoglobulins Drugs 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 238000013507 mapping Methods 0.000 description 3
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 230000003076 paracrine Effects 0.000 description 3
- 238000012510 peptide mapping method Methods 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000012552 review Methods 0.000 description 3
- 230000002269 spontaneous effect Effects 0.000 description 3
- 201000000498 stomach carcinoma Diseases 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 229940124597 therapeutic agent Drugs 0.000 description 3
- 210000001685 thyroid gland Anatomy 0.000 description 3
- 229910052720 vanadium Inorganic materials 0.000 description 3
- 238000002424 x-ray crystallography Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 240000003291 Armoracia rusticana Species 0.000 description 2
- 235000011330 Armoracia rusticana Nutrition 0.000 description 2
- 206010006187 Breast cancer Diseases 0.000 description 2
- 241000282836 Camelus dromedarius Species 0.000 description 2
- 208000005623 Carcinogenesis Diseases 0.000 description 2
- 241000282693 Cercopithecidae Species 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000009161 IPT domains Human genes 0.000 description 2
- 108050000019 IPT domains Proteins 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- 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 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 230000006978 adaptation Effects 0.000 description 2
- 230000001464 adherent effect Effects 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 239000002246 antineoplastic agent Substances 0.000 description 2
- 230000006907 apoptotic process Effects 0.000 description 2
- -1 c-Met Proteins 0.000 description 2
- 230000036952 cancer formation Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 231100000504 carcinogenesis Toxicity 0.000 description 2
- 230000005754 cellular signaling Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 238000002784 cytotoxicity assay Methods 0.000 description 2
- 231100000263 cytotoxicity test Toxicity 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000006240 deamidation Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 238000009510 drug design Methods 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000000099 in vitro assay Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 238000006317 isomerization reaction Methods 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 210000005229 liver cell Anatomy 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 238000010899 nucleation Methods 0.000 description 2
- 230000002611 ovarian Effects 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 208000008443 pancreatic carcinoma Diseases 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 230000009145 protein modification Effects 0.000 description 2
- 230000005180 public health Effects 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 238000012916 structural analysis Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 235000011149 sulphuric acid Nutrition 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 241000282552 Chlorocebus aethiops Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 230000008836 DNA modification Effects 0.000 description 1
- 206010012335 Dependence Diseases 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 1
- 101001057612 Homo sapiens Dual specificity protein phosphatase 5 Proteins 0.000 description 1
- 101000998947 Homo sapiens Immunoglobulin heavy variable 1-46 Proteins 0.000 description 1
- 101000604674 Homo sapiens Immunoglobulin kappa variable 4-1 Proteins 0.000 description 1
- 101000956888 Homo sapiens Immunoglobulin lambda variable 2-18 Proteins 0.000 description 1
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 1
- 101000917858 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-A Proteins 0.000 description 1
- 101000917839 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-B Proteins 0.000 description 1
- 101150085452 IPT1 gene Proteins 0.000 description 1
- 108010073807 IgG Receptors Proteins 0.000 description 1
- 102000009490 IgG Receptors Human genes 0.000 description 1
- 102100036888 Immunoglobulin heavy variable 1-46 Human genes 0.000 description 1
- 102100038198 Immunoglobulin kappa variable 4-1 Human genes 0.000 description 1
- 102100038431 Immunoglobulin lambda variable 2-18 Human genes 0.000 description 1
- 208000008839 Kidney Neoplasms Diseases 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
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-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
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-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
- 241000282852 Lama guanicoe Species 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000282560 Macaca mulatta Species 0.000 description 1
- 101000913072 Mus musculus Low affinity immunoglobulin gamma Fc region receptor III Proteins 0.000 description 1
- 230000004989 O-glycosylation Effects 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 206010033128 Ovarian cancer Diseases 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 102000004278 Receptor Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000873 Receptor Protein-Tyrosine Kinases Proteins 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- PLXBWHJQWKZRKG-UHFFFAOYSA-N Resazurin Chemical compound C1=CC(=O)C=C2OC3=CC(O)=CC=C3[N+]([O-])=C21 PLXBWHJQWKZRKG-UHFFFAOYSA-N 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 208000024770 Thyroid neoplasm Diseases 0.000 description 1
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 1
- 244000000188 Vaccinium ovalifolium Species 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 241000282840 Vicugna vicugna Species 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 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 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000003314 affinity selection Methods 0.000 description 1
- 230000001270 agonistic effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 229940041181 antineoplastic drug Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000000712 assembly Effects 0.000 description 1
- 238000000429 assembly Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000013357 binding ELISA Methods 0.000 description 1
- 230000007321 biological mechanism Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 239000003560 cancer drug Substances 0.000 description 1
- 125000001314 canonical amino-acid group Chemical group 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000004709 cell invasion Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 208000019065 cervical carcinoma Diseases 0.000 description 1
- 210000003679 cervix uteri Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000001461 cytolytic effect Effects 0.000 description 1
- 230000009615 deamination Effects 0.000 description 1
- 238000006481 deamination reaction Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000029578 entry into host Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 208000021045 exocrine pancreatic carcinoma Diseases 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012997 ficoll-paque Substances 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 125000002446 fucosyl group Chemical group C1([C@@H](O)[C@H](O)[C@H](O)[C@@H](O1)C)* 0.000 description 1
- 238000009650 gentamicin protection assay Methods 0.000 description 1
- 208000005017 glioblastoma Diseases 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 125000003712 glycosamine group Chemical group 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 210000003128 head Anatomy 0.000 description 1
- 201000003911 head and neck carcinoma Diseases 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 102000043381 human DUSP5 Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229940042743 immune sera Drugs 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 201000010982 kidney cancer Diseases 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- FFEARJCKVFRZRR-UHFFFAOYSA-N methionine Chemical compound CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 230000024799 morphogenesis of a branching structure Effects 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 210000003739 neck Anatomy 0.000 description 1
- 210000004237 neck muscle Anatomy 0.000 description 1
- 230000027405 negative regulation of phosphorylation Effects 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 201000008968 osteosarcoma Diseases 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 230000029279 positive regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000002516 postimmunization Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 201000001514 prostate carcinoma Diseases 0.000 description 1
- 230000004224 protection Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 239000002464 receptor antagonist Substances 0.000 description 1
- 229940044551 receptor antagonist Drugs 0.000 description 1
- 102000027426 receptor tyrosine kinases Human genes 0.000 description 1
- 108091008598 receptor tyrosine kinases Proteins 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 201000009410 rhabdomyosarcoma Diseases 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 206010041823 squamous cell carcinoma Diseases 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 229940036185 synagis Drugs 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 210000003932 urinary bladder Anatomy 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for 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
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
-
- 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
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
-
- 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
-
- 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
- C07K2317/32—Immunoglobulins specific features characterized by aspects of specificity or valency specific for a neo-epitope on a complex, e.g. antibody-antigen or ligand-receptor
-
- 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
- C07K2317/74—Inducing 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
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- 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)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Oncology (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (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 (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US40986610P | 2010-11-03 | 2010-11-03 | |
| US409866P | 2010-11-03 | ||
| PCT/EP2011/069369 WO2012059561A1 (en) | 2010-11-03 | 2011-11-03 | Anti c-met antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2594493T3 true ES2594493T3 (es) | 2016-12-20 |
Family
ID=44906140
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES11778618.6T Active ES2594493T3 (es) | 2010-11-03 | 2011-11-03 | Anticuerpos anti-c-Met |
Country Status (12)
| Country | Link |
|---|---|
| US (7) | US9688773B2 (show.php) |
| EP (3) | EP3165538A1 (show.php) |
| JP (3) | JP2013545738A (show.php) |
| CN (2) | CN103562223B (show.php) |
| AU (3) | AU2011325097B2 (show.php) |
| BR (3) | BR112013010687A2 (show.php) |
| CA (2) | CA2816745C (show.php) |
| DK (1) | DK2635602T3 (show.php) |
| ES (1) | ES2594493T3 (show.php) |
| IL (2) | IL226112B (show.php) |
| RU (2) | RU2013125457A (show.php) |
| WO (2) | WO2012059562A1 (show.php) |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8444976B2 (en) | 2008-07-02 | 2013-05-21 | Argen-X B.V. | Antigen binding polypeptides |
| EP2143441A1 (en) | 2008-07-08 | 2010-01-13 | Pierre Fabre Medicament | Combination of a c-Met antagonist and an aminoheteroaryl compound for the treatment of cancer |
| AU2011325097B2 (en) | 2010-11-03 | 2015-05-21 | Argenx Bvba | Anti c-Met antibodies |
| KR20130036993A (ko) * | 2011-10-05 | 2013-04-15 | 삼성전자주식회사 | ｃ-Ｍｅｔ의 ＳＥＭＡ 도메인 내의 에피토프에 특이적으로 결합하는 항체 |
| WO2013088259A2 (en) * | 2011-10-19 | 2013-06-20 | Novimmune S.A. | Methods of purifying antibodies |
| US9926364B2 (en) | 2011-11-03 | 2018-03-27 | Argen-X N.V. | Chimeric human-llama antigens and methods of use |
| AU2012340826A1 (en) | 2011-11-21 | 2014-05-29 | Genentech, Inc. | Purification of anti-c-met antibodies |
| WO2013079973A1 (en) * | 2011-12-02 | 2013-06-06 | Di Cara Danielle Marie | Antibodies against hgf - receptor and uses |
| WO2013110531A1 (en) | 2012-01-23 | 2013-08-01 | Ablynx Nv | Sequences directed against hepatocyte growth factor (hgf) and polypeptides comprising the same for the treatment of cancers and/or tumors |
| US9931400B2 (en) | 2012-09-12 | 2018-04-03 | Samsung Electronics Co., Ltd. | Method of combination therapy for prevention or treatment of c-Met or angiogenesis factor induced diseases |
| US9168300B2 (en) | 2013-03-14 | 2015-10-27 | Oncomed Pharmaceuticals, Inc. | MET-binding agents and uses thereof |
| US9535055B2 (en) * | 2013-03-28 | 2017-01-03 | Samsung Electronics Co., Ltd. | Marker for determining effects of anti-c-Met antibody and method of determining effects of anti-c-Met antibody using the marker |
| KR102139607B1 (ko) * | 2013-04-01 | 2020-07-30 | 삼성전자주식회사 | 항 c-Met 항체 및 FGFR 저해제를 포함하는 병용 투여용 약학 조성물 |
| EP2786765B1 (en) * | 2013-04-01 | 2018-10-03 | Samsung Electronics Co., Ltd. | Composition for combination therapy comprising an anti-C-met antibody and a FGFR inhibitor |
| US10214593B2 (en) | 2013-04-02 | 2019-02-26 | Samsung Electronics Co., Ltd. | Anti-idiotype antibody against anti-c-MET antibody |
| KR102060540B1 (ko) | 2013-04-03 | 2019-12-31 | 삼성전자주식회사 | 항 c-Met 항체 및 항 Ang2 항체를 포함하는 병용 투여용 약학 조성물 |
| SG11201508875TA (en) | 2013-04-30 | 2015-11-27 | Agency Science Tech & Res | Mab 2 anti-met antibody |
| KR102186363B1 (ko) * | 2013-09-06 | 2020-12-04 | 삼성전자주식회사 | c-Met 저해제 및 베타-카테닌 저해제를 포함하는 병용 투여용 약학 조성물 |
| KR102192591B1 (ko) * | 2013-09-09 | 2020-12-18 | 삼성전자주식회사 | c-Met 저해제 및 c-Myc 저해제를 포함하는 병용 투여용 약학 조성물 |
| EP3800270B1 (en) * | 2014-07-29 | 2021-10-27 | Wellmarker Bio Co., Ltd. | Inhibitors of met and igsf1 for treating gastric and lung cancer |
| KR102200274B1 (ko) * | 2014-09-16 | 2021-01-08 | 심포젠 에이/에스 | 항-ｍｅｔ 항체 및 조성물 |
| WO2016149265A1 (en) * | 2015-03-16 | 2016-09-22 | Kolltan Pharmaceuticals, Inc. | Anti-met antibodies and methods of use thereof |
| GB201611123D0 (en) * | 2016-06-27 | 2016-08-10 | Euremab Srl | Anti met antibodiesand uses thereof |
| US11673971B2 (en) * | 2016-09-23 | 2023-06-13 | Marengo Therapeutics, Inc. | Multispecific antibody molecules comprising lambda and kappa light chains |
| TWI782930B (zh) | 2016-11-16 | 2022-11-11 | 美商再生元醫藥公司 | 抗ｍｅｔ抗體，結合ｍｅｔ之雙特異性抗原結合分子及其使用方法 |
| WO2018221969A1 (en) * | 2017-05-30 | 2018-12-06 | Chong Kun Dang Pharmaceutical Corp. | A novel anti-c-met antibody and use thereof |
| US11479612B2 (en) * | 2017-05-30 | 2022-10-25 | Chong Kun Dang Pharmaceutical Corp. | Anti-c-Met antibody and use thereof |
| CA3070100A1 (en) * | 2017-07-17 | 2019-01-24 | Janssen Biotech, Inc. | Antigen binding regions against fibronectin type iii domains and methods of using the same |
| CN109771642B (zh) * | 2017-11-13 | 2022-09-20 | 同济大学苏州研究院 | c-MET激动型抗体及其用途 |
| US11591390B2 (en) | 2018-09-27 | 2023-02-28 | Celgene Corporation | SIRP-α binding proteins and methods of use thereof |
| JP7266670B2 (ja) | 2018-09-27 | 2023-04-28 | セルジーン コーポレイション | ＳＩＲＰα結合タンパク質及びその使用方法 |
| CN114340684B (zh) | 2019-09-16 | 2025-09-12 | 瑞泽恩制药公司 | 用于免疫pet成像的放射性标记的met结合蛋白 |
| EP4320152A1 (en) | 2021-04-08 | 2024-02-14 | Byondis B.V. | Anti-c-met antibodies and antibody-drug conjugates |
| US20250136701A1 (en) * | 2021-09-03 | 2025-05-01 | Go Therapeutics, Inc. | Anti-glyco-cmet antibodies and their uses |
| TW202500584A (zh) | 2023-05-19 | 2025-01-01 | 法商施維雅藥廠 | 抗met抗體、抗體-藥物結合物、組合物及其用途 |
Family Cites Families (28)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5892019A (en) | 1987-07-15 | 1999-04-06 | The United States Of America, As Represented By The Department Of Health And Human Services | Production of a single-gene-encoded immunoglobulin |
| US5648273A (en) | 1989-12-27 | 1997-07-15 | The United States Of America, As Represented By The Department Of Health And Human Services | Hepatic growth factor receptor is the MET proto-oncogene |
| DE69334159D1 (de) | 1992-09-18 | 2007-09-13 | Us Gov Health & Human Serv | Medizinische Verwendung eines Antikörpers oder eines Antikörperfragments gegen die extrazelluläre Domäne von Met zur Prevention von Metastasen |
| US5686292A (en) | 1995-06-02 | 1997-11-11 | Genentech, Inc. | Hepatocyte growth factor receptor antagonist antibodies and uses thereof |
| US6214344B1 (en) | 1995-06-02 | 2001-04-10 | Genetech, Inc. | Hepatocyte growth factor receptor antagonists and uses thereof |
| ATE465257T1 (de) | 1996-07-03 | 2010-05-15 | Genentech Inc | Agonisten für den rezeptor des hepatozyten- wachstumsfaktors und deren anwendungen |
| ITMI20031127A1 (it) | 2003-06-05 | 2004-12-06 | Uni Degli Studi Del Piemont E Orientale Am | Anticorpi anti-hgf-r e loro uso |
| CN100538364C (zh) * | 2003-06-06 | 2009-09-09 | 健泰科生物技术公司 | 调节HGFβ链和C-MET的相互作用 |
| HN2004000285A (es) | 2003-08-04 | 2006-04-27 | Pfizer Prod Inc | ANTICUERPOS DIRIGIDOS A c-MET |
| KR100556660B1 (ko) * | 2003-11-11 | 2006-03-10 | 국립암센터 | Ｈｇｆ의 중화가능 에피토프 및 이에 결합하는 중화 항체 |
| RU2006124743A (ru) | 2003-12-11 | 2008-01-20 | Дженентек, Инк. (Us) | СПОСОБЫ И КОМПОЗИЦИИ ДЛЯ ИНГИБИРОВАНИЯ ДИМЕРИЗАЦИИ И АКТИВАЦИИ с-Мет |
| KR101397851B1 (ko) * | 2004-08-05 | 2014-05-22 | 제넨테크, 인크. | 인간화 항-ｃｍｅｔ 길항제 |
| ATE541584T1 (de) | 2005-11-16 | 2012-02-15 | Fariba Nayeri | Verfahren zur hemmung von krebsbildung und/oder metastasen bei einer person durch endogene c-met- liganden und -hemmer |
| AU2007213804B2 (en) | 2006-02-06 | 2012-12-13 | Vertical Bio Ag | Anti-met monoclonal antibody, fragments and vectors thereof, for the treatment of tumors and corresponding products |
| CN103183738B (zh) | 2006-03-30 | 2014-08-06 | 诺瓦提斯公司 | c-Met抗体的组合物和使用方法 |
| FR2906533B1 (fr) | 2006-09-28 | 2013-02-22 | Pf Medicament | Procede de generation d'anticorps actifs contre un antigene de resistance,anticorps obtenus par ledit procede et leurs utilisations |
| EP2014681A1 (en) * | 2007-07-12 | 2009-01-14 | Pierre Fabre Medicament | Novel antibodies inhibiting c-met dimerization, and uses thereof |
| EP2177623A4 (en) | 2007-07-19 | 2010-12-29 | Eisai R&D Man Co Ltd | SCREENING METHOD USING C-MET, A NEW SUBSTRATE FOR GAMMA SECRETASE |
| US7892770B2 (en) | 2007-08-24 | 2011-02-22 | Van Andel Research Institute | Monoclonal antibody which binds cMet (HGFR) in formalin-fixed and paraffin-embedded tissues and related methods |
| IL198545A0 (en) | 2008-05-14 | 2011-07-31 | Metheresis Translational Res Sa | High affinity binding site of hgfr and methods for identification of antagonists thereof |
| US8455623B2 (en) | 2008-05-21 | 2013-06-04 | Oncomed Pharmaceuticals, Inc. | Compositions and methods for diagnosing and treating cancer |
| EP2297301A1 (en) | 2008-05-28 | 2011-03-23 | U-Protein Express B.V. | Method for the production of proteins or protein fragments |
| GB2461546B (en) | 2008-07-02 | 2010-07-07 | Argen X Bv | Antigen binding polypeptides |
| WO2010005965A1 (en) | 2008-07-08 | 2010-01-14 | Aronchick Craig A | Colonic purgative formulations and methods of using the same |
| PA8849001A1 (es) | 2008-11-21 | 2010-06-28 | Lilly Co Eli | Anticuerpos de c-met |
| AR074439A1 (es) | 2008-12-02 | 2011-01-19 | Pf Medicament | Anticuerpo anti-cmet (receptor c-met) |
| US8545839B2 (en) | 2008-12-02 | 2013-10-01 | Pierre Fabre Medicament | Anti-c-Met antibody |
| AU2011325097B2 (en) | 2010-11-03 | 2015-05-21 | Argenx Bvba | Anti c-Met antibodies |
-
2011
- 2011-11-03 AU AU2011325097A patent/AU2011325097B2/en active Active
- 2011-11-03 CA CA2816745A patent/CA2816745C/en active Active
- 2011-11-03 WO PCT/EP2011/069372 patent/WO2012059562A1/en not_active Ceased
- 2011-11-03 US US13/288,587 patent/US9688773B2/en active Active
- 2011-11-03 AU AU2011325098A patent/AU2011325098B2/en not_active Ceased
- 2011-11-03 JP JP2013537139A patent/JP2013545738A/ja active Pending
- 2011-11-03 EP EP16187257.7A patent/EP3165538A1/en not_active Withdrawn
- 2011-11-03 DK DK11778618.6T patent/DK2635602T3/en active
- 2011-11-03 EP EP11778618.6A patent/EP2635602B1/en active Active
- 2011-11-03 CN CN201180052993.1A patent/CN103562223B/zh active Active
- 2011-11-03 RU RU2013125457/10A patent/RU2013125457A/ru unknown
- 2011-11-03 BR BR112013010687A patent/BR112013010687A2/pt not_active IP Right Cessation
- 2011-11-03 EP EP11778887.7A patent/EP2635603B1/en active Active
- 2011-11-03 JP JP2013537138A patent/JP5857060B2/ja active Active
- 2011-11-03 BR BR112013010688-3A patent/BR112013010688B1/pt active IP Right Grant
- 2011-11-03 BR BR122014027420-3A patent/BR122014027420A2/pt not_active Application Discontinuation
- 2011-11-03 WO PCT/EP2011/069369 patent/WO2012059561A1/en not_active Ceased
- 2011-11-03 RU RU2013125459A patent/RU2608644C2/ru active
- 2011-11-03 ES ES11778618.6T patent/ES2594493T3/es active Active
- 2011-11-03 US US13/288,566 patent/US8637027B2/en active Active
- 2011-11-03 CA CA2816919A patent/CA2816919A1/en not_active Abandoned
- 2011-11-03 CN CN201180063338.6A patent/CN103764678A/zh active Pending
-
2013
- 2013-05-02 IL IL226112A patent/IL226112B/en active IP Right Grant
- 2013-05-02 IL IL226113A patent/IL226113A0/en unknown
- 2013-12-06 US US14/098,849 patent/US9884917B2/en active Active
-
2015
- 2015-02-17 US US14/624,216 patent/US9631027B2/en active Active
- 2015-02-17 US US14/624,193 patent/US9688774B2/en active Active
- 2015-08-07 AU AU2015210420A patent/AU2015210420B2/en active Active
- 2015-09-09 JP JP2015177202A patent/JP2016034957A/ja active Pending
-
2017
- 2017-05-16 US US15/596,890 patent/US20170349667A1/en not_active Abandoned
- 2017-12-26 US US15/854,312 patent/US10676535B2/en active Active
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2594493T3 (es) | Anticuerpos anti-c-Met | |
| CN104334579A (zh) | 抗c-met抗体及其用途 | |
| ES2903412T3 (es) | Anticuerpos anti-IL-22R | |
| CA2968510C (en) | Novel egfrviii antibody and composition comprising same | |
| Anna et al. | Anti C-met Antibodies-granted patent (Canada) | |
| WO2025108427A1 (zh) | 结合分子及抗体药物偶联物和用途 | |
| CN120813606A (zh) | 抗cldn6抗体和使用方法 |