SK10472003A3 - Zvýšený výťažok aktívnych proteínov - Google Patents
Zvýšený výťažok aktívnych proteínov Download PDFInfo
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- SK10472003A3 SK10472003A3 SK1047-2003A SK10472003A SK10472003A3 SK 10472003 A3 SK10472003 A3 SK 10472003A3 SK 10472003 A SK10472003 A SK 10472003A SK 10472003 A3 SK10472003 A3 SK 10472003A3
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- protein
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- recombinant protein
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
-
- 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70575—NGF/TNF-superfamily, e.g. CD70, CD95L, CD153, CD154
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US27103301P | 2001-02-23 | 2001-02-23 | |
| PCT/US2002/005645 WO2002068455A2 (fr) | 2001-02-23 | 2002-02-22 | Augmentation du taux de recuperation de proteines actives |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| SK10472003A3 true SK10472003A3 (sk) | 2004-03-02 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK1047-2003A SK10472003A3 (sk) | 2001-02-23 | 2002-02-22 | Zvýšený výťažok aktívnych proteínov |
Country Status (21)
| Country | Link |
|---|---|
| US (2) | US7157557B2 (fr) |
| EP (1) | EP1366062B1 (fr) |
| JP (1) | JP2005505494A (fr) |
| KR (1) | KR20040052481A (fr) |
| CN (1) | CN1547586A (fr) |
| AT (1) | ATE517909T1 (fr) |
| AU (1) | AU2002255600B2 (fr) |
| BG (1) | BG108087A (fr) |
| CA (1) | CA2438094C (fr) |
| CZ (1) | CZ20032208A3 (fr) |
| EE (1) | EE200300408A (fr) |
| ES (1) | ES2370235T3 (fr) |
| HK (1) | HK1059267A1 (fr) |
| HU (1) | HUP0303246A2 (fr) |
| IL (1) | IL157446A0 (fr) |
| MX (1) | MXPA03007563A (fr) |
| PL (1) | PL374045A1 (fr) |
| RU (1) | RU2316563C2 (fr) |
| SK (1) | SK10472003A3 (fr) |
| WO (1) | WO2002068455A2 (fr) |
| ZA (1) | ZA200305909B (fr) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CZ20032208A3 (cs) * | 2001-02-23 | 2004-01-14 | Immunex Corporation | Zvýšený výtěžek aktivních proteinů |
| WO2005019434A2 (fr) | 2003-08-26 | 2005-03-03 | The Regents Of The University Of Colorado, A Body Corporate | Inhibiteurs de l'activite de la protease serine et leurs utilisations dans des methodes et preparations de traitement d'infections bacteriennes |
| NZ554520A (en) | 2004-10-22 | 2010-03-26 | Amgen Inc | Methods for refolding of recombinant antibodies |
| CA2584137A1 (fr) * | 2004-10-22 | 2006-06-08 | Amgen Inc. | Methodes de repliement de polypeptides |
| EP1844069A4 (fr) * | 2005-01-28 | 2009-05-20 | Apollo Life Sciences Ltd | Molécules et leurs molécules chimériques |
| MX2007014148A (es) | 2005-05-19 | 2008-01-11 | Amgen Inc | Composiciones y metodos para incrementar la estabilidad de anticuerpos. |
| WO2006138181A2 (fr) | 2005-06-14 | 2006-12-28 | Amgen Inc. | Preparations de proteines a tamponnage spontane |
| JP5335422B2 (ja) * | 2005-06-17 | 2013-11-06 | ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト | 少なくとも１つの非天然のシステインを含んでいる操作されたタンパク質の選択的な還元および誘導体化 |
| DE602007012412D1 (de) | 2005-12-22 | 2011-03-24 | Genentech Inc | Rekombinante produktion heparinbindender proteine |
| WO2007102946A2 (fr) | 2006-01-23 | 2007-09-13 | Amgen Inc. | Polypeptides cristallins |
| JP5566104B2 (ja) | 2006-07-14 | 2014-08-06 | ジェネンテック， インコーポレイテッド | 組み換えタンパク質の再折り畳み |
| JP5623743B2 (ja) | 2006-10-20 | 2014-11-12 | アムジエン・インコーポレーテツド | 安定なポリペプチド製剤 |
| ES2751022T3 (es) | 2007-07-09 | 2020-03-30 | Genentech Inc | Prevención de la reducción de enlaces disulfuro durante la producción recombinante de polipéptidos |
| EP2197911A2 (fr) * | 2007-09-14 | 2010-06-23 | Amgen Inc. | Populations d'anticorps homogènes |
| MX2011013898A (es) | 2009-06-22 | 2012-05-22 | Amgen Inc | Proteínas replegadas que usan un estado de oxido-reduccion quimicamente controlado. |
| JP2012531428A (ja) | 2009-06-25 | 2012-12-10 | アムジエン・インコーポレーテツド | 哺乳類以外の系で発現されるタンパク質の捕獲精製プロセス |
| US9005926B2 (en) | 2009-10-02 | 2015-04-14 | Biogen Idec Ma Inc. | Methods of preventing and removing trisulfide bonds |
| US8722615B2 (en) * | 2009-12-02 | 2014-05-13 | Acceleron Pharma, Inc. | Compositions and methods for increasing serum half-life |
| HUE042314T2 (hu) | 2011-02-07 | 2019-06-28 | Cerenis Therapeutics Holding Sa | Lipoprotein komplexek és azok gyártása és alkalmazásai |
| WO2012170938A1 (fr) | 2011-06-08 | 2012-12-13 | Acceleron Pharma Inc. | Compositions et procédés pour augmenter la demi-vie sérique |
| WO2012178102A2 (fr) | 2011-06-24 | 2012-12-27 | The Regents Of The Unversity Of Colorado, A Body Corporate | Compositions, procédés et utilisations de molécules de fusion de l'alpha-1 antitrypsine |
| EP2802653A4 (fr) | 2012-01-10 | 2015-09-02 | Univ Colorado Regents | Compositions de molécules de fusion de l'alpha-1 antitrypsine, procédés et utilisations associés |
| US9353165B2 (en) * | 2012-07-25 | 2016-05-31 | Grifols, S.A. | Purification of cell culture derived alpha1 protease inhibitor |
| KR20150037959A (ko) | 2012-08-02 | 2015-04-08 | 에프. 호프만-라 로슈 아게 | 단량체 및 다량체 분자의 제조 방법 및 이의 용도 |
| CN104902914B (zh) | 2012-09-11 | 2019-01-01 | 科荣生生物科学公司 | 高纯度和优异产量的正确折叠的依那西普 |
| WO2014137903A2 (fr) | 2013-03-08 | 2014-09-12 | Genzyme Corporation | Fabrication continue intégrée de substances de médicament de protéine thérapeutique |
| TWI671312B (zh) | 2014-01-17 | 2019-09-11 | 美商健臻公司 | 無菌層析法及製法 |
| TWI709569B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析樹脂及其用於製造方法的用途 |
| AR103172A1 (es) * | 2014-12-22 | 2017-04-19 | Novartis Ag | Reducción selectiva de residuos de cisteina en anticuerpos il-17 |
| EP3528787A4 (fr) | 2016-10-21 | 2020-05-06 | Amgen Inc. | Formulations pharmaceutiques et leurs procédés de préparation |
| CN112638488A (zh) | 2018-08-31 | 2021-04-09 | 建新公司 | 灭菌的层析树脂及其在制造工艺中的用途 |
| AU2019356564A1 (en) | 2018-10-11 | 2021-04-29 | Amgen Inc. | Downstream processing of bispecific antibody constructs |
| EP4267717A1 (fr) | 2020-12-22 | 2023-11-01 | Amgen Inc. | Procédé de culture cellulaire |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5453363A (en) * | 1985-10-23 | 1995-09-26 | Boehringer Mannheim Gmbh | Process for the activation of t-PA or Ing after genetic expression in prokaryotes |
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| EP0293785A3 (fr) | 1987-05-29 | 1990-05-02 | Oncogen Limited Partnership | Clonage et expression du facteur de croissance transformant simien SS-1 |
| US4970067A (en) * | 1988-12-12 | 1990-11-13 | Helene Curtis, Inc. | Method and composition to condition hair and impart semi-permanent hair set retention properties |
| GB8927546D0 (en) * | 1989-12-06 | 1990-02-07 | Ciba Geigy | Process for the production of biologically active tgf-beta |
| AU648214B2 (en) * | 1991-12-31 | 1994-04-14 | Lucky Limited | Recombinant gene coding for human alpha interferon and expression vector thereof, etc. |
| US5447851B1 (en) * | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
| AU685835B2 (en) * | 1993-08-04 | 1998-01-29 | Novartis Ag | High molecular weight desulphatohirudin |
| US6310185B1 (en) * | 1994-03-08 | 2001-10-30 | Memorial Sloan Kettering Cancer Center | Recombinant human anti-Lewis Y antibodies |
| WO1995032216A1 (fr) * | 1994-05-25 | 1995-11-30 | University Of Nebraska Board Of Regents | Hormones glycoproteiques biologiquement actives produites dans des cellules procaryotes |
| CA2195665A1 (fr) | 1994-07-22 | 1996-02-08 | Robert Frederick Geoffrey Booth | Compositions pharmaceutiques comprenant une proteine chimere liant le facteur de necrose tumorale |
| US5879673A (en) * | 1996-01-25 | 1999-03-09 | Genentech, Inc. | Administration of thrombopoietin on a single day only |
| US5935824A (en) * | 1996-01-31 | 1999-08-10 | Technologene, Inc. | Protein expression system |
| US6808902B1 (en) | 1999-11-12 | 2004-10-26 | Amgen Inc. | Process for correction of a disulfide misfold in IL-1Ra Fc fusion molecules |
| FR2803303B1 (fr) * | 2000-01-04 | 2002-05-10 | Aventis Pasteur | Glycoproteine d'enveloppe du vih modifiee chimiquement |
| CZ20032208A3 (cs) * | 2001-02-23 | 2004-01-14 | Immunex Corporation | Zvýšený výtěžek aktivních proteinů |
-
2002
- 2002-02-22 CZ CZ20032208A patent/CZ20032208A3/cs unknown
- 2002-02-22 US US10/080,471 patent/US7157557B2/en not_active Expired - Lifetime
- 2002-02-22 AT AT02725004T patent/ATE517909T1/de not_active IP Right Cessation
- 2002-02-22 SK SK1047-2003A patent/SK10472003A3/sk not_active Application Discontinuation
- 2002-02-22 HU HU0303246A patent/HUP0303246A2/hu unknown
- 2002-02-22 MX MXPA03007563A patent/MXPA03007563A/es active IP Right Grant
- 2002-02-22 IL IL15744602A patent/IL157446A0/xx unknown
- 2002-02-22 EE EEP200300408A patent/EE200300408A/xx unknown
- 2002-02-22 KR KR10-2003-7010687A patent/KR20040052481A/ko not_active Application Discontinuation
- 2002-02-22 WO PCT/US2002/005645 patent/WO2002068455A2/fr active Application Filing
- 2002-02-22 PL PL02374045A patent/PL374045A1/xx unknown
- 2002-02-22 AU AU2002255600A patent/AU2002255600B2/en not_active Expired
- 2002-02-22 JP JP2002567965A patent/JP2005505494A/ja active Pending
- 2002-02-22 EP EP02725004A patent/EP1366062B1/fr not_active Expired - Lifetime
- 2002-02-22 ES ES02725004T patent/ES2370235T3/es not_active Expired - Lifetime
- 2002-02-22 CA CA2438094A patent/CA2438094C/fr not_active Expired - Fee Related
- 2002-02-22 RU RU2003127830/13A patent/RU2316563C2/ru active
- 2002-02-22 CN CNA02805444XA patent/CN1547586A/zh active Pending
-
2003
- 2003-07-31 ZA ZA200305909A patent/ZA200305909B/en unknown
- 2003-08-13 BG BG108087A patent/BG108087A/bg unknown
-
2004
- 2004-01-30 HK HK04100666.9A patent/HK1059267A1/xx not_active IP Right Cessation
-
2006
- 2006-11-22 US US11/603,544 patent/US7544784B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| RU2003127830A (ru) | 2005-04-10 |
| WO2002068455A2 (fr) | 2002-09-06 |
| MXPA03007563A (es) | 2003-12-11 |
| ES2370235T3 (es) | 2011-12-13 |
| CZ20032208A3 (cs) | 2004-01-14 |
| CA2438094C (fr) | 2011-10-11 |
| BG108087A (bg) | 2005-04-30 |
| ZA200305909B (en) | 2004-06-04 |
| HUP0303246A2 (hu) | 2003-12-29 |
| US20070270577A1 (en) | 2007-11-22 |
| WO2002068455A3 (fr) | 2003-09-18 |
| IL157446A0 (en) | 2004-03-28 |
| KR20040052481A (ko) | 2004-06-23 |
| CN1547586A (zh) | 2004-11-17 |
| JP2005505494A (ja) | 2005-02-24 |
| EP1366062A2 (fr) | 2003-12-03 |
| US7157557B2 (en) | 2007-01-02 |
| US20020182665A1 (en) | 2002-12-05 |
| EP1366062B1 (fr) | 2011-07-27 |
| ATE517909T1 (de) | 2011-08-15 |
| CA2438094A1 (fr) | 2002-09-06 |
| EE200300408A (et) | 2003-12-15 |
| RU2316563C2 (ru) | 2008-02-10 |
| US7544784B2 (en) | 2009-06-09 |
| HK1059267A1 (en) | 2004-06-25 |
| PL374045A1 (en) | 2005-09-19 |
| AU2002255600B2 (en) | 2008-01-24 |
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| FC9A | Refused patent application |