ES2557741T3 - Procedimientos para incrementar la producción de polipéptidos - Google Patents
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- ES2557741T3 ES2557741T3 ES03716840.8T ES03716840T ES2557741T3 ES 2557741 T3 ES2557741 T3 ES 2557741T3 ES 03716840 T ES03716840 T ES 03716840T ES 2557741 T3 ES2557741 T3 ES 2557741T3
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| US20090023186A1 (en) * | 2007-07-22 | 2009-01-22 | Excellgene Sa | Use of valproic acid for enhancing production of recombinant proteins in mammalian cells |
| US20110014624A1 (en) * | 2008-03-12 | 2011-01-20 | Wyeth Llc | Methods For Identifying Cells Suitable For Large-Scale Production of Recombinant Proteins |
| RU2012127383A (ru) * | 2009-12-02 | 2014-01-10 | Акселерон Фарма Инк. | Композиции и способы для увеличения времени полужизни fc-слитых белков в сыворотке |
| EP2623556A4 (en) | 2010-09-30 | 2015-03-11 | Daikin Ind Ltd | DRIP AND RESIN CONNECTION |
| US20130295613A1 (en) * | 2010-12-28 | 2013-11-07 | Chugai Seiyaku Kabushiki Kaisha | Animal cell culturing method |
| EP2702077A2 (en) | 2011-04-27 | 2014-03-05 | AbbVie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| EP2718328A4 (en) | 2011-06-08 | 2014-12-24 | Acceleron Pharma Inc | COMPOSITIONS AND METHODS FOR INCREASING THE HALF TIME OF SERUM |
| HUE033279T2 (en) | 2011-07-01 | 2017-11-28 | Amgen Inc | Mammalian cell culture |
| EP2653548A1 (de) | 2012-04-17 | 2013-10-23 | Greenovation Biotech GmbH | Verfahren zur Erhöhung der Sekretion rekombinanter Proteine |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| WO2013158279A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Protein purification methods to reduce acidic species |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| BR112015004467A2 (pt) | 2012-09-02 | 2017-03-21 | Abbvie Inc | método para controlar a heterogeneidade de proteínas |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| CN105189736A (zh) * | 2013-03-15 | 2015-12-23 | 斯欧考普控股公司 | 适用于提高胎儿体重增加并增强骨特性的可可碱组合物 |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | Abbvie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| AU2017345490B2 (en) | 2016-10-21 | 2022-07-07 | Amgen Inc. | Pharmaceutical formulations and methods of making the same |
| KR102190790B1 (ko) * | 2018-10-19 | 2020-12-15 | 주식회사 프로젠 | 변형된 egf 단백질의 생산 방법 |
| JP6963336B2 (ja) * | 2017-10-23 | 2021-11-05 | プロゲン・シーオー., エルティーディー.Progen Co., Ltd. | 改変ｅｇｆタンパク質、その製造方法及びその使用 |
| EP4267717A1 (en) | 2020-12-22 | 2023-11-01 | Amgen Inc. | Cell culture method |
Family Cites Families (49)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3824286A (en) | 1970-07-07 | 1974-07-16 | Lever Brothers Ltd | Preparation of polyacetylalkylene diamines |
| EP0005476B1 (de) | 1978-05-17 | 1981-12-30 | Dr. Karl Thomae GmbH | Verfahren zur Herstellung von Humaninterferon |
| US4301249A (en) * | 1980-07-23 | 1981-11-17 | Merck & Co., Inc. | High titer production of hepatitis A virus |
| US4357422A (en) | 1980-08-14 | 1982-11-02 | Massachusetts Institute Of Technology | Method of enhancing interferon production |
| US4416986A (en) * | 1981-01-16 | 1983-11-22 | Merck & Co., Inc. | Methods of producing HBsAg |
| US4473647A (en) | 1981-02-27 | 1984-09-25 | Amf Inc. | Tissue culture medium |
| US6936694B1 (en) | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| AU588819B2 (en) | 1984-10-29 | 1989-09-28 | Immunex Corporation | Cloning of human granulocyte-macrophage colony stimulating factor gene |
| US4992472A (en) | 1987-06-16 | 1991-02-12 | The United States Of America As Represented By The Department Of Health And Human Services | Chemical differentiating agents |
| US4965195A (en) | 1987-10-26 | 1990-10-23 | Immunex Corp. | Interleukin-7 |
| US4968607A (en) | 1987-11-25 | 1990-11-06 | Immunex Corporation | Interleukin-1 receptors |
| US5075222A (en) | 1988-05-27 | 1991-12-24 | Synergen, Inc. | Interleukin-1 inhibitors |
| WO1990005183A1 (en) | 1988-10-31 | 1990-05-17 | Immunex Corporation | Interleukin-4 receptors |
| US5055608A (en) | 1988-11-14 | 1991-10-08 | Sloan-Kettering Institute For Cancer Research | Novel potent inducers of thermal differentiation and method of use thereof |
| US5330744A (en) | 1988-11-14 | 1994-07-19 | Sloan-Kettering Institute For Cancer Research | Method for increasing sensitivity to chemically induced terminal differentiation |
| ZA899421B (en) | 1988-12-14 | 1990-09-26 | Merrell Dow Pharma | Method of potentiating natural killer cell activity |
| IL94611A (en) | 1989-06-05 | 1994-12-29 | Organogenesis Inc | Medium for cell cultures containing insulin or growth factor similar to insulin, transferrin or iron ion, triiodothyronine or thyroxine and method of use |
| US5395760A (en) | 1989-09-05 | 1995-03-07 | Immunex Corporation | DNA encoding tumor necrosis factor-α and -β receptors |
| DE10399023I2 (de) | 1989-09-12 | 2006-11-23 | Ahp Mfg B V | TFN-bindende Proteine |
| US6204363B1 (en) | 1989-10-16 | 2001-03-20 | Amgen Inc. | Stem cell factor |
| US5272064A (en) | 1989-12-19 | 1993-12-21 | Amgen Inc. | DNA molecules encoding platelet-derived growth factor B chain analogs and method for expression thereof |
| US5149792A (en) | 1989-12-19 | 1992-09-22 | Amgen Inc. | Platelet-derived growth factor B chain analogs |
| US5272071A (en) | 1989-12-22 | 1993-12-21 | Applied Research Systems Ars Holding N.V. | Method for the modification of the expression characteristics of an endogenous gene of a given cell line |
| US5350683A (en) | 1990-06-05 | 1994-09-27 | Immunex Corporation | DNA encoding type II interleukin-1 receptors |
| WO1991018982A1 (en) | 1990-06-05 | 1991-12-12 | Immunex Corporation | Type ii interleukin-1 receptors |
| US5369108A (en) | 1991-10-04 | 1994-11-29 | Sloan-Kettering Institute For Cancer Research | Potent inducers of terminal differentiation and methods of use thereof |
| JP3589665B2 (ja) | 1992-10-23 | 2004-11-17 | イミュネックス・コーポレーション | 可溶性オリゴマー蛋白質の調製法 |
| US5420019A (en) | 1993-02-02 | 1995-05-30 | Xoma Corporation | Stable bactericidal/permeability-increasing protein muteins |
| US5554512A (en) | 1993-05-24 | 1996-09-10 | Immunex Corporation | Ligands for flt3 receptors |
| US20010010922A1 (en) | 1994-06-09 | 2001-08-02 | Riccardo Dalla-Favera | Cloning and uses of the genetic locus bcl-6 |
| US5981713A (en) | 1994-10-13 | 1999-11-09 | Applied Research Systems Ars Holding N.V. | Antibodies to intereleukin-1 antagonists |
| US5705364A (en) | 1995-06-06 | 1998-01-06 | Genentech, Inc. | Mammalian cell culture process |
| KR101004174B1 (ko) | 1995-06-29 | 2010-12-24 | 임뮤넥스 코포레이션 | 세포소멸을 유도하는 시토킨 |
| JP4306813B2 (ja) | 1995-09-19 | 2009-08-05 | アスビオファーマ株式会社 | 動物細胞の新規培養方法 |
| US6613544B1 (en) | 1995-12-22 | 2003-09-02 | Amgen Inc. | Osteoprotegerin |
| US6096728A (en) | 1996-02-09 | 2000-08-01 | Amgen Inc. | Composition and method for treating inflammatory diseases |
| USRE37234E1 (en) | 1996-11-01 | 2001-06-19 | Nitromed, Inc. | Nitrosated and nitrosylated phosphodiestrase inhibitor compounds, compositions and their uses |
| US6271349B1 (en) | 1996-12-23 | 2001-08-07 | Immunex Corporation | Receptor activator of NF-κB |
| WO1998028010A2 (en) | 1996-12-24 | 1998-07-02 | Hyal Pharmaceutical Corporation | Use of moieties for binding to hyaluronan and icam-1 |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| WO1999032605A1 (en) | 1997-12-19 | 1999-07-01 | Novo Nordisk A/S | Method for producing heterologous proteins in eukaryotic cells on an industrial scale using nucleotide-manipulating agents |
| US6337072B1 (en) | 1998-04-03 | 2002-01-08 | Hyseq, Inc. | Interleukin-1 receptor antagonist and recombinant production thereof |
| EP1117778A2 (en) | 1998-10-02 | 2001-07-25 | THE GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Methods and compositions for inducing differentiation and apoptosis in cells that overexpress the notch protein |
| US6660843B1 (en) | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| ATE348173T1 (de) | 1999-04-26 | 2007-01-15 | Genentech Inc | Zellenzuchtverfahren für glycoproteine |
| ATE312186T1 (de) | 1999-10-13 | 2005-12-15 | Immunex Corp | Vektoren und verfahren für rekombinante proteinexpression |
| WO2001036637A1 (en) | 1999-11-17 | 2001-05-25 | Immunex Corporation | Receptor activator of nf-kappa b |
| AU2001259432B2 (en) | 2000-05-03 | 2005-04-21 | Amgen Inc. | Modified peptides, comprising an FC domain, as therapeutic agents |
| WO2003083066A2 (en) * | 2002-03-27 | 2003-10-09 | Immunex Corporation | Methods for increasing polypeptide production |
-
2003
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- 2003-03-27 EP EP03716840.8A patent/EP1497444B1/en not_active Expired - Lifetime
- 2003-03-27 ES ES03716840.8T patent/ES2557741T3/es not_active Expired - Lifetime
- 2003-03-27 JP JP2003580502A patent/JP2005521401A/ja active Pending
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- 2003-03-27 CA CA2480121A patent/CA2480121C/en not_active Expired - Fee Related
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| MXPA04009381A (es) | 2005-01-25 |
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| JP2008167760A (ja) | 2008-07-24 |
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| PL376821A1 (pl) | 2006-01-09 |
| CA2480121C (en) | 2012-02-28 |
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| JP4414472B2 (ja) | 2010-02-10 |
| EP1497444A4 (en) | 2006-08-30 |
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| US20030211579A1 (en) | 2003-11-13 |
| EP1497444A2 (en) | 2005-01-19 |
| US20050233415A1 (en) | 2005-10-20 |
| JP2005521401A (ja) | 2005-07-21 |
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