NO321777B1 - Hybridproteiner som danner heterodimerer, DNA, ekspresjonsvektorer og vertsceller som koder for eller uttrykker disse, samt farmasoytisk sammensetning og anvendelse av hybridproteinene for fremstilling av et medikament for behandling av humane lidelser med behov for inhibering av TNF. - Google Patents
Hybridproteiner som danner heterodimerer, DNA, ekspresjonsvektorer og vertsceller som koder for eller uttrykker disse, samt farmasoytisk sammensetning og anvendelse av hybridproteinene for fremstilling av et medikament for behandling av humane lidelser med behov for inhibering av TNF. Download PDFInfo
- Publication number
- NO321777B1 NO321777B1 NO19983799A NO983799A NO321777B1 NO 321777 B1 NO321777 B1 NO 321777B1 NO 19983799 A NO19983799 A NO 19983799A NO 983799 A NO983799 A NO 983799A NO 321777 B1 NO321777 B1 NO 321777B1
- Authority
- NO
- Norway
- Prior art keywords
- hybrid protein
- protein according
- sequence
- receptor
- hcg
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 113
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 104
- 239000013604 expression vector Substances 0.000 title claims abstract description 13
- 239000008194 pharmaceutical composition Substances 0.000 title claims abstract description 6
- 239000003814 drug Substances 0.000 title claims description 7
- 241000282414 Homo sapiens Species 0.000 title claims description 6
- 229940079593 drug Drugs 0.000 title claims description 6
- 230000005764 inhibitory process Effects 0.000 title claims description 6
- 102100040296 TATA-box-binding protein Human genes 0.000 claims abstract description 39
- 108020004414 DNA Proteins 0.000 claims abstract description 25
- 101000891654 Homo sapiens TATA-box-binding protein Proteins 0.000 claims abstract description 22
- 101001125540 Homo sapiens 26S proteasome regulatory subunit 6A Proteins 0.000 claims abstract description 21
- 238000000034 method Methods 0.000 claims abstract description 17
- 239000003446 ligand Substances 0.000 claims abstract description 15
- 239000000833 heterodimer Substances 0.000 claims abstract description 9
- 239000000539 dimer Substances 0.000 claims abstract description 8
- 101000653510 Homo sapiens TATA box-binding protein-like 2 Proteins 0.000 claims abstract description 4
- 102100030631 TATA box-binding protein-like 2 Human genes 0.000 claims abstract description 4
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 6
- 210000004027 cell Anatomy 0.000 claims description 61
- 239000012634 fragment Substances 0.000 claims description 33
- 102000005962 receptors Human genes 0.000 claims description 31
- 108020003175 receptors Proteins 0.000 claims description 31
- 238000004519 manufacturing process Methods 0.000 claims description 12
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 11
- 238000003776 cleavage reaction Methods 0.000 claims description 9
- 229940088597 hormone Drugs 0.000 claims description 9
- 230000007017 scission Effects 0.000 claims description 9
- 102000004190 Enzymes Human genes 0.000 claims description 8
- 108090000790 Enzymes Proteins 0.000 claims description 8
- 229940088598 enzyme Drugs 0.000 claims description 8
- 239000005556 hormone Substances 0.000 claims description 8
- 102000053602 DNA Human genes 0.000 claims description 7
- 102000008175 FSH Receptors Human genes 0.000 claims description 6
- 108010060374 FSH Receptors Proteins 0.000 claims description 6
- 108090000190 Thrombin Proteins 0.000 claims description 5
- 108020001756 ligand binding domains Proteins 0.000 claims description 5
- 210000001672 ovary Anatomy 0.000 claims description 5
- 229960004072 thrombin Drugs 0.000 claims description 5
- 102000001895 Gonadotropin Receptors Human genes 0.000 claims description 4
- 108010040490 Gonadotropin Receptors Proteins 0.000 claims description 4
- 230000004071 biological effect Effects 0.000 claims description 4
- 230000000717 retained effect Effects 0.000 claims description 4
- 102000006771 Gonadotropins Human genes 0.000 claims description 3
- 108010086677 Gonadotropins Proteins 0.000 claims description 3
- 230000001588 bifunctional effect Effects 0.000 claims description 3
- 239000002622 gonadotropin Substances 0.000 claims description 3
- 238000002360 preparation method Methods 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 2
- 230000003325 follicular Effects 0.000 claims description 2
- 230000006698 induction Effects 0.000 claims description 2
- 239000000893 inhibin Substances 0.000 claims description 2
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 claims description 2
- 230000035800 maturation Effects 0.000 claims description 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 1
- 125000000539 amino acid group Chemical group 0.000 claims 1
- 210000004899 c-terminal region Anatomy 0.000 claims 1
- 238000002955 isolation Methods 0.000 claims 1
- 230000014509 gene expression Effects 0.000 abstract description 8
- 108090001005 Interleukin-6 Proteins 0.000 abstract description 2
- 102100026720 Interferon beta Human genes 0.000 abstract 1
- 108090000467 Interferon-beta Proteins 0.000 abstract 1
- 101710113649 Thyroid peroxidase Proteins 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 72
- 102000011022 Chorionic Gonadotropin Human genes 0.000 description 31
- 108010062540 Chorionic Gonadotropin Proteins 0.000 description 31
- 229940084986 human chorionic gonadotropin Drugs 0.000 description 30
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 21
- 102100040247 Tumor necrosis factor Human genes 0.000 description 21
- 239000013612 plasmid Substances 0.000 description 19
- 101710145783 TATA-box-binding protein Proteins 0.000 description 18
- 230000000694 effects Effects 0.000 description 16
- 230000004927 fusion Effects 0.000 description 16
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 14
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 14
- 239000002609 medium Substances 0.000 description 12
- 239000013598 vector Substances 0.000 description 12
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 11
- 238000006243 chemical reaction Methods 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- 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 10
- 239000012091 fetal bovine serum Substances 0.000 description 10
- 239000002953 phosphate buffered saline Substances 0.000 description 10
- 239000000047 product Substances 0.000 description 10
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 9
- 238000001890 transfection Methods 0.000 description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 description 8
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 8
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 8
- 238000010276 construction Methods 0.000 description 8
- 108020001507 fusion proteins Proteins 0.000 description 8
- 102000037865 fusion proteins Human genes 0.000 description 8
- 150000001413 amino acids Chemical group 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 6
- 108060003951 Immunoglobulin Proteins 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 102000018358 immunoglobulin Human genes 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 230000001681 protective effect Effects 0.000 description 6
- 102000002265 Human Growth Hormone Human genes 0.000 description 5
- 108010000521 Human Growth Hormone Proteins 0.000 description 5
- 239000000854 Human Growth Hormone Substances 0.000 description 5
- 239000011543 agarose gel Substances 0.000 description 5
- 102000023732 binding proteins Human genes 0.000 description 5
- 108091008324 binding proteins Proteins 0.000 description 5
- 238000004166 bioassay Methods 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 230000002776 aggregation Effects 0.000 description 4
- 238000004220 aggregation Methods 0.000 description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 4
- 231100000135 cytotoxicity Toxicity 0.000 description 4
- 230000003013 cytotoxicity Effects 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 238000004520 electroporation Methods 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108010003189 recombinant human tumor necrosis factor-binding protein-1 Proteins 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 230000010473 stable expression Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 230000002103 transcriptional effect Effects 0.000 description 3
- 230000010474 transient expression Effects 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 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 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 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 2
- 238000003149 assay kit Methods 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- 238000006471 dimerization reaction Methods 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 230000009144 enzymatic modification Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 238000003306 harvesting Methods 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000000463 material Substances 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
- 229960000485 methotrexate Drugs 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 230000016087 ovulation Effects 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 230000004850 protein–protein interaction Effects 0.000 description 2
- 239000012264 purified product Substances 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 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 2
- 239000013638 trimer Substances 0.000 description 2
- 208000030507 AIDS Diseases 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 241000701822 Bovine papillomavirus Species 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 108010041884 CD4 Immunoadhesins Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000003864 Human Follicle Stimulating Hormone Human genes 0.000 description 1
- 108010082302 Human Follicle Stimulating Hormone Proteins 0.000 description 1
- -1 IFN-B Proteins 0.000 description 1
- 102000016844 Immunoglobulin-like domains Human genes 0.000 description 1
- 108050006430 Immunoglobulin-like domains Proteins 0.000 description 1
- 102000007438 Interferon alpha-beta Receptor Human genes 0.000 description 1
- 108010086140 Interferon alpha-beta Receptor Proteins 0.000 description 1
- 102000004889 Interleukin-6 Human genes 0.000 description 1
- 102000010781 Interleukin-6 Receptors Human genes 0.000 description 1
- 108010038501 Interleukin-6 Receptors Proteins 0.000 description 1
- 102100037792 Interleukin-6 receptor subunit alpha Human genes 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 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
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000609499 Palicourea Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101710156592 Putative TATA-binding protein pB263R Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 101800001271 Surface protein Proteins 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 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 1
- 230000009471 action Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 230000003698 anagen phase 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
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 201000008275 breast carcinoma Diseases 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000002771 cell marker Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000001143 conditioned effect Effects 0.000 description 1
- 230000003750 conditioning effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 238000003235 crystal violet staining Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000002784 cytotoxicity assay Methods 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000004720 fertilization Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229940094892 gonadotropins Drugs 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 102000045334 human TBP Human genes 0.000 description 1
- 102000057041 human TNF Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect 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
- 230000002452 interceptive effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000006525 intracellular process Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 150000007523 nucleic acids Chemical group 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 230000002611 ovarian Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 235000020030 perry Nutrition 0.000 description 1
- 150000008300 phosphoramidites Chemical class 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000003153 stable transfection Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C209/00—Preparation of compounds containing amino groups bound to a carbon skeleton
- C07C209/04—Preparation of compounds containing amino groups bound to a carbon skeleton by substitution of functional groups by amino groups
- C07C209/22—Preparation of compounds containing amino groups bound to a carbon skeleton by substitution of functional groups by amino groups by substitution of other functional groups
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- 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
- A61K38/22—Hormones
- A61K38/24—Follicle-stimulating hormone [FSH]; Chorionic gonadotropins, e.g. HCG; Luteinising hormone [LH]; Thyroid-stimulating hormone [TSH]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
- A61P15/08—Drugs for genital or sexual disorders; Contraceptives for gonadal disorders or for enhancing fertility, e.g. inducers of ovulation or of spermatogenesis
-
- 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
- A61P5/00—Drugs for disorders of the endocrine system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/06—Drugs for disorders of the endocrine system of the anterior pituitary hormones, e.g. TSH, ACTH, FSH, LH, PRL, GH
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/14—Drugs for disorders of the endocrine system of the thyroid hormones, e.g. T3, T4
- A61P5/16—Drugs for disorders of the endocrine system of the thyroid hormones, e.g. T3, T4 for decreasing, blocking or antagonising the activity of the thyroid hormones
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/59—Follicle-stimulating hormone [FSH]; Chorionic gonadotropins, e.g.hCG [human chorionic gonadotropin]; Luteinising hormone [LH]; Thyroid-stimulating hormone [TSH]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- 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
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Endocrinology (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Reproductive Health (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Immunology (AREA)
- Diabetes (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Cell Biology (AREA)
- Gynecology & Obstetrics (AREA)
- Pregnancy & Childbirth (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US1193696P | 1996-02-20 | 1996-02-20 | |
PCT/US1997/002315 WO1997030161A1 (en) | 1996-02-20 | 1997-02-20 | Hybrid proteins which form heterodimers |
Publications (3)
Publication Number | Publication Date |
---|---|
NO983799D0 NO983799D0 (no) | 1998-08-19 |
NO983799L NO983799L (no) | 1998-10-19 |
NO321777B1 true NO321777B1 (no) | 2006-07-03 |
Family
ID=21752599
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19983799A NO321777B1 (no) | 1996-02-20 | 1998-08-19 | Hybridproteiner som danner heterodimerer, DNA, ekspresjonsvektorer og vertsceller som koder for eller uttrykker disse, samt farmasoytisk sammensetning og anvendelse av hybridproteinene for fremstilling av et medikament for behandling av humane lidelser med behov for inhibering av TNF. |
Country Status (25)
Country | Link |
---|---|
US (5) | US6193972B1 (hu) |
EP (1) | EP0894141B1 (hu) |
JP (2) | JP4140927B2 (hu) |
KR (1) | KR100369985B1 (hu) |
CN (1) | CN1261579C (hu) |
AT (1) | ATE295887T1 (hu) |
AU (1) | AU706504B2 (hu) |
BG (1) | BG64510B1 (hu) |
BR (1) | BR9707589A (hu) |
CA (1) | CA2245877C (hu) |
CZ (1) | CZ291212B6 (hu) |
DE (1) | DE69733309T2 (hu) |
DK (1) | DK0894141T3 (hu) |
EA (1) | EA002474B1 (hu) |
EE (1) | EE04025B1 (hu) |
ES (1) | ES2241040T3 (hu) |
HU (1) | HUP9900619A3 (hu) |
IL (1) | IL125864A (hu) |
NO (1) | NO321777B1 (hu) |
NZ (1) | NZ331539A (hu) |
PL (1) | PL187400B1 (hu) |
PT (1) | PT894141E (hu) |
SK (1) | SK282326B6 (hu) |
UA (1) | UA52646C2 (hu) |
WO (1) | WO1997030161A1 (hu) |
Families Citing this family (18)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
NZ331539A (en) * | 1996-02-20 | 2000-01-28 | Applied Research Systems | Hybrid proteins from two coexpressed receptors to form a heterodimer |
US6635740B1 (en) * | 1997-03-27 | 2003-10-21 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Ligand/lytic peptide compositions and methods of use |
CA2301846A1 (en) | 1997-09-04 | 1999-03-11 | Gryphon Sciences | Modular protein libraries and methods of preparation |
EA006605B1 (ru) * | 2000-02-22 | 2006-02-24 | Апплайд Резеч Системз Арс Холдинг Н.В. | СПОСОБ ОЧИСТКИ РЕКОМБИНАНТНОГО чХГ |
US20030228600A1 (en) * | 2000-07-14 | 2003-12-11 | Eppendorf 5 Prime, Inc. | DNA isolation method and kit |
IL147414A0 (en) * | 2001-12-31 | 2002-08-14 | Yeda Res & Dev | Ifnar2 mutants, their production and use |
US20030157091A1 (en) * | 2002-02-14 | 2003-08-21 | Dyax Corporation | Multi-functional proteins |
DE10247755B4 (de) * | 2002-10-14 | 2006-01-19 | Pfizenmaier, Klaus, Prof. Dr. | Selektive, lokale Aktivierung von Mitgliedern der TNF-Rezeptorfamilie durch systemisch inaktive nicht-Antikörper-TNF-Liganden-Fusionsproteine |
AU2005207960A1 (en) * | 2004-01-28 | 2005-08-11 | Syntonix Pharmaceuticals, Inc. | Heterodimeric follicle stimulating hormone-Fc (FSH-Fc) fusion proteins for the treatment of infertility |
JP2008525002A (ja) | 2004-12-23 | 2008-07-17 | ラボラトワール セローノ ソシエテ アノニム | Bcmaポリペプチド及びその使用 |
PT1885753E (pt) | 2005-06-03 | 2011-10-06 | Ares Trading Sa | Produção de proteína recombinante de ligação a il-18 |
CN108129573B (zh) * | 2007-09-21 | 2021-10-08 | 加利福尼亚大学董事会 | 被导靶的干扰素显示强的细胞凋亡和抗肿瘤活性 |
EP3009513A1 (en) * | 2008-02-01 | 2016-04-20 | Chromocell Corporation | Novel cell lines and methods |
CN102002495B (zh) * | 2009-08-31 | 2012-07-18 | 成都蓉生药业有限责任公司 | 用于表达异二聚体糖蛋白激素的表达框、表达载体及制备方法 |
SG10201602371VA (en) * | 2011-03-25 | 2016-04-28 | Glenmark Pharmaceuticals Sa | Hetero-dimeric immunoglobulins |
ES2771478T3 (es) | 2013-02-18 | 2020-07-06 | Vegenics Pty Ltd | Moléculas de unión a ligando y usos de las mismas |
JP7439372B2 (ja) * | 2018-06-21 | 2024-02-28 | シャタック ラボ,インコーポレイテッド | ヘテロ二量体タンパク質及びその使用 |
US20220227837A1 (en) * | 2019-05-24 | 2022-07-21 | Proviva Therapeutics (Hong Kong) Limited | Il-2 compositions and methods of use thereof |
Family Cites Families (13)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0721983A1 (en) * | 1988-01-22 | 1996-07-17 | ZymoGenetics, Inc. | Methods of producing biologically active peptide dimers |
US5705478A (en) * | 1989-02-21 | 1998-01-06 | Washington University | Covalently linked β subunits of the glycoprotein hormones as antagonists |
US6225449B1 (en) * | 1991-10-04 | 2001-05-01 | Washington University | Hormone analogs with multiple CTP extensions |
US5116964A (en) * | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
AU5355790A (en) * | 1989-04-19 | 1990-11-16 | Cetus Corporation | Multifunctional m-csf proteins and genes encoding therefor |
US5650150A (en) * | 1990-11-09 | 1997-07-22 | Gillies; Stephen D. | Recombinant antibody cytokine fusion proteins |
IL99120A0 (en) * | 1991-08-07 | 1992-07-15 | Yeda Res & Dev | Multimers of the soluble forms of tnf receptors,their preparation and pharmaceutical compositions containing them |
US5932448A (en) * | 1991-11-29 | 1999-08-03 | Protein Design Labs., Inc. | Bispecific antibody heterodimers |
ATE242322T1 (de) | 1992-03-30 | 2003-06-15 | Immunex Corp | Fusionsprotein , das zwei rezeptoren des tumornekrose-faktors enthält |
US5447851B1 (en) * | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
IL111125A0 (en) | 1994-05-11 | 1994-12-29 | Yeda Res & Dev | Soluble oligomeric tnf/ngf super family ligand receptors and their use |
NZ331539A (en) * | 1996-02-20 | 2000-01-28 | Applied Research Systems | Hybrid proteins from two coexpressed receptors to form a heterodimer |
US6194177B1 (en) * | 1996-02-20 | 2001-02-27 | Applied Research Systems Ars Holding N.V. | DNA encoding a hybrid heterodimeric protein |
-
1997
- 1997-02-20 NZ NZ331539A patent/NZ331539A/xx unknown
- 1997-02-20 US US08/804,166 patent/US6193972B1/en not_active Expired - Lifetime
- 1997-02-20 CN CNB971924112A patent/CN1261579C/zh not_active Expired - Fee Related
- 1997-02-20 EP EP97906604A patent/EP0894141B1/en not_active Expired - Lifetime
- 1997-02-20 IL IL125864A patent/IL125864A/en not_active IP Right Cessation
- 1997-02-20 CZ CZ19982644A patent/CZ291212B6/cs not_active IP Right Cessation
- 1997-02-20 WO PCT/US1997/002315 patent/WO1997030161A1/en active IP Right Grant
- 1997-02-20 EE EE9800256A patent/EE04025B1/xx not_active IP Right Cessation
- 1997-02-20 EA EA199800744A patent/EA002474B1/ru not_active IP Right Cessation
- 1997-02-20 KR KR10-1998-0706215A patent/KR100369985B1/ko not_active IP Right Cessation
- 1997-02-20 PL PL97328454A patent/PL187400B1/pl not_active IP Right Cessation
- 1997-02-20 DE DE69733309T patent/DE69733309T2/de not_active Expired - Lifetime
- 1997-02-20 ES ES97906604T patent/ES2241040T3/es not_active Expired - Lifetime
- 1997-02-20 HU HU9900619A patent/HUP9900619A3/hu unknown
- 1997-02-20 JP JP52949897A patent/JP4140927B2/ja not_active Expired - Fee Related
- 1997-02-20 CA CA2245877A patent/CA2245877C/en not_active Expired - Fee Related
- 1997-02-20 AT AT97906604T patent/ATE295887T1/de not_active IP Right Cessation
- 1997-02-20 DK DK97906604T patent/DK0894141T3/da active
- 1997-02-20 UA UA98094928A patent/UA52646C2/uk unknown
- 1997-02-20 BR BR9707589-2A patent/BR9707589A/pt not_active Application Discontinuation
- 1997-02-20 PT PT97906604T patent/PT894141E/pt unknown
- 1997-02-20 AU AU21252/97A patent/AU706504B2/en not_active Ceased
- 1997-02-20 SK SK1148-98A patent/SK282326B6/sk unknown
-
1998
- 1998-08-19 NO NO19983799A patent/NO321777B1/no unknown
- 1998-08-20 BG BG102705A patent/BG64510B1/bg unknown
-
2001
- 2001-01-09 US US09/756,186 patent/US6663867B2/en not_active Expired - Fee Related
-
2003
- 2003-12-01 US US10/724,226 patent/US7291339B2/en not_active Expired - Fee Related
-
2007
- 2007-07-10 JP JP2007181534A patent/JP2008019258A/ja active Pending
- 2007-09-26 US US11/861,835 patent/US20100075402A1/en not_active Abandoned
- 2007-10-30 US US11/929,292 patent/US20090240039A1/en not_active Abandoned
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US20090240039A1 (en) | Polypeptide fusion | |
US6194177B1 (en) | DNA encoding a hybrid heterodimeric protein | |
JP6995151B2 (ja) | synTacポリペプチド及びその使用 | |
CN1358198A (zh) | 嵌合多肽、其产生方法及应用 | |
AU6064400A (en) | Fusion peptides comprising a peptide ligand domain and a multimerization domain | |
JP2007519611A (ja) | 分泌された三量体受容体類似体及び生物学的活性融合タンパク質を製造するための方法及び組成物 | |
CN113667004A (zh) | 一种白介素2突变体 | |
EP1557432B1 (en) | Hybrid proteins which form heterodimers | |
Ashkenazi et al. | Immunoadhesins: an alternative to human monoclonal antibodies | |
MOOSMAYER et al. | Characterization of different soluble TNF receptor (TNFR80) derivatives: positive influence of the intracellular domain on receptor/ligand interaction and TNF neutralization capacity | |
Lobel et al. | Expression and Characterization of recombinant β-subunit hCG homodimer | |
NO322479B1 (no) | IL-6 mutein, fremgangsmate for fremstilling av muteinet, DNA-molekyl som koder for muteinet, samt vektor og vertscelle som inneholder DNA-molekylet og farmasoytisk blanding som omfatter muteinet. | |
Lin et al. | Addition of an N-terminal dimerization domain promotes assembly of hCG analogs: implications for subunit combination and structure–function analysis | |
Campbell et al. | Assembly and expression of a synthetic gene encoding the bovine glycoprotein hormone α-subunit | |
MOOSMAYER | Receptor/Ligand Interaction and TNF Neutralization Capacity |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
CREP | Change of representative |
Representative=s name: ONSAGERS AS, POSTBOKS 6963 ST OLAVS PLASS, 0130 OS |
|
CREP | Change of representative |
Representative=s name: ZACCO NORWAY AS, POSTBOKS 2003 VIKA, 0125 OSLO, NO |