ES2439702T3 - Etiquetas de solubilidad para la expresión y purificación de péptidos bioactivos - Google Patents
Etiquetas de solubilidad para la expresión y purificación de péptidos bioactivos Download PDFInfo
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- ES2439702T3 ES2439702T3 ES08782229.2T ES08782229T ES2439702T3 ES 2439702 T3 ES2439702 T3 ES 2439702T3 ES 08782229 T ES08782229 T ES 08782229T ES 2439702 T3 ES2439702 T3 ES 2439702T3
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Classifications
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- 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
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- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
Landscapes
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- General Engineering & Computer Science (AREA)
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- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
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| PCT/US2008/070802 WO2009015165A1 (en) | 2007-07-25 | 2008-07-23 | Solubility tags for the expression and purification of bioactive peptides |
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| US9101687B2 (en) | 2002-07-15 | 2015-08-11 | University Of Leeds | Beta sheet tapes ribbons in tissue engineering |
| US8586539B2 (en) | 2002-07-15 | 2013-11-19 | University Of Leeds | Beta sheet tapes ribbons in tissue engineering |
| US7951559B2 (en) * | 2007-07-25 | 2011-05-31 | E.I. Du Pont De Nemours And Company | Recombinant peptide production using a cross-linkable solubility tag |
| US7829311B2 (en) * | 2007-07-25 | 2010-11-09 | E.I. Du Pont De Nemours And Company | Ketosteroid isomerase inclusion body tag engineered to be acid-resistant by replacing aspartates with glutamate |
| US7915011B2 (en) * | 2009-03-05 | 2011-03-29 | E.I. Du Pont De Nemours And Company | Host cell modifications that improve peptide production and downstream processing |
| WO2011063264A1 (en) | 2009-11-20 | 2011-05-26 | University Of Chicago | Methods and compositions related to immunogenic fibrils |
| US8609621B2 (en) | 2010-11-15 | 2013-12-17 | E I Du Pont De Nemours And Company | Acid-cleavable linkers exhibiting altered rates of acid hydrolysis |
| US9273336B2 (en) | 2011-02-21 | 2016-03-01 | E. I. Du Pont De Nemours And Company | Recombinant host cells having an increase in buoyant density |
| US9062312B2 (en) * | 2011-06-21 | 2015-06-23 | Danisco Us Inc. | Fusion peptides comprising multi-functional peptidic solubility tags for efficient production, processing and surface applications |
| US9115182B2 (en) | 2011-06-21 | 2015-08-25 | E I Du Pont De Nemours And Company | Cysteine cross-linked structural peptides |
| WO2014056199A1 (zh) * | 2012-10-12 | 2014-04-17 | 清华大学 | 多肽的产生和纯化方法 |
| GB201306338D0 (en) | 2013-04-08 | 2013-05-22 | Univ Leeds | Novel proteoglycans |
| CN104513298B (zh) * | 2014-12-09 | 2018-07-17 | 山东信得科技股份有限公司 | 一种表达鸡传染性法氏囊可溶性vp 2-4-3多肽的方法 |
| US10704051B2 (en) * | 2014-12-29 | 2020-07-07 | Agricultural Technology Research Institute | Expression element, expression cassette, and vector containing the same |
| GB2540763A (en) | 2015-07-24 | 2017-02-01 | Evocatal Gmbh | Catalytically active protein aggregates and methods for producing the same |
| EP4775593A2 (en) * | 2018-09-11 | 2026-07-15 | NanoTag Biotechnologies GmbH | Epitope tags recognized by specific binders |
| WO2023008415A1 (ja) * | 2021-07-27 | 2023-02-02 | ＳＴＡＮＤ Ｔｈｅｒａｐｅｕｔｉｃｓ株式会社 | ペプチドタグおよび当該ペプチドタグをコードする核酸 |
| EP4444739A2 (en) | 2021-12-08 | 2024-10-16 | Oakgrove Bio LLC | Biological production of histidine-rich peptides |
| EP4567108A1 (en) * | 2023-12-05 | 2025-06-11 | Kutzner, Christoph | Screening of target peptides using fusion polypeptides |
Family Cites Families (54)
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| US935642A (en) * | 1908-01-09 | 1909-10-05 | Gerhard Coenen | Flushing apparatus. |
| US5206154A (en) | 1985-01-28 | 1993-04-27 | Xoma Corporation | Method of producing cecropins by microbiological techniques |
| US5215896A (en) | 1987-03-20 | 1993-06-01 | Creative Biomolecules, Inc. | Leader sequences for the production of recombinant proteins |
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| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| ES2118066T3 (es) | 1989-10-05 | 1998-09-16 | Optein Inc | Sintesis y aislamiento, exentos de celulas, de nuevos genes y polipeptidos. |
| US5449754A (en) | 1991-08-07 | 1995-09-12 | H & N Instruments, Inc. | Generation of combinatorial libraries |
| US5639603A (en) | 1991-09-18 | 1997-06-17 | Affymax Technologies N.V. | Synthesizing and screening molecular diversity |
| WO1994004688A2 (en) | 1992-08-21 | 1994-03-03 | The University Of British Columbia | Cationic peptides and method for production |
| US5585275A (en) | 1992-09-02 | 1996-12-17 | Arris Pharmaceutical Corporation | Pilot apparatus for peptide synthesis and screening |
| US5480971A (en) | 1993-06-17 | 1996-01-02 | Houghten Pharmaceuticals, Inc. | Peralkylated oligopeptide mixtures |
| US5648244A (en) | 1993-09-27 | 1997-07-15 | President And Fellows Of Harvard College | Production, purification, cleavage and use of fusion peptides |
| US6037145A (en) | 1994-09-07 | 2000-03-14 | Suntory Limited | Process for production of protein |
| US6261804B1 (en) | 1997-01-21 | 2001-07-17 | The General Hospital Corporation | Selection of proteins using RNA-protein fusions |
| IL131016A (en) | 1997-01-21 | 2004-12-15 | Gen Hospital Corp | Selection of proteins using RNA-protein blends |
| US6281018B1 (en) * | 1998-02-26 | 2001-08-28 | Coulter International Corp. | Selective purification and enrichment sorting of flow cytometer droplets based upon analysis of droplet precursor regions |
| US6846655B1 (en) | 1998-06-29 | 2005-01-25 | Phylos, Inc. | Methods for generating highly diverse libraries |
| US6613548B1 (en) | 1998-07-31 | 2003-09-02 | Pierce Biotechnology, Inc. | Fusion products containing insoluble proteinaceous tag |
| CA2334946A1 (en) | 1998-08-17 | 2000-02-24 | Phylos, Inc. | Methods for producing nucleic acids lacking 3'-untranslated regions and optimizing cellular rna-protein fusion formation |
| DK1105360T3 (da) | 1998-08-17 | 2009-11-02 | Bristol Myers Squibb Co | Identifikation af forbindelse-protein-interaktioner ved anvendelse af biblioteker af protein-nukleinsyrefusionsmolekyler |
| US6696089B2 (en) | 1998-09-03 | 2004-02-24 | Board Of Regents Of The University Of Nebraska | Nanogel networks including polyion polymer fragments and biological agent compositions thereof |
| FR2783169B1 (fr) | 1998-09-15 | 2001-11-02 | Sederma Sa | Utilisation cosmetique ou dermopharmaceutique de peptides pour la cicatrisation et pour l'amelioration de l'aspect cutane lors du vieillissement naturel ou accelere (heliodermie, pollution) |
| CA2350417C (en) | 1998-12-02 | 2010-02-09 | Bristol-Myers Squibb Company | Dna-protein fusions and uses thereof |
| US6242219B1 (en) | 1999-03-18 | 2001-06-05 | Xoma (Us) Llc | Methods for recombinant peptide production |
| CA2377468C (en) | 1999-07-27 | 2010-04-20 | Phylos, Inc. | Peptide acceptor ligation methods |
| CA2382545C (en) | 1999-08-27 | 2013-08-13 | Phylos, Inc. | Methods for encoding and sorting in vitro translated proteins |
| WO2001075097A2 (en) | 2000-03-31 | 2001-10-11 | Cambridge Antibody Technology Limited | Improvements to ribosome display |
| US7129326B2 (en) | 2000-04-14 | 2006-10-31 | Genencor International, Inc. | Methods for selective targeting |
| EP1360500B1 (en) | 2000-04-14 | 2010-01-13 | Genencor International, Inc. | Methods for selective targeting |
| GB0117011D0 (en) * | 2001-07-12 | 2001-09-05 | Univ Leeds | Peptide barrels |
| JP2005518442A (ja) | 2001-11-20 | 2005-06-23 | デューク・ユニバーシティー | 界面バイオマテリアル |
| ATE457355T1 (de) * | 2002-05-24 | 2010-02-15 | Medtronic Inc | Verfahren und dna-konstrukte zur produktion von polypeptiden mit hoher ausbeute |
| WO2003100022A2 (en) * | 2002-05-24 | 2003-12-04 | Restoragen, Inc. | Methods and dna constructs for high yield production of polypeptides |
| DE10227238A1 (de) | 2002-06-19 | 2004-01-15 | Wella Ag | Hochaffine kosmetische Mittel |
| GB0216286D0 (en) * | 2002-07-15 | 2002-08-21 | Univ Leeds | Network |
| CN102584951A (zh) | 2002-11-25 | 2012-07-18 | 金克克国际有限公司 | 皮肤或毛发结合肽 |
| WO2004060257A2 (en) | 2002-12-26 | 2004-07-22 | Gendron, Inc. | Bariatric patient management system |
| US20050054752A1 (en) | 2003-09-08 | 2005-03-10 | O'brien John P. | Peptide-based diblock and triblock dispersants and diblock polymers |
| US7285264B2 (en) | 2003-09-08 | 2007-10-23 | E.I. Du Pont De Nemours And Company | Peptide-based body surface coloring reagents |
| US7309482B2 (en) | 2003-09-08 | 2007-12-18 | E.I. Du Pont De Nemours And Company | Long lasting waterproof sunscreen comprising metal oxide and peptide conditioner |
| US20050226839A1 (en) | 2003-09-08 | 2005-10-13 | Xueying Huang | Pepetide-based body surface reagents for personal care |
| US7220405B2 (en) | 2003-09-08 | 2007-05-22 | E. I. Du Pont De Nemours And Company | Peptide-based conditioners and colorants for hair, skin, and nails |
| US7736633B2 (en) | 2005-09-28 | 2010-06-15 | E.I. Du Pont De Nemours And Company | Method for enhancing effects of colorants and conditioners |
| US7709601B2 (en) | 2005-12-15 | 2010-05-04 | E. I. Du Pont De Nemours And Company | Nylon binding peptides and methods of use |
| US7928076B2 (en) | 2005-12-15 | 2011-04-19 | E. I. Du Pont De Nemours And Company | Polypropylene binding peptides and methods of use |
| US7906617B2 (en) | 2005-12-15 | 2011-03-15 | E. I. Du Pont De Nemours And Company | Polyethylene binding peptides and methods of use |
| US7700716B2 (en) | 2005-12-15 | 2010-04-20 | E. I. Du Pont De Nemours And Company | Polytetrafluoroethylene binding peptides and methods of use |
| US7632919B2 (en) | 2005-12-15 | 2009-12-15 | E.I. Du Pont De Nemours And Company | Polystyrene binding peptides and methods of use |
| US7749957B2 (en) | 2006-04-06 | 2010-07-06 | E.I. Du Pont De Nemours And Company | Clay-binding peptides and methods of use |
| US7732569B2 (en) | 2006-10-19 | 2010-06-08 | E.I. Du Pont De Nemours And Company | Zein-based peptide tags for the expression and purification of bioactive peptides |
| US7662913B2 (en) | 2006-10-19 | 2010-02-16 | E. I. Du Pont De Nemours And Company | Cystatin-based peptide tags for the expression and purification of bioactive peptides |
-
2007
- 2007-07-25 US US11/782,836 patent/US7678883B2/en not_active Expired - Fee Related
-
2008
- 2008-07-23 CA CA002689099A patent/CA2689099A1/en not_active Abandoned
- 2008-07-23 ES ES08782229.2T patent/ES2439702T3/es active Active
- 2008-07-23 AU AU2008279186A patent/AU2008279186B2/en not_active Ceased
- 2008-07-23 EP EP08782229.2A patent/EP2173877B1/en not_active Not-in-force
- 2008-07-23 JP JP2010518341A patent/JP5453261B2/ja not_active Expired - Fee Related
- 2008-07-23 KR KR1020107004040A patent/KR20100057016A/ko not_active Ceased
- 2008-07-23 WO PCT/US2008/070802 patent/WO2009015165A1/en not_active Ceased
- 2008-07-23 CN CN2008800253760A patent/CN101835898B/zh not_active Expired - Fee Related
-
2009
- 2009-12-27 IL IL203002A patent/IL203002A0/en unknown
-
2010
- 2010-01-25 US US12/692,665 patent/US7794979B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| US20090029412A1 (en) | 2009-01-29 |
| KR20100057016A (ko) | 2010-05-28 |
| US20100136621A1 (en) | 2010-06-03 |
| JP2010534477A (ja) | 2010-11-11 |
| EP2173877B1 (en) | 2013-10-02 |
| WO2009015165A1 (en) | 2009-01-29 |
| IL203002A0 (en) | 2011-08-01 |
| AU2008279186A1 (en) | 2009-01-29 |
| US7678883B2 (en) | 2010-03-16 |
| EP2173877A1 (en) | 2010-04-14 |
| US7794979B2 (en) | 2010-09-14 |
| AU2008279186B2 (en) | 2013-09-05 |
| CA2689099A1 (en) | 2009-01-29 |
| JP5453261B2 (ja) | 2014-03-26 |
| CN101835898A (zh) | 2010-09-15 |
| CN101835898B (zh) | 2013-01-02 |
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