DK175898B1 - Fremgangsmåde til at udtrykke ikke-gærprotein i en gærvært og transformeret gærvært samt anvendelsen af en transformeret gær til fremstilling af gærværten - Google Patents
Fremgangsmåde til at udtrykke ikke-gærprotein i en gærvært og transformeret gærvært samt anvendelsen af en transformeret gær til fremstilling af gærværten Download PDFInfo
- Publication number
- DK175898B1 DK175898B1 DK198902215A DK221589A DK175898B1 DK 175898 B1 DK175898 B1 DK 175898B1 DK 198902215 A DK198902215 A DK 198902215A DK 221589 A DK221589 A DK 221589A DK 175898 B1 DK175898 B1 DK 175898B1
- Authority
- DK
- Denmark
- Prior art keywords
- yeast
- adr
- promoter
- expression cassette
- host
- Prior art date
Links
- 240000004808 Saccharomyces cerevisiae Species 0.000 title claims abstract description 146
- 238000000034 method Methods 0.000 title claims abstract description 19
- 108090000623 proteins and genes Proteins 0.000 title description 40
- 102000004169 proteins and genes Human genes 0.000 title description 28
- 230000014509 gene expression Effects 0.000 claims abstract description 63
- 102100034044 All-trans-retinol dehydrogenase [NAD(+)] ADH1B Human genes 0.000 claims abstract description 31
- 101710193111 All-trans-retinol dehydrogenase [NAD(+)] ADH4 Proteins 0.000 claims abstract description 31
- 108010058643 Fungal Proteins Proteins 0.000 claims abstract description 21
- 239000013612 plasmid Substances 0.000 claims description 37
- 108091026890 Coding region Proteins 0.000 claims description 34
- 239000013598 vector Substances 0.000 claims description 29
- 230000005026 transcription initiation Effects 0.000 claims description 23
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 claims description 20
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 20
- 230000005030 transcription termination Effects 0.000 claims description 18
- 238000011144 upstream manufacturing Methods 0.000 claims description 15
- 101100490563 Caenorhabditis elegans adr-1 gene Proteins 0.000 claims description 14
- 230000004913 activation Effects 0.000 claims description 11
- 101150022075 ADR1 gene Proteins 0.000 claims description 10
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 230000008569 process Effects 0.000 claims description 2
- 238000011084 recovery Methods 0.000 claims 1
- 230000001105 regulatory effect Effects 0.000 abstract description 12
- 210000004027 cell Anatomy 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 20
- 239000012634 fragment Substances 0.000 description 11
- 108091029865 Exogenous DNA Proteins 0.000 description 8
- 101710187573 Alcohol dehydrogenase 2 Proteins 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 7
- 230000010354 integration Effects 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- 238000013518 transcription Methods 0.000 description 7
- 238000010276 construction Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 108020004999 messenger RNA Proteins 0.000 description 6
- 102000053602 DNA Human genes 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 229920001184 polypeptide Polymers 0.000 description 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 101150078509 ADH2 gene Proteins 0.000 description 4
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 4
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 4
- 241000235070 Saccharomyces Species 0.000 description 4
- 102000019197 Superoxide Dismutase Human genes 0.000 description 4
- 108010012715 Superoxide dismutase Proteins 0.000 description 4
- 101150050575 URA3 gene Proteins 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 3
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000725303 Human immunodeficiency virus Species 0.000 description 3
- 241000235649 Kluyveromyces Species 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 241000235648 Pichia Species 0.000 description 2
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 108700009124 Transcription Initiation Site Proteins 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 230000008021 deposition Effects 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- FQVLRGLGWNWPSS-BXBUPLCLSA-N (4r,7s,10s,13s,16r)-16-acetamido-13-(1h-imidazol-5-ylmethyl)-10-methyl-6,9,12,15-tetraoxo-7-propan-2-yl-1,2-dithia-5,8,11,14-tetrazacycloheptadecane-4-carboxamide Chemical compound N1C(=O)[C@@H](NC(C)=O)CSSC[C@@H](C(N)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@@H]1CC1=CN=CN1 FQVLRGLGWNWPSS-BXBUPLCLSA-N 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 101710187578 Alcohol dehydrogenase 1 Proteins 0.000 description 1
- 102100034035 Alcohol dehydrogenase 1A Human genes 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 102100034613 Annexin A2 Human genes 0.000 description 1
- 108090000668 Annexin A2 Proteins 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 241000235172 Bullera Species 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000490729 Cryptococcaceae Species 0.000 description 1
- 241000221199 Cryptococcus <basidiomycete yeast> Species 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 241000221207 Filobasidium Species 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 101000892220 Geobacillus thermodenitrificans (strain NG80-2) Long-chain-alcohol dehydrogenase 1 Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 101000780443 Homo sapiens Alcohol dehydrogenase 1A Proteins 0.000 description 1
- 108010020056 Hydrogenase Proteins 0.000 description 1
- 101150062179 II gene Proteins 0.000 description 1
- 241001138401 Kluyveromyces lactis Species 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 101710149086 Nuclease S1 Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000009569 Phosphoglucomutase Human genes 0.000 description 1
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 1
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 108700005075 Regulator Genes Proteins 0.000 description 1
- 241000223252 Rhodotorula Species 0.000 description 1
- 244000206963 Saccharomyces cerevisiae var. diastaticus Species 0.000 description 1
- 241001407717 Saccharomyces norbensis Species 0.000 description 1
- 241000235344 Saccharomycetaceae Species 0.000 description 1
- 241000235343 Saccharomycetales Species 0.000 description 1
- 241000228389 Sporidiobolus Species 0.000 description 1
- 241000222068 Sporobolomyces <Sporidiobolaceae> Species 0.000 description 1
- 240000006345 Trifolium hybridum Species 0.000 description 1
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 229940126864 fibroblast growth factor Drugs 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000034659 glycolysis Effects 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 210000000003 hoof Anatomy 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000002262 irrigation Effects 0.000 description 1
- 238000003973 irrigation Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000011278 mitosis Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 150000007523 nucleic acids Chemical group 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 108091000115 phosphomannomutase Proteins 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 229940107700 pyruvic acid Drugs 0.000 description 1
- 108091035233 repetitive DNA sequence Proteins 0.000 description 1
- 102000053632 repetitive DNA sequence Human genes 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 210000005253 yeast cell Anatomy 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
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
- C12N15/90—Stable introduction of foreign DNA into chromosome
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/50—Fibroblast growth factor [FGF]
- C07K14/503—Fibroblast growth factor [FGF] basic FGF [bFGF]
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
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)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Mycology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US19086888A | 1988-05-06 | 1988-05-06 | |
| US19086888 | 1988-05-06 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| DK221589D0 DK221589D0 (da) | 1989-05-05 |
| DK221589A DK221589A (da) | 1989-11-07 |
| DK175898B1 true DK175898B1 (da) | 2005-05-30 |
Family
ID=22703135
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK198902215A DK175898B1 (da) | 1988-05-06 | 1989-05-05 | Fremgangsmåde til at udtrykke ikke-gærprotein i en gærvært og transformeret gærvært samt anvendelsen af en transformeret gær til fremstilling af gærværten |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US6183985B1 (es) |
| EP (1) | EP0340986B1 (es) |
| JP (4) | JP3074174B2 (es) |
| AT (1) | ATE123521T1 (es) |
| CA (1) | CA1324969C (es) |
| DE (1) | DE68922932T2 (es) |
| DK (1) | DK175898B1 (es) |
| ES (1) | ES2072900T3 (es) |
Families Citing this family (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE207538T1 (de) * | 1995-02-09 | 2001-11-15 | Behringwerke Ag | Verfahren zur produktion von proteinen |
| DE19544233A1 (de) * | 1995-11-28 | 1997-06-05 | Hoechst Ag | Verfahren zur Nutzung des Hefe-ADH II-Promotorsystems zur biotechnologischen Produktion heterologer Proteine in hohen Ausbeuten |
| EP1437405B1 (en) * | 2001-09-20 | 2009-12-23 | Toyota Jidosha Kabushiki Kaisha | Gene overexpression system |
| CA2553040A1 (en) * | 2004-02-02 | 2005-08-18 | Ambrx, Inc. | Modified human four helical bundle polypeptides and their uses |
| CN102603895B (zh) | 2004-06-18 | 2016-09-28 | Ambrx公司 | 新颖抗原结合多肽和其用途 |
| BRPI0512396A (pt) * | 2004-07-21 | 2008-03-11 | Ambrx Inc | polipeptìdeos biossintéticos utilizando aminoácidos codificados não naturalmente |
| NZ555386A (en) | 2004-12-22 | 2011-01-28 | Ambrx Inc | Formulations of human growth hormone comprising a non-naturally encoded amino acid |
| KR20070090023A (ko) | 2004-12-22 | 2007-09-04 | 암브룩스, 인코포레이티드 | 변형 인간 성장 호르몬 |
| KR101252835B1 (ko) * | 2004-12-22 | 2013-04-10 | 암브룩스, 인코포레이티드 | 아미노아실-ｔＲＮＡ 합성효소의 조성물 및 그것의 용도 |
| WO2006073846A2 (en) | 2004-12-22 | 2006-07-13 | Ambrx, Inc. | Methods for expression and purification of recombinant human growth hormone |
| US7385028B2 (en) | 2004-12-22 | 2008-06-10 | Ambrx, Inc | Derivatization of non-natural amino acids and polypeptides |
| CN101247821B (zh) * | 2005-06-03 | 2013-01-23 | Ambrx公司 | 经改良人类干扰素分子和其用途 |
| DE102005029170A1 (de) * | 2005-06-23 | 2006-12-28 | Consortium für elektrochemische Industrie GmbH | System zur Genexpression in Hefen der Gattung Sporidiobolus |
| KR101285904B1 (ko) | 2005-08-18 | 2013-07-15 | 암브룩스, 인코포레이티드 | ｔＲＮＡ 조성물 및 이의 용도 |
| PL1954710T3 (pl) * | 2005-11-08 | 2011-09-30 | Ambrx Inc | Przyspieszacze do modyfikacji aminokwasów niewystępujących w przyrodzie i polipeptydów zbudowanych z aminokwasów nie występujących w przyrodzie |
| KR20080079643A (ko) | 2005-11-16 | 2008-09-01 | 암브룩스, 인코포레이티드 | 비-천연 아미노산을 포함하는 방법 및 조성물 |
| ES2514316T3 (es) | 2005-11-22 | 2014-10-28 | Novartis Vaccines And Diagnostics, Inc. | Partículas similares a virus (VLPs) de Norovirus y Sapovirus |
| EP2069396B1 (en) * | 2006-09-08 | 2015-10-21 | Ambrx, Inc. | Modified human plasma polypeptide or fc scaffolds and their uses |
| KR20090051227A (ko) * | 2006-09-08 | 2009-05-21 | 암브룩스, 인코포레이티드 | 척추동물 세포를 위한 하이브리드 서프레서 ｔＲＮＡ |
| PT2064333E (pt) * | 2006-09-08 | 2014-06-09 | Ambrx Inc | Supressor híbrido arnt para células de vertebrados |
| EP2106447B1 (en) | 2007-01-26 | 2013-04-17 | Novozymes A/S | Method for methanol independent induction from methanol inducible promoters in pichia |
| CN104163864B (zh) | 2007-03-30 | 2017-08-01 | Ambrx公司 | 经修饰fgf‑21多肽和其用途 |
| AU2008247815B2 (en) | 2007-05-02 | 2012-09-06 | Ambrx, Inc. | Modified interferon beta polypeptides and their uses |
| MX338336B (es) | 2007-11-20 | 2016-04-07 | Ambrx Inc | Polipeptidos de insulina modificados y sus usos. |
| CN101939443B (zh) | 2008-02-08 | 2014-01-29 | Ambrx公司 | 经修饰瘦素多肽和其用途 |
| US20110129874A1 (en) * | 2008-07-11 | 2011-06-02 | Novozymes A/S | Pichia Pastoris Das Promoter Variants |
| PT2318029T (pt) | 2008-07-23 | 2018-01-10 | Ambrx Inc | Polipéptidos de g-csf bovino modificados e suas utilizações |
| ES2660000T3 (es) | 2008-09-26 | 2018-03-20 | Ambrx, Inc. | Vacunas y microorganismos dependientes de la replicación de aminoácidos no naturales |
| EP2342223B1 (en) | 2008-09-26 | 2017-04-26 | Ambrx, Inc. | Modified animal erythropoietin polypeptides and their uses |
| SG181769A1 (en) | 2009-12-21 | 2012-07-30 | Ambrx Inc | Modified porcine somatotropin polypeptides and their uses |
| US20120283171A1 (en) | 2009-12-21 | 2012-11-08 | Ambrx, Inc. | Modified bovine somatotropin polypeptides and their uses |
| WO2012006293A1 (en) | 2010-07-06 | 2012-01-12 | Novartis Ag | Norovirus derived immunogenic compositions and methods |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| PL2605789T3 (pl) | 2010-08-17 | 2019-11-29 | Ambrx Inc | Zmodyfikowane polipeptydy relaksyny i ich zastosowania |
| AR083006A1 (es) | 2010-09-23 | 2013-01-23 | Lilly Co Eli | Formulaciones para el factor estimulante de colonias de granulocitos (g-csf) bovino y variantes de las mismas |
| KR20240024362A (ko) | 2014-10-24 | 2024-02-23 | 브리스톨-마이어스 스큅 컴퍼니 | 변형된 fgf-21 폴리펩티드 및 그의 용도 |
| SG10201912034UA (en) | 2017-02-08 | 2020-02-27 | Bristol Myers Squibb Co | Modified relaxin polypeptides comprising a pharmacokinetic enhancer and uses thereof |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4880734A (en) * | 1984-05-11 | 1989-11-14 | Chiron Corporation | Eukaryotic regulatable transcription |
| CA1260858A (en) * | 1985-03-28 | 1989-09-26 | Lawrence S. Cousens | Expression using fused genes providing for protein product |
| EP0234871A3 (en) | 1986-02-28 | 1988-10-12 | Merck & Co. Inc. | Regulatable expression of recombinant proteins in yeast |
| US5068185A (en) | 1986-07-10 | 1991-11-26 | Merck & Co., Inc. | Trains of yeast for the expression of heterologous genes |
-
1989
- 1989-04-21 CA CA000597461A patent/CA1324969C/en not_active Expired - Lifetime
- 1989-04-28 AT AT89304297T patent/ATE123521T1/de not_active IP Right Cessation
- 1989-04-28 DE DE68922932T patent/DE68922932T2/de not_active Expired - Lifetime
- 1989-04-28 EP EP89304297A patent/EP0340986B1/en not_active Expired - Lifetime
- 1989-04-28 ES ES89304297T patent/ES2072900T3/es not_active Expired - Lifetime
- 1989-05-02 JP JP01113585A patent/JP3074174B2/ja not_active Expired - Lifetime
- 1989-05-05 DK DK198902215A patent/DK175898B1/da not_active IP Right Cessation
-
1995
- 1995-03-01 US US08/397,553 patent/US6183985B1/en not_active Expired - Lifetime
-
2000
- 2000-01-12 JP JP2000004098A patent/JP3484386B2/ja not_active Expired - Lifetime
-
2002
- 2002-08-14 JP JP2002236635A patent/JP3561513B2/ja not_active Expired - Fee Related
-
2003
- 2003-12-10 JP JP2003412625A patent/JP2004081222A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| JP2003116525A (ja) | 2003-04-22 |
| CA1324969C (en) | 1993-12-07 |
| JP2000300277A (ja) | 2000-10-31 |
| JPH02104291A (ja) | 1990-04-17 |
| JP3484386B2 (ja) | 2004-01-06 |
| US6183985B1 (en) | 2001-02-06 |
| DE68922932T2 (de) | 1995-10-19 |
| EP0340986B1 (en) | 1995-06-07 |
| JP3074174B2 (ja) | 2000-08-07 |
| JP2004081222A (ja) | 2004-03-18 |
| JP3561513B2 (ja) | 2004-09-02 |
| EP0340986A3 (en) | 1991-07-31 |
| DK221589A (da) | 1989-11-07 |
| DE68922932D1 (de) | 1995-07-13 |
| EP0340986A2 (en) | 1989-11-08 |
| DK221589D0 (da) | 1989-05-05 |
| ES2072900T3 (es) | 1995-08-01 |
| ATE123521T1 (de) | 1995-06-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK175898B1 (da) | Fremgangsmåde til at udtrykke ikke-gærprotein i en gærvært og transformeret gærvært samt anvendelsen af en transformeret gær til fremstilling af gærværten | |
| US5674706A (en) | High level expression of proteins in yeast | |
| CA1340772C (en) | Expression and secretion of heterologous protiens in yeast employing truncated alpha-factor leader sequences | |
| FI81379C (fi) | Anvaendning av kluyveromyces-jaest saosom vaerd foer transformering och uttryckning av fraemmande gener. | |
| Doel et al. | The dominant PNM2-mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. | |
| EP0329203B1 (en) | Yeast expression systems with vectors having pyk promoters, and synthesis of foreign protein | |
| Hansen et al. | Characterization of a transpositionally active Ty3 element and identification of the Ty3 integrase protein | |
| NO840200L (no) | Glukoamylase cdna. | |
| Jia et al. | The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase | |
| Filho et al. | Stable Yeast Transformants that Secrete Functional α–Amylase Encoded by Cloned Mouse Pancreatic cDNA | |
| EP0329684A1 (en) | Composite yeast vectors | |
| Nishi et al. | The GCR1 requirement for yeast glycolytic gene expression is suppressed by dominant mutations in the SGC1 gene, which encodes a novel basic-helix-loop-helix protein | |
| WO1993018167A1 (en) | A method for production of proteins in yeast | |
| Icho et al. | Metal-binding, nucleic acid-binding finger sequences in the CDC16 gene of Saccharomyces cerevisiae | |
| KR20010020482A (ko) | 개량된 단백질 발현균주 | |
| DK176000B1 (da) | Fremgangsmåde til fremstilling af et protein ud fra gærsvampe under anvendelse af et inducerbart system, samt vektorer og transformerede stammer til brug ved fremgangsmåden | |
| Munholland et al. | DNA sequences required for yeast actin gene transcription do not include conserved CCAAT motifs | |
| JPH06165691A (ja) | プロテアーゼ阻害剤の生産方法 | |
| JP6112548B2 (ja) | 自己倍数化抑制に基づく酵母の育種方法 | |
| JP2006075122A (ja) | 転写活性化タンパク質をコードするキャンディダユティリス由来の遺伝子 | |
| Phillips | Isolation and characterization of QCR9 the nuclear gene encoding the 7.3 kDa subunit 9 of the Saccharomyces cerevisiae bc (1) complex | |
| JP2000507107A (ja) | 少なくとも１つの疎水性ドメインを有するタンパク質をコードする組換え核酸配列、及びそれらの用途 | |
| Greve | University Undergraduate Fellow, 1990-91 | |
| JPH03262487A (ja) | ヒト血清アルブミンの安定な製造方法 | |
| JPH02502964A (ja) | Ｌｅｕ３を用いるアミノ酸合成の調節 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PUP | Patent expired |