WO2015161832A1 - Protéine de fusion recombinante à action prolongée d'interféron humain α2b-fc - Google Patents
Protéine de fusion recombinante à action prolongée d'interféron humain α2b-fc Download PDFInfo
- Publication number
- WO2015161832A1 WO2015161832A1 PCT/CN2015/077504 CN2015077504W WO2015161832A1 WO 2015161832 A1 WO2015161832 A1 WO 2015161832A1 CN 2015077504 W CN2015077504 W CN 2015077504W WO 2015161832 A1 WO2015161832 A1 WO 2015161832A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- fusion protein
- long
- human interferon
- recombinant human
- acting recombinant
- Prior art date
Links
- 108020001507 fusion proteins Proteins 0.000 title claims abstract description 84
- 102000037865 fusion proteins Human genes 0.000 title claims abstract description 82
- 108010050904 Interferons Proteins 0.000 title claims abstract description 38
- 102000014150 Interferons Human genes 0.000 title claims abstract description 38
- 229940079322 interferon Drugs 0.000 title claims abstract description 37
- 230000014509 gene expression Effects 0.000 claims abstract description 41
- 230000000840 anti-viral effect Effects 0.000 claims abstract description 14
- 108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 5
- 150000007523 nucleic acids Chemical group 0.000 claims abstract description 5
- 238000002360 preparation method Methods 0.000 claims abstract description 5
- 229940041181 antineoplastic drug Drugs 0.000 claims abstract description 3
- 210000004027 cell Anatomy 0.000 claims description 35
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 16
- 108010022394 Threonine synthase Proteins 0.000 claims description 7
- 102000004419 dihydrofolate reductase Human genes 0.000 claims description 7
- 108010047761 Interferon-alpha Proteins 0.000 claims description 4
- 102000006992 Interferon-alpha Human genes 0.000 claims description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 claims description 4
- 210000004962 mammalian cell Anatomy 0.000 claims description 4
- 241000238631 Hexapoda Species 0.000 claims description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 3
- 239000002246 antineoplastic agent Substances 0.000 claims description 2
- 239000003443 antiviral agent Substances 0.000 claims description 2
- 239000000710 homodimer Substances 0.000 claims description 2
- 102220315697 rs1553622313 Human genes 0.000 claims description 2
- 230000007812 deficiency Effects 0.000 claims 1
- 230000035772 mutation Effects 0.000 claims 1
- 108010079944 Interferon-alpha2b Proteins 0.000 abstract description 6
- 238000001727 in vivo Methods 0.000 abstract description 6
- 102100040018 Interferon alpha-2 Human genes 0.000 abstract description 3
- 230000002035 prolonged effect Effects 0.000 abstract description 3
- 210000004899 c-terminal region Anatomy 0.000 abstract 1
- 108090000623 proteins and genes Proteins 0.000 description 33
- 102000004169 proteins and genes Human genes 0.000 description 29
- 230000000694 effects Effects 0.000 description 11
- 210000004369 blood Anatomy 0.000 description 8
- 239000008280 blood Substances 0.000 description 8
- 229940027941 immunoglobulin g Drugs 0.000 description 8
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 7
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 7
- 125000003275 alpha amino acid group Chemical group 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 239000003814 drug Substances 0.000 description 6
- 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 5
- 238000000338 in vitro Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000003833 cell viability Effects 0.000 description 4
- 230000008030 elimination Effects 0.000 description 4
- 238000003379 elimination reaction Methods 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 229940002988 pegasys Drugs 0.000 description 4
- 108010092853 peginterferon alfa-2a Proteins 0.000 description 4
- 108010092851 peginterferon alfa-2b Proteins 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000007774 longterm Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 229940106366 pegintron Drugs 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 108091006020 Fc-tagged proteins Proteins 0.000 description 2
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000012911 assay medium Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 239000012470 diluted sample Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 230000009465 prokaryotic expression Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000012807 shake-flask culturing Methods 0.000 description 2
- 230000035939 shock Effects 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000012192 staining solution Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 239000013598 vector Substances 0.000 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 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000000419 Chronic Hepatitis B Diseases 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 241000710188 Encephalomyocarditis virus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 208000018522 Gastrointestinal disease Diseases 0.000 description 1
- BCCRXDTUTZHDEU-VKHMYHEASA-N Gly-Ser Chemical group NCC(=O)N[C@@H](CO)C(O)=O BCCRXDTUTZHDEU-VKHMYHEASA-N 0.000 description 1
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 description 1
- 208000005176 Hepatitis C Diseases 0.000 description 1
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 description 1
- 206010022004 Influenza like illness Diseases 0.000 description 1
- 208000007766 Kaposi sarcoma Diseases 0.000 description 1
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 208000000389 T-cell leukemia Diseases 0.000 description 1
- 208000028530 T-cell lymphoblastic leukemia/lymphoma Diseases 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 230000010100 anticoagulation Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000000306 component Substances 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000005138 cryopreservation Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 206010014599 encephalitis Diseases 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000024924 glomerular filtration Effects 0.000 description 1
- 201000009277 hairy cell leukemia Diseases 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- ZFGMDIBRIDKWMY-PASTXAENSA-N heparin Chemical compound CC(O)=N[C@@H]1[C@@H](O)[C@H](O)[C@@H](COS(O)(=O)=O)O[C@@H]1O[C@@H]1[C@@H](C(O)=O)O[C@@H](O[C@H]2[C@@H]([C@@H](OS(O)(=O)=O)[C@@H](O[C@@H]3[C@@H](OC(O)[C@H](OS(O)(=O)=O)[C@H]3O)C(O)=O)O[C@@H]2O)CS(O)(=O)=O)[C@H](O)[C@H]1O ZFGMDIBRIDKWMY-PASTXAENSA-N 0.000 description 1
- 229960001008 heparin sodium Drugs 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 229940098197 human immunoglobulin g Drugs 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 239000012516 mab select resin Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 108010068617 neonatal Fc receptor Proteins 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 206010043554 thrombocytopenia Diseases 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A61K38/21—Interferons [IFN]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/56—IFN-alpha
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Toxicology (AREA)
- Mycology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
L'invention concerne une protéine de fusion d'interféron humain α2b-Fc, l'extrémité C de l'interféron humain α2b étant reliée à l'extrémité N de Fc par un segment de liaison peptidique. La présente invention concerne une séquence d'acide nucléique codant pour la protéine de fusion et un système d'expression eucaryote exprimant la protéine de fusion. L'invention concerne également une utilisation de la protéine de fusion dans la préparation d'un médicament antitumoral ou antiviral. La protéine de fusion présente une activité antivirale améliorée et une demi-vie in vivo prolongée.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201410170133.3 | 2014-04-25 | ||
CN201410170133 | 2014-04-25 |
Publications (2)
Publication Number | Publication Date |
---|---|
WO2015161832A1 true WO2015161832A1 (fr) | 2015-10-29 |
WO2015161832A8 WO2015161832A8 (fr) | 2016-03-17 |
Family
ID=54331779
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/CN2015/077504 WO2015161832A1 (fr) | 2014-04-25 | 2015-04-27 | Protéine de fusion recombinante à action prolongée d'interféron humain α2b-fc |
Country Status (1)
Country | Link |
---|---|
WO (1) | WO2015161832A1 (fr) |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1206350A (zh) * | 1995-12-28 | 1999-01-27 | 泰诺克斯生物系统公司 | 具有经非免疫原性肽连接在一起的干扰素α和免疫球蛋白Fc的杂合体 |
-
2015
- 2015-04-27 WO PCT/CN2015/077504 patent/WO2015161832A1/fr active Application Filing
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1206350A (zh) * | 1995-12-28 | 1999-01-27 | 泰诺克斯生物系统公司 | 具有经非免疫原性肽连接在一起的干扰素α和免疫球蛋白Fc的杂合体 |
Non-Patent Citations (1)
Title |
---|
WANG, LEI ET AL.: "Enhanced Circulation Half-life for Human IFNa2b and IgG Fc Fusion Protein", CHINESE JOURNAL OF BIOTECHNOLOGY, vol. 24, no. 1, 25 January 2008 (2008-01-25), XP008134213 * |
Also Published As
Publication number | Publication date |
---|---|
WO2015161832A8 (fr) | 2016-03-17 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US20210177983A1 (en) | SINGLE CHAIN Fc FUSION PROTEINS | |
CN107759697B (zh) | 制备融合蛋白的方法 | |
KR102493543B1 (ko) | 자가면역 질환의 치료를 위한 조절 t 세포를 선택적으로 활성화시키는 분자 | |
JP6923115B2 (ja) | 高グリコシル化ヒト血液凝固第viii因子の融合タンパク質、その調製方法、および使用 | |
JP2019001793A (ja) | 免疫グロブリンFc変異体 | |
JP2019507589A (ja) | 自己免疫疾患の治療のために制御性t細胞を選択的に活性化する分子 | |
WO2011060583A1 (fr) | Protéine non naturelle de type collagène et son utilisation | |
US20210300995A1 (en) | Long-acting fibronectin type III domain fusion protein | |
WO2015062349A1 (fr) | Protéine de fusion fc-hormone folliculostimulante humaine recombinée à longue durée d'action | |
CN104293834A (zh) | GLP-1或其类似物与抗体Fc片段融合蛋白的制备方法 | |
EP2975062B1 (fr) | Préparation et utilisation d'une protéine de fusion dimérisée | |
Ji et al. | Intact bioactivities and improved pharmacokinetic of the SL335-IFN-β-1a fusion protein that created by genetic fusion of SL335, a human anti-serum albumin fab, and human interferon-β | |
WO2015161832A1 (fr) | Protéine de fusion recombinante à action prolongée d'interféron humain α2b-fc | |
US20220144903A1 (en) | Recombinant ccn domain proteins and fusion proteins | |
EP3307304B1 (fr) | Protéines de fusion à base d'immunoglobulines et leurs utilisations | |
CN116621989A (zh) | 一种多聚化结构单体及其用途 | |
TW201714894A (zh) | 免疫球蛋白融合蛋白質 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
121 | Ep: the epo has been informed by wipo that ep was designated in this application |
Ref document number: 15783016 Country of ref document: EP Kind code of ref document: A1 |
|
NENP | Non-entry into the national phase |
Ref country code: DE |
|
32PN | Ep: public notification in the ep bulletin as address of the adressee cannot be established |
Free format text: NOTING OF LOSS OF RIGHTS PURSUANT TO RULE 112(1) EPC (EPO FORM 1205A DATED 23/03/2017) |
|
122 | Ep: pct application non-entry in european phase |
Ref document number: 15783016 Country of ref document: EP Kind code of ref document: A1 |