ES2743558T3 - Anticuerpos de-EphA3 - Google Patents
Anticuerpos de-EphA3 Download PDFInfo
- Publication number
- ES2743558T3 ES2743558T3 ES10777137T ES10777137T ES2743558T3 ES 2743558 T3 ES2743558 T3 ES 2743558T3 ES 10777137 T ES10777137 T ES 10777137T ES 10777137 T ES10777137 T ES 10777137T ES 2743558 T3 ES2743558 T3 ES 2743558T3
- Authority
- ES
- Spain
- Prior art keywords
- antibody
- sequence
- amino acid
- seq
- segment
- 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
- 108010055191 EphA3 Receptor Proteins 0.000 title claims abstract description 79
- 102000021607 EphA3 Receptor Human genes 0.000 title claims abstract 7
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 60
- 210000004602 germ cell Anatomy 0.000 claims abstract description 51
- 150000001413 amino acids Chemical class 0.000 claims abstract description 44
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 claims abstract description 10
- 210000004027 cell Anatomy 0.000 claims description 89
- 238000000034 method Methods 0.000 claims description 45
- 206010028980 Neoplasm Diseases 0.000 claims description 38
- 201000010099 disease Diseases 0.000 claims description 24
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 24
- 201000011510 cancer Diseases 0.000 claims description 19
- 239000005557 antagonist Substances 0.000 claims description 18
- 238000002360 preparation method Methods 0.000 claims description 16
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 claims description 12
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 claims description 12
- 210000004881 tumor cell Anatomy 0.000 claims description 10
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 claims description 8
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 claims description 8
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 claims description 8
- 238000002560 therapeutic procedure Methods 0.000 claims description 8
- 208000017733 acquired polycythemia vera Diseases 0.000 claims description 7
- 208000037244 polycythemia vera Diseases 0.000 claims description 7
- 208000031261 Acute myeloid leukaemia Diseases 0.000 claims description 4
- 108010060686 dual specificity phosphatase 12 Proteins 0.000 claims description 4
- 201000003793 Myelodysplastic syndrome Diseases 0.000 claims description 3
- 208000033776 Myeloid Acute Leukemia Diseases 0.000 claims description 3
- 230000001419 dependent effect Effects 0.000 claims description 3
- 210000003038 endothelium Anatomy 0.000 claims description 3
- 239000008194 pharmaceutical composition Substances 0.000 claims description 3
- 208000003476 primary myelofibrosis Diseases 0.000 claims description 3
- 206010043554 thrombocytopenia Diseases 0.000 claims description 3
- 206010025323 Lymphomas Diseases 0.000 claims description 2
- 210000004204 blood vessel Anatomy 0.000 claims description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 claims 3
- 229910052799 carbon Inorganic materials 0.000 abstract description 3
- 102100030324 Ephrin type-A receptor 3 Human genes 0.000 description 73
- 238000009739 binding Methods 0.000 description 65
- 230000027455 binding Effects 0.000 description 65
- 102100035361 Cerebellar degeneration-related protein 2 Human genes 0.000 description 42
- 101000737796 Homo sapiens Cerebellar degeneration-related protein 2 Proteins 0.000 description 42
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 41
- 108090000623 proteins and genes Proteins 0.000 description 40
- 235000001014 amino acid Nutrition 0.000 description 39
- 229940024606 amino acid Drugs 0.000 description 39
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 38
- 101000737793 Homo sapiens Cerebellar degeneration-related antigen 1 Proteins 0.000 description 37
- 150000007523 nucleic acids Chemical group 0.000 description 32
- 235000018102 proteins Nutrition 0.000 description 32
- 102000004169 proteins and genes Human genes 0.000 description 32
- 108020004707 nucleic acids Proteins 0.000 description 28
- 102000039446 nucleic acids Human genes 0.000 description 28
- 108090000765 processed proteins & peptides Proteins 0.000 description 25
- 239000000427 antigen Substances 0.000 description 22
- 108091007433 antigens Proteins 0.000 description 22
- 102000036639 antigens Human genes 0.000 description 22
- 108060003951 Immunoglobulin Proteins 0.000 description 21
- 102000018358 immunoglobulin Human genes 0.000 description 21
- 102000004196 processed proteins & peptides Human genes 0.000 description 20
- 229920001184 polypeptide Polymers 0.000 description 19
- 239000003446 ligand Substances 0.000 description 17
- 230000013595 glycosylation Effects 0.000 description 15
- 238000006206 glycosylation reaction Methods 0.000 description 15
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 14
- 239000012636 effector Substances 0.000 description 14
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 13
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 13
- 239000012634 fragment Substances 0.000 description 13
- 239000002953 phosphate buffered saline Substances 0.000 description 12
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 11
- 238000004458 analytical method Methods 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 230000006870 function Effects 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 238000002965 ELISA Methods 0.000 description 8
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 8
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 8
- 241001529936 Murinae Species 0.000 description 8
- 230000002998 immunogenetic effect Effects 0.000 description 8
- 102000005962 receptors Human genes 0.000 description 8
- 108020003175 receptors Proteins 0.000 description 8
- 230000002829 reductive effect Effects 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 108020004705 Codon Proteins 0.000 description 7
- 102000009109 Fc receptors Human genes 0.000 description 7
- 108010087819 Fc receptors Proteins 0.000 description 7
- 125000000539 amino acid group Chemical group 0.000 description 7
- 230000006907 apoptotic process Effects 0.000 description 7
- 238000000684 flow cytometry Methods 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 210000004962 mammalian cell Anatomy 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 6
- 108091008815 Eph receptors Proteins 0.000 description 6
- 108091005461 Nucleic proteins Chemical group 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 6
- 238000010494 dissociation reaction Methods 0.000 description 6
- 230000005593 dissociations Effects 0.000 description 6
- 239000003814 drug Substances 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 230000001613 neoplastic effect Effects 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- 235000000346 sugar Nutrition 0.000 description 6
- 102000050554 Eph Family Receptors Human genes 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 150000001720 carbohydrates Chemical class 0.000 description 5
- 235000014633 carbohydrates Nutrition 0.000 description 5
- 230000029087 digestion Effects 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 230000033581 fucosylation Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- 229910052757 nitrogen Inorganic materials 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 229940124597 therapeutic agent Drugs 0.000 description 5
- 101100383373 Arabidopsis thaliana CPFTSY gene Proteins 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
- 102100021966 Coiled-coil domain-containing protein 34 Human genes 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 4
- 102100030322 Ephrin type-A receptor 1 Human genes 0.000 description 4
- 101000938354 Homo sapiens Ephrin type-A receptor 1 Proteins 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000010276 construction Methods 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 230000006882 induction of apoptosis Effects 0.000 description 4
- 208000032839 leukemia Diseases 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 230000026731 phosphorylation Effects 0.000 description 4
- 238000006366 phosphorylation reaction Methods 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 238000000159 protein binding assay Methods 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 150000008163 sugars Chemical class 0.000 description 4
- 229910052717 sulfur Inorganic materials 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 102100033890 Arylsulfatase G Human genes 0.000 description 3
- 201000009030 Carcinoma Diseases 0.000 description 3
- 108010055196 EphA2 Receptor Proteins 0.000 description 3
- 108010055182 EphA5 Receptor Proteins 0.000 description 3
- 102100030340 Ephrin type-A receptor 2 Human genes 0.000 description 3
- 102100021605 Ephrin type-A receptor 5 Human genes 0.000 description 3
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 3
- 101150008942 J gene Proteins 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
- 208000014767 Myeloproliferative disease Diseases 0.000 description 3
- 201000007224 Myeloproliferative neoplasm Diseases 0.000 description 3
- 206010029113 Neovascularisation Diseases 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 102000057297 Pepsin A Human genes 0.000 description 3
- 108090000284 Pepsin A Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 230000001594 aberrant effect Effects 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 238000013357 binding ELISA Methods 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 238000006471 dimerization reaction Methods 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 238000001802 infusion Methods 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- 150000002482 oligosaccharides Polymers 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 229940111202 pepsin Drugs 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 3
- 108091008598 receptor tyrosine kinases Proteins 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 238000002864 sequence alignment Methods 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 3
- 230000002792 vascular Effects 0.000 description 3
- UCTWMZQNUQWSLP-VIFPVBQESA-N (R)-adrenaline Chemical compound CNC[C@H](O)C1=CC=C(O)C(O)=C1 UCTWMZQNUQWSLP-VIFPVBQESA-N 0.000 description 2
- 229930182837 (R)-adrenaline Natural products 0.000 description 2
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 2
- 108090000672 Annexin A5 Proteins 0.000 description 2
- 102000004121 Annexin A5 Human genes 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 101710115232 Arylsulfatase G Proteins 0.000 description 2
- 206010003445 Ascites Diseases 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102100031983 Ephrin type-B receptor 4 Human genes 0.000 description 2
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 2
- 108091006027 G proteins Proteins 0.000 description 2
- 102000030782 GTP binding Human genes 0.000 description 2
- 108091000058 GTP-Binding Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 2
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 2
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-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
- 241001590997 Moolgarda engeli Species 0.000 description 2
- 101100174574 Mus musculus Pikfyve gene Proteins 0.000 description 2
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 2
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical group CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 2
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 2
- 206010030113 Oedema Diseases 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 206010060862 Prostate cancer Diseases 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 201000004681 Psoriasis Diseases 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 206010038933 Retinopathy of prematurity Diseases 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 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
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 101150117115 V gene Proteins 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 230000005907 cancer growth Effects 0.000 description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 208000037976 chronic inflammation Diseases 0.000 description 2
- 230000006020 chronic inflammation Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 2
- 230000003511 endothelial effect Effects 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 229960005139 epinephrine Drugs 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 125000002446 fucosyl group Chemical group C1([C@@H](O)[C@H](O)[C@H](O)[C@@H](O1)C)* 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 201000011066 hemangioma Diseases 0.000 description 2
- 229960002591 hydroxyproline Drugs 0.000 description 2
- 230000001969 hypertrophic effect Effects 0.000 description 2
- YLMAHDNUQAMNNX-UHFFFAOYSA-N imatinib methanesulfonate Chemical compound CS(O)(=O)=O.C1CN(C)CCN1CC1=CC=C(C(=O)NC=2C=C(NC=3N=C(C=CN=3)C=3C=NC=CC=3)C(C)=CC=2)C=C1 YLMAHDNUQAMNNX-UHFFFAOYSA-N 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 230000004660 morphological change Effects 0.000 description 2
- 210000000822 natural killer cell Anatomy 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 201000008482 osteoarthritis Diseases 0.000 description 2
- 230000006320 pegylation Effects 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 230000035755 proliferation 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
- 102000027426 receptor tyrosine kinases Human genes 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 230000000982 vasogenic effect Effects 0.000 description 2
- 238000011179 visual inspection Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical group OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- UKAUYVFTDYCKQA-UHFFFAOYSA-N -2-Amino-4-hydroxybutanoic acid Natural products OC(=O)C(N)CCO UKAUYVFTDYCKQA-UHFFFAOYSA-N 0.000 description 1
- 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 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- HHDUMDVQUCBCEY-UHFFFAOYSA-N 4-[10,15,20-tris(4-carboxyphenyl)-21,23-dihydroporphyrin-5-yl]benzoic acid Chemical compound OC(=O)c1ccc(cc1)-c1c2ccc(n2)c(-c2ccc(cc2)C(O)=O)c2ccc([nH]2)c(-c2ccc(cc2)C(O)=O)c2ccc(n2)c(-c2ccc(cc2)C(O)=O)c2ccc1[nH]2 HHDUMDVQUCBCEY-UHFFFAOYSA-N 0.000 description 1
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 208000003120 Angiofibroma Diseases 0.000 description 1
- 101100446451 Aquifex aeolicus (strain VF5) fdx4 gene Proteins 0.000 description 1
- 208000022211 Arteriovenous Malformations Diseases 0.000 description 1
- 206010003571 Astrocytoma Diseases 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 208000037260 Atherosclerotic Plaque Diseases 0.000 description 1
- 208000032800 BCR-ABL1 positive blast phase chronic myelogenous leukemia Diseases 0.000 description 1
- 208000004860 Blast Crisis Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 208000003174 Brain Neoplasms Diseases 0.000 description 1
- 206010048962 Brain oedema Diseases 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- KLWPJMFMVPTNCC-UHFFFAOYSA-N Camptothecin Natural products CCC1(O)C(=O)OCC2=C1C=C3C4Nc5ccccc5C=C4CN3C2=O KLWPJMFMVPTNCC-UHFFFAOYSA-N 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 208000017897 Carcinoma of esophagus Diseases 0.000 description 1
- 208000010667 Carcinoma of liver and intrahepatic biliary tract Diseases 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 208000003163 Cavernous Hemangioma Diseases 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 208000006332 Choriocarcinoma Diseases 0.000 description 1
- 208000005590 Choroidal Neovascularization Diseases 0.000 description 1
- 206010060823 Choroidal neovascularisation Diseases 0.000 description 1
- 208000032544 Cicatrix Diseases 0.000 description 1
- 206010009900 Colitis ulcerative Diseases 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 208000001333 Colorectal Neoplasms Diseases 0.000 description 1
- 206010011017 Corneal graft rejection Diseases 0.000 description 1
- 206010055665 Corneal neovascularisation Diseases 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 201000004624 Dermatitis Diseases 0.000 description 1
- 206010012688 Diabetic retinal oedema Diseases 0.000 description 1
- 206010012689 Diabetic retinopathy Diseases 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101000827763 Drosophila melanogaster Fibroblast growth factor receptor homolog 1 Proteins 0.000 description 1
- 101150016325 EPHA3 gene Proteins 0.000 description 1
- 206010063045 Effusion Diseases 0.000 description 1
- 206010014733 Endometrial cancer Diseases 0.000 description 1
- 206010014759 Endometrial neoplasm Diseases 0.000 description 1
- 201000009273 Endometriosis Diseases 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 102100031984 Ephrin type-B receptor 6 Human genes 0.000 description 1
- 102100033941 Ephrin-A5 Human genes 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 208000032027 Essential Thrombocythemia Diseases 0.000 description 1
- 208000004248 Familial Primary Pulmonary Hypertension Diseases 0.000 description 1
- 102100037362 Fibronectin Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 201000008808 Fibrosarcoma Diseases 0.000 description 1
- 108010019236 Fucosyltransferases Proteins 0.000 description 1
- 208000010412 Glaucoma Diseases 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
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 206010018498 Goitre Diseases 0.000 description 1
- 208000003807 Graves Disease Diseases 0.000 description 1
- 208000015023 Graves' disease Diseases 0.000 description 1
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 1
- 206010073069 Hepatic cancer Diseases 0.000 description 1
- 101000925538 Homo sapiens Arylsulfatase G Proteins 0.000 description 1
- 101000938351 Homo sapiens Ephrin type-A receptor 3 Proteins 0.000 description 1
- 101001064451 Homo sapiens Ephrin type-B receptor 6 Proteins 0.000 description 1
- 101000925251 Homo sapiens Ephrin-A5 Proteins 0.000 description 1
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 1
- 101000840258 Homo sapiens Immunoglobulin J chain Proteins 0.000 description 1
- 101000917858 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-A Proteins 0.000 description 1
- 101000582320 Homo sapiens Neurogenic differentiation factor 6 Proteins 0.000 description 1
- LCWXJXMHJVIJFK-UHFFFAOYSA-N Hydroxylysine Chemical group NCC(O)CC(N)CC(O)=O LCWXJXMHJVIJFK-UHFFFAOYSA-N 0.000 description 1
- 206010020880 Hypertrophy Diseases 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102100029571 Immunoglobulin J chain Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 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
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- UKAUYVFTDYCKQA-VKHMYHEASA-N L-homoserine Chemical compound OC(=O)[C@@H](N)CCO UKAUYVFTDYCKQA-VKHMYHEASA-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
- QEFRNWWLZKMPFJ-ZXPFJRLXSA-N L-methionine (R)-S-oxide Chemical compound C[S@@](=O)CC[C@H]([NH3+])C([O-])=O QEFRNWWLZKMPFJ-ZXPFJRLXSA-N 0.000 description 1
- QEFRNWWLZKMPFJ-UHFFFAOYSA-N L-methionine sulphoxide Natural products CS(=O)CCC(N)C(O)=O QEFRNWWLZKMPFJ-UHFFFAOYSA-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 group C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-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
- 239000005517 L01XE01 - Imatinib Substances 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 208000000172 Medulloblastoma Diseases 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 201000002481 Myositis Diseases 0.000 description 1
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 208000002454 Nasopharyngeal Carcinoma Diseases 0.000 description 1
- 206010061306 Nasopharyngeal cancer Diseases 0.000 description 1
- 241001045988 Neogene Species 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 206010029164 Nephrotic syndrome Diseases 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 102100030589 Neurogenic differentiation factor 6 Human genes 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 208000008589 Obesity Diseases 0.000 description 1
- 206010030155 Oesophageal carcinoma Diseases 0.000 description 1
- 201000010133 Oligodendroglioma Diseases 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 102000016979 Other receptors Human genes 0.000 description 1
- 206010033128 Ovarian cancer Diseases 0.000 description 1
- 206010033645 Pancreatitis Diseases 0.000 description 1
- 102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 1
- 108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 1
- 208000005228 Pericardial Effusion Diseases 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 208000002151 Pleural effusion Diseases 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 206010036595 Premature delivery Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 206010064911 Pulmonary arterial hypertension Diseases 0.000 description 1
- 206010037649 Pyogenic granuloma Diseases 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- 208000006265 Renal cell carcinoma Diseases 0.000 description 1
- 201000000582 Retinoblastoma Diseases 0.000 description 1
- 206010038934 Retinopathy proliferative Diseases 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 206010039710 Scleroderma Diseases 0.000 description 1
- 206010040047 Sepsis Diseases 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 208000030886 Traumatic Brain injury Diseases 0.000 description 1
- 206010064390 Tumour invasion Diseases 0.000 description 1
- 201000006704 Ulcerative Colitis Diseases 0.000 description 1
- 206010046798 Uterine leiomyoma Diseases 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 206010047741 Vulval cancer Diseases 0.000 description 1
- 208000013058 Weber syndrome Diseases 0.000 description 1
- 208000008383 Wilms tumor Diseases 0.000 description 1
- 229960000446 abciximab Drugs 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 206010069351 acute lung injury Diseases 0.000 description 1
- 210000000577 adipose tissue Anatomy 0.000 description 1
- 201000000028 adult respiratory distress syndrome Diseases 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 206010064930 age-related macular degeneration Diseases 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 230000002494 anti-cea effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 238000011091 antibody purification Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000005744 arteriovenous malformation Effects 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit 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
- 108091008324 binding proteins Proteins 0.000 description 1
- 238000012575 bio-layer interferometry Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 208000006752 brain edema Diseases 0.000 description 1
- 208000029028 brain injury Diseases 0.000 description 1
- 201000007293 brain stem infarction Diseases 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 201000008275 breast carcinoma Diseases 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 229940127093 camptothecin Drugs 0.000 description 1
- VSJKWCGYPAHWDS-FQEVSTJZSA-N camptothecin Chemical compound C1=CC=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 VSJKWCGYPAHWDS-FQEVSTJZSA-N 0.000 description 1
- 230000009400 cancer invasion Effects 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 208000019065 cervical carcinoma Diseases 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000009614 chemical analysis method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 201000010989 colorectal carcinoma Diseases 0.000 description 1
- 206010010121 compartment syndrome Diseases 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 230000030944 contact inhibition Effects 0.000 description 1
- 201000000159 corneal neovascularization Diseases 0.000 description 1
- 239000012228 culture supernatant Substances 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
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Chemical group NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
- 230000002074 deregulated effect Effects 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 201000011190 diabetic macular edema Diseases 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- VSJKWCGYPAHWDS-UHFFFAOYSA-N dl-camptothecin Natural products C1=CC=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)C5(O)CC)C4=NC2=C1 VSJKWCGYPAHWDS-UHFFFAOYSA-N 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 201000003914 endometrial carcinoma Diseases 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical group NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 1
- 201000005619 esophageal carcinoma Diseases 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 208000021045 exocrine pancreatic carcinoma Diseases 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000012530 fluid 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
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- -1 frame 2 Proteins 0.000 description 1
- 101150023212 fut8 gene Proteins 0.000 description 1
- 206010017758 gastric cancer Diseases 0.000 description 1
- 208000010749 gastric carcinoma Diseases 0.000 description 1
- 229940080856 gleevec Drugs 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
- 239000003102 growth factor Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000003779 hair growth Effects 0.000 description 1
- 201000010536 head and neck cancer Diseases 0.000 description 1
- 208000014829 head and neck neoplasm Diseases 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 201000002222 hemangioblastoma Diseases 0.000 description 1
- 208000006359 hepatoblastoma Diseases 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 102000057266 human FCGR3A Human genes 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-N hydroperoxyl Chemical compound O[O] OUUQCZGPVNCOIJ-UHFFFAOYSA-N 0.000 description 1
- QJHBJHUKURJDLG-UHFFFAOYSA-N hydroxy-L-lysine Chemical group NCCCCC(NO)C(O)=O QJHBJHUKURJDLG-UHFFFAOYSA-N 0.000 description 1
- 229960003685 imatinib mesylate Drugs 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 201000001371 inclusion conjunctivitis Diseases 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000005305 interferometry Methods 0.000 description 1
- 208000028774 intestinal disease Diseases 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 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
- 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
- 210000003734 kidney Anatomy 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- 201000005264 laryngeal carcinoma Diseases 0.000 description 1
- 201000010260 leiomyoma Diseases 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 201000002250 liver carcinoma Diseases 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 208000002780 macular degeneration Diseases 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 206010027191 meningioma Diseases 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 150000002772 monosaccharides Chemical group 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 206010028537 myelofibrosis Diseases 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
- 201000011216 nasopharynx carcinoma Diseases 0.000 description 1
- 101150091879 neo gene Proteins 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 210000005170 neoplastic cell Anatomy 0.000 description 1
- 230000009826 neoplastic cell growth Effects 0.000 description 1
- 230000010309 neoplastic transformation Effects 0.000 description 1
- 201000003142 neovascular glaucoma Diseases 0.000 description 1
- 208000007538 neurilemmoma Diseases 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 235000020824 obesity Nutrition 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000011164 ossification Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 230000003285 pharmacodynamic effect Effects 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
- 238000003566 phosphorylation assay Methods 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 201000010065 polycystic ovary syndrome Diseases 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- IEMCJUJOHAEFFW-UHFFFAOYSA-M potassium 2-[(2-acetyloxybenzoyl)amino]ethanesulfonate Chemical compound CC(=O)OC1=CC=CC=C1C(=O)NCCS(=O)(=O)[O-].[K+] IEMCJUJOHAEFFW-UHFFFAOYSA-M 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 201000011461 pre-eclampsia Diseases 0.000 description 1
- 201000008312 primary pulmonary hypertension Diseases 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
- 239000012562 protein A resin Substances 0.000 description 1
- 238000000455 protein structure prediction Methods 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 201000010174 renal carcinoma Diseases 0.000 description 1
- 208000037803 restenosis Diseases 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000000979 retarding effect Effects 0.000 description 1
- 201000009410 rhabdomyosarcoma Diseases 0.000 description 1
- 201000000306 sarcoidosis Diseases 0.000 description 1
- 231100000241 scar Toxicity 0.000 description 1
- 230000037387 scars Effects 0.000 description 1
- 206010039667 schwannoma Diseases 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229940074404 sodium succinate Drugs 0.000 description 1
- ZDQYSKICYIVCPN-UHFFFAOYSA-L sodium succinate (anhydrous) Chemical compound [Na+].[Na+].[O-]C(=O)CCC([O-])=O ZDQYSKICYIVCPN-UHFFFAOYSA-L 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 201000000498 stomach carcinoma Diseases 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000011149 sulphuric acid Nutrition 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000008409 synovial inflammation Effects 0.000 description 1
- 201000004595 synovitis Diseases 0.000 description 1
- 238000012876 topography Methods 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 206010044325 trachoma Diseases 0.000 description 1
- 230000017105 transposition Effects 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- 230000005747 tumor angiogenesis Effects 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- 230000005751 tumor progression Effects 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
- 239000004474 valine Substances 0.000 description 1
- 230000006459 vascular development Effects 0.000 description 1
- 201000004916 vulva carcinoma Diseases 0.000 description 1
- 208000013013 vulvar carcinoma Diseases 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 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
-
- 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
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- 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
- C07K16/2866—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 cytokines, lymphokines, interferons
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/54—F(ab')2
-
- 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
- C07K2317/72—Increased effector function due to an Fc-modification
-
- 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
- C07K2317/90—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)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Oncology (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)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US25166809P | 2009-10-14 | 2009-10-14 | |
| PCT/US2010/052725 WO2011053465A1 (en) | 2009-10-14 | 2010-10-14 | Antibodies to epha3 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2743558T3 true ES2743558T3 (es) | 2020-02-19 |
Family
ID=43499991
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES10777137T Active ES2743558T3 (es) | 2009-10-14 | 2010-10-14 | Anticuerpos de-EphA3 |
Country Status (11)
| Country | Link |
|---|---|
| US (2) | US8664365B2 (enExample) |
| EP (1) | EP2488554B1 (enExample) |
| JP (2) | JP2013508292A (enExample) |
| CN (1) | CN102666589B (enExample) |
| AU (1) | AU2010313621C1 (enExample) |
| CA (1) | CA2777068C (enExample) |
| DK (1) | DK2488554T3 (enExample) |
| ES (1) | ES2743558T3 (enExample) |
| PL (1) | PL2488554T3 (enExample) |
| PT (1) | PT2488554T (enExample) |
| WO (1) | WO2011053465A1 (enExample) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2011235867B2 (en) * | 2010-04-01 | 2015-12-03 | Kalobios Pharmaceuticals, Inc. | EphA3 antibodies for the treatment of multiple myeloma |
| JP2013537403A (ja) * | 2010-06-18 | 2013-10-03 | カロバイオス ファーマシューティカルズ インコーポレイティッド | 固形腫瘍の存在のマーカーとしてのＥｐｈＡ３の検出 |
| US9109032B2 (en) | 2011-08-12 | 2015-08-18 | Kalobios Pharmaceuticals, Inc. | Methods of treating hematological proliferative disorders by targeting EphA3 expressed on aberrant vasculature in bone marrow |
| PL3708583T3 (pl) | 2013-08-01 | 2022-06-06 | Five Prime Therapeutics, Inc. | Afukozylowane przeciwciała anty-fgfr2iiib |
| JP7349787B2 (ja) | 2015-11-23 | 2023-09-25 | ファイヴ プライム セラピューティクス インク | 癌治療におけるｆｇｆｒ２阻害剤単独または免疫刺激剤との組み合わせ |
| US20190270821A1 (en) * | 2016-09-13 | 2019-09-05 | Humanigen, Inc. | Epha3 antibodies for the treatment of pulmonary fibrosis |
| JP7299842B2 (ja) | 2017-05-16 | 2023-06-28 | ファイヴ プライム セラピューティクス インク | がん治療における化学療法剤と組み合わせた抗ｆｇｆｒ２抗体 |
| WO2019165982A1 (en) * | 2018-02-28 | 2019-09-06 | WuXi Biologics Ireland Limited | Monoclonal antibody against human lag-3, method for preparing same, and use thereof |
| WO2021068040A1 (en) * | 2019-10-09 | 2021-04-15 | The Council Of The Queensland Institute Of Medical Research | Targeting epha3 and uses thereof |
| TW202134278A (zh) | 2019-11-08 | 2021-09-16 | 美商胡曼尼根公司 | 用於治療腫瘤之ｅｐｈａ３導向ｃａｒ－ｔ細胞 |
| US20240025971A1 (en) * | 2020-10-23 | 2024-01-25 | Atreca, Inc. | Antibodies to coronavirus sars-cov-2 |
| JP7726496B2 (ja) * | 2021-08-06 | 2025-08-20 | コリア リサーチ インスティチュート オブ バイオサイエンス アンド バイオテクノロジー | 新規な抗ＥｐｈＡ２キメラ抗原受容体及びそれを発現する免疫細胞 |
Family Cites Families (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US5677425A (en) | 1987-09-04 | 1997-10-14 | Celltech Therapeutics Limited | Recombinant antibody |
| WO1993000425A1 (en) | 1991-06-21 | 1993-01-07 | Amrad Corporation Limited | A novel receptor-type tyrosine kinase and use thereof |
| US5714350A (en) | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
| AU4116793A (en) | 1992-04-24 | 1993-11-29 | Board Of Regents, The University Of Texas System | Recombinant production of immunoglobulin-like domains in prokaryotic cells |
| NO175798C (no) | 1992-07-22 | 1994-12-07 | Sinvent As | Fremgangsmåte og anordning til aktiv stöydemping i et lokalt område |
| US5885573A (en) | 1993-06-01 | 1999-03-23 | Arch Development Corporation | Methods and materials for modulation of the immunosuppressive activity and toxicity of monoclonal antibodies |
| US6121022A (en) | 1995-04-14 | 2000-09-19 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| PT2180007E (pt) | 1998-04-20 | 2013-11-25 | Roche Glycart Ag | Engenharia de glicosilação de anticorpos para melhorar a citotoxicidade celular dependente de anticorpos |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| HUP0104865A3 (en) | 1999-01-15 | 2004-07-28 | Genentech Inc | Polypeptide variants with altered effector function |
| DK2270147T4 (da) | 1999-04-09 | 2020-08-31 | Kyowa Kirin Co Ltd | Fremgangsmåde til at kontrollere aktiviteten af immunologisk funktionelt molekyle |
| ATE309385T1 (de) | 2000-06-28 | 2005-11-15 | Glycofi Inc | Verfahren für die herstellung modifizierter glykoproteine |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| PT1355919E (pt) | 2000-12-12 | 2011-03-02 | Medimmune Llc | Moléculas com semivida longa, composições que as contêm e suas utilizações |
| US7317091B2 (en) | 2002-03-01 | 2008-01-08 | Xencor, Inc. | Optimized Fc variants |
| WO2003078637A2 (en) | 2002-03-19 | 2003-09-25 | Plant Research International B.V. | Optimizing glycan processing in plants |
| CA2832136C (en) | 2002-09-27 | 2015-11-17 | Xencor | Optimized fc variants and methods for their generation |
| US7981843B2 (en) * | 2004-01-20 | 2011-07-19 | Kalobios Pharmaceuticals, Inc. | Antibody specificity transfer using minimal essential binding determinants |
| CA2577329A1 (en) | 2004-08-16 | 2006-03-02 | Medimmune, Inc. | Eph receptor fc variants with enhanced antibody dependent cell-mediated cytotoxicity activity |
| US8222253B2 (en) * | 2004-10-23 | 2012-07-17 | Case Western Reserve University | Peptide and small molecule agonists of EphA and their uses |
| WO2006055778A2 (en) | 2004-11-16 | 2006-05-26 | Kalobios, Inc. | Immunoglobulin variable region cassette exchange |
| US8211648B2 (en) | 2005-07-22 | 2012-07-03 | Kalobios Pharmaceuticals, Inc. | Secretion of antibodies without signal peptides from bacteria |
| US7846724B2 (en) | 2006-04-11 | 2010-12-07 | Hoffmann-La Roche Inc. | Method for selecting CHO cell for production of glycosylated antibodies |
| WO2008060092A1 (en) | 2006-11-17 | 2008-05-22 | Sang Yun Park | Rotative force generator |
| CA2679986C (en) | 2007-03-08 | 2018-03-06 | Martin Lackmann | Epha3 antibodies for the treatment of solid tumors |
| CL2008002782A1 (es) | 2007-09-21 | 2009-07-31 | Genentech Inc | Anticuerpo anti-bv8 neutralizante; composicion que lo comprende; y su uso para tratar tumores en humanos previamente tratados con un antagonista del factor de crecimiento endotelial vascular. |
| CN102405237A (zh) * | 2009-03-06 | 2012-04-04 | 卡罗拜奥斯制药公司 | 利用EphA3抗体治疗白血病和慢性骨髓增生性疾病 |
-
2010
- 2010-10-14 CN CN201080056618.XA patent/CN102666589B/zh active Active
- 2010-10-14 ES ES10777137T patent/ES2743558T3/es active Active
- 2010-10-14 DK DK10777137.0T patent/DK2488554T3/da active
- 2010-10-14 US US12/904,953 patent/US8664365B2/en active Active
- 2010-10-14 JP JP2012534368A patent/JP2013508292A/ja active Pending
- 2010-10-14 PT PT10777137T patent/PT2488554T/pt unknown
- 2010-10-14 AU AU2010313621A patent/AU2010313621C1/en active Active
- 2010-10-14 CA CA2777068A patent/CA2777068C/en active Active
- 2010-10-14 WO PCT/US2010/052725 patent/WO2011053465A1/en not_active Ceased
- 2010-10-14 EP EP10777137.0A patent/EP2488554B1/en active Active
- 2010-10-14 PL PL10777137T patent/PL2488554T3/pl unknown
-
2013
- 2013-12-30 US US14/143,427 patent/US9290571B2/en active Active
-
2015
- 2015-11-25 JP JP2015229465A patent/JP2016094424A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| CA2777068A1 (en) | 2011-05-05 |
| CA2777068C (en) | 2020-05-26 |
| WO2011053465A1 (en) | 2011-05-05 |
| PT2488554T (pt) | 2019-09-13 |
| PL2488554T3 (pl) | 2020-03-31 |
| JP2013508292A (ja) | 2013-03-07 |
| CN102666589A (zh) | 2012-09-12 |
| AU2010313621A1 (en) | 2012-05-03 |
| US20140120114A1 (en) | 2014-05-01 |
| DK2488554T3 (da) | 2019-09-02 |
| US20110123549A1 (en) | 2011-05-26 |
| AU2010313621C1 (en) | 2015-11-26 |
| AU2010313621B2 (en) | 2015-07-30 |
| EP2488554A1 (en) | 2012-08-22 |
| JP2016094424A (ja) | 2016-05-26 |
| US9290571B2 (en) | 2016-03-22 |
| EP2488554B1 (en) | 2019-07-24 |
| CN102666589B (zh) | 2014-08-20 |
| US8664365B2 (en) | 2014-03-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2743558T3 (es) | Anticuerpos de-EphA3 | |
| CN111683970B (zh) | C-kit结合剂 | |
| ES2860988T3 (es) | Anticuerpos anti-TFR y su uso en el tratamiento de trastornos proliferativos e inflamatorios | |
| ES2942636T3 (es) | Proteínas de unión a IL-11R y usos de las mismas | |
| EP2280732B1 (en) | Antibodies to granulocyte-macrophage colony-stimulating factor | |
| KR20220050971A (ko) | 신규 항-cd39 항체 | |
| CN112062853A (zh) | 双特异性her2抗体及使用方法 | |
| MX2012012790A (es) | Anticuerpos que se unen a factor estimulante de colonias 1 (csf1r). | |
| CA3183389A1 (en) | Bispecific antibody and use thereof | |
| WO2021222861A1 (en) | Antibodies specific to abcb5 and uses thereof | |
| US20190352386A1 (en) | Highly potent monoclonal antibodies to angiogenic factors | |
| TW202227498A (zh) | 新型抗ｃｌａｕｄｉｎ１８抗體 | |
| US11820816B2 (en) | Anti-VEGF antibodies and methods of use | |
| WO2022166846A1 (zh) | 抗tnfr2抗体及其用途 | |
| CN103747801A (zh) | 抗emr1抗体 | |
| WO2022052846A1 (zh) | 抗cd47抗体及其用途 | |
| CN119546630A (zh) | 特异性结合rsv的抗体 | |
| HK40075433A (en) | Anti-mertk antibodies and methods of use thereof | |
| HK1235412A1 (en) | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use | |
| HK40040431B (zh) | 双特异性her2抗体及使用方法 | |
| HK1148222A (en) | Antibodies to granulocyte-macrophage colony-stimulating factor | |
| HK1148222B (en) | Antibodies to granulocyte-macrophage colony-stimulating factor |