JP2011516041A - 抗ｔｙｒｐ１抗体 - Google Patents
抗ｔｙｒｐ１抗体 Download PDFInfo
- Publication number
- JP2011516041A JP2011516041A JP2010550830A JP2010550830A JP2011516041A JP 2011516041 A JP2011516041 A JP 2011516041A JP 2010550830 A JP2010550830 A JP 2010550830A JP 2010550830 A JP2010550830 A JP 2010550830A JP 2011516041 A JP2011516041 A JP 2011516041A
- Authority
- JP
- Japan
- Prior art keywords
- antibody
- seq
- antibodies
- human
- fragment
- 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.)
- Pending
Links
- 201000001441 melanoma Diseases 0.000 claims abstract description 49
- 238000000034 method Methods 0.000 claims abstract description 42
- 239000002246 antineoplastic agent Substances 0.000 claims abstract description 19
- 101000773083 Homo sapiens 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 claims abstract description 18
- 102000046634 human TYRP1 Human genes 0.000 claims abstract description 14
- 208000035250 cutaneous malignant susceptibility to 1 melanoma Diseases 0.000 claims abstract description 10
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 7
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 7
- 239000012634 fragment Substances 0.000 claims description 70
- 206010028980 Neoplasm Diseases 0.000 claims description 40
- 238000011282 treatment Methods 0.000 claims description 29
- FDKXTQMXEQVLRF-ZHACJKMWSA-N (E)-dacarbazine Chemical group CN(C)\N=N\c1[nH]cnc1C(N)=O FDKXTQMXEQVLRF-ZHACJKMWSA-N 0.000 claims description 19
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 19
- 239000013604 expression vector Substances 0.000 claims description 11
- 238000010494 dissociation reaction Methods 0.000 claims description 9
- 150000001413 amino acids Chemical class 0.000 claims description 8
- 201000011510 cancer Diseases 0.000 claims description 8
- 230000005593 dissociations Effects 0.000 claims description 8
- 239000003814 drug Substances 0.000 claims description 6
- 150000007523 nucleic acids Chemical group 0.000 claims description 6
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 claims description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 5
- 238000012258 culturing Methods 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 4
- 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 claims description 2
- 239000008194 pharmaceutical composition Substances 0.000 claims description 2
- 238000002560 therapeutic procedure Methods 0.000 claims description 2
- 238000011284 combination treatment Methods 0.000 claims 1
- 239000003085 diluting agent Substances 0.000 claims 1
- 239000000546 pharmaceutical excipient Substances 0.000 claims 1
- 102100030310 5,6-dihydroxyindole-2-carboxylic acid oxidase Human genes 0.000 abstract description 51
- 239000000427 antigen Substances 0.000 abstract description 22
- 108091007433 antigens Proteins 0.000 abstract description 22
- 102000036639 antigens Human genes 0.000 abstract description 22
- 241000124008 Mammalia Species 0.000 abstract description 13
- 230000000694 effects Effects 0.000 abstract description 11
- 241001529936 Murinae Species 0.000 abstract description 3
- 238000011394 anticancer treatment Methods 0.000 abstract description 3
- 230000009702 cancer cell proliferation Effects 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 81
- 108010014402 tyrosinase-related protein-1 Proteins 0.000 description 48
- 238000009739 binding Methods 0.000 description 32
- 230000027455 binding Effects 0.000 description 31
- 108090000623 proteins and genes Proteins 0.000 description 27
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 23
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 22
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 19
- 241000699670 Mus sp. Species 0.000 description 19
- 101710117290 Aldo-keto reductase family 1 member C4 Proteins 0.000 description 18
- 241001465754 Metazoa Species 0.000 description 17
- 102000004169 proteins and genes Human genes 0.000 description 15
- 241000699666 Mus <mouse, genus> Species 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 14
- 108090000765 processed proteins & peptides Proteins 0.000 description 14
- 201000010099 disease Diseases 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 13
- 108020004414 DNA Proteins 0.000 description 12
- 206010027476 Metastases Diseases 0.000 description 12
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 12
- 238000001727 in vivo Methods 0.000 description 12
- 210000004072 lung Anatomy 0.000 description 12
- 230000002829 reductive effect Effects 0.000 description 12
- 230000000259 anti-tumor effect Effects 0.000 description 11
- 230000005764 inhibitory process Effects 0.000 description 11
- 102000004196 processed proteins & peptides Human genes 0.000 description 11
- 239000013598 vector Substances 0.000 description 11
- 241000588724 Escherichia coli Species 0.000 description 10
- 125000000539 amino acid group Chemical group 0.000 description 10
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 10
- 239000012091 fetal bovine serum Substances 0.000 description 10
- 230000009401 metastasis Effects 0.000 description 10
- 238000007920 subcutaneous administration Methods 0.000 description 10
- 230000001225 therapeutic effect Effects 0.000 description 10
- 208000035475 disorder Diseases 0.000 description 9
- 238000005516 engineering process Methods 0.000 description 9
- 238000000338 in vitro Methods 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 229920001184 polypeptide Polymers 0.000 description 9
- 241000282412 Homo Species 0.000 description 8
- 108060003951 Immunoglobulin Proteins 0.000 description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 8
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 8
- 239000012980 RPMI-1640 medium Substances 0.000 description 8
- 230000003013 cytotoxicity Effects 0.000 description 8
- 231100000135 cytotoxicity Toxicity 0.000 description 8
- 102000018358 immunoglobulin Human genes 0.000 description 8
- 230000001394 metastastic effect Effects 0.000 description 8
- 206010061289 metastatic neoplasm Diseases 0.000 description 8
- 230000004614 tumor growth Effects 0.000 description 8
- 241000699660 Mus musculus Species 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 229960003901 dacarbazine Drugs 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 229940034982 antineoplastic agent Drugs 0.000 description 6
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 6
- 239000012636 effector Substances 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 210000004408 hybridoma Anatomy 0.000 description 6
- 239000012642 immune effector Substances 0.000 description 6
- 229940121354 immunomodulator Drugs 0.000 description 6
- 238000011580 nude mouse model Methods 0.000 description 6
- 230000004044 response Effects 0.000 description 6
- 241000894007 species Species 0.000 description 6
- 206010035226 Plasma cell myeloma Diseases 0.000 description 5
- 230000009089 cytolysis Effects 0.000 description 5
- 210000004602 germ cell Anatomy 0.000 description 5
- 210000002752 melanocyte Anatomy 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 201000000050 myeloid neoplasm Diseases 0.000 description 5
- 238000002823 phage display Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 230000003248 secreting effect Effects 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 4
- 206010027480 Metastatic malignant melanoma Diseases 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 108010082117 matrigel Proteins 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 208000021039 metastatic melanoma Diseases 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000005855 radiation Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 230000002269 spontaneous effect Effects 0.000 description 4
- 230000008685 targeting Effects 0.000 description 4
- 230000003442 weekly effect Effects 0.000 description 4
- 241000283707 Capra Species 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 101150006914 TRP1 gene Proteins 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 230000005907 cancer growth Effects 0.000 description 3
- 210000004748 cultured cell Anatomy 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 238000000684 flow cytometry Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 230000005917 in vivo anti-tumor Effects 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 238000009097 single-agent therapy Methods 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 230000009261 transgenic effect Effects 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 2
- 208000001382 Experimental Melanoma Diseases 0.000 description 2
- 102000009109 Fc receptors Human genes 0.000 description 2
- 108010087819 Fc receptors Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-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
- 101100154912 Mus musculus Tyrp1 gene Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 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
- 241000700605 Viruses Species 0.000 description 2
- 230000009824 affinity maturation Effects 0.000 description 2
- 229940100198 alkylating agent Drugs 0.000 description 2
- 239000002168 alkylating agent Substances 0.000 description 2
- 239000004037 angiogenesis inhibitor Substances 0.000 description 2
- 230000000340 anti-metabolite Effects 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 229940100197 antimetabolite Drugs 0.000 description 2
- 239000002256 antimetabolite Substances 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 238000002648 combination therapy Methods 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000002405 diagnostic procedure Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 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 2
- 210000005260 human cell Anatomy 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 210000002780 melanosome Anatomy 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000001613 neoplastic effect Effects 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 229940012957 plasmin Drugs 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000002708 random mutagenesis Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 SBKVPJHMSUXZTA-MEJXFZFPSA-N 0.000 description 1
- HKZAAJSTFUZYTO-LURJTMIESA-N (2s)-2-[[2-[[2-[[2-[(2-aminoacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoic acid Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(O)=O HKZAAJSTFUZYTO-LURJTMIESA-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
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-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
- STQGQHZAVUOBTE-UHFFFAOYSA-N 7-Cyan-hept-2t-en-4,6-diinsaeure Natural products C1=2C(O)=C3C(=O)C=4C(OC)=CC=CC=4C(=O)C3=C(O)C=2CC(O)(C(C)=O)CC1OC1CC(N)C(O)C(C)O1 STQGQHZAVUOBTE-UHFFFAOYSA-N 0.000 description 1
- 102000013563 Acid Phosphatase Human genes 0.000 description 1
- 108010051457 Acid Phosphatase Proteins 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241001131785 Escherichia coli HB101 Species 0.000 description 1
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 102100025591 Glycerate kinase Human genes 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 101000690301 Homo sapiens Aldo-keto reductase family 1 member C4 Proteins 0.000 description 1
- 101001116548 Homo sapiens Protein CBFA2T1 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 108010038049 Mating Factor Proteins 0.000 description 1
- 206010027145 Melanocytic naevus Diseases 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 206010027458 Metastases to lung Diseases 0.000 description 1
- 101100274524 Mus musculus Clec18a gene Proteins 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 208000007256 Nevus Diseases 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 101150012394 PHO5 gene Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 229930012538 Paclitaxel Natural products 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 206010042553 Superficial spreading melanoma stage unspecified Diseases 0.000 description 1
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 238000012867 alanine scanning Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229940121369 angiogenesis inhibitor Drugs 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 230000000118 anti-neoplastic effect Effects 0.000 description 1
- 230000006023 anti-tumor response Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 229940041181 antineoplastic drug Drugs 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000001045 blue dye Substances 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
- 229960004316 cisplatin Drugs 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 229960000975 daunorubicin Drugs 0.000 description 1
- STQGQHZAVUOBTE-VGBVRHCVSA-N daunorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(C)=O)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 STQGQHZAVUOBTE-VGBVRHCVSA-N 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000035614 depigmentation Effects 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 230000003467 diminishing effect 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
- 208000018459 dissociative disease Diseases 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 238000009093 first-line therapy Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000012239 gene modification Methods 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- -1 glucose or lactose) Chemical class 0.000 description 1
- 102000005396 glutamine synthetase Human genes 0.000 description 1
- 108020002326 glutamine synthetase Proteins 0.000 description 1
- 108010086476 glycerate kinase Proteins 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 239000011544 gradient gel Substances 0.000 description 1
- 230000037308 hair color Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 102000054751 human RUNX1T1 Human genes 0.000 description 1
- 229940098197 human immunoglobulin g Drugs 0.000 description 1
- 230000008348 humoral response Effects 0.000 description 1
- 230000003463 hyperproliferative effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229960004768 irinotecan Drugs 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 238000002843 lactate dehydrogenase assay Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000008099 melanin synthesis Effects 0.000 description 1
- SGDBTWWWUNNDEQ-LBPRGKRZSA-N melphalan Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N(CCCl)CCCl)C=C1 SGDBTWWWUNNDEQ-LBPRGKRZSA-N 0.000 description 1
- 229960001924 melphalan Drugs 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 208000004649 neutrophil actin dysfunction Diseases 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 229960003552 other antineoplastic agent in atc Drugs 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 229960001592 paclitaxel Drugs 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 208000030457 superficial spreading melanoma Diseases 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- RCINICONZNJXQF-MZXODVADSA-N taxol Chemical compound O([C@@H]1[C@@]2(C[C@@H](C(C)=C(C2(C)C)[C@H](C([C@]2(C)[C@@H](O)C[C@H]3OC[C@]3([C@H]21)OC(C)=O)=O)OC(=O)C)OC(=O)[C@H](O)[C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)O)C(=O)C1=CC=CC=C1 RCINICONZNJXQF-MZXODVADSA-N 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229960000303 topotecan Drugs 0.000 description 1
- UCFGDBYHRUNTLO-QHCPKHFHSA-N topotecan Chemical compound C1=C(O)C(CN(C)C)=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 UCFGDBYHRUNTLO-QHCPKHFHSA-N 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 238000012549 training Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 238000007693 zone electrophoresis Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3053—Skin, nerves, brain
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/39558—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against tumor tissues, cells, antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- 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
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—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
- C07K2317/70—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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Biomedical Technology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Neurology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Cell Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Oncology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US6919908P | 2008-03-12 | 2008-03-12 | |
| US61/069,199 | 2008-03-12 | ||
| PCT/US2009/036739 WO2009114585A1 (en) | 2008-03-12 | 2009-03-11 | Anti-tyrp1 antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2011516041A true JP2011516041A (ja) | 2011-05-26 |
| JP2011516041A5 JP2011516041A5 (enExample) | 2014-03-06 |
Family
ID=40790741
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2010550830A Pending JP2011516041A (ja) | 2008-03-12 | 2009-03-11 | 抗ｔｙｒｐ１抗体 |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US7951370B2 (enExample) |
| EP (1) | EP2268672A1 (enExample) |
| JP (1) | JP2011516041A (enExample) |
| KR (1) | KR101203777B1 (enExample) |
| CN (1) | CN101970500B (enExample) |
| AR (1) | AR070821A1 (enExample) |
| AU (1) | AU2009222998B2 (enExample) |
| BR (1) | BRPI0909633A2 (enExample) |
| CA (1) | CA2718289A1 (enExample) |
| CL (1) | CL2009000567A1 (enExample) |
| EA (1) | EA019517B1 (enExample) |
| IL (1) | IL207581A0 (enExample) |
| MX (1) | MX2010010021A (enExample) |
| NZ (1) | NZ587305A (enExample) |
| PE (1) | PE20091679A1 (enExample) |
| TW (1) | TWI384997B (enExample) |
| UA (1) | UA99339C2 (enExample) |
| WO (1) | WO2009114585A1 (enExample) |
| ZA (1) | ZA201006099B (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2022546590A (ja) * | 2019-09-06 | 2022-11-04 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | がんの処置のためのキメラ抗原受容体ならびに関連した方法および組成物 |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2167540B1 (en) * | 2007-06-29 | 2018-02-14 | F. Hoffmann-La Roche AG | Heavy chain mutant leading to improved immunoglobulin production |
| MX2016010177A (es) | 2014-02-07 | 2017-01-09 | Dong Wha Pharm Co Ltd | Composicion adyuvante anticancerosa que contiene promotor de la expresion de rip3 como principio activo, metodo para la deteccion de adyuvante anticanceroso que potencia la sensibilidad al farmaco anticanceroso mediante la estimulacion de la expresion de rip3 y metodo para controlar la sensibilidad del farmaco anticanceroso. |
| DK3233907T3 (da) | 2014-12-19 | 2021-06-07 | Genmab As | Bispecifikke heterodimeriske proteiner hos gnavere |
| RU2630647C1 (ru) * | 2016-05-27 | 2017-09-11 | Федеральное государственное унитарное предприятие "Государственный научно-исследовательский институт особо чистых биопрепаратов" Федерального медико-биологического агентства | ГУМАНИЗИРОВАННОЕ АНТИТЕЛО К КОНФОРМАЦИОННОМУ ЭПИТОПУ С3 КОМПОНЕНТА КОМПЛЕМЕНТА ЧЕЛОВЕКА, ПОСЛЕДОВАТЕЛЬНОСТЬ ДНК (ВАРИАНТЫ), ЭКСПРЕССИОННЫЙ ВЕКТОР, СОДЕРЖАЩИЙ ПОСЛЕДОВАТЕЛЬНОСТЬ ДНК (ВАРИАНТЫ), И ШТАММ КЛЕТОК ЯИЧНИКОВ КИТАЙСКОГО ХОМЯЧКА CHO-humC34-ПРОДУЦЕНТ ДАННОГО ГУМАНИЗИРОВАННОГО АНТИТЕЛА |
| GB201613167D0 (en) | 2016-07-29 | 2016-09-14 | Univ Southampton | Cancer and b-cell related disease therapy |
| WO2018075586A1 (en) * | 2016-10-18 | 2018-04-26 | Memorial Sloan-Kettering Cancer Center | Antigen-binding proteins targeting melanoma differentiation antigens and uses thereof |
| MX2019015053A (es) * | 2017-06-14 | 2020-02-13 | Adicet Bio Inc | Anticuerpos capaces de unirse a hla-a2/tyrd de forma restringida por hla y usos de estos. |
| RU2687609C1 (ru) * | 2018-05-30 | 2019-05-15 | Федеральное государственное унитарное предприятие "Государственный научно-исследовательский институт особо чистых биопрепаратов" Федерального медико-биологического агентства | Гуманизированное антитело к конформационному эпитопу сз компонента комплемента человека |
| EP3856775B9 (en) | 2018-09-27 | 2025-01-22 | Autolus Limited | Chimeric antigen receptor |
| EP3876988A4 (en) * | 2018-11-09 | 2022-11-09 | Beth Israel Deaconess Medical Center | THERAPIES TARGETED AGAINST CDCP1 |
| TWI881476B (zh) * | 2018-12-21 | 2025-04-21 | 瑞士商赫孚孟拉羅股份公司 | 結合cd3之抗體 |
| WO2023094569A1 (en) * | 2021-11-26 | 2023-06-01 | F. Hoffmann-La Roche Ag | Combination therapy of anti-tyrp1/anti-cd3 bispecific antibodies and tyrp1-specific antibodies |
| WO2025104289A1 (en) | 2023-11-17 | 2025-05-22 | Medincell S.A. | Antineoplastic combinations |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2004508014A (ja) * | 2000-05-16 | 2004-03-18 | ボルダー バイオテクノロジー， インコーポレイテッド | 遊離システイン残基を含有するタンパク質をリフォールディングする方法 |
| WO2006047340A2 (en) * | 2004-10-22 | 2006-05-04 | Amgen Inc. | Methods for refolding of recombinant antibodies |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4798790A (en) | 1985-07-18 | 1989-01-17 | Sloan-Kettering Institute | Monoclonal antibody specific for a pigmentation associated antigen |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| DE3853515T3 (de) | 1987-05-21 | 2005-08-25 | Micromet Ag | Multifunktionelle proteine mit vorbestimmter zielsetzung. |
| IL89489A0 (en) | 1988-03-09 | 1989-09-10 | Hybritech Inc | Chimeric antibodies directed against human carcinoembryonic antigen |
| EP0362371A4 (en) | 1988-04-15 | 1990-10-24 | Protein Design Labs, Inc. | Il-2 receptor-specific chimeric antibodies |
| ATE119198T1 (de) | 1988-04-16 | 1995-03-15 | Celltech Ltd | Verfahren zur herstellung von proteinen mittels rekombinanter dna. |
| IE910820A1 (en) | 1990-03-22 | 1991-09-25 | Sloan Kettering Inst Cancer | Gp75 as a tumor vaccine for melanoma |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| WO1993021319A1 (en) | 1992-04-08 | 1993-10-28 | Cetus Oncology Corporation | HUMANIZED C-erbB-2 SPECIFIC ANTIBODIES |
| AU6171196A (en) * | 1995-06-07 | 1996-12-30 | Sloan-Kettering Institute For Cancer Research | Therapeutic uses of ta99 |
| US5840839A (en) | 1996-02-09 | 1998-11-24 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Alternative open reading frame DNA of a normal gene and a novel human cancer antigen encoded therein |
| BR9815289A (pt) * | 1997-11-14 | 2001-12-26 | Euro Celtique Sa | Imunoglobulina modificada, molécula, ácidonucleico isolado, célula contendo o mesmo, animalnão-humano recombinante, composiçãofarmacêutica, composição de vacina, processospara identificar ou medir ou detectar um antìgenode câncer, um antìgeno de um agente de doençainfecciosa, um ligante, e um receptor em umaamostra a ser testada, kits para detecção de umantìgeno de câncer, de um antìgeno de um agentede doença infecciosa, de um receptor celular paraum agente de doença infecciosa, de um ligante, e deum antìgeno de câncer, processos de diagnósticoou de exame para a presença de ou umapredisposição para desenvolvimento de um câncertipificado pela presença aumentada de umantìgeno de câncer, e para a presença de umagente de doença infecciosa, processos detratamento ou de prevenção de um câncertipificado pela presença de um antìgeno de câncer,de uma doença infecciosa tipificada pela presençade um antìgeno de agente de doença infecciosa, ede uma doença causada por um agente de doençainfecciosa que se liga em um receptor celular,processos para modulação de atividade de umprimeiro membro de um par de ligação, processo deprodução de uma imunoglobulina modificada,processo de produção de um ácido nucleicocodificador de imunoglobulina modificada, e, ácidonucleico isolado |
-
2009
- 2009-03-11 NZ NZ587305A patent/NZ587305A/en not_active IP Right Cessation
- 2009-03-11 KR KR1020107020296A patent/KR101203777B1/ko not_active Expired - Fee Related
- 2009-03-11 PE PE2009000356A patent/PE20091679A1/es not_active Application Discontinuation
- 2009-03-11 MX MX2010010021A patent/MX2010010021A/es active IP Right Grant
- 2009-03-11 CL CL2009000567A patent/CL2009000567A1/es unknown
- 2009-03-11 JP JP2010550830A patent/JP2011516041A/ja active Pending
- 2009-03-11 BR BRPI0909633A patent/BRPI0909633A2/pt not_active IP Right Cessation
- 2009-03-11 WO PCT/US2009/036739 patent/WO2009114585A1/en not_active Ceased
- 2009-03-11 CN CN2009801085150A patent/CN101970500B/zh not_active Expired - Fee Related
- 2009-03-11 UA UAA201010912A patent/UA99339C2/ru unknown
- 2009-03-11 AU AU2009222998A patent/AU2009222998B2/en not_active Ceased
- 2009-03-11 CA CA2718289A patent/CA2718289A1/en not_active Abandoned
- 2009-03-11 TW TW098107909A patent/TWI384997B/zh not_active IP Right Cessation
- 2009-03-11 US US12/401,800 patent/US7951370B2/en not_active Expired - Fee Related
- 2009-03-11 AR ARP090100858A patent/AR070821A1/es not_active Application Discontinuation
- 2009-03-11 EA EA201071068A patent/EA019517B1/ru not_active IP Right Cessation
- 2009-03-11 EP EP09719438A patent/EP2268672A1/en not_active Withdrawn
-
2010
- 2010-08-12 IL IL207581A patent/IL207581A0/en unknown
- 2010-08-26 ZA ZA2010/06099A patent/ZA201006099B/en unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2004508014A (ja) * | 2000-05-16 | 2004-03-18 | ボルダー バイオテクノロジー， インコーポレイテッド | 遊離システイン残基を含有するタンパク質をリフォールディングする方法 |
| WO2006047340A2 (en) * | 2004-10-22 | 2006-05-04 | Amgen Inc. | Methods for refolding of recombinant antibodies |
Non-Patent Citations (3)
| Title |
|---|
| JPN5011011952; ＰＡＴＥＬ ＤＩＰＡ: 'ＧＥＮＥＲＡＴＩＯＮ ＡＮＤ ＣＨＡＲＡＣＴＥＲＩＺＡＴＩＯＮ ＯＦ Ａ ＴＨＥＲＡＰＥＵＴＩＣ ＨＵＭＡＮ ＡＮＴＩＢＯＤＹ ＴＯ ＭＥＬＡＮＯＭＡ ＡＮＴＩＧＥＮ ＴＹＲＰ１' ＨＵＭＡＮ ＡＮＴＩＢＯＤＩＥＳ Ｖ１６ Ｎ３-４, 20070101, Ｐ１２７-１３６ * |
| JPN6013051596; Ｒｏｂｅｒｔ Ｇ． Ｈａｍｉｌｔｏｎ: Ｔｈｅ Ｈｕｍａｎ ＩｇＧ Ｓｕｂｃｌａｓｓｅｓ , 2001, Ｃａｌｂｉｏｃｈｅｍ-Ｎｏｖａｂｉｏｃｈｅｍ Ｃｏｒｐｏｒａｔｉｏｎ * |
| JPN6013051598; ＢＹ ＧＥＲＡＬＤ Ｍ． ＥＤＥＬＭＡＮ， ＢＲＵＣＥ Ａ． ＣＵＮＮＩＮＧＨＡＭ， Ｗ． ＥＩＮＡＲ ＧＡＬＬ，ＰＡＵＬ Ｄ． ＧＯＴＴＬＩＥＢ， ＵＲＳ ＲＵＴＩＳＨＡＵＳＥＲ， ＡＮＤ ＭＹＲＯ: 'ＴＨＥ ＣＯＶＡＬＥＮＴ ＳＴＲＵＣＴＵＲＥ ＯＦ ＡＮ ＥＮＴＩＲＥ ＴＧ ＩＭＭＵＮＯＧＬＯＢＵＬＩＮ ＭＯＬＥＣＵＬＥ' Ｐｒｏｃｅｅｄｉｎｇｓ ｏｆ ｔｈｅ Ｎａｔｉｏｎａｌ Ａｃａｄｅｍｙ ｏｆ Ｓｃｉｅｎｃｅｓ ｏｆ ｔｈｅ Ｕｎｉｔｅｄ Ｓｔａｔｅｓ ｏｆ Ａｍｅｒｉｃａ Ｖｏｌ． ６３，　 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2022546590A (ja) * | 2019-09-06 | 2022-11-04 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | がんの処置のためのキメラ抗原受容体ならびに関連した方法および組成物 |
Also Published As
| Publication number | Publication date |
|---|---|
| CL2009000567A1 (es) | 2010-02-26 |
| KR20100113631A (ko) | 2010-10-21 |
| UA99339C2 (ru) | 2012-08-10 |
| CN101970500A (zh) | 2011-02-09 |
| TWI384997B (zh) | 2013-02-11 |
| AU2009222998B2 (en) | 2013-05-23 |
| KR101203777B1 (ko) | 2012-11-21 |
| AR070821A1 (es) | 2010-05-05 |
| NZ587305A (en) | 2012-05-25 |
| EA019517B1 (ru) | 2014-04-30 |
| EP2268672A1 (en) | 2011-01-05 |
| AU2009222998A1 (en) | 2009-09-17 |
| IL207581A0 (en) | 2010-12-30 |
| MX2010010021A (es) | 2011-02-15 |
| US7951370B2 (en) | 2011-05-31 |
| CN101970500B (zh) | 2013-08-14 |
| US20090232823A1 (en) | 2009-09-17 |
| CA2718289A1 (en) | 2009-09-17 |
| EA201071068A1 (ru) | 2011-04-29 |
| BRPI0909633A2 (pt) | 2015-09-22 |
| PE20091679A1 (es) | 2009-11-04 |
| WO2009114585A1 (en) | 2009-09-17 |
| TW200944232A (en) | 2009-11-01 |
| ZA201006099B (en) | 2012-01-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR101203777B1 (ko) | 항-ｔｙｒｐ１ 항체 | |
| EP3683239B1 (en) | Antibodies binding human claudin 18.2 and uses thereof | |
| TWI402078B (zh) | 抗ｃｓｆ－１ｒ抗體 | |
| US8071099B2 (en) | Anti-FLT3 antibodies | |
| AU2007324509B2 (en) | Novel antiproliferation antibodies | |
| JP2011516041A5 (enExample) | ||
| JP2018526974A (ja) | Ｐｄｌ−１抗体、その医薬組成物及びその使用 | |
| KR20240162588A (ko) | Cd3 및 bcma에 대한 항체, 및 이로부터 제조된 이중특이적 결합 단백질 | |
| CN114907479B (zh) | 抗cd112r抗体及其用途 | |
| JP7505148B2 (ja) | Ｌａｇ３に結合する抗体およびその使用 | |
| JP2025157317A (ja) | Ｉｌ４ｒに結合する抗体とその使用 | |
| JP2022502417A (ja) | 抗ｏｘ４０抗体、その抗原結合フラグメント、および医薬用途 | |
| HK40090114A (en) | Antibodies binding human claudin 18.2 and uses thereof | |
| HK40029982B (en) | Antibodies binding human claudin 18.2 and uses thereof | |
| HK40089230A (zh) | 药物组合物及用途 | |
| HK40040207A (en) | Antibody binding tim-3 and use thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20120125 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20120125 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20131022 |
|
| A524 | Written submission of copy of amendment under article 19 pct |
Free format text: JAPANESE INTERMEDIATE CODE: A524 Effective date: 20140115 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20140120 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20140812 |