SG177577A1 - Methods for purifying a target protein from one or more impurities in a sample - Google Patents
Methods for purifying a target protein from one or more impurities in a sample Download PDFInfo
- Publication number
- SG177577A1 SG177577A1 SG2012001483A SG2012001483A SG177577A1 SG 177577 A1 SG177577 A1 SG 177577A1 SG 2012001483 A SG2012001483 A SG 2012001483A SG 2012001483 A SG2012001483 A SG 2012001483A SG 177577 A1 SG177577 A1 SG 177577A1
- Authority
- SG
- Singapore
- Prior art keywords
- protein
- buffer
- target protein
- region containing
- cation exchange
- Prior art date
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Classifications
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- 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
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes
-
- 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
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- 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
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
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| US27370909P | 2009-08-07 | 2009-08-07 | |
| PCT/US2010/044539 WO2011017514A1 (en) | 2009-08-07 | 2010-08-05 | Methods for purifying a target protein from one or more impurities in a sample |
Publications (1)
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|---|---|
| SG177577A1 true SG177577A1 (en) | 2012-03-29 |
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Family Applications (1)
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|---|---|---|---|
| SG2012001483A SG177577A1 (en) | 2009-08-07 | 2010-08-05 | Methods for purifying a target protein from one or more impurities in a sample |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US8536316B2 (OSRAM) |
| EP (1) | EP2462157B1 (OSRAM) |
| JP (2) | JP5791602B2 (OSRAM) |
| KR (1) | KR101415660B1 (OSRAM) |
| CN (2) | CN102574911B (OSRAM) |
| ES (1) | ES2817802T3 (OSRAM) |
| IN (1) | IN2012DN00338A (OSRAM) |
| SG (1) | SG177577A1 (OSRAM) |
| WO (1) | WO2011017514A1 (OSRAM) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3237179B2 (ja) | 1992-03-18 | 2001-12-10 | 栗田工業株式会社 | 排超純水中の過酸化水素の除去方法 |
| EP2695889A1 (en) * | 2009-12-29 | 2014-02-12 | Dr. Reddy's Laboratories Limited | Protein purification by ion exchange |
| PL3299380T3 (pl) | 2010-05-25 | 2024-12-16 | F. Hoffmann-La Roche Ag | Sposoby oczyszczania polipeptydów |
| CN104722101A (zh) | 2010-07-30 | 2015-06-24 | Emd密理博公司 | 层析介质和方法 |
| BR102012012673A8 (pt) | 2011-05-27 | 2021-02-17 | Abbott Biotherapeutics Corp | célula ns0 modificada, métodos de produzir uma proteína recombinante, de obter uma célula hospedeira de mamífero, de sanitizar uma coluna de cromatografia com afinidade para proteína a e de tratar um paciente sofrendo de esclerose múltipla, vetor, composição, processos para colher uma proteína recombinante de uma cultura de célula e para produzir uma composição purificada de daclizumab, meios, e, tampão |
| EP2721052A1 (en) | 2011-06-16 | 2014-04-23 | DSM IP Assets B.V. | Single unit chromatography antibody purification |
| US9556258B2 (en) | 2011-07-08 | 2017-01-31 | Merck Sharp & Dohme Corp. | Purification of fusion proteins |
| JP2014527518A (ja) * | 2011-07-20 | 2014-10-16 | ゼプテオン インコーポレイテッド | ポリペプチド分離法 |
| BR112014002133A2 (pt) * | 2011-08-01 | 2017-02-21 | Avaxia Biologics Inc | anticorpo policlonal bovino específico para tnf humano |
| US9096648B2 (en) * | 2011-08-19 | 2015-08-04 | Emd Millipore Corporation | Methods of reducing level of one or more impurities in a sample during protein purification |
| KR20140062500A (ko) * | 2011-09-01 | 2014-05-23 | 휴먼 게놈 사이언시즈, 인크. | 바이러스 클리어런스 방법 |
| EP2578286A1 (en) | 2011-10-04 | 2013-04-10 | Merck Patent GmbH | Method and apparatus for chromatographic purification |
| SI2773438T2 (sl) * | 2011-11-02 | 2022-05-31 | F.Hoffmann-La Roche Ag | Izpiralna kromatografija s preobremenitvijo |
| WO2013075740A1 (en) | 2011-11-23 | 2013-05-30 | Sanofi | Antibody purification method |
| CN102492040B (zh) * | 2011-12-29 | 2014-06-25 | 嘉和生物药业有限公司 | 一种抗her2或/和抗her3抗体蛋白的纯化方法 |
| SG10201701224UA (en) * | 2012-03-12 | 2017-04-27 | Merck Patent Gmbh | Removal of protein aggregates from biopharmaceutical preparations in a flowthrough mode |
| EP2682168A1 (en) * | 2012-07-02 | 2014-01-08 | Millipore Corporation | Purification of biological molecules |
| EP2889617B1 (en) | 2012-08-27 | 2017-10-11 | Asahi Kasei Medical Co., Ltd. | Antibody purification method by means of temperature-responsive chromatography |
| PE20150996A1 (es) | 2012-09-11 | 2015-08-01 | Coherus Biosciences Inc | Etanercept correctamente plegado de alta pureza y excelente rendimiento |
| JP6360482B2 (ja) | 2012-09-17 | 2018-07-18 | ダブリュー・アール・グレース・アンド・カンパニー−コーンＷ Ｒ Ｇｒａｃｅ ＆ Ｃｏ−Ｃｏｎｎ | クロマトグラフィー担体及びデバイス |
| EP2931301B2 (en) * | 2012-12-17 | 2021-09-15 | Merck Sharp & Dohme Corp. | Process for purifying insulin and analogues thereof |
| RU2658909C2 (ru) | 2013-02-14 | 2018-06-26 | НАНОПАРЕЙЛ, ЭлЭлСи | Гибридные войлоки из нановолокон, полученных электропрядением |
| MX368177B (es) * | 2013-05-06 | 2019-09-23 | Sanofi Sa | Proceso continuo de múltiples etapas para purificar anticuerpos. |
| CN105848746B (zh) | 2013-09-05 | 2019-07-09 | 豪夫迈·罗氏有限公司 | 用于层析重复利用的方法 |
| US10519195B2 (en) * | 2013-09-17 | 2019-12-31 | Kaneka Corporation | Antibody purification method, antibody obtained therefrom, novel antibody purification method using cation exchanger, and antibody obtained therefrom |
| CN105980047B (zh) | 2013-12-12 | 2019-01-04 | Emd密理博公司 | 使用含丙烯酰胺的过滤器分离蛋白 |
| US10429359B2 (en) | 2014-02-14 | 2019-10-01 | Ge Healthcare Bio-Sciences Ab | Automated multi-step purification system |
| PL3116891T3 (pl) | 2014-03-10 | 2020-07-27 | Richter Gedeon Nyrt. | Oczyszczanie immunoglobuliny z zastosowaniem etapów wstępnego oczyszczania |
| CN104826617B (zh) * | 2014-03-25 | 2017-06-13 | 西北大学 | 一种用于蛋白质分离的wax/hic双功能混合模式色谱固定相及其制备方法 |
| JP6914189B2 (ja) | 2014-05-02 | 2021-08-04 | ダブリュー・アール・グレース・アンド・カンパニー−コーンＷ Ｒ Ｇｒａｃｅ ＆ Ｃｏ−Ｃｏｎｎ | 官能化担体材料並びに官能化担体材料を作製及び使用する方法 |
| EP3145951A1 (en) * | 2014-06-24 | 2017-03-29 | InSight Biopharmaceuticals Ltd. | Methods of purifying antibodies |
| DE102014010353B4 (de) | 2014-07-10 | 2024-09-12 | Sartorius Stedim Biotech Gmbh | Vorrichtung, Verwendung dieser Vorrichtung und Verfahren für die Stofftrennung mit verbesserter Ausnutzung der Kapazität chromatographischer Medien |
| WO2016093926A1 (en) | 2014-12-08 | 2016-06-16 | Emd Millipore Corporation | Mixed bed ion exchange adsorber |
| SG10201911134QA (en) | 2015-06-05 | 2020-01-30 | Grace W R & Co | Adsorbent bioprocessing clarification agents and methods of making and using the same |
| EP3440093B1 (en) * | 2016-04-05 | 2024-11-13 | Haemonetics Corporation | Methods and devices for the enrichment of immunoglobulin from blood |
| CN107964044B (zh) * | 2016-10-19 | 2021-11-19 | 无锡科捷诺生物科技有限责任公司 | 从乳样中纯化抗cd20单克隆抗体的方法 |
| WO2019183334A1 (en) | 2018-03-21 | 2019-09-26 | Waters Technologies Corporation | Non-antibody high-affinity-based sample preparation, sorbents, devices and methods |
| EP3546475A1 (en) | 2018-03-27 | 2019-10-02 | Sanofi | Full flow-through process for purifying recombinant proteins |
| CN113166200B (zh) * | 2018-12-21 | 2024-03-01 | 上海药明生物技术有限公司 | 一种提高蛋白a层析法去除聚集体的方法 |
| FR3099066B1 (fr) | 2019-07-26 | 2021-08-13 | Novasep Process | Procédé de purification d’une substance cible avec inactivation virale |
| TW202128264A (zh) * | 2019-09-25 | 2021-08-01 | 瑞士商赫孚孟拉羅股份公司 | 使用經預測之溶離緩衝鹽濃度的陽離子層析法 |
| CA3156649A1 (en) * | 2019-10-04 | 2021-04-08 | Merck Patent Gmbh | PROTEIN PURIFICATION AND VIRAL INACTIVATION |
| CN110724204B (zh) * | 2019-11-18 | 2021-10-22 | 广东菲鹏制药股份有限公司 | Fc融合蛋白的纯化方法 |
| CN113845562A (zh) * | 2020-06-28 | 2021-12-28 | 佛山汉腾生物科技有限公司 | 目的蛋白纯化方法 |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4490937A (en) * | 1981-12-07 | 1985-01-01 | Amcor Ltd. | Insect electrocution device |
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5256694A (en) * | 1984-09-22 | 1993-10-26 | Basf Aktiengesellschaft | Diarylacetylenes, their preparation and their use |
| US5091178A (en) * | 1986-02-21 | 1992-02-25 | Oncogen | Tumor therapy with biologically active anti-tumor antibodies |
| US6054051A (en) * | 1996-01-17 | 2000-04-25 | Genentech, Inc. | Tangential-flow filtration system |
| ES2545067T3 (es) * | 2002-04-26 | 2015-09-08 | Genentech, Inc. | Purificación de proteínas basada en la no afinidad |
| WO2004024752A1 (ja) * | 2002-09-11 | 2004-03-25 | Chugai Seiyaku Kabushiki Kaisha | タンパク質精製方法 |
| GB0304576D0 (en) * | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
| EP1685161A1 (en) * | 2004-08-30 | 2006-08-02 | Lonza Biologics plc | Affinity- plus ion exchange-chromatography for purifying antibodies |
| EP2069387A4 (en) | 2006-06-14 | 2011-02-02 | Glaxosmithkline Llc | METHODS OF PURIFYING ANTIBODIES USING HYDROXYAPATITE CERAMIC |
| EA017152B1 (ru) * | 2006-08-28 | 2012-10-30 | Арес Трейдинг С.А. | СПОСОБ ОЧИСТКИ Fc-СОДЕРЖАЩИХ БЕЛКОВ |
| UA99263C2 (ru) * | 2006-08-28 | 2012-08-10 | Арес Трейдинг С.А. | СПОСОБ ОЧИСТКИ Fc-СЛИТОГО БЕЛКА |
| CA2673771A1 (en) * | 2007-01-17 | 2008-07-24 | Merck Serono S.A. | Process for the purification of fc-containing proteins |
| US9433922B2 (en) * | 2007-08-14 | 2016-09-06 | Emd Millipore Corporation | Media for membrane ion exchange chromatography based on polymeric primary amines, sorption device containing that media, and chromatography scheme and purification method using the same |
| US20090149638A1 (en) * | 2007-10-03 | 2009-06-11 | Ley Arthur C | Systems and methods for purifying proteins |
| CN102027010A (zh) * | 2008-05-15 | 2011-04-20 | 诺沃-诺迪斯克有限公司 | 抗体纯化方法 |
| WO2010048192A2 (en) * | 2008-10-20 | 2010-04-29 | Abbott Laboratories | Viral inactivation during purification of antibodies |
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- 2010-08-05 CN CN201080035153.XA patent/CN102574911B/zh not_active Expired - Fee Related
- 2010-08-05 JP JP2012523945A patent/JP5791602B2/ja not_active Expired - Fee Related
- 2010-08-05 ES ES10807153T patent/ES2817802T3/es active Active
- 2010-08-05 CN CN201710418825.9A patent/CN107188960A/zh active Pending
- 2010-08-05 KR KR1020127001161A patent/KR101415660B1/ko not_active Expired - Fee Related
- 2010-08-05 SG SG2012001483A patent/SG177577A1/en unknown
- 2010-08-05 EP EP10807153.1A patent/EP2462157B1/en active Active
- 2010-08-05 IN IN338DEN2012 patent/IN2012DN00338A/en unknown
- 2010-08-05 WO PCT/US2010/044539 patent/WO2011017514A1/en not_active Ceased
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2015
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Also Published As
| Publication number | Publication date |
|---|---|
| EP2462157A1 (en) | 2012-06-13 |
| JP2015157846A (ja) | 2015-09-03 |
| IN2012DN00338A (OSRAM) | 2015-05-22 |
| WO2011017514A1 (en) | 2011-02-10 |
| JP6335838B2 (ja) | 2018-05-30 |
| ES2817802T3 (es) | 2021-04-08 |
| CN102574911A (zh) | 2012-07-11 |
| EP2462157A4 (en) | 2012-12-26 |
| EP2462157B1 (en) | 2020-06-17 |
| JP5791602B2 (ja) | 2015-10-07 |
| JP2013501721A (ja) | 2013-01-17 |
| CN102574911B (zh) | 2017-06-06 |
| KR20120089432A (ko) | 2012-08-10 |
| KR101415660B1 (ko) | 2014-07-16 |
| CN107188960A (zh) | 2017-09-22 |
| US20110065901A1 (en) | 2011-03-17 |
| US8536316B2 (en) | 2013-09-17 |
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