BR112020015238A2 - Gene precursor otimizado por códon e gene de peptídeo sinal de análogo de insulina humana - Google Patents
Gene precursor otimizado por códon e gene de peptídeo sinal de análogo de insulina humana Download PDFInfo
- Publication number
- BR112020015238A2 BR112020015238A2 BR112020015238-2A BR112020015238A BR112020015238A2 BR 112020015238 A2 BR112020015238 A2 BR 112020015238A2 BR 112020015238 A BR112020015238 A BR 112020015238A BR 112020015238 A2 BR112020015238 A2 BR 112020015238A2
- Authority
- BR
- Brazil
- Prior art keywords
- nucleic acid
- acid molecule
- seq
- human insulin
- precursor
- Prior art date
Links
- 239000002243 precursor Substances 0.000 title claims abstract description 78
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical class C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 title claims abstract description 72
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 23
- 108090000623 proteins and genes Proteins 0.000 title abstract description 40
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 98
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 93
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 93
- 108010076504 Protein Sorting Signals Proteins 0.000 claims abstract description 28
- 241000235058 Komagataella pastoris Species 0.000 claims abstract description 16
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 11
- 239000013598 vector Substances 0.000 claims description 27
- 101000976075 Homo sapiens Insulin Proteins 0.000 claims description 24
- 239000013604 expression vector Substances 0.000 claims description 16
- 150000001413 amino acids Chemical group 0.000 claims description 15
- 229920001184 polypeptide Polymers 0.000 claims description 14
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 14
- 101800001707 Spacer peptide Proteins 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 10
- 238000012545 processing Methods 0.000 claims description 9
- 238000012217 deletion Methods 0.000 claims description 7
- 230000037430 deletion Effects 0.000 claims description 7
- 238000004519 manufacturing process Methods 0.000 claims description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 6
- 239000004472 Lysine Substances 0.000 claims description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 4
- 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 description 3
- 238000006467 substitution reaction Methods 0.000 claims description 3
- 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 claims description 2
- 239000002253 acid Substances 0.000 claims 1
- 230000009465 prokaryotic expression Effects 0.000 claims 1
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical class N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 abstract description 86
- 230000014509 gene expression Effects 0.000 abstract description 29
- 230000003248 secreting effect Effects 0.000 abstract description 7
- 239000004026 insulin derivative Substances 0.000 abstract description 5
- 230000004927 fusion Effects 0.000 abstract 1
- 102000004877 Insulin Human genes 0.000 description 40
- 108090001061 Insulin Proteins 0.000 description 40
- 229940125396 insulin Drugs 0.000 description 40
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 18
- 210000004027 cell Anatomy 0.000 description 17
- 108020004705 Codon Proteins 0.000 description 14
- 241000894006 Bacteria Species 0.000 description 9
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 9
- 238000005457 optimization Methods 0.000 description 9
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical group C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 8
- 230000001580 bacterial effect Effects 0.000 description 8
- 239000012634 fragment Substances 0.000 description 8
- 238000003259 recombinant expression Methods 0.000 description 7
- 239000002609 medium Substances 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 241001506991 Komagataella phaffii GS115 Species 0.000 description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 238000009776 industrial production Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 108010025188 Alcohol oxidase Proteins 0.000 description 2
- 102100036826 Aldehyde oxidase Human genes 0.000 description 2
- 101000928314 Homo sapiens Aldehyde oxidase Proteins 0.000 description 2
- 101500025354 Homo sapiens Insulin B chain Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 241000235648 Pichia Species 0.000 description 2
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 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
- 229960000723 ampicillin Drugs 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000003000 inclusion body Anatomy 0.000 description 2
- 150000004668 long chain fatty acids Chemical class 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 108010005636 polypeptide C Proteins 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 239000007222 ypd medium Substances 0.000 description 2
- 208000010444 Acidosis Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108010075254 C-Peptide Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 208000007976 Ketosis Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 230000007950 acidosis Effects 0.000 description 1
- 208000026545 acidosis disease Diseases 0.000 description 1
- -1 antibody Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000004153 glucose metabolism Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 150000002576 ketones Chemical class 0.000 description 1
- 230000004140 ketosis Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
Classifications
-
- 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
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
-
- 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
- C07K14/62—Insulins
-
- 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
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
- C12N15/815—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts for yeasts other than Saccharomyces
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/645—Fungi ; Processes using fungi
- C12R2001/84—Pichia
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201810131794 | 2018-02-09 | ||
| CN201810131794.3 | 2018-02-09 | ||
| PCT/CN2019/074384 WO2019154311A1 (zh) | 2018-02-09 | 2019-02-01 | 一种密码子优化的人胰岛素类似物前体基因和信号肽基因 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| BR112020015238A2 true BR112020015238A2 (pt) | 2020-12-29 |
Family
ID=67548783
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BR112020015238-2A BR112020015238A2 (pt) | 2018-02-09 | 2019-02-01 | Gene precursor otimizado por códon e gene de peptídeo sinal de análogo de insulina humana |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US20210032307A1 (https=) |
| EP (1) | EP3750998A4 (https=) |
| JP (1) | JP2021513330A (https=) |
| KR (1) | KR20200119237A (https=) |
| CN (1) | CN111094572B (https=) |
| AU (1) | AU2019218315A1 (https=) |
| BR (1) | BR112020015238A2 (https=) |
| CA (1) | CA3086618A1 (https=) |
| MX (1) | MX2020007929A (https=) |
| RU (1) | RU2020128190A (https=) |
| TW (1) | TW201934752A (https=) |
| WO (1) | WO2019154311A1 (https=) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111560379B (zh) * | 2020-05-26 | 2022-09-13 | 北京惠之衡生物科技有限公司 | 密码子优化的门冬胰岛素前体基因、重组载体、基因工程菌及其应用 |
| CN116751817B (zh) * | 2023-05-29 | 2024-07-09 | 广东东阳光药业股份有限公司 | 检测胰岛素或其类似物的生物学活性的方法及试剂盒 |
| CN117384275B (zh) * | 2023-12-13 | 2024-03-15 | 北京科为博生物科技有限公司 | 胰岛素样生长因子突变体igf1m及其应用 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1340772C (en) * | 1987-12-30 | 1999-09-28 | Patricia Tekamp-Olson | Expression and secretion of heterologous protiens in yeast employing truncated alpha-factor leader sequences |
| EP1132404A3 (en) | 1993-09-17 | 2002-03-27 | Novo Nordisk A/S | Acylated insulin |
| US5639642A (en) * | 1994-06-16 | 1997-06-17 | Novo Nordisk A/S | Synthetic leader peptide sequences |
| ES2258797T3 (es) * | 1996-12-20 | 2006-09-01 | Novo Nordisk A/S | Proteinas con extension n-terminal expresadas en la levadura. |
| CN1302333A (zh) * | 1998-01-23 | 2001-07-04 | 诺沃挪第克公司 | 在酵母中制备目的多肽的方法 |
| AR025646A1 (es) * | 2000-09-13 | 2002-12-04 | Beta Lab Sa | Cepa de levaduras metilotroficas recombinantes productoras de un precursor de insulina, construcciones de adn y metodo para obtener la cepa. |
| PL1633876T3 (pl) * | 2003-06-17 | 2009-01-30 | Sembiosys Genetics Inc | Sposoby wytwarzania insuliny w roślinach |
| CA2531988C (en) | 2003-08-05 | 2016-06-28 | Novo Nordisk A/S | Novel insulin derivatives |
| CN1873006A (zh) * | 2005-05-30 | 2006-12-06 | 上海新生源医药研究有限公司 | 一种重组人胰岛素原的生产方法 |
| MY161552A (en) * | 2009-03-12 | 2017-04-28 | Bigtec Private Ltd | A polynucleotide and polypeptide sequence and methods thereof |
| AR087433A1 (es) * | 2011-08-08 | 2014-03-26 | Merck Sharp & Dohme | Analogos de insulina n-glicosilados |
| KR20140104994A (ko) * | 2011-12-15 | 2014-08-29 | 샹하이 헨그루이 파마수티컬 컴퍼니 리미티드 | 인간 인슐린 유사체 및 이의 아실화 유도체 |
| WO2018024186A1 (zh) | 2016-08-02 | 2018-02-08 | 江苏恒瑞医药股份有限公司 | 一种人胰岛素或其类似物的酰化衍生物 |
-
2019
- 2019-02-01 CN CN201980004477.8A patent/CN111094572B/zh active Active
- 2019-02-01 JP JP2020541883A patent/JP2021513330A/ja not_active Withdrawn
- 2019-02-01 KR KR1020207020915A patent/KR20200119237A/ko not_active Withdrawn
- 2019-02-01 WO PCT/CN2019/074384 patent/WO2019154311A1/zh not_active Ceased
- 2019-02-01 MX MX2020007929A patent/MX2020007929A/es unknown
- 2019-02-01 CA CA3086618A patent/CA3086618A1/en active Pending
- 2019-02-01 TW TW108104187A patent/TW201934752A/zh unknown
- 2019-02-01 US US16/967,117 patent/US20210032307A1/en not_active Abandoned
- 2019-02-01 EP EP19751736.0A patent/EP3750998A4/en not_active Withdrawn
- 2019-02-01 RU RU2020128190A patent/RU2020128190A/ru unknown
- 2019-02-01 AU AU2019218315A patent/AU2019218315A1/en not_active Abandoned
- 2019-02-01 BR BR112020015238-2A patent/BR112020015238A2/pt not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| JP2021513330A (ja) | 2021-05-27 |
| EP3750998A4 (en) | 2022-02-23 |
| RU2020128190A3 (https=) | 2022-03-09 |
| MX2020007929A (es) | 2020-10-01 |
| CA3086618A1 (en) | 2019-08-15 |
| KR20200119237A (ko) | 2020-10-19 |
| TW201934752A (zh) | 2019-09-01 |
| AU2019218315A1 (en) | 2020-07-09 |
| CN111094572B (zh) | 2023-04-04 |
| US20210032307A1 (en) | 2021-02-04 |
| CN111094572A (zh) | 2020-05-01 |
| WO2019154311A1 (zh) | 2019-08-15 |
| RU2020128190A (ru) | 2022-03-09 |
| EP3750998A1 (en) | 2020-12-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN108350056B (zh) | 新型胰岛素类似物及其用途 | |
| WO2022012020A1 (zh) | Glp-1类似物多肽的制备方法及在ⅱ型糖尿病中应用 | |
| BR112020015238A2 (pt) | Gene precursor otimizado por códon e gene de peptídeo sinal de análogo de insulina humana | |
| JP5808671B2 (ja) | 機能グループｉｉ莢膜遺伝子クラスターを有しないｅ．ｃｏｌｉｂｌ２１株 | |
| WO2020187271A1 (zh) | 利用双质粒系统在蛋白中引入非天然氨基酸 | |
| WO2023125178A1 (zh) | 一种融合蛋白及其制备司美格鲁肽中间体多肽的方法 | |
| JP2022528151A (ja) | 蛍光タンパク質フラグメントを含む融合タンパク質およびその用途 | |
| CN111378027A (zh) | 一种索玛鲁肽前体的制备方法 | |
| CN115029404B (zh) | 用于lpp单基因敲除或突变的大肠杆菌分泌表达短肽类蛋白的发酵培养基及应用 | |
| CN113735959A (zh) | 一种新型治疗nash的fgf类似物 | |
| KR20080039879A (ko) | Pdi를 융합파트너로 이용한 수용성 및 활성형 재조합단백질의 제조방법 | |
| EP3904520A1 (en) | Gene expression cassette for expressing n-terminal methionine-truncated protein of interest and method for producing n-terminal methionine-truncated protein of interest by using same | |
| CN114686504A (zh) | Lpp或其突变体作为分子伴侣在大肠杆菌中分泌表达重组蛋白的应用 | |
| CN119735705B (zh) | 一种融合蛋白及其在制备司美格鲁肽前体多肽中的应用 | |
| WO2012048856A1 (en) | Proinsulin with helper sequence | |
| US12522838B2 (en) | Promoter for yeast | |
| HK40025349A (en) | Codon optimized precursor gene and signal peptide gene of human insulin analogue | |
| RU2515061C1 (ru) | РЕКОМБИНАТНАЯ ПЛАЗМИДНАЯ ДНК рНI03 КОДИРУЮЩАЯ, ГИБРИДНЫЙ БЕЛОК С ПРОИНСУЛИНОМ ЧЕЛОВЕКА, КЛЕТКА Escherichia coli, ТРАНСФОРМИРОВАННАЯ РЕКОМБИНАНТНОЙ ПЛАЗМИДНОЙ ДНК рНI03, И ШТАММ БАКТЕРИЙ Escherichia coli JM109/pHI03-ПРОДУЦЕНТ ГИБРИДНОГО БЕЛКА-ПРЕДШЕСТВЕННИКА ИНСУЛИНА ЧЕЛОВЕКА | |
| RU2263147C1 (ru) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pHINS05, КОДИРУЮЩАЯ ГИБРИДНЫЙ ПОЛИПЕПТИД, СОДЕРЖАЩИЙ ПРОИНСУЛИН ЧЕЛОВЕКА, КЛЕТКА ESCHERICHIA COLI, ТРАНСФОРМИРОВАННАЯ РЕКОМБИНАНТНОЙ ПЛАЗМИДНОЙ ДНК pHINS05, И ШТАММ БАКТЕРИЙ ESCHERICHIA COLI JM109/pHINS05 - ПРОДУЦЕНТ ГИБРИДНОГО ПОЛИПЕПТИДА, СОДЕРЖАЩЕГО ПРОИНСУЛИН ЧЕЛОВЕКА | |
| RU2728611C1 (ru) | РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pF265, КОДИРУЮЩАЯ ГИБРИДНЫЙ ПОЛИПЕПТИД, СОДЕРЖАЩИЙ ПРОИНСУЛИН ЧЕЛОВЕКА, И ШТАММ БАКТЕРИЙ Escherichia coli - ПРОДУЦЕНТ ГИБРИДНОГО ПОЛИПЕПТИДА, СОДЕРЖАЩЕГО ПРОИНСУЛИН ЧЕЛОВЕКА | |
| CN119613527A (zh) | 鸡肝细胞生长因子的截短突变体及其在防治肝脏相关疾病方面的用途 | |
| EP2867250A2 (en) | Proinsulin with enhanced helper sequence | |
| CN1740195B (zh) | 一种多肽gapM1及其制备方法 | |
| CN104672334B (zh) | 重组长链人胰岛素样生长因子-i的制备方法 | |
| WO2017219455A1 (zh) | 编码截短型人角质细胞生长因子的基因及其制备方法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| B350 | Update of information on the portal [chapter 15.35 patent gazette] | ||
| B08F | Application dismissed because of non-payment of annual fees [chapter 8.6 patent gazette] |
Free format text: REFERENTE A 5A ANUIDADE. |
|
| B08K | Patent lapsed as no evidence of payment of the annual fee has been furnished to inpi [chapter 8.11 patent gazette] |
Free format text: EM VIRTUDE DO ARQUIVAMENTO PUBLICADO NA RPI 2760 DE 28-11-2023 E CONSIDERANDO AUSENCIA DE MANIFESTACAO DENTRO DOS PRAZOS LEGAIS, INFORMO QUE CABE SER MANTIDO O ARQUIVAMENTO DO PEDIDO DE PATENTE, CONFORME O DISPOSTO NO ARTIGO 12, DA RESOLUCAO 113/2013. |