UA73276C2 - A humanized antiboby being specifically bonded to the protein of alpha-activation of fibroplasts (fap?). - Google Patents
A humanized antiboby being specifically bonded to the protein of alpha-activation of fibroplasts (fap?). Download PDFInfo
- Publication number
- UA73276C2 UA73276C2 UA2000116786A UA2000116786A UA73276C2 UA 73276 C2 UA73276 C2 UA 73276C2 UA 2000116786 A UA2000116786 A UA 2000116786A UA 2000116786 A UA2000116786 A UA 2000116786A UA 73276 C2 UA73276 C2 UA 73276C2
- Authority
- UA
- Ukraine
- Prior art keywords
- bek
- antibody
- cells
- human
- mai
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title abstract description 137
- 102000004169 proteins and genes Human genes 0.000 title abstract description 112
- 150000001413 amino acids Chemical class 0.000 claims description 50
- 210000002950 fibroblast Anatomy 0.000 claims description 31
- 230000004913 activation Effects 0.000 claims description 15
- 230000006303 immediate early viral mRNA transcription Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 230000004071 biological effect Effects 0.000 claims 1
- 238000012876 topography Methods 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 173
- 235000018102 proteins Nutrition 0.000 description 110
- 239000013615 primer Substances 0.000 description 100
- 108020004414 DNA Proteins 0.000 description 88
- 238000000034 method Methods 0.000 description 59
- 206010028980 Neoplasm Diseases 0.000 description 45
- 230000014509 gene expression Effects 0.000 description 44
- 239000013598 vector Substances 0.000 description 38
- 230000027455 binding Effects 0.000 description 37
- 108091028043 Nucleic acid sequence Proteins 0.000 description 35
- 241000699666 Mus <mouse, genus> Species 0.000 description 26
- 238000010276 construction Methods 0.000 description 26
- 210000001519 tissue Anatomy 0.000 description 25
- 239000002609 medium Substances 0.000 description 24
- 101100460719 Mus musculus Noto gene Proteins 0.000 description 23
- 101100187345 Xenopus laevis noto gene Proteins 0.000 description 23
- 235000001014 amino acid Nutrition 0.000 description 23
- 239000013604 expression vector Substances 0.000 description 23
- 239000002773 nucleotide Substances 0.000 description 23
- 125000003729 nucleotide group Chemical group 0.000 description 23
- 239000000427 antigen Substances 0.000 description 22
- 239000000047 product Substances 0.000 description 22
- 229940024606 amino acid Drugs 0.000 description 21
- 210000004881 tumor cell Anatomy 0.000 description 20
- 108091007433 antigens Proteins 0.000 description 19
- 102000036639 antigens Human genes 0.000 description 19
- 201000011510 cancer Diseases 0.000 description 19
- 239000002299 complementary DNA Substances 0.000 description 19
- 230000000295 complement effect Effects 0.000 description 18
- 238000002474 experimental method Methods 0.000 description 17
- 230000006870 function Effects 0.000 description 17
- 238000011534 incubation Methods 0.000 description 17
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 16
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 16
- 239000000203 mixture Substances 0.000 description 16
- 239000006228 supernatant Substances 0.000 description 16
- 230000015572 biosynthetic process Effects 0.000 description 15
- 229940098773 bovine serum albumin Drugs 0.000 description 15
- 230000009089 cytolysis Effects 0.000 description 15
- 239000012634 fragment Substances 0.000 description 15
- 238000011282 treatment Methods 0.000 description 15
- 230000010076 replication Effects 0.000 description 12
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 11
- 230000000977 initiatory effect Effects 0.000 description 11
- 108091008146 restriction endonucleases Proteins 0.000 description 11
- 210000002966 serum Anatomy 0.000 description 11
- 238000001890 transfection Methods 0.000 description 11
- 238000004458 analytical method Methods 0.000 description 10
- 210000004962 mammalian cell Anatomy 0.000 description 10
- 230000001404 mediated effect Effects 0.000 description 10
- 230000004048 modification Effects 0.000 description 10
- 238000012986 modification Methods 0.000 description 10
- 241001529936 Murinae Species 0.000 description 9
- 102100034937 Poly(A) RNA polymerase, mitochondrial Human genes 0.000 description 9
- 229910052796 boron Inorganic materials 0.000 description 9
- 239000003814 drug Substances 0.000 description 9
- 239000008194 pharmaceutical composition Substances 0.000 description 9
- 238000003786 synthesis reaction Methods 0.000 description 9
- 229940124597 therapeutic agent Drugs 0.000 description 9
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 8
- 241000238631 Hexapoda Species 0.000 description 8
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 8
- 108060003951 Immunoglobulin Proteins 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 239000012636 effector Substances 0.000 description 8
- 102000018358 immunoglobulin Human genes 0.000 description 8
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 7
- 230000000692 anti-sense effect Effects 0.000 description 7
- 208000027697 autoimmune lymphoproliferative syndrome due to CTLA4 haploinsuffiency Diseases 0.000 description 7
- 238000010367 cloning Methods 0.000 description 7
- 241000283707 Capra Species 0.000 description 6
- 238000012408 PCR amplification Methods 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 229960000723 ampicillin Drugs 0.000 description 6
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 210000003527 eukaryotic cell Anatomy 0.000 description 6
- 210000004907 gland Anatomy 0.000 description 6
- 210000005260 human cell Anatomy 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 231100000219 mutagenic Toxicity 0.000 description 6
- 230000003505 mutagenic effect Effects 0.000 description 6
- 239000013642 negative control Substances 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 229920000936 Agarose Polymers 0.000 description 5
- 208000026310 Breast neoplasm Diseases 0.000 description 5
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 5
- 235000010469 Glycine max Nutrition 0.000 description 5
- 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 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 5
- 239000003623 enhancer Substances 0.000 description 5
- 210000000981 epithelium Anatomy 0.000 description 5
- 239000000284 extract Substances 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 238000002347 injection Methods 0.000 description 5
- 239000007924 injection Substances 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 229960000485 methotrexate Drugs 0.000 description 5
- 210000003739 neck Anatomy 0.000 description 5
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 238000013207 serial dilution Methods 0.000 description 5
- 238000012800 visualization Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 4
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 4
- 208000003174 Brain Neoplasms Diseases 0.000 description 4
- 201000009030 Carcinoma Diseases 0.000 description 4
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 229930193140 Neomycin Natural products 0.000 description 4
- 206010061535 Ovarian neoplasm Diseases 0.000 description 4
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 4
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 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 4
- 201000010099 disease Diseases 0.000 description 4
- 238000004520 electroporation Methods 0.000 description 4
- 239000012530 fluid Substances 0.000 description 4
- 239000012216 imaging agent Substances 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 210000004185 liver Anatomy 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 208000037841 lung tumor Diseases 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 230000001394 metastastic effect Effects 0.000 description 4
- 206010061289 metastatic neoplasm Diseases 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 229960004927 neomycin Drugs 0.000 description 4
- 210000000056 organ Anatomy 0.000 description 4
- 201000002528 pancreatic cancer Diseases 0.000 description 4
- 239000002953 phosphate buffered saline Substances 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000002285 radioactive effect Effects 0.000 description 4
- 238000004153 renaturation Methods 0.000 description 4
- 210000003491 skin Anatomy 0.000 description 4
- 210000002784 stomach Anatomy 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 241000701447 unidentified baculovirus Species 0.000 description 4
- 101100492787 Caenorhabditis elegans mai-1 gene Proteins 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 201000008808 Fibrosarcoma Diseases 0.000 description 3
- 208000009119 Giant Axonal Neuropathy Diseases 0.000 description 3
- 244000068988 Glycine max Species 0.000 description 3
- 101001035654 Homo sapiens 28 kDa heat- and acid-stable phosphoprotein Proteins 0.000 description 3
- 101000785915 Homo sapiens Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 Proteins 0.000 description 3
- 101000735427 Homo sapiens Poly(A) RNA polymerase, mitochondrial Proteins 0.000 description 3
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 206010023774 Large cell lung cancer Diseases 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 229930040373 Paraformaldehyde Natural products 0.000 description 3
- 235000013447 Xanthosoma atrovirens Nutrition 0.000 description 3
- 240000001781 Xanthosoma sagittifolium Species 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- -1 aliphatic amino acids Chemical class 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- 210000000481 breast Anatomy 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 239000007979 citrate buffer Substances 0.000 description 3
- 210000001072 colon Anatomy 0.000 description 3
- 230000003013 cytotoxicity Effects 0.000 description 3
- 231100000135 cytotoxicity Toxicity 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 239000013024 dilution buffer Substances 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- 239000000975 dye Substances 0.000 description 3
- 210000003890 endocrine cell Anatomy 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 201000003382 giant axonal neuropathy 1 Diseases 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 210000003128 head Anatomy 0.000 description 3
- 208000014829 head and neck neoplasm Diseases 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000002991 immunohistochemical analysis Methods 0.000 description 3
- 238000001802 infusion Methods 0.000 description 3
- 210000004153 islets of langerhan Anatomy 0.000 description 3
- 210000003292 kidney cell Anatomy 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 210000004072 lung Anatomy 0.000 description 3
- 201000009546 lung large cell carcinoma Diseases 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- JLESVLCTIOAHPT-UHFFFAOYSA-N mmai Chemical compound C1=C(C)C(OC)=CC2=C1CC(N)C2 JLESVLCTIOAHPT-UHFFFAOYSA-N 0.000 description 3
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 3
- 230000001613 neoplastic effect Effects 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 229920002866 paraformaldehyde Polymers 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 230000005855 radiation Effects 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 230000008925 spontaneous activity Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000004448 titration Methods 0.000 description 3
- IDOQDZANRZQBTP-UHFFFAOYSA-N 2-[2-(2,4,4-trimethylpentan-2-yl)phenoxy]ethanol Chemical compound CC(C)(C)CC(C)(C)C1=CC=CC=C1OCCO IDOQDZANRZQBTP-UHFFFAOYSA-N 0.000 description 2
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- 102100025674 Angiopoietin-related protein 4 Human genes 0.000 description 2
- 206010006187 Breast cancer Diseases 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 101000693076 Homo sapiens Angiopoietin-related protein 4 Proteins 0.000 description 2
- 101000840540 Homo sapiens Iduronate 2-sulfatase Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 206010070834 Sensitisation Diseases 0.000 description 2
- 108700009124 Transcription Initiation Site Proteins 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 229920004929 Triton X-114 Polymers 0.000 description 2
- 206010052428 Wound Diseases 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- 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 2
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 244000309466 calf Species 0.000 description 2
- 239000006143 cell culture medium Substances 0.000 description 2
- 230000005889 cellular cytotoxicity Effects 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 230000005251 gamma ray Effects 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 201000010536 head and neck cancer Diseases 0.000 description 2
- 230000035876 healing Effects 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000010166 immunofluorescence Methods 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 231100000682 maximum tolerated dose Toxicity 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 239000002480 mineral oil Substances 0.000 description 2
- 235000010446 mineral oil Nutrition 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000010413 mother solution Substances 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 210000004789 organ system Anatomy 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 230000008313 sensitization Effects 0.000 description 2
- 230000001235 sensitizing effect Effects 0.000 description 2
- 239000012679 serum free medium Substances 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 210000002460 smooth muscle Anatomy 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 230000010474 transient expression Effects 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 239000003656 tris buffered saline Substances 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 210000004291 uterus Anatomy 0.000 description 2
- 210000003462 vein Anatomy 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- OPCHFPHZPIURNA-MFERNQICSA-N (2s)-2,5-bis(3-aminopropylamino)-n-[2-(dioctadecylamino)acetyl]pentanamide Chemical compound CCCCCCCCCCCCCCCCCCN(CC(=O)NC(=O)[C@H](CCCNCCCN)NCCCN)CCCCCCCCCCCCCCCCCC OPCHFPHZPIURNA-MFERNQICSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- PMJHNEFCWLUZBC-UHFFFAOYSA-N 4-(4-amino-3-methylphenyl)-2,6,6-trimethylcyclohexa-1,3-dien-1-amine Chemical compound CC1=C(N)C(C)(C)CC(C=2C=C(C)C(N)=CC=2)=C1 PMJHNEFCWLUZBC-UHFFFAOYSA-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
- ZGXJTSGNIOSYLO-UHFFFAOYSA-N 88755TAZ87 Chemical compound NCC(=O)CCC(O)=O ZGXJTSGNIOSYLO-UHFFFAOYSA-N 0.000 description 1
- 108700032845 Ala(2)- enkephalinamide-Met Proteins 0.000 description 1
- 241000796533 Arna Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 1
- 241000283725 Bos Species 0.000 description 1
- 101100167365 Caenorhabditis elegans cha-1 gene Proteins 0.000 description 1
- 101100401100 Caenorhabditis elegans mes-1 gene Proteins 0.000 description 1
- 101100256965 Caenorhabditis elegans sip-1 gene Proteins 0.000 description 1
- 101100478320 Caenorhabditis elegans sre-2 gene Proteins 0.000 description 1
- 101100366936 Caenorhabditis elegans sto-3 gene Proteins 0.000 description 1
- 101100478734 Caenorhabditis elegans stt-3 gene Proteins 0.000 description 1
- 241000282552 Chlorocebus aethiops Species 0.000 description 1
- 241000543381 Cliftonia monophylla Species 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 101100203200 Danio rerio shha gene Proteins 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 206010016654 Fibrosis Diseases 0.000 description 1
- 102100030393 G-patch domain and KOW motifs-containing protein Human genes 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 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 1
- 101150055539 HADH gene Proteins 0.000 description 1
- 101001014213 Homo sapiens Morphogenetic neuropeptide Proteins 0.000 description 1
- 101000772267 Homo sapiens Thyrotropin receptor Proteins 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 108010058683 Immobilized Proteins Proteins 0.000 description 1
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 101710141452 Major surface glycoprotein G Proteins 0.000 description 1
- 208000006644 Malignant Fibrous Histiocytoma Diseases 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 101100121460 Mus musculus Gcsam gene Proteins 0.000 description 1
- 101100018424 Mus musculus Ids gene Proteins 0.000 description 1
- 244000004005 Nypa fruticans Species 0.000 description 1
- 235000005305 Nypa fruticans Nutrition 0.000 description 1
- 101100491259 Oryza sativa subsp. japonica AP2-2 gene Proteins 0.000 description 1
- 208000005141 Otitis Diseases 0.000 description 1
- 241000610691 Pelucha Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 101100150299 Penicillium chrysogenum SREP gene Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108700012364 REG1 Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108091006503 SLC26A1 Proteins 0.000 description 1
- 240000005481 Salvia hispanica Species 0.000 description 1
- 229940125377 Selective β-Amyloid-Lowering Agent Drugs 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 208000018359 Systemic autoimmune disease Diseases 0.000 description 1
- 101150005767 TUBB5 gene Proteins 0.000 description 1
- 102100029337 Thyrotropin receptor Human genes 0.000 description 1
- 241000838698 Togo Species 0.000 description 1
- 108091061763 Triple-stranded DNA Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108091006585 UT-B Proteins 0.000 description 1
- 208000015778 Undifferentiated pleomorphic sarcoma Diseases 0.000 description 1
- 101150100931 VI gene Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 241000289690 Xenarthra Species 0.000 description 1
- SXEHKFHPFVVDIR-UHFFFAOYSA-N [4-(4-hydrazinylphenyl)phenyl]hydrazine Chemical compound C1=CC(NN)=CC=C1C1=CC=C(NN)C=C1 SXEHKFHPFVVDIR-UHFFFAOYSA-N 0.000 description 1
- 208000009956 adenocarcinoma Diseases 0.000 description 1
- 101150067366 adh gene Proteins 0.000 description 1
- 101150004356 adhC gene Proteins 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 238000011398 antitumor immunotherapy Methods 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 1
- 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 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 201000008274 breast adenocarcinoma Diseases 0.000 description 1
- 201000008275 breast carcinoma Diseases 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 125000001314 canonical amino-acid group Chemical group 0.000 description 1
- 239000003990 capacitor Substances 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 229910052956 cinnabar Inorganic materials 0.000 description 1
- 230000007882 cirrhosis Effects 0.000 description 1
- 208000019425 cirrhosis of liver Diseases 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- 238000003113 dilution method Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 208000019258 ear infection Diseases 0.000 description 1
- 230000002357 endometrial effect Effects 0.000 description 1
- 230000029578 entry into host Effects 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 208000037828 epithelial carcinoma Diseases 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 210000000630 fibrocyte Anatomy 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000000684 flow cytometry 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
- 238000005194 fractionation Methods 0.000 description 1
- 239000012520 frozen sample Substances 0.000 description 1
- 108010074605 gamma-Globulins Proteins 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 210000003780 hair follicle Anatomy 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 244000144980 herd Species 0.000 description 1
- 102000057422 human IDS Human genes 0.000 description 1
- 210000004293 human mammary gland Anatomy 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
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000012151 immunohistochemical method Methods 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 210000000867 larynx Anatomy 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
- 238000001638 lipofection Methods 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000003810 lymphokine-activated killer cell Anatomy 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 108091047102 miR-4 stem-loop Proteins 0.000 description 1
- 108091049748 miR-4-1 stem-loop Proteins 0.000 description 1
- 108091058497 miR-4-2 stem-loop Proteins 0.000 description 1
- 108091023818 miR-7 stem-loop Proteins 0.000 description 1
- 238000001690 micro-dialysis Methods 0.000 description 1
- 229910052982 molybdenum disulfide Inorganic materials 0.000 description 1
- 210000002433 mononuclear leukocyte Anatomy 0.000 description 1
- 210000003097 mucus Anatomy 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000004165 myocardium Anatomy 0.000 description 1
- 210000000754 myometrium Anatomy 0.000 description 1
- DVEKCXOJTLDBFE-UHFFFAOYSA-N n-dodecyl-n,n-dimethylglycinate Chemical compound CCCCCCCCCCCC[N+](C)(C)CC([O-])=O DVEKCXOJTLDBFE-UHFFFAOYSA-N 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000001711 oxyntic cell Anatomy 0.000 description 1
- 210000004738 parenchymal cell Anatomy 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 230000002572 peristaltic effect Effects 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 210000004043 pneumocyte Anatomy 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 235000008001 rakum palm Nutrition 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
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000004071 soot Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 206010041823 squamous cell carcinoma Diseases 0.000 description 1
- 101150024950 sstT gene Proteins 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 101150095744 tin-9.1 gene Proteins 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 239000003440 toxic substance Substances 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
- 230000009466 transformation Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 210000003932 urinary bladder Anatomy 0.000 description 1
- 210000001215 vagina Anatomy 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- 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
- 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
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/567—Framework region [FR]
-
- 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
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2799/00—Uses of viruses
- C12N2799/02—Uses of viruses as vector
- C12N2799/021—Uses of viruses as vector for the expression of a heterologous nucleic acid
- C12N2799/026—Uses of viruses as vector for the expression of a heterologous nucleic acid where the vector is derived from a baculovirus
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Immunology (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)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP98107925A EP0953639A1 (en) | 1998-04-30 | 1998-04-30 | FAPalpha-specific antibody with improved producibility |
PCT/EP1999/002711 WO1999057151A2 (en) | 1998-04-30 | 1999-04-22 | FAP α-SPECIFIC ANTIBODY WITH IMPROVED PRODUCIBILITY |
Publications (1)
Publication Number | Publication Date |
---|---|
UA73276C2 true UA73276C2 (en) | 2005-07-15 |
Family
ID=8231860
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
UA2000116786A UA73276C2 (en) | 1998-04-30 | 1999-04-22 | A humanized antiboby being specifically bonded to the protein of alpha-activation of fibroplasts (fap?). |
Country Status (27)
Country | Link |
---|---|
EP (2) | EP0953639A1 (es) |
JP (1) | JP4421779B2 (es) |
KR (1) | KR100580936B1 (es) |
CN (1) | CN1303430A (es) |
AR (1) | AR016243A1 (es) |
AT (1) | ATE356873T1 (es) |
AU (1) | AU760305B2 (es) |
BG (1) | BG65034B1 (es) |
BR (1) | BR9910577A (es) |
CA (1) | CA2327586C (es) |
CO (1) | CO5050255A1 (es) |
DE (1) | DE69935516T2 (es) |
EA (1) | EA005401B1 (es) |
EE (1) | EE200000642A (es) |
ES (1) | ES2283114T3 (es) |
HU (1) | HUP0101501A3 (es) |
ID (1) | ID26555A (es) |
IL (1) | IL138701A0 (es) |
NO (1) | NO20005412L (es) |
NZ (1) | NZ508456A (es) |
PL (1) | PL358087A1 (es) |
SK (1) | SK16192000A3 (es) |
TR (1) | TR200003181T2 (es) |
UA (1) | UA73276C2 (es) |
WO (1) | WO1999057151A2 (es) |
YU (1) | YU66300A (es) |
ZA (1) | ZA200005506B (es) |
Families Citing this family (77)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6914128B1 (en) | 1999-03-25 | 2005-07-05 | Abbott Gmbh & Co. Kg | Human antibodies that bind human IL-12 and methods for producing |
US7883704B2 (en) | 1999-03-25 | 2011-02-08 | Abbott Gmbh & Co. Kg | Methods for inhibiting the activity of the P40 subunit of human IL-12 |
EP1268550A2 (en) * | 2000-03-17 | 2003-01-02 | Boehringer Ingelheim Pharma KG | Human fap-alpha-specific antibodies |
PE20021080A1 (es) * | 2001-04-12 | 2003-02-12 | Boehringer Ingelheim Int | Un anticuerpo especifico fapo bibh1 en el tratamiento del cancer |
EP2365004B1 (en) * | 2002-06-21 | 2016-01-06 | Johns Hopkins University School of Medicine | Membrane associated tumor endothelium markers |
US8187593B2 (en) | 2002-08-14 | 2012-05-29 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8968730B2 (en) | 2002-08-14 | 2015-03-03 | Macrogenics Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8530627B2 (en) | 2002-08-14 | 2013-09-10 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8946387B2 (en) | 2002-08-14 | 2015-02-03 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8044180B2 (en) | 2002-08-14 | 2011-10-25 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
ATE536188T1 (de) * | 2002-08-14 | 2011-12-15 | Macrogenics Inc | Fcgammariib-spezifische antikörper und verfahren zur verwendung davon |
US8193318B2 (en) | 2002-08-14 | 2012-06-05 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US7384744B2 (en) | 2002-11-29 | 2008-06-10 | Boehringer Ingelheim Pharma Gmbh & Co., Kg | Expression vector, methods for the production of heterologous gene products and for the selection of recombinant cells producing high levels of such products |
US7960512B2 (en) | 2003-01-09 | 2011-06-14 | Macrogenics, Inc. | Identification and engineering of antibodies with variant Fc regions and methods of using same |
WO2004063351A2 (en) | 2003-01-09 | 2004-07-29 | Macrogenics, Inc. | IDENTIFICATION AND ENGINEERING OF ANTIBODIES WITH VARIANT Fc REGIONS AND METHODS OF USING SAME |
AU2004213797B2 (en) * | 2003-02-14 | 2009-09-17 | Biogen Ma Inc. | An expression cassette and vector for transient or stable expression of exogenous molecules |
WO2005110474A2 (en) | 2004-05-10 | 2005-11-24 | Macrogenics, Inc. | HUMANIZED FcϜRIIB SPECIFIC ANTIBODIES AND METHODS OF USE THEREOF |
AU2005335714B2 (en) | 2004-11-10 | 2012-07-26 | Macrogenics, Inc. | Engineering Fc antibody regions to confer effector function |
ES2526811T3 (es) | 2005-08-10 | 2015-01-15 | Macrogenics, Inc. | Identificación y modificación de anticuerpos con regiones Fc variantes y métodos de uso de estos |
KR20080090406A (ko) * | 2005-11-28 | 2008-10-08 | 젠맵 에이/에스 | 재조합 1가 항체 및 그의 제조 방법 |
EP1806365A1 (en) | 2006-01-05 | 2007-07-11 | Boehringer Ingelheim International GmbH | Antibody molecules specific for fibroblast activation protein and immunoconjugates containing them |
US7786270B2 (en) | 2006-05-26 | 2010-08-31 | Macrogenics, Inc. | Humanized FcγRIIB-specific antibodies and methods of use thereof |
JP5764290B2 (ja) | 2006-06-26 | 2015-08-19 | マクロジェニクス,インコーポレーテッド | FcγRIIB特異的抗体およびその使用法 |
CA2656224C (en) | 2006-06-26 | 2018-01-09 | Macrogenics, Inc. | Combination of fc.gamma.riib antibodies and cd20-specific antibodies and methods of use thereof |
WO2008140603A2 (en) | 2006-12-08 | 2008-11-20 | Macrogenics, Inc. | METHODS FOR THE TREATMENT OF DISEASE USING IMMUNOGLOBULINS HAVING FC REGIONS WITH ALTERED AFFINITIES FOR FCγR ACTIVATING AND FCγR INHIBITING |
CN104524567A (zh) | 2007-01-16 | 2015-04-22 | 阿布维公司 | 用于治疗银屑病的方法 |
WO2008121301A1 (en) | 2007-03-29 | 2008-10-09 | Abbott Laboratories | Crystalline anti-human il-12 antibodies |
DK3216802T3 (da) * | 2007-08-20 | 2021-01-04 | Glaxo Group Ltd | Produktionsfremgangsmåde |
EP2071337A1 (en) * | 2007-12-10 | 2009-06-17 | F.Hoffmann-La Roche Ag | Seprase as a marker for cancer |
CN101896817A (zh) * | 2007-12-10 | 2010-11-24 | 霍夫曼-拉罗奇有限公司 | 用于结直肠癌的标记物组 |
ATE524740T1 (de) * | 2007-12-10 | 2011-09-15 | Hoffmann La Roche | Seprase als krebsmarker |
KR20100126515A (ko) | 2008-03-18 | 2010-12-01 | 아보트 러보러터리즈 | 건선의 치료방법 |
PL2247304T3 (pl) | 2008-04-02 | 2017-01-31 | Macrogenics, Inc. | Przeciwciała specyficzne wobec HER2/neu oraz sposoby ich zastosowania |
ES2589912T3 (es) | 2008-04-02 | 2016-11-17 | Macrogenics, Inc. | Anticuerpos específicos para el complejo BCR y procedimientos de uso de los mismos |
WO2011032148A1 (en) | 2009-09-14 | 2011-03-17 | Abbott Laboratories | Methods for treating psoriasis |
SI2486141T1 (en) | 2009-10-07 | 2018-06-29 | Macrogenics, Inc. | FC REGION-CONTAINING POLYPETHYDE, AFFECTING A BETTERED EFFECTORAL FUNCTION, BY CHANGES IN THE SCOPE OF FUKOZILATION AND METHODS FOR THEIR USE |
NZ701539A (en) | 2010-03-04 | 2015-04-24 | Macrogenics Inc | Antibodies reactive with b7-h3, immunologically active fragments thereof and uses thereof |
US8802091B2 (en) | 2010-03-04 | 2014-08-12 | Macrogenics, Inc. | Antibodies reactive with B7-H3 and uses thereof |
UA113712C2 (xx) * | 2010-08-13 | 2017-02-27 | Антитіло до fap і способи його застосування | |
NZ729044A (en) | 2010-09-09 | 2020-07-31 | Pfizer | 4-1bb binding molecules |
EP3075745B1 (en) | 2011-02-10 | 2018-09-05 | Roche Glycart AG | Mutant interleukin-2 polypeptides |
EP2859017B1 (en) | 2012-06-08 | 2019-02-20 | Sutro Biopharma, Inc. | Antibodies comprising site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
US9487587B2 (en) | 2013-03-05 | 2016-11-08 | Macrogenics, Inc. | Bispecific molecules that are immunoreactive with immune effector cells of a companion animal that express an activating receptor and cells that express B7-H3 and uses thereof |
UA118028C2 (uk) | 2013-04-03 | 2018-11-12 | Рош Глікарт Аг | Біспецифічне антитіло, специфічне щодо fap і dr5, антитіло, специфічне щодо dr5, і спосіб їх застосування |
CN103267852B (zh) * | 2013-05-15 | 2015-03-25 | 中国医学科学院北京协和医院 | 成纤维激活蛋白α在制备胰腺癌预后试剂盒中的用途 |
US9764039B2 (en) | 2013-07-10 | 2017-09-19 | Sutro Biopharma, Inc. | Antibodies comprising multiple site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
GB201402006D0 (en) | 2014-02-06 | 2014-03-26 | Oncomatryx Biopharma S L | Antibody-drug conjugates and immunotoxins |
CN106536553B (zh) * | 2014-03-26 | 2021-03-12 | 尤利乌斯·马克西米利安维尔茨堡大学 | 生长和分化因子15(gdf-15)的单克隆抗体及其治疗癌性恶病质和癌症的用途 |
CN105646710B (zh) * | 2014-11-17 | 2020-08-25 | 四川科伦博泰生物医药股份有限公司 | 一种全人源化抗vegfr-2单克隆抗体及其制备方法 |
MX2018003820A (es) | 2015-10-02 | 2018-12-10 | F Hoffmann La Roche Ag | Anticuerpos biespecificos especificos para un receptor de tnf coestimulador. |
RU2018130757A (ru) * | 2016-01-27 | 2020-02-27 | Сутро Биофарма, Инк. | Конъюгаты антитела к cd74, композиции, содержащие конъюгаты антитела к cd74, и способы использования конъюгатов антитела к cd74 |
PE20190353A1 (es) | 2016-04-15 | 2019-03-07 | Macrogenics Inc | Moleculas de union b7-h3 novedosas, conjugados anticuerpo-farmaco de los mismos y metodos de uso de los mismos |
SG11201811600PA (en) | 2016-06-30 | 2019-01-30 | Oncorus Inc | Pseudotyped oncolytic viral delivery of therapeutic polypeptides |
JP2018035137A (ja) | 2016-07-13 | 2018-03-08 | マブイミューン ダイアグノスティックス エイジーMabimmune Diagnostics Ag | 新規な抗線維芽細胞活性化タンパク質(fap)結合薬剤およびその使用 |
CN110291401B (zh) | 2016-12-14 | 2023-04-11 | 普渡研究基金会 | 成纤维细胞活化蛋白(fap)-靶向成像和治疗 |
WO2019133847A1 (en) | 2017-12-29 | 2019-07-04 | Oncorus, Inc. | Oncolytic viral delivery of therapeutic polypeptides |
CN110526991A (zh) * | 2018-05-25 | 2019-12-03 | 深圳宾德生物技术有限公司 | 靶向fap的嵌合抗原受体、嵌合抗原受体t细胞及其制备方法和应用 |
CN110526979A (zh) * | 2018-05-25 | 2019-12-03 | 深圳宾德生物技术有限公司 | 靶向fap的单链抗体、嵌合抗原受体t细胞及其制备方法和应用 |
CN109053893B (zh) * | 2018-08-15 | 2021-03-30 | 智享生物(苏州)有限公司 | 一种抗d-二聚体单克隆抗体及其制备方法 |
CN110882385B (zh) * | 2018-09-07 | 2021-07-09 | 上海君实生物医药科技股份有限公司 | 抗pd-1抗体在治疗肿瘤中的用途 |
CN114853908B (zh) * | 2019-05-16 | 2024-06-07 | 浙江道尔生物科技有限公司 | 一种治疗代谢疾病的融合蛋白 |
US20220273831A1 (en) | 2019-07-08 | 2022-09-01 | 3B Pharmaceuticals Gmbh | Compounds comprising a fibroblast activation protein ligand and use thereof |
WO2021005131A1 (en) | 2019-07-08 | 2021-01-14 | 3B Pharmaceuticals Gmbh | Compounds comprising a fibroblast activation protein ligand and use thereof |
EP3763726A1 (en) | 2019-07-08 | 2021-01-13 | 3B Pharmaceuticals GmbH | Compounds comprising a fibroblast activation protein ligand and use thereof |
JP2022547850A (ja) * | 2019-09-03 | 2022-11-16 | バイオ - テラ ソリューションズ、リミテッド | 抗tigit免疫阻害剤及び応用 |
CN113512116B (zh) * | 2020-04-10 | 2022-09-20 | 苏州普乐康医药科技有限公司 | 一种抗igf-1r抗体及其应用 |
KR102363980B1 (ko) * | 2020-04-13 | 2022-02-15 | 전남대학교산학협력단 | 전이성 뇌종양의 진단 또는 예후 분석용 바이오마커 및 이를 이용한 진단방법 |
CN115643797A (zh) * | 2020-04-30 | 2023-01-24 | 天境生物科技(上海)有限公司 | 包含抗cd47抗体的药物组合物 |
JP2023504675A (ja) | 2020-05-19 | 2023-02-06 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | ガンの処置のための結合分子 |
CN112540176B (zh) * | 2020-07-08 | 2021-09-28 | 深圳霁因生物医药转化研究院 | 用于诊断fap表达异常相关疾病的试剂盒、方法及计算机可读存储介质 |
EP4274835A1 (en) | 2021-01-07 | 2023-11-15 | 3B Pharmaceuticals GmbH | Compounds comprising a fibroblast activation protein ligand and use thereof |
EP4050018A1 (en) | 2021-01-07 | 2022-08-31 | 3B Pharmaceuticals GmbH | Compounds comprising a fibroblast activation protein ligand and use thereof |
WO2023031644A1 (en) | 2021-08-31 | 2023-03-09 | Full-Life Technologies Limited | Anti-fibroblast activation protein (fap) single domain antibodies and uses thereof |
WO2023125796A1 (en) * | 2021-12-30 | 2023-07-06 | Concept To Medicine Biotech Co., Ltd. | Human antibodies against fap-alpha |
WO2024027771A1 (zh) * | 2022-08-03 | 2024-02-08 | 南京维立志博生物科技有限公司 | 靶向FAP和TGFβ的抗体融合蛋白及其用途 |
WO2024074727A1 (en) | 2022-10-07 | 2024-04-11 | Genethon | Immunotherapy of skeletal myopathies using anti-fap car-t cells |
CN116589566A (zh) * | 2022-11-18 | 2023-08-15 | 昆明医科大学第一附属医院 | 一种HIV-1中和抗体的改造重组单克隆IgM抗体及其应用 |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5059523A (en) * | 1988-05-02 | 1991-10-22 | Sloan-Kettering Institute For Cancer Research | Cell-surface glycoproteins of human sarcomas |
US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
WO1993005804A1 (en) * | 1991-09-18 | 1993-04-01 | Sloan-Kettering Institute For Cancer Research | Activated stromal fibroblast-specific antibody, f19 and methods of using the same |
ZA936260B (en) * | 1992-09-09 | 1994-03-18 | Smithkline Beecham Corp | Novel antibodies for conferring passive immunity against infection by a pathogen in man |
JP4436457B2 (ja) * | 1995-08-18 | 2010-03-24 | モルフォシス アイピー ゲーエムベーハー | 蛋白質/(ポリ)ペプチドライブラリー |
EP0910655B1 (en) * | 1996-05-01 | 2010-02-10 | Genitope Corporation | Vaccines for treatment of lymphoma and leukemia |
-
1998
- 1998-04-30 EP EP98107925A patent/EP0953639A1/en not_active Withdrawn
-
1999
- 1999-04-22 EP EP99923439A patent/EP1098979B1/en not_active Expired - Lifetime
- 1999-04-22 NZ NZ508456A patent/NZ508456A/xx unknown
- 1999-04-22 DE DE69935516T patent/DE69935516T2/de not_active Expired - Lifetime
- 1999-04-22 ES ES99923439T patent/ES2283114T3/es not_active Expired - Lifetime
- 1999-04-22 IL IL13870199A patent/IL138701A0/xx unknown
- 1999-04-22 EA EA200001023A patent/EA005401B1/ru not_active IP Right Cessation
- 1999-04-22 CA CA2327586A patent/CA2327586C/en not_active Expired - Lifetime
- 1999-04-22 BR BR9910577-2A patent/BR9910577A/pt not_active IP Right Cessation
- 1999-04-22 UA UA2000116786A patent/UA73276C2/uk unknown
- 1999-04-22 HU HU0101501A patent/HUP0101501A3/hu unknown
- 1999-04-22 CN CN99806582A patent/CN1303430A/zh active Pending
- 1999-04-22 ID IDW20002198A patent/ID26555A/id unknown
- 1999-04-22 PL PL99358087A patent/PL358087A1/xx not_active IP Right Cessation
- 1999-04-22 AT AT99923439T patent/ATE356873T1/de active
- 1999-04-22 SK SK1619-2000A patent/SK16192000A3/sk unknown
- 1999-04-22 WO PCT/EP1999/002711 patent/WO1999057151A2/en not_active Application Discontinuation
- 1999-04-22 EE EEP200000642A patent/EE200000642A/xx unknown
- 1999-04-22 JP JP2000547119A patent/JP4421779B2/ja not_active Expired - Lifetime
- 1999-04-22 YU YU66300A patent/YU66300A/sh unknown
- 1999-04-22 TR TR2000/03181T patent/TR200003181T2/xx unknown
- 1999-04-22 KR KR1020007011585A patent/KR100580936B1/ko not_active IP Right Cessation
- 1999-04-22 AU AU40322/99A patent/AU760305B2/en not_active Ceased
- 1999-04-29 CO CO99025997A patent/CO5050255A1/es unknown
- 1999-04-30 AR ARP990102015A patent/AR016243A1/es unknown
-
2000
- 2000-10-05 BG BG104828A patent/BG65034B1/bg unknown
- 2000-10-09 ZA ZA200005506A patent/ZA200005506B/en unknown
- 2000-10-27 NO NO20005412A patent/NO20005412L/no not_active Application Discontinuation
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
UA73276C2 (en) | A humanized antiboby being specifically bonded to the protein of alpha-activation of fibroplasts (fap?). | |
EP1575484B1 (en) | Humanized immunomodulatory monoclonal antibodies for the treatment of neoplastic disease or immunodeficiency | |
JP4932883B2 (ja) | 血管系の特異的凝固のための方法および組成物 | |
US6506883B2 (en) | Humanized and chimeric monoclonal antibodies that recognize epidermal growth factor receptor (EGF-R); diagnostic and therapeutic use | |
US5489525A (en) | Monoclonal antibodies to prostate cells | |
ES2277341T3 (es) | Anticuerpo bioespecifico para tratar el linfoma de linfocitos b y linea celular. | |
US20140212946A1 (en) | Non-natural ribonuclease conjugates as cytotoxic agents | |
WO2016112855A1 (zh) | 抗cd19单克隆抗体及其制备方法 | |
HU211881A9 (en) | Recombinant antibodies for human therapy | |
CA2186455A1 (en) | Antibodies against e-selectin | |
WO2021052307A1 (zh) | 一种抗b7-h3抗体及其应用 | |
KR20220012856A (ko) | 항 pd―l1 항체 및 그의 용도 | |
US20030165508A1 (en) | Monoclonal antibodies that suppress B cell growth and/or differentiation | |
JP2005507373A (ja) | カテプシンb活性を中和するモノクロナール抗体及びその使用 | |
Morrison et al. | Genetically engineered antibody molecules: new tools for cancer therapy | |
KR101442323B1 (ko) | 항-연장된 ⅰ형 글라이코스핑고지질 항체, 이의 유도체 및 용도 | |
CA2481829A1 (en) | Anti-idiotype anti-cea antibody molecules and its use as cancer vaccine | |
CN116113433A (zh) | 结合人cd38的抗体、其制备方法和用途 | |
CN101287485A (zh) | 抗血管生成化合物 | |
MXPA06005540A (es) | Anticuerpo del receptor anti-igf-i. | |
WO2022142272A1 (zh) | Cldn18.2抗体及其应用 | |
WO1993010221A1 (en) | Chimeric murine/human anti-idiotype monoclonal antibodies | |
AU2013201832A1 (en) | Anti-extended type I glycosphingolipid antibody, derivatives thereof and use | |
TW200526682A (en) | Laminin-5γ2-binding peptides, related compositions, and use thereof |