CA2508808A1 - Cold-induced expression vector - Google Patents
Cold-induced expression vector Download PDFInfo
- Publication number
- CA2508808A1 CA2508808A1 CA002508808A CA2508808A CA2508808A1 CA 2508808 A1 CA2508808 A1 CA 2508808A1 CA 002508808 A CA002508808 A CA 002508808A CA 2508808 A CA2508808 A CA 2508808A CA 2508808 A1 CA2508808 A1 CA 2508808A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- gene
- vector
- untranslated region
- seq
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 239000013604 expression vector Substances 0.000 title description 14
- 239000013598 vector Substances 0.000 claims abstract description 43
- 230000035772 mutation Effects 0.000 claims abstract description 22
- 108010049152 Cold Shock Proteins and Peptides Proteins 0.000 claims abstract description 11
- 108090000623 proteins and genes Proteins 0.000 claims description 94
- 102000004169 proteins and genes Human genes 0.000 claims description 65
- 239000002773 nucleotide Substances 0.000 claims description 62
- 125000003729 nucleotide group Chemical group 0.000 claims description 62
- 108091026898 Leader sequence (mRNA) Proteins 0.000 claims description 42
- 108020004999 messenger RNA Proteins 0.000 claims description 17
- 238000003780 insertion Methods 0.000 claims description 14
- 230000037431 insertion Effects 0.000 claims description 14
- 238000000034 method Methods 0.000 claims description 12
- 239000013600 plasmid vector Substances 0.000 claims description 12
- 230000000295 complement effect Effects 0.000 claims description 7
- 238000012217 deletion Methods 0.000 claims description 6
- 230000037430 deletion Effects 0.000 claims description 6
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 3
- 230000001131 transforming effect Effects 0.000 claims description 3
- 238000011144 upstream manufacturing Methods 0.000 claims description 3
- 108020004414 DNA Proteins 0.000 description 52
- 230000014509 gene expression Effects 0.000 description 50
- 239000013612 plasmid Substances 0.000 description 36
- 101150110403 cspA gene Proteins 0.000 description 34
- 241000588724 Escherichia coli Species 0.000 description 32
- 108020003589 5' Untranslated Regions Proteins 0.000 description 28
- 239000012634 fragment Substances 0.000 description 26
- 239000011541 reaction mixture Substances 0.000 description 16
- 238000010276 construction Methods 0.000 description 13
- 230000000694 effects Effects 0.000 description 11
- 238000001962 electrophoresis Methods 0.000 description 11
- 239000000499 gel Substances 0.000 description 11
- 239000008223 sterile water Substances 0.000 description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 11
- 239000011543 agarose gel Substances 0.000 description 10
- 230000008018 melting Effects 0.000 description 10
- 238000002844 melting Methods 0.000 description 10
- 108090000765 processed proteins & peptides Proteins 0.000 description 10
- 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 9
- 229960000723 ampicillin Drugs 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 8
- 230000006698 induction Effects 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 239000006142 Luria-Bertani Agar Substances 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 238000001712 DNA sequencing Methods 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 229920001184 polypeptide Polymers 0.000 description 5
- 101100007857 Bacillus subtilis (strain 168) cspB gene Proteins 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108091081024 Start codon Proteins 0.000 description 4
- 101150049887 cspB gene Proteins 0.000 description 4
- 101150041068 cspJ gene Proteins 0.000 description 4
- 101150068339 cspLA gene Proteins 0.000 description 4
- 210000003000 inclusion body Anatomy 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000013519 translation 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
- 241000672609 Escherichia coli BL21 Species 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000010191 image analysis Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 108020004465 16S ribosomal RNA Proteins 0.000 description 2
- 101150066002 GFP gene Proteins 0.000 description 2
- 102000005720 Glutathione transferase Human genes 0.000 description 2
- 108010070675 Glutathione transferase Proteins 0.000 description 2
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
- 238000005481 NMR spectroscopy Methods 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 101710137500 T7 RNA polymerase Proteins 0.000 description 2
- 108700009124 Transcription Initiation Site Proteins 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 2
- 101150026451 csp gene Proteins 0.000 description 2
- 101150096074 cspG gene Proteins 0.000 description 2
- 101150010904 cspLB gene Proteins 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 101150066555 lacZ gene Proteins 0.000 description 2
- 239000008101 lactose Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000005026 transcription initiation Effects 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 241000242764 Aequorea victoria Species 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 101100018293 Clostridioides difficile pflE gene Proteins 0.000 description 1
- 101710088599 Cold shock-like protein CspLB Proteins 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 241000701832 Enterobacteria phage T3 Species 0.000 description 1
- 108010074124 Escherichia coli Proteins Proteins 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101710202013 Protein 1.5 Proteins 0.000 description 1
- 108700005075 Regulator Genes Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 101150039316 Ybx3 gene Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 238000010420 art technique Methods 0.000 description 1
- 230000037429 base substitution Effects 0.000 description 1
- 238000007630 basic procedure Methods 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 101150008232 csdA gene Proteins 0.000 description 1
- 101150077693 deaD gene Proteins 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000009878 intermolecular interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- -1 isopropyl- Chemical group 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 238000005312 nonlinear dynamic Methods 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 238000013492 plasmid preparation Methods 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 239000012138 yeast extract 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
-
- 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
- C12N15/67—General methods for enhancing the expression
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
Landscapes
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measurement And Recording Of Electrical Phenomena And Electrical Characteristics Of The Living Body (AREA)
- Measuring Pulse, Heart Rate, Blood Pressure Or Blood Flow (AREA)
- Medicines Containing Plant Substances (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2002359956 | 2002-12-11 | ||
| JP2002-359956 | 2002-12-11 | ||
| PCT/JP2003/015835 WO2004053126A1 (ja) | 2002-12-11 | 2003-12-11 | 低温誘導発現ベクター |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2508808A1 true CA2508808A1 (en) | 2004-06-24 |
Family
ID=32500967
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002508808A Abandoned CA2508808A1 (en) | 2002-12-11 | 2003-12-11 | Cold-induced expression vector |
Country Status (11)
| Country | Link |
|---|---|
| US (1) | US7244588B2 (enExample) |
| EP (1) | EP1582587B1 (enExample) |
| JP (1) | JPWO2004053126A1 (enExample) |
| KR (1) | KR20050085190A (enExample) |
| CN (1) | CN100379870C (enExample) |
| AT (1) | ATE408692T1 (enExample) |
| AU (1) | AU2003289023B2 (enExample) |
| CA (1) | CA2508808A1 (enExample) |
| DE (1) | DE60323678D1 (enExample) |
| TW (1) | TW200510534A (enExample) |
| WO (1) | WO2004053126A1 (enExample) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100385004C (zh) * | 2002-03-01 | 2008-04-30 | 宝生物工程株式会社 | 冷休克诱导的异源多肽的表达和生产 |
| AU2007339423B2 (en) * | 2006-08-14 | 2012-11-15 | Biocontrol Systems, Inc. | Method for detecting pathogens |
| WO2024154061A1 (en) * | 2023-01-18 | 2024-07-25 | Pfizer Inc. | Compositions and methods for stabilizing rna |
| WO2024256962A1 (en) * | 2023-06-14 | 2024-12-19 | Pfizer Inc. | Method for stabilizing rna |
| WO2025126071A1 (en) * | 2023-12-14 | 2025-06-19 | Pfizer Inc. | Rna molecules |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5981280A (en) * | 1996-03-22 | 1999-11-09 | The University Of Medicine And Denistry Of New Jersey | Method and constructs for inhibiting protein expression in bacteria |
| US5726039A (en) * | 1994-07-21 | 1998-03-10 | Yissum Research Development Co. Of The Hebrew University Of Jerusalem | Vectors and transformed host cells for recombinant protein production at reduced temperatures |
| US5654169A (en) * | 1994-07-21 | 1997-08-05 | Yissum Research & Development Company Of The Hebrew University | Vectors and transformed host cells for recombinant protein production at reduced temperatures |
| ATE377647T1 (de) * | 1997-11-20 | 2007-11-15 | Takara Bio Inc | Durch kälte induzierbarer expressionsvektor |
| AU5493599A (en) * | 1998-08-20 | 2000-03-14 | University Of Medicine And Dentistry Of New Jersey | Cold-shock regulatory elements, constructs thereof, and methods of use |
| US6610533B1 (en) * | 2000-03-01 | 2003-08-26 | University Of Medicine And Dentistry Of New Jersey | Cold-shock regulatory elements, constructs thereof, and methods of use |
| CN100385004C (zh) * | 2002-03-01 | 2008-04-30 | 宝生物工程株式会社 | 冷休克诱导的异源多肽的表达和生产 |
-
2003
- 2003-12-10 TW TW092134844A patent/TW200510534A/zh not_active IP Right Cessation
- 2003-12-11 AT AT03778794T patent/ATE408692T1/de not_active IP Right Cessation
- 2003-12-11 CA CA002508808A patent/CA2508808A1/en not_active Abandoned
- 2003-12-11 EP EP03778794A patent/EP1582587B1/en not_active Expired - Lifetime
- 2003-12-11 DE DE60323678T patent/DE60323678D1/de not_active Expired - Lifetime
- 2003-12-11 JP JP2004558468A patent/JPWO2004053126A1/ja active Pending
- 2003-12-11 US US10/538,793 patent/US7244588B2/en not_active Expired - Fee Related
- 2003-12-11 AU AU2003289023A patent/AU2003289023B2/en not_active Ceased
- 2003-12-11 CN CNB200380109675XA patent/CN100379870C/zh not_active Expired - Fee Related
- 2003-12-11 WO PCT/JP2003/015835 patent/WO2004053126A1/ja not_active Ceased
- 2003-12-11 KR KR1020057009634A patent/KR20050085190A/ko not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| US20060148033A1 (en) | 2006-07-06 |
| AU2003289023A1 (en) | 2004-06-30 |
| EP1582587A1 (en) | 2005-10-05 |
| WO2004053126A1 (ja) | 2004-06-24 |
| EP1582587A4 (en) | 2006-10-25 |
| US7244588B2 (en) | 2007-07-17 |
| DE60323678D1 (de) | 2008-10-30 |
| TW200510534A (en) | 2005-03-16 |
| ATE408692T1 (de) | 2008-10-15 |
| CN100379870C (zh) | 2008-04-09 |
| EP1582587B1 (en) | 2008-09-17 |
| CN1748027A (zh) | 2006-03-15 |
| TWI316091B (enExample) | 2009-10-21 |
| AU2003289023B2 (en) | 2008-07-31 |
| JPWO2004053126A1 (ja) | 2006-04-13 |
| KR20050085190A (ko) | 2005-08-29 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |