MXPA04003533A - Agentes de intensificacion de afinidad. - Google Patents
Agentes de intensificacion de afinidad.Info
- Publication number
- MXPA04003533A MXPA04003533A MXPA04003533A MXPA04003533A MXPA04003533A MX PA04003533 A MXPA04003533 A MX PA04003533A MX PA04003533 A MXPA04003533 A MX PA04003533A MX PA04003533 A MXPA04003533 A MX PA04003533A MX PA04003533 A MXPA04003533 A MX PA04003533A
- Authority
- MX
- Mexico
- Prior art keywords
- binding protein
- seq
- polypeptide
- binding
- diabody
- Prior art date
Links
- 230000027455 binding Effects 0.000 claims abstract description 78
- 108091008324 binding proteins Proteins 0.000 claims abstract description 48
- 239000000427 antigen Substances 0.000 claims abstract description 28
- 102000036639 antigens Human genes 0.000 claims abstract description 27
- 108091007433 antigens Proteins 0.000 claims abstract description 27
- 239000003814 drug Substances 0.000 claims abstract description 25
- 229940124597 therapeutic agent Drugs 0.000 claims abstract description 21
- 239000000032 diagnostic agent Substances 0.000 claims abstract description 15
- 229940039227 diagnostic agent Drugs 0.000 claims abstract description 15
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 94
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 77
- 229920001184 polypeptide Polymers 0.000 claims description 75
- 206010028980 Neoplasm Diseases 0.000 claims description 45
- 238000000034 method Methods 0.000 claims description 32
- 108010022366 Carcinoembryonic Antigen Proteins 0.000 claims description 25
- 108020004707 nucleic acids Proteins 0.000 claims description 15
- 102000039446 nucleic acids Human genes 0.000 claims description 15
- 150000007523 nucleic acids Chemical class 0.000 claims description 15
- 125000000539 amino acid group Chemical group 0.000 claims description 12
- 239000003795 chemical substances by application Substances 0.000 claims description 9
- 239000013612 plasmid Substances 0.000 claims description 9
- 241001529936 Murinae Species 0.000 claims description 8
- 239000002299 complementary DNA Substances 0.000 claims description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 5
- 208000035475 disorder Diseases 0.000 claims description 5
- 201000011510 cancer Diseases 0.000 claims description 4
- 229940079593 drug Drugs 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 208000023275 Autoimmune disease Diseases 0.000 claims description 2
- 208000024172 Cardiovascular disease Diseases 0.000 claims description 2
- 208000035473 Communicable disease Diseases 0.000 claims description 2
- 108090000695 Cytokines Proteins 0.000 claims description 2
- 102000004127 Cytokines Human genes 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 239000003102 growth factor Substances 0.000 claims description 2
- 239000005556 hormone Substances 0.000 claims description 2
- 229940088597 hormone Drugs 0.000 claims description 2
- 208000027866 inflammatory disease Diseases 0.000 claims description 2
- 239000003053 toxin Substances 0.000 claims description 2
- 231100000765 toxin Toxicity 0.000 claims description 2
- 108700012359 toxins Proteins 0.000 claims description 2
- 102000023732 binding proteins Human genes 0.000 claims 33
- 102100025475 Carcinoembryonic antigen-related cell adhesion molecule 5 Human genes 0.000 claims 5
- 108020004635 Complementary DNA Proteins 0.000 claims 3
- 239000000562 conjugate Substances 0.000 claims 1
- 239000013598 vector Substances 0.000 abstract description 28
- 102000014914 Carrier Proteins Human genes 0.000 abstract description 15
- 230000000813 microbial effect Effects 0.000 abstract description 6
- 230000009870 specific binding Effects 0.000 abstract 1
- 108091026890 Coding region Proteins 0.000 description 83
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 39
- 108090000623 proteins and genes Proteins 0.000 description 35
- 238000003752 polymerase chain reaction Methods 0.000 description 31
- 102000004169 proteins and genes Human genes 0.000 description 31
- 235000001014 amino acid Nutrition 0.000 description 28
- 235000018102 proteins Nutrition 0.000 description 28
- 238000002347 injection Methods 0.000 description 27
- 239000007924 injection Substances 0.000 description 27
- 108010076504 Protein Sorting Signals Proteins 0.000 description 26
- 229940024606 amino acid Drugs 0.000 description 26
- 102000012406 Carcinoembryonic Antigen Human genes 0.000 description 24
- 150000001413 amino acids Chemical class 0.000 description 24
- 101100136076 Aspergillus oryzae (strain ATCC 42149 / RIB 40) pel1 gene Proteins 0.000 description 23
- 101150040383 pel2 gene Proteins 0.000 description 23
- 101150050446 pelB gene Proteins 0.000 description 23
- 238000010276 construction Methods 0.000 description 21
- 210000001519 tissue Anatomy 0.000 description 21
- 241000588724 Escherichia coli Species 0.000 description 18
- 210000004027 cell Anatomy 0.000 description 18
- 230000035772 mutation Effects 0.000 description 18
- 210000004369 blood Anatomy 0.000 description 15
- 239000008280 blood Substances 0.000 description 15
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 15
- 238000004128 high performance liquid chromatography Methods 0.000 description 14
- 239000012634 fragment Substances 0.000 description 12
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 12
- 230000001225 therapeutic effect Effects 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 11
- 108020004414 DNA Proteins 0.000 description 10
- 108091034117 Oligonucleotide Proteins 0.000 description 10
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 10
- 238000006467 substitution reaction Methods 0.000 description 10
- 230000002068 genetic effect Effects 0.000 description 9
- 239000012614 Q-Sepharose Substances 0.000 description 8
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 8
- 210000003734 kidney Anatomy 0.000 description 8
- 210000004185 liver Anatomy 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 238000001155 isoelectric focusing Methods 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 6
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
- 230000004044 response Effects 0.000 description 6
- 210000000952 spleen Anatomy 0.000 description 6
- 238000002965 ELISA Methods 0.000 description 5
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 125000003275 alpha amino acid group Chemical group 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 239000000539 dimer Substances 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 210000002429 large intestine Anatomy 0.000 description 5
- 210000004072 lung Anatomy 0.000 description 5
- 230000014759 maintenance of location Effects 0.000 description 5
- 210000000813 small intestine Anatomy 0.000 description 5
- 229910000162 sodium phosphate Inorganic materials 0.000 description 5
- 210000002784 stomach Anatomy 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 4
- 239000004473 Threonine Substances 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 230000003302 anti-idiotype Effects 0.000 description 4
- 239000004202 carbamide Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 230000007717 exclusion Effects 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 230000002797 proteolythic effect Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- 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 3
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- 101100113084 Schizosaccharomyces pombe (strain 972 / ATCC 24843) mcs2 gene Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 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 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 238000005349 anion exchange Methods 0.000 description 3
- 238000005571 anion exchange chromatography Methods 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 239000013599 cloning vector Substances 0.000 description 3
- 230000002860 competitive effect Effects 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 210000003705 ribosome Anatomy 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000013638 trimer Substances 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 102000013392 Carboxylesterase Human genes 0.000 description 2
- 108010051152 Carboxylesterase Proteins 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- WDLRUFUQRNWCPK-UHFFFAOYSA-N Tetraxetan Chemical compound OC(=O)CN1CCN(CC(O)=O)CCN(CC(O)=O)CCN(CC(O)=O)CC1 WDLRUFUQRNWCPK-UHFFFAOYSA-N 0.000 description 2
- 102000025171 antigen binding proteins Human genes 0.000 description 2
- 108091000831 antigen binding proteins Proteins 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 239000002198 insoluble material Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000005496 tempering Methods 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 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
- RAZLJUXJEOEYAM-UHFFFAOYSA-N 2-[bis[2-(2,6-dioxomorpholin-4-yl)ethyl]azaniumyl]acetate Chemical compound C1C(=O)OC(=O)CN1CCN(CC(=O)O)CCN1CC(=O)OC(=O)C1 RAZLJUXJEOEYAM-UHFFFAOYSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000124815 Barbus barbus Species 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 241000672609 Escherichia coli BL21 Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 208000033229 Immune-mediated cerebellar ataxia Diseases 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus 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
- 229920002684 Sepharose Polymers 0.000 description 1
- 108010034546 Serratia marcescens nuclease Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 101710137500 T7 RNA polymerase Proteins 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- HSANJBZMPJBTRT-UHFFFAOYSA-N acetic acid;1,4,7,10-tetrazacyclododecane Chemical compound CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O.C1CNCCNCCNCCN1 HSANJBZMPJBTRT-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 210000000084 barbel Anatomy 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 238000001815 biotherapy Methods 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- FDJOLVPMNUYSCM-WZHZPDAFSA-L cobalt(3+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+3].N#[C-].N([C@@H]([C@]1(C)[N-]\C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C(\C)/C1=N/C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C\C1=N\C([C@H](C1(C)C)CCC(N)=O)=C/1C)[C@@H]2CC(N)=O)=C\1[C@]2(C)CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@H]1[C@@H](O)[C@@H](N2C3=CC(C)=C(C)C=C3N=C2)O[C@@H]1CO FDJOLVPMNUYSCM-WZHZPDAFSA-L 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 231100000371 dose-limiting toxicity Toxicity 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 230000002601 intratumoral effect Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- -1 isotopes Substances 0.000 description 1
- OOYGSFOGFJDDHP-KMCOLRRFSA-N kanamycin A sulfate Chemical compound OS(O)(=O)=O.O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N OOYGSFOGFJDDHP-KMCOLRRFSA-N 0.000 description 1
- 229960002064 kanamycin sulfate Drugs 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 238000002953 preparative HPLC Methods 0.000 description 1
- 208000008128 pulmonary tuberculosis Diseases 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 238000011363 radioimmunotherapy Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000004088 simulation Methods 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/18—Growth factors; Growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- 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
- C07K16/3007—Carcino-embryonic Antigens
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/44—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material not provided for elsewhere, e.g. haptens, metals, DNA, RNA, amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—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
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/626—Diabody or triabody
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Epidemiology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Oncology (AREA)
- Cell Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Heart & Thoracic Surgery (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Communicable Diseases (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Cardiology (AREA)
- Transplantation (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US32883501P | 2001-10-15 | 2001-10-15 | |
| US34188101P | 2001-12-21 | 2001-12-21 | |
| PCT/US2002/032717 WO2003033653A2 (en) | 2001-10-15 | 2002-10-15 | Affinity enhancement agents |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MXPA04003533A true MXPA04003533A (es) | 2005-06-20 |
Family
ID=26986533
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MXPA04003533A MXPA04003533A (es) | 2001-10-15 | 2002-10-15 | Agentes de intensificacion de afinidad. |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US20030113333A1 (enExample) |
| EP (1) | EP1444267B1 (enExample) |
| JP (1) | JP4443923B2 (enExample) |
| KR (1) | KR101027889B1 (enExample) |
| CN (1) | CN1604910A (enExample) |
| AU (1) | AU2002335808B2 (enExample) |
| BR (1) | BR0213284A (enExample) |
| CA (1) | CA2463616C (enExample) |
| IL (1) | IL161417A0 (enExample) |
| MX (1) | MXPA04003533A (enExample) |
| PL (1) | PL374426A1 (enExample) |
| RU (1) | RU2004114878A (enExample) |
| WO (1) | WO2003033653A2 (enExample) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6962702B2 (en) * | 1998-06-22 | 2005-11-08 | Immunomedics Inc. | Production and use of novel peptide-based agents for use with bi-specific antibodies |
| US6346454B1 (en) * | 1999-01-12 | 2002-02-12 | Agere Systems Guardian Corp. | Method of making dual damascene interconnect structure and metal electrode capacitor |
| US20040018557A1 (en) * | 2002-03-01 | 2004-01-29 | Immunomedics, Inc. | Bispecific antibody point mutations for enhancing rate of clearance |
| EP1618181B1 (en) * | 2003-04-22 | 2014-10-15 | IBC Pharmaceuticals | Polyvalent protein complex |
| KR20060041205A (ko) * | 2003-07-01 | 2006-05-11 | 이뮤노메딕스, 인코오포레이티드 | 양특이성 항체들의 다가 담체들 |
| EP3332808B1 (en) | 2005-03-03 | 2020-09-09 | Immunomedics Inc. | Humanized l243 antibodies |
| ES2613844T3 (es) | 2008-04-21 | 2017-05-26 | Lawrence Livermore National Security, Llc | Ligandos polidentados de alta afinidad selectivos y métodos para producirlos |
| WO2011003780A1 (en) * | 2009-07-06 | 2011-01-13 | F. Hoffmann-La Roche Ag | Bi-specific digoxigenin binding antibodies |
| US9264453B2 (en) | 2013-11-08 | 2016-02-16 | At&T Mobility Ii Llc | Front end processor for short message service centers |
| KR20250150051A (ko) * | 2023-03-03 | 2025-10-17 | 온코원 리서치 앤드 디벨롭먼트 게엠베하 | 과증식성 질환의 예비 표적화를 위한 개선된 이중특이적 항종양 항원/항hsg 항체 |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5618920A (en) * | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US4946778A (en) * | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| FR2604092B1 (fr) * | 1986-09-19 | 1990-04-13 | Immunotech Sa | Immunoreactifs destines a cibler les cellules animales pour leur visualisation ou leur destruction in vivo |
| US5258498A (en) * | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| US5132405A (en) * | 1987-05-21 | 1992-07-21 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| GB8928874D0 (en) * | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US6027725A (en) * | 1991-11-25 | 2000-02-22 | Enzon, Inc. | Multivalent antigen-binding proteins |
| US6096289A (en) * | 1992-05-06 | 2000-08-01 | Immunomedics, Inc. | Intraoperative, intravascular, and endoscopic tumor and lesion detection, biopsy and therapy |
| WO1994007921A1 (en) * | 1992-09-25 | 1994-04-14 | Commonwealth Scientific And Industrial Research Organisation | Target binding polypeptide |
| EP0672142B1 (en) * | 1992-12-04 | 2001-02-28 | Medical Research Council | Multivalent and multispecific binding proteins, their manufacture and use |
| US5874540A (en) * | 1994-10-05 | 1999-02-23 | Immunomedics, Inc. | CDR-grafted type III anti-CEA humanized mouse monoclonal antibodies |
| BR9606706A (pt) * | 1995-10-16 | 1999-04-06 | Unilever Nv | Análogo de fragmento de anticorpo biespecífico ou bivalente uso processo para produzir o mesmo |
| CA2249320C (en) * | 1996-03-20 | 2008-12-23 | Immunomedics, Inc. | Glycosylated humanized b-cell specific antibodies |
| ES2225961T3 (es) * | 1996-04-04 | 2005-03-16 | Unilever N.V. | Proteina de union a antigeno multivalente y multiespecifica. |
| JP4113670B2 (ja) * | 1998-06-22 | 2008-07-09 | イムノメディクス， インコーポレイテッド | プレターゲッティング診断およびプレターゲッティング治療のための二重特異性抗体の使用 |
| US6962702B2 (en) * | 1998-06-22 | 2005-11-08 | Immunomedics Inc. | Production and use of novel peptide-based agents for use with bi-specific antibodies |
| US20030162709A1 (en) * | 2001-12-26 | 2003-08-28 | Edmund Rossi | Methods of generating multispecific, multivalent agents from VH and VL domains |
-
2002
- 2002-10-15 CN CNA028250710A patent/CN1604910A/zh active Pending
- 2002-10-15 WO PCT/US2002/032717 patent/WO2003033653A2/en not_active Ceased
- 2002-10-15 EP EP02770573.0A patent/EP1444267B1/en not_active Expired - Lifetime
- 2002-10-15 AU AU2002335808A patent/AU2002335808B2/en not_active Ceased
- 2002-10-15 US US10/270,071 patent/US20030113333A1/en not_active Abandoned
- 2002-10-15 JP JP2003536383A patent/JP4443923B2/ja not_active Expired - Fee Related
- 2002-10-15 IL IL16141702A patent/IL161417A0/xx unknown
- 2002-10-15 CA CA2463616A patent/CA2463616C/en not_active Expired - Fee Related
- 2002-10-15 MX MXPA04003533A patent/MXPA04003533A/es not_active Application Discontinuation
- 2002-10-15 RU RU2004114878/13A patent/RU2004114878A/ru not_active Application Discontinuation
- 2002-10-15 BR BRPI0213284-2A patent/BR0213284A/pt not_active IP Right Cessation
- 2002-10-15 KR KR1020047005675A patent/KR101027889B1/ko not_active Expired - Fee Related
- 2002-10-15 PL PL02374426A patent/PL374426A1/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CA2463616C (en) | 2011-07-12 |
| WO2003033653A3 (en) | 2003-11-13 |
| KR20050036873A (ko) | 2005-04-20 |
| US20030113333A1 (en) | 2003-06-19 |
| WO2003033653B1 (en) | 2004-02-12 |
| KR101027889B1 (ko) | 2011-04-07 |
| RU2004114878A (ru) | 2005-04-20 |
| PL374426A1 (en) | 2005-10-17 |
| EP1444267A2 (en) | 2004-08-11 |
| JP2005518344A (ja) | 2005-06-23 |
| WO2003033653A2 (en) | 2003-04-24 |
| CN1604910A (zh) | 2005-04-06 |
| AU2002335808B2 (en) | 2009-08-27 |
| JP4443923B2 (ja) | 2010-03-31 |
| EP1444267B1 (en) | 2016-08-10 |
| BR0213284A (pt) | 2006-05-23 |
| CA2463616A1 (en) | 2003-04-24 |
| EP1444267A4 (en) | 2009-12-02 |
| IL161417A0 (en) | 2004-09-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN112646031B (zh) | 抗4-1bb纳米抗体及其用途 | |
| JP7691720B2 (ja) | 抗ヒトｃｄ７３抗体およびその適用 | |
| US20240368264A1 (en) | Anti-TSLP nanobodies and their applications | |
| JP2012511033A (ja) | 多価化合物の可逆阻害用マスキングリガンド | |
| IL263329A (en) | Lysine-coupled immunoglobulins | |
| CN109485726B (zh) | 放射性标记抗纳米抗体在癌症的预后、诊断中的应用 | |
| US20230001004A1 (en) | Cys80 conjugated immunoglobulins | |
| EP4130046A1 (en) | Platform for constructing multispecific antibody | |
| JP2021508314A (ja) | 血清中のタンパク質の半減期を増加させるための組成物及び方法 | |
| CN111718415A (zh) | 一种抗tigit纳米抗体及其应用 | |
| EP1444267B1 (en) | Affinity enhancement agents | |
| CN117279950A (zh) | 一种靶向il-18bp的抗体及其应用 | |
| AU2002335808A1 (en) | Affinity enhancement agents | |
| WO2023031644A1 (en) | Anti-fibroblast activation protein (fap) single domain antibodies and uses thereof | |
| CN111247249B (zh) | Dna、多肽、抗间皮素抗体、肿瘤成像剂和复合体 | |
| CN115124621B (zh) | 靶向pd-l1的纳米抗体及其制备方法和应用 | |
| Yang et al. | A strategy for high-level expression of a single-chain variable fragment against TNFα by subcloning antibody variable regions from the phage display vector pCANTAB 5E into pBV220 | |
| CN114380907B (zh) | 靶向cmtm6的纳米抗体及其制备方法和应用 | |
| CN109879966A (zh) | 基于鼠源cd19抗体的人源化设计及表达验证 | |
| JP2015062367A (ja) | Ｒｏｂｏ１タンパク質に対するダイアボディ型二重特異性抗体 | |
| CN119912562B (en) | Anti-beta-catenin nano antibody, preparation method and application | |
| EP2953975B1 (en) | Immuno imaging agent for use with antibody-drug conjugate therapy | |
| HK40083794A (en) | Platform for constructing multispecific antibody | |
| TW202540163A (zh) | 利用環境應答性胜肽的蛋白質之製造方法 | |
| CN119912562A (zh) | 抗β-catenin的纳米抗体及制备方法和应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FA | Abandonment or withdrawal |