NO314595B1 - Fremgangsmåte for fremstilling av et kim¶rt terapeutisk aktivt humanisert antistoff eller et terapeutisk aktivt fragment derav, DNA-sekvenssom koder for antistoffet, samt plasmid og stabil vertscellelinje som omfatterDNA-sekvensen - Google Patents
Fremgangsmåte for fremstilling av et kim¶rt terapeutisk aktivt humanisert antistoff eller et terapeutisk aktivt fragment derav, DNA-sekvenssom koder for antistoffet, samt plasmid og stabil vertscellelinje som omfatterDNA-sekvensen Download PDFInfo
- Publication number
- NO314595B1 NO314595B1 NO19930825A NO930825A NO314595B1 NO 314595 B1 NO314595 B1 NO 314595B1 NO 19930825 A NO19930825 A NO 19930825A NO 930825 A NO930825 A NO 930825A NO 314595 B1 NO314595 B1 NO 314595B1
- Authority
- NO
- Norway
- Prior art keywords
- antibody
- dna sequence
- genetic engineering
- fragment
- human
- Prior art date
Links
- 239000012634 fragment Substances 0.000 title claims description 67
- 238000000034 method Methods 0.000 title claims description 38
- 108091028043 Nucleic acid sequence Proteins 0.000 title claims description 34
- 239000013612 plasmid Substances 0.000 title claims description 30
- 102000007298 Mucin-1 Human genes 0.000 claims abstract description 14
- 108010008707 Mucin-1 Proteins 0.000 claims abstract description 14
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims abstract description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims abstract description 6
- 241001529936 Murinae Species 0.000 claims abstract 2
- 108090000623 proteins and genes Proteins 0.000 claims description 49
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 claims description 21
- 238000004519 manufacturing process Methods 0.000 claims description 19
- 150000001413 amino acids Chemical group 0.000 claims description 16
- 238000010353 genetic engineering Methods 0.000 claims description 15
- 241000588724 Escherichia coli Species 0.000 claims description 14
- 101001034314 Homo sapiens Lactadherin Proteins 0.000 claims description 11
- 102100039648 Lactadherin Human genes 0.000 claims description 11
- 239000011324 bead Substances 0.000 claims description 9
- 239000002773 nucleotide Substances 0.000 claims description 7
- 125000003729 nucleotide group Chemical group 0.000 claims description 7
- 102000004169 proteins and genes Human genes 0.000 claims description 7
- 108020004414 DNA Proteins 0.000 claims description 3
- 235000020256 human milk Nutrition 0.000 claims description 3
- 230000001131 transforming effect Effects 0.000 claims description 3
- DEAGTWNKODHUIY-MRFFXTKBSA-N Ala-Tyr-Trp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O DEAGTWNKODHUIY-MRFFXTKBSA-N 0.000 claims description 2
- BWMMKQPATDUYKB-IHRRRGAJSA-N Arg-Tyr-Asn Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(O)=O)CC1=CC=C(O)C=C1 BWMMKQPATDUYKB-IHRRRGAJSA-N 0.000 claims description 2
- KXFCBAHYSLJCCY-ZLUOBGJFSA-N Asn-Asn-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O KXFCBAHYSLJCCY-ZLUOBGJFSA-N 0.000 claims description 2
- QXDXIXFSFHUYAX-MNXVOIDGSA-N Glu-Ile-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](N)CCC(O)=O QXDXIXFSFHUYAX-MNXVOIDGSA-N 0.000 claims description 2
- MFNUFCFRAZPJFW-JYJNAYRXSA-N Glu-Lys-Phe Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 MFNUFCFRAZPJFW-JYJNAYRXSA-N 0.000 claims description 2
- XREQQOATSMMAJP-MGHWNKPDSA-N Lys-Ile-Tyr Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O XREQQOATSMMAJP-MGHWNKPDSA-N 0.000 claims description 2
- DIBZLYZXTSVGLN-CIUDSAMLSA-N Lys-Ser-Ser Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O DIBZLYZXTSVGLN-CIUDSAMLSA-N 0.000 claims description 2
- NEHSHYOUIWBYSA-DCPHZVHLSA-N Phe-Ala-Trp Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)O)NC(=O)[C@H](CC3=CC=CC=C3)N NEHSHYOUIWBYSA-DCPHZVHLSA-N 0.000 claims description 2
- NOFBJKKOPKJDCO-KKXDTOCCSA-N Phe-Ala-Tyr Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O NOFBJKKOPKJDCO-KKXDTOCCSA-N 0.000 claims description 2
- DXTOOBDIIAJZBJ-BQBZGAKWSA-N Pro-Gly-Ser Chemical compound [H]N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CO)C(O)=O DXTOOBDIIAJZBJ-BQBZGAKWSA-N 0.000 claims description 2
- VMLONWHIORGALA-SRVKXCTJSA-N Ser-Leu-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]([NH3+])CO VMLONWHIORGALA-SRVKXCTJSA-N 0.000 claims description 2
- GSCVDSBEYVGMJQ-SRVKXCTJSA-N Ser-Tyr-Asp Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)NC(=O)[C@H](CO)N)O GSCVDSBEYVGMJQ-SRVKXCTJSA-N 0.000 claims description 2
- UKBSDLHIKIXJKH-HJGDQZAQSA-N Thr-Arg-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O UKBSDLHIKIXJKH-HJGDQZAQSA-N 0.000 claims description 2
- AVYVKJMBNLPWRX-WFBYXXMGSA-N Trp-Ala-Ser Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O)=CNC2=C1 AVYVKJMBNLPWRX-WFBYXXMGSA-N 0.000 claims description 2
- AUZADXNWQMBZOO-JYJNAYRXSA-N Tyr-Pro-Arg Chemical compound C([C@H](N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=C(O)C=C1 AUZADXNWQMBZOO-JYJNAYRXSA-N 0.000 claims description 2
- UMSZZGTXGKHTFJ-SRVKXCTJSA-N Tyr-Ser-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 UMSZZGTXGKHTFJ-SRVKXCTJSA-N 0.000 claims description 2
- GPLTZEMVOCZVAV-UFYCRDLUSA-N Tyr-Tyr-Arg Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=C(O)C=C1 GPLTZEMVOCZVAV-UFYCRDLUSA-N 0.000 claims description 2
- 108010069205 aspartyl-phenylalanine Proteins 0.000 claims description 2
- 210000004251 human milk Anatomy 0.000 claims description 2
- 108010057821 leucylproline Proteins 0.000 claims description 2
- 108010071635 tyrosyl-prolyl-arginine Proteins 0.000 claims description 2
- AUEJLPRZGVVDNU-UHFFFAOYSA-N N-L-tyrosyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CC1=CC=C(O)C=C1 AUEJLPRZGVVDNU-UHFFFAOYSA-N 0.000 claims 1
- 108010057952 lysyl-phenylalanyl-lysine Proteins 0.000 claims 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 abstract description 34
- 206010028980 Neoplasm Diseases 0.000 abstract description 12
- 201000011510 cancer Diseases 0.000 abstract description 10
- 238000003745 diagnosis Methods 0.000 abstract description 3
- 210000004408 hybridoma Anatomy 0.000 abstract description 3
- 210000004027 cell Anatomy 0.000 description 23
- 241000699666 Mus <mouse, genus> Species 0.000 description 18
- 108091034117 Oligonucleotide Proteins 0.000 description 16
- 239000013604 expression vector Substances 0.000 description 16
- 239000002299 complementary DNA Substances 0.000 description 15
- 230000027455 binding Effects 0.000 description 14
- 239000013598 vector Substances 0.000 description 14
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 13
- 239000003153 chemical reaction reagent Substances 0.000 description 12
- 239000003623 enhancer Substances 0.000 description 10
- 238000010367 cloning Methods 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 7
- 108090000765 processed proteins & peptides Proteins 0.000 description 7
- 230000009870 specific binding Effects 0.000 description 7
- 239000000872 buffer Substances 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 239000000427 antigen Substances 0.000 description 5
- 108091007433 antigens Proteins 0.000 description 5
- 102000036639 antigens Human genes 0.000 description 5
- 238000003384 imaging method Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 102000015728 Mucins Human genes 0.000 description 4
- 108010063954 Mucins Proteins 0.000 description 4
- 206010035226 Plasma cell myeloma Diseases 0.000 description 4
- 241000283984 Rodentia Species 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 201000000050 myeloid neoplasm Diseases 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 241000282412 Homo Species 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 3
- 230000005907 cancer growth Effects 0.000 description 3
- 239000002738 chelating agent Substances 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 206010006187 Breast cancer Diseases 0.000 description 2
- 208000026310 Breast neoplasm Diseases 0.000 description 2
- 108091035707 Consensus sequence Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 108091036078 conserved sequence Proteins 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000012869 ethanol precipitation Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000003993 interaction Effects 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
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 238000010998 test method Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 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
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 108700004676 Bence Jones Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101100148606 Caenorhabditis elegans pst-1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 229910052688 Gadolinium Inorganic materials 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- KTGFOCFYOZQVRJ-ZKWXMUAHSA-N Ile-Glu Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O KTGFOCFYOZQVRJ-ZKWXMUAHSA-N 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 206010033128 Ovarian cancer Diseases 0.000 description 1
- 206010061535 Ovarian neoplasm Diseases 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- GKLVYJBZJHMRIY-OUBTZVSYSA-N Technetium-99 Chemical compound [99Tc] GKLVYJBZJHMRIY-OUBTZVSYSA-N 0.000 description 1
- VWQVUPCCIRVNHF-OUBTZVSYSA-N Yttrium-90 Chemical compound [90Y] VWQVUPCCIRVNHF-OUBTZVSYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000006838 adverse reaction Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 229910052788 barium Inorganic materials 0.000 description 1
- DSAJWYNOEDNPEQ-UHFFFAOYSA-N barium atom Chemical compound [Ba] DSAJWYNOEDNPEQ-UHFFFAOYSA-N 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- KPLQYGBQNPPQGA-UHFFFAOYSA-N cobalt samarium Chemical compound [Co].[Sm] KPLQYGBQNPPQGA-UHFFFAOYSA-N 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000002872 contrast media Substances 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- RYGMFSIKBFXOCR-IGMARMGPSA-N copper-64 Chemical compound [64Cu] RYGMFSIKBFXOCR-IGMARMGPSA-N 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 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
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- KAKKHKRHCKCAGH-UHFFFAOYSA-L disodium;(4-nitrophenyl) phosphate;hexahydrate Chemical compound O.O.O.O.O.O.[Na+].[Na+].[O-][N+](=O)C1=CC=C(OP([O-])([O-])=O)C=C1 KAKKHKRHCKCAGH-UHFFFAOYSA-L 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- UIWYJDYFSGRHKR-UHFFFAOYSA-N gadolinium atom Chemical compound [Gd] UIWYJDYFSGRHKR-UHFFFAOYSA-N 0.000 description 1
- 238000003197 gene knockdown Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 101150106093 gpt gene Proteins 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- APFVFJFRJDLVQX-AHCXROLUSA-N indium-111 Chemical compound [111In] APFVFJFRJDLVQX-AHCXROLUSA-N 0.000 description 1
- 229940055742 indium-111 Drugs 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 235000021243 milk fat Nutrition 0.000 description 1
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000013492 plasmid preparation Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 229910000938 samarium–cobalt magnet Inorganic materials 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 125000002088 tosyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1C([H])([H])[H])S(*)(=O)=O 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
- C07K16/464—Igs containing CDR-residues from one specie grafted between FR-residues from another
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (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)
- Saccharide Compounds (AREA)
- Transition And Organic Metals Composition Catalysts For Addition Polymerization (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Pretreatment Of Seeds And Plants (AREA)
- Nonmetallic Welding Materials (AREA)
- Nitrogen Condensed Heterocyclic Rings (AREA)
- Heterocyclic Carbon Compounds Containing A Hetero Ring Having Oxygen Or Sulfur (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Low-Molecular Organic Synthesis Reactions Using Catalysts (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB909019553A GB9019553D0 (en) | 1990-09-07 | 1990-09-07 | Specific binding agents |
PCT/GB1991/001511 WO1992004380A1 (en) | 1990-09-07 | 1991-09-05 | Specific binding agents |
Publications (3)
Publication Number | Publication Date |
---|---|
NO930825D0 NO930825D0 (no) | 1993-03-05 |
NO930825L NO930825L (no) | 1993-05-05 |
NO314595B1 true NO314595B1 (no) | 2003-04-14 |
Family
ID=10681827
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19930825A NO314595B1 (no) | 1990-09-07 | 1993-03-05 | Fremgangsmåte for fremstilling av et kim¶rt terapeutisk aktivt humanisert antistoff eller et terapeutisk aktivt fragment derav, DNA-sekvenssom koder for antistoffet, samt plasmid og stabil vertscellelinje som omfatterDNA-sekvensen |
NO20014822A NO315239B1 (no) | 1990-09-07 | 2001-10-04 | Kim¶rt humanisert antistoff eller fragment derav, samt anvendelse av samme |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20014822A NO315239B1 (no) | 1990-09-07 | 2001-10-04 | Kim¶rt humanisert antistoff eller fragment derav, samt anvendelse av samme |
Country Status (18)
Country | Link |
---|---|
US (2) | US6204366B1 (bg) |
EP (1) | EP0483961B1 (bg) |
JP (2) | JP3514456B2 (bg) |
KR (1) | KR930702526A (bg) |
AT (1) | ATE233279T1 (bg) |
AU (1) | AU653167B2 (bg) |
BG (1) | BG60716B1 (bg) |
CA (1) | CA2090961C (bg) |
DE (1) | DE69133200T2 (bg) |
DK (1) | DK0483961T3 (bg) |
ES (1) | ES2193129T3 (bg) |
FI (2) | FI113873B (bg) |
GB (1) | GB9019553D0 (bg) |
HU (2) | HUT67796A (bg) |
NO (2) | NO314595B1 (bg) |
RO (1) | RO113432B1 (bg) |
UA (1) | UA46691C2 (bg) |
WO (1) | WO1992004380A1 (bg) |
Families Citing this family (27)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6800738B1 (en) | 1991-06-14 | 2004-10-05 | Genentech, Inc. | Method for making humanized antibodies |
WO1994004679A1 (en) * | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
WO1992022653A1 (en) * | 1991-06-14 | 1992-12-23 | Genentech, Inc. | Method for making humanized antibodies |
US5869619A (en) * | 1991-12-13 | 1999-02-09 | Xoma Corporation | Modified antibody variable domains |
CA2103887C (en) * | 1991-12-13 | 2005-08-30 | Gary M. Studnicka | Methods and materials for preparation of modified antibody variable domains and therapeutic uses thereof |
WO1994011508A2 (en) * | 1992-11-13 | 1994-05-26 | Cancer Research Fund Of Contra Costa | Polypeptides with specificity for neoplasias, kit, and diagnostic, vaccination, and therapeutic methods |
US5792852A (en) * | 1992-11-16 | 1998-08-11 | Cancer Research Fund Of Contra Costa | Polynucleotides encoding modified antibodies with human milk fat globule specificity |
DE69332930T2 (de) * | 1992-11-16 | 2004-02-26 | Cancer Research Fund Of Contra Costa, Walnut Creek | Peptide mit breiter neoplastischer spezifizität |
US6281335B1 (en) * | 1993-10-08 | 2001-08-28 | Coulter Corporation | Hybridoma and anti-KC-4 humanized monoclonal antibody |
US5804187A (en) * | 1992-11-16 | 1998-09-08 | Cancer Research Fund Of Contra Costa | Modified antibodies with human milk fat globule specificity |
JPH07203974A (ja) * | 1994-01-13 | 1995-08-08 | Tosoh Corp | 癌特異的ムチンを認識する抗体の遺伝子断片等 |
EP0781847A1 (en) * | 1995-11-06 | 1997-07-02 | MERCK PATENT GmbH | Humanized monoclonal antibody |
EP1032420A4 (en) * | 1997-11-14 | 2004-09-15 | Euro Celtique Sa | IMMUNOGLOBULIN MOLECULES WITH SYNTHETIC VARIABLE REGION AND MODIFIED SPECIFICITY |
GB2360771A (en) * | 2000-03-28 | 2001-10-03 | Antisoma Res Ltd | Compounds for targeting |
AU4430701A (en) * | 2000-04-03 | 2001-10-15 | Antisoma Research Limited | Compounds for targeting |
AU2002307064A1 (en) * | 2001-04-02 | 2002-10-15 | Purdue Pharma L.P. | Immunoglobulin construct containing anti-mucin variable domain sequences for eliciting an anti-idiotype anti-tumor response |
GB0200657D0 (en) * | 2002-01-12 | 2002-02-27 | Antisoma Plc | Cancer treatment |
CA2488441C (en) * | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
WO2004007687A2 (en) * | 2002-07-16 | 2004-01-22 | Stuart Bussell | Methods to construct multimeric dna and polymeric protein sequences as direct fusions or with linkers |
CA2534055A1 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Antibody cdr polypeptide sequences with restricted diversity |
GB0519398D0 (en) * | 2005-09-23 | 2005-11-02 | Antisoma Plc | Biological materials and uses thereof |
EP1957531B1 (en) | 2005-11-07 | 2016-04-13 | Genentech, Inc. | Binding polypeptides with diversified and consensus vh/vl hypervariable sequences |
US20070237764A1 (en) * | 2005-12-02 | 2007-10-11 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
CN103261223B (zh) | 2010-10-13 | 2017-03-29 | 詹森生物科技公司 | 人制瘤素m抗体及使用方法 |
US20140079722A1 (en) * | 2011-03-09 | 2014-03-20 | Centrose, Llc | Extracellular targeted drug conjugates |
RU2493165C1 (ru) * | 2012-02-28 | 2013-09-20 | Общество с ограниченной ответственностью "Технофарма" | Наноантитело, специфически связывающее белок muc1, способ детекции белка muc1 с помощью наноантител |
EP2844262B1 (en) | 2012-04-30 | 2018-01-10 | Biothera, Inc. | Beta-glucan immunotherapeutic preparation |
Family Cites Families (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB8607679D0 (en) * | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
CA1339204C (en) * | 1987-01-07 | 1997-08-05 | Joyce Taylor-Papadimitriou | Mucin core polypeptide, antibodies and probes |
DE3856559T2 (de) * | 1987-05-21 | 2004-04-29 | Micromet Ag | Multifunktionelle Proteine mit vorbestimmter Zielsetzung |
JPH03503120A (ja) * | 1988-02-08 | 1991-07-18 | ジョン ミュア キャンサー アンド エージング インスティチュート ディビジョン オブ ジョン ミュア メモリアル ホスピタル | ヒトのガン細胞における新規なムチン様糖蛋白質表面抗原に特異的なモノクローナル抗体 |
EP0442926A1 (en) * | 1988-11-10 | 1991-08-28 | Imperial Cancer Research Technology Limited | Polypeptides |
JPH02273195A (ja) | 1988-11-17 | 1990-11-07 | Univ Melbourne | ヒト多型性上皮ムチンと反応するモノクローナル抗体 |
US5075219A (en) * | 1989-04-05 | 1991-12-24 | John Muir Cancer & Aging Institute | Monoclonal antibody which recognizes a specific glycoprotein of a human milk-fat globule membrane mucin antigen and said mucin antigen |
HUT64600A (en) * | 1989-11-17 | 1994-01-28 | Unilever Nv | Method for producing specific binding materials |
-
1990
- 1990-09-07 GB GB909019553A patent/GB9019553D0/en active Pending
-
1991
- 1991-09-05 UA UA93080844A patent/UA46691C2/uk unknown
- 1991-09-05 US US07/987,264 patent/US6204366B1/en not_active Expired - Lifetime
- 1991-09-05 AT AT91308147T patent/ATE233279T1/de not_active IP Right Cessation
- 1991-09-05 DE DE69133200T patent/DE69133200T2/de not_active Expired - Lifetime
- 1991-09-05 WO PCT/GB1991/001511 patent/WO1992004380A1/en active IP Right Grant
- 1991-09-05 AU AU84953/91A patent/AU653167B2/en not_active Expired
- 1991-09-05 CA CA002090961A patent/CA2090961C/en not_active Expired - Lifetime
- 1991-09-05 ES ES91308147T patent/ES2193129T3/es not_active Expired - Lifetime
- 1991-09-05 HU HU9300609A patent/HUT67796A/hu unknown
- 1991-09-05 DK DK91308147T patent/DK0483961T3/da active
- 1991-09-05 RO RO93-00310A patent/RO113432B1/ro unknown
- 1991-09-05 KR KR1019930700678A patent/KR930702526A/ko not_active Application Discontinuation
- 1991-09-05 HU HU9300609A patent/HU9300609D0/hu unknown
- 1991-09-05 EP EP91308147A patent/EP0483961B1/en not_active Expired - Lifetime
- 1991-09-05 JP JP51496191A patent/JP3514456B2/ja not_active Expired - Lifetime
-
1993
- 1993-03-05 FI FI930984A patent/FI113873B/fi not_active IP Right Cessation
- 1993-03-05 NO NO19930825A patent/NO314595B1/no not_active IP Right Cessation
- 1993-04-05 BG BG97607A patent/BG60716B1/bg unknown
-
2000
- 2000-12-28 US US09/749,831 patent/US20020086978A1/en not_active Abandoned
-
2001
- 2001-08-31 FI FI20011739A patent/FI114611B/fi not_active IP Right Cessation
- 2001-10-04 NO NO20014822A patent/NO315239B1/no not_active IP Right Cessation
-
2002
- 2002-05-30 JP JP2002157535A patent/JP2003061689A/ja not_active Withdrawn
Also Published As
Publication number | Publication date |
---|---|
CA2090961A1 (en) | 1992-03-08 |
FI113873B (fi) | 2004-06-30 |
EP0483961B1 (en) | 2003-02-26 |
DE69133200D1 (de) | 2003-04-03 |
NO20014822L (no) | 1993-05-05 |
GB9019553D0 (en) | 1990-10-24 |
NO20014822D0 (no) | 2001-10-04 |
NO315239B1 (no) | 2003-08-04 |
UA46691C2 (uk) | 2002-06-17 |
ES2193129T3 (es) | 2003-11-01 |
AU8495391A (en) | 1992-03-30 |
FI930984A (fi) | 1993-03-05 |
US6204366B1 (en) | 2001-03-20 |
EP0483961A1 (en) | 1992-05-06 |
NO930825D0 (no) | 1993-03-05 |
ATE233279T1 (de) | 2003-03-15 |
RO113432B1 (ro) | 1998-07-30 |
BG60716B1 (en) | 1996-01-31 |
JP2003061689A (ja) | 2003-03-04 |
US20020086978A1 (en) | 2002-07-04 |
CA2090961C (en) | 2004-01-20 |
HU9300609D0 (en) | 1993-05-28 |
FI930984A0 (fi) | 1993-03-05 |
KR930702526A (ko) | 1993-09-09 |
JPH06500468A (ja) | 1994-01-20 |
FI114611B (fi) | 2004-11-30 |
JP3514456B2 (ja) | 2004-03-31 |
WO1992004380A1 (en) | 1992-03-19 |
HUT67796A (en) | 1995-04-28 |
DE69133200T2 (de) | 2003-11-20 |
BG97607A (bg) | 1994-03-31 |
AU653167B2 (en) | 1994-09-22 |
NO930825L (no) | 1993-05-05 |
DK0483961T3 (da) | 2003-06-23 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO314595B1 (no) | Fremgangsmåte for fremstilling av et kim¶rt terapeutisk aktivt humanisert antistoff eller et terapeutisk aktivt fragment derav, DNA-sekvenssom koder for antistoffet, samt plasmid og stabil vertscellelinje som omfatterDNA-sekvensen | |
US5891996A (en) | Humanized and chimeric monoclonal antibodies that recognize epidermal growth factor receptor (EGF-R); diagnostic and therapeutic use | |
RU2112037C1 (ru) | Гибридное моноклональное антитело, взаимодействующее с cd4-антигеном т-хелперных клеток человека, и способ его получения | |
EP0491031B1 (en) | Cdr grafted anti-cea antibodies and their production | |
Sharon et al. | Recurrent somatic mutations in mouse antibodies to p-azophenylarsonate increase affinity for hapten. | |
JPH02501191A (ja) | 組換え抗体及び方法 | |
JP2004073210A (ja) | 変性された抗体、それに関連する生成物及び方法 | |
GB2276169A (en) | Antibodies specific for carcinoembryonic antigen | |
KR970007782B1 (ko) | 특이적 결합제 | |
Sompuram et al. | Analysis of antigen binding and idiotypic expression by antibodies with polyglycine-replaced complementarity-determining regions. | |
RU2102479C1 (ru) | Химерное моноклональное антитело, взаимодействующее с человеческой плацентарной щелочной фосфатазой, вариабельная область тяжелой гамма-цепи химерного моноклонального антитела, вариабельная область легкой k-цепи химерного моноклонального антитела, фрагмент кднк, кодирующий вариабельную область тяжелой гамма-цепи химерного моноклонального антитела и фрагмент кднк, кодирующий вариабельную область легкой k-цепи химерного моноклонального антитела | |
JPH06189768A (ja) | B型肝炎ウイルスのpre−S2抗原に対するキメラ抗体およびその産生細胞株 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MK1K | Patent expired |