AU2014264697B2 - Continuous multistep process for purifying antibodies - Google Patents
Continuous multistep process for purifying antibodies Download PDFInfo
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- AU2014264697B2 AU2014264697B2 AU2014264697A AU2014264697A AU2014264697B2 AU 2014264697 B2 AU2014264697 B2 AU 2014264697B2 AU 2014264697 A AU2014264697 A AU 2014264697A AU 2014264697 A AU2014264697 A AU 2014264697A AU 2014264697 B2 AU2014264697 B2 AU 2014264697B2
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- 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
-
- 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
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12M—APPARATUS FOR ENZYMOLOGY OR MICROBIOLOGY; APPARATUS FOR CULTURING MICROORGANISMS FOR PRODUCING BIOMASS, FOR GROWING CELLS OR FOR OBTAINING FERMENTATION OR METABOLIC PRODUCTS, i.e. BIOREACTORS OR FERMENTERS
- C12M47/00—Means for after-treatment of the produced biomass or of the fermentation or metabolic products, e.g. storage of biomass
- C12M47/12—Purification
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Sustainable Development (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Water Supply & Treatment (AREA)
- Oncology (AREA)
- Cell Biology (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP13305593 | 2013-05-06 | ||
| EP13305593.9 | 2013-05-06 | ||
| PCT/EP2014/059246 WO2014180852A1 (en) | 2013-05-06 | 2014-05-06 | Continuous multistep process for purifying antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2014264697A1 AU2014264697A1 (en) | 2015-11-26 |
| AU2014264697B2 true AU2014264697B2 (en) | 2019-08-22 |
Family
ID=48430636
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2014264697A Active AU2014264697B2 (en) | 2013-05-06 | 2014-05-06 | Continuous multistep process for purifying antibodies |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US10793622B2 (enExample) |
| EP (2) | EP3301115B1 (enExample) |
| JP (2) | JP6463734B2 (enExample) |
| KR (1) | KR102272851B1 (enExample) |
| CN (2) | CN105358572A (enExample) |
| AU (1) | AU2014264697B2 (enExample) |
| BR (1) | BR112015027812B1 (enExample) |
| CA (1) | CA2911462C (enExample) |
| CY (1) | CY1125281T1 (enExample) |
| DK (2) | DK3301115T3 (enExample) |
| ES (2) | ES2665645T3 (enExample) |
| HU (2) | HUE038741T2 (enExample) |
| IL (1) | IL242408B (enExample) |
| MX (1) | MX368177B (enExample) |
| NO (1) | NO2994485T3 (enExample) |
| RU (1) | RU2662668C2 (enExample) |
| SG (1) | SG11201508968XA (enExample) |
| TW (2) | TWI631132B (enExample) |
| WO (1) | WO2014180852A1 (enExample) |
Families Citing this family (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10967298B2 (en) | 2012-03-15 | 2021-04-06 | Flodesign Sonics, Inc. | Driver and control for variable impedence load |
| US9458450B2 (en) | 2012-03-15 | 2016-10-04 | Flodesign Sonics, Inc. | Acoustophoretic separation technology using multi-dimensional standing waves |
| US9950282B2 (en) | 2012-03-15 | 2018-04-24 | Flodesign Sonics, Inc. | Electronic configuration and control for acoustic standing wave generation |
| US10704021B2 (en) | 2012-03-15 | 2020-07-07 | Flodesign Sonics, Inc. | Acoustic perfusion devices |
| AU2013334644B2 (en) * | 2012-10-24 | 2018-07-12 | Genzyme Corporation | Elution of biomolecules from multi-modal resins using mes and mops as mobile phase modifiers |
| EP3048109A4 (en) * | 2013-09-17 | 2017-04-19 | Kaneka Corporation | Novel antibody purification method and antibody obtained therefrom, and novel antibody purification method using cation exchanger and antibody obtained therefrom |
| CA2935960C (en) | 2014-01-08 | 2023-01-10 | Bart Lipkens | Acoustophoresis device with dual acoustophoretic chamber |
| GB201503578D0 (en) * | 2015-03-03 | 2015-04-15 | Ge Healthcare Bio Sciences Ab | Sanitization method for affinity chromatography matrices |
| US11021699B2 (en) | 2015-04-29 | 2021-06-01 | FioDesign Sonics, Inc. | Separation using angled acoustic waves |
| US11708572B2 (en) | 2015-04-29 | 2023-07-25 | Flodesign Sonics, Inc. | Acoustic cell separation techniques and processes |
| US11377651B2 (en) | 2016-10-19 | 2022-07-05 | Flodesign Sonics, Inc. | Cell therapy processes utilizing acoustophoresis |
| EP3015542A1 (de) * | 2015-05-07 | 2016-05-04 | Bayer Technology Services GmbH | Modulare anlage und verfahren zur kontinuierlichen, keimreduzierten produktion und/oder aufbereitung eines produktes |
| US11459540B2 (en) | 2015-07-28 | 2022-10-04 | Flodesign Sonics, Inc. | Expanded bed affinity selection |
| US11474085B2 (en) | 2015-07-28 | 2022-10-18 | Flodesign Sonics, Inc. | Expanded bed affinity selection |
| US20170101437A1 (en) * | 2015-10-09 | 2017-04-13 | Hetero Drugs Ltd. | Process for purification of darbepoetin alfa |
| US11214789B2 (en) | 2016-05-03 | 2022-01-04 | Flodesign Sonics, Inc. | Concentration and washing of particles with acoustics |
| US11085035B2 (en) | 2016-05-03 | 2021-08-10 | Flodesign Sonics, Inc. | Therapeutic cell washing, concentration, and separation utilizing acoustophoresis |
| US20190211055A1 (en) * | 2016-09-14 | 2019-07-11 | Kinbio Ltd. | Methods of purifying and qualifying antibodies |
| CN110494543A (zh) | 2016-10-19 | 2019-11-22 | 弗洛设计声能学公司 | 通过声学的亲和细胞提取 |
| CN110582510B (zh) * | 2017-03-24 | 2023-09-15 | 科学与工业研究委员会 | 用于纯化重组抗体片段的方法 |
| GB201711481D0 (en) * | 2017-07-17 | 2017-08-30 | Ucb Biopharma Sprl | Protein purification |
| US11584777B2 (en) | 2017-08-31 | 2023-02-21 | Green Cross Corporation | Method for purifying a sulfatase protein |
| KR20220066413A (ko) | 2017-12-14 | 2022-05-24 | 프로디자인 소닉스, 인크. | 음향 트랜스듀서 구동기 및 제어기 |
| CN119881293A (zh) | 2018-03-21 | 2025-04-25 | 沃特世科技公司 | 基于非抗体高亲和力的样品制备、吸附剂、装置和方法 |
| EP3546475A1 (en) | 2018-03-27 | 2019-10-02 | Sanofi | Full flow-through process for purifying recombinant proteins |
| US12071607B2 (en) * | 2018-06-01 | 2024-08-27 | Lonza Ltd. | Midscale model for organic growth and phasing |
| KR102337683B1 (ko) | 2018-09-21 | 2021-12-13 | 주식회사 녹십자 | 고효율 항-tfpi 항체 조성물 |
| EP3636657A1 (en) | 2018-10-08 | 2020-04-15 | Ablynx N.V. | Chromatography-free antibody purification method |
| WO2020084503A1 (en) * | 2018-10-26 | 2020-04-30 | Cadila Healthcare Limited | A composition comprising antibody with reduced level of basic variants thereof |
| WO2020183332A1 (en) * | 2019-03-11 | 2020-09-17 | Intas Pharmaceuticals Ltd. | Purification of adalimumab using tandem chromatography |
| AU2020253381A1 (en) * | 2019-04-03 | 2021-12-02 | Genzyme Corporation | Continuous production of recombinant proteins |
| CN114026108B (zh) * | 2019-06-28 | 2024-09-10 | 夏尔巴生物技术(苏州)有限公司 | 无缝连续流层析方法 |
| JP2023500775A (ja) * | 2019-09-23 | 2023-01-11 | メルク・シャープ・アンド・ドーム・エルエルシー | 宿主細胞タンパク質が減少し、ポリソルベート－８０安定性が増加した、抗ｃｔｌａ４モノクローナル抗体を含む方法および組成物 |
| KR102154952B1 (ko) * | 2020-02-21 | 2020-09-10 | 프레스티지바이오로직스 주식회사 | 아달리무맙의 Non-Protein A 정제방법 |
| CN112574321B (zh) * | 2020-12-30 | 2023-10-20 | 上海赛金生物医药有限公司 | 一种捕获单克隆抗体-肿瘤坏死因子融合蛋白的亲和纯化方法 |
| WO2022234412A1 (en) | 2021-05-03 | 2022-11-10 | Lupin Limited | A process for purification of fc-fusion proteins |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070259453A1 (en) * | 2004-10-21 | 2007-11-08 | Ge Healthcare Bio-Sciences Ab | Method of Antibody Purification |
| WO2009099829A1 (en) * | 2008-01-30 | 2009-08-13 | Genentech, Inc. | Composition comprising antibody that binds to domain ii of her2 and acidic variants thereof |
| WO2009111347A1 (en) * | 2008-02-29 | 2009-09-11 | Biogen Idec Ma Inc. | Purified immunoglobulin fusion proteins and methods of their purification |
| WO2011090719A2 (en) * | 2009-12-29 | 2011-07-28 | Dr. Reddy's Laboratories Ltd. | Protein purification by ion exchange |
| WO2013075849A1 (en) * | 2011-11-23 | 2013-05-30 | Sanofi | Protein purification using bis-tris buffer |
Family Cites Families (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0391934A1 (en) | 1987-10-23 | 1990-10-17 | Schering Corporation | Method of purifying protein |
| CA2106612C (en) | 1993-09-21 | 2001-02-06 | Diana Pliura | Displacement chromatography process |
| DE69416103T2 (de) | 1993-09-21 | 1999-08-05 | Hemosol Inc., Etobicoke, Ontario | Verdrängungschromatographisches verfahren und gereinigtes hämoglobin |
| US5891741A (en) | 1997-05-16 | 1999-04-06 | Coulter International Corp. | Antibody-aminodextran-phycobiliprotein conjugates |
| CN1136317C (zh) | 1999-03-12 | 2004-01-28 | 中国人民解放军第四军医大学 | 单克隆抗体双段和单段的制备方法 |
| US20020009445A1 (en) | 2000-07-12 | 2002-01-24 | Yansheng Du | Human beta-amyloid antibody and use thereof for treatment of alzheimer's disease |
| US6602855B2 (en) | 2001-04-30 | 2003-08-05 | Syn X Pharma, Inc. | Biopolymer marker indicative of disease state having a molecular weight of 1449 daltons |
| CN1504482A (zh) | 2002-12-03 | 2004-06-16 | 北京优力凯生物技术有限责任公司 | 无细胞百日咳抗原蛋白的分离纯化方法 |
| DK1745075T3 (da) | 2004-04-21 | 2013-06-24 | Brigham & Womens Hospital | Poly-n-acetylglucosamin (pnag/dpnag)-bindende peptider og fremgangsmåder til anvendelse deraf |
| EA015584B1 (ru) | 2005-03-23 | 2011-10-31 | Генмаб А/С | Антитело к cd38 человека и его применение |
| CN1814775A (zh) | 2005-12-06 | 2006-08-09 | 中国海洋大学 | 一种抗病毒活性寡聚肽的制备方法 |
| EP1914242A1 (en) * | 2006-10-19 | 2008-04-23 | Sanofi-Aventis | Novel anti-CD38 antibodies for the treatment of cancer |
| EP2167526B1 (en) | 2007-07-11 | 2011-03-30 | Novo Nordisk A/S | Purification of factor viii using a mixed-mode or multimodal resin |
| ME01026B (me) | 2007-11-16 | 2012-10-20 | Univ Rockefeller | Antitijela specifična za protofibrilni oblik beta-amiloid proteina |
| US20110105725A1 (en) | 2008-05-15 | 2011-05-05 | Novo Nordisk A/S | Antibody purification process |
| US20110237781A1 (en) * | 2008-07-18 | 2011-09-29 | Talecris Biotherapeutics, Inc. | Method of preparing alpha-1 proteinase inhibitor |
| EP2360183B1 (en) | 2008-12-19 | 2016-07-27 | Takeda Pharmaceutical Company Limited | Antibody purification method by mixed mode chromatography utilizing an arginine-containing loading solution |
| AU2010205007A1 (en) | 2009-01-13 | 2011-07-07 | Ge Healthcare Bio-Sciences Ab | Precipitation of biomolecules with negatively charged polymers |
| KR101224468B1 (ko) * | 2009-05-20 | 2013-01-23 | 주식회사 파멥신 | 신규한 형태의 이중표적항체 및 그 용도 |
| CN102574911B (zh) * | 2009-08-07 | 2017-06-06 | Emd密理博公司 | 从样品的一或多种杂质中纯化靶蛋白的方法 |
| US9527010B2 (en) * | 2009-09-25 | 2016-12-27 | Ge Healthcare Bio-Sciences Corp. | Separation system and method |
| EP2490780A4 (en) | 2009-10-20 | 2014-04-09 | Merck Sharp & Dohme | USE OF A MIXED MODE CHROMATOGRAPHY FOR THE DETECTION AND PURIFICATION OF BASIC ANTIBODY PRODUCTS |
| EP2415779B1 (en) | 2010-08-02 | 2015-01-21 | ratiopharm GmbH | Method of producing and purifying an active soluble sialyltransferase |
| US20120238730A1 (en) * | 2011-03-15 | 2012-09-20 | Abbott Laboratories | Integrated approach to the isolation and purification of antibodies |
| CN107915769A (zh) * | 2011-03-29 | 2018-04-17 | 葛兰素史密斯克莱有限责任公司 | 用于蛋白纯化的缓冲液体系 |
| CA2839542A1 (en) | 2011-06-17 | 2012-12-20 | Constitution Medical, Inc. | Fixative and staining solutions |
| WO2013028330A2 (en) | 2011-08-19 | 2013-02-28 | Emd Millipore Corporation | Methods of reducing level of one of more impurities in a sample during protein purification |
| EP2578286A1 (en) * | 2011-10-04 | 2013-04-10 | Merck Patent GmbH | Method and apparatus for chromatographic purification |
| SG11201401360XA (en) * | 2011-10-25 | 2014-05-29 | Onclave Therapeutics Ltd | Antibody formulations and methods |
-
2014
- 2014-05-06 HU HUE14722194A patent/HUE038741T2/hu unknown
- 2014-05-06 SG SG11201508968XA patent/SG11201508968XA/en unknown
- 2014-05-06 TW TW103116153A patent/TWI631132B/zh not_active IP Right Cessation
- 2014-05-06 EP EP17200909.4A patent/EP3301115B1/en active Active
- 2014-05-06 WO PCT/EP2014/059246 patent/WO2014180852A1/en not_active Ceased
- 2014-05-06 RU RU2015151869A patent/RU2662668C2/ru active
- 2014-05-06 DK DK17200909.4T patent/DK3301115T3/da active
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- 2014-05-06 TW TW107117528A patent/TWI675041B/zh not_active IP Right Cessation
- 2014-05-06 CA CA2911462A patent/CA2911462C/en active Active
- 2014-05-06 MX MX2015015482A patent/MX368177B/es active IP Right Grant
- 2014-05-06 AU AU2014264697A patent/AU2014264697B2/en active Active
- 2014-05-06 DK DK14722194.9T patent/DK2994485T3/en active
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- 2014-05-06 US US14/889,397 patent/US10793622B2/en active Active
- 2014-05-06 CN CN201480038360.9A patent/CN105358572A/zh active Pending
- 2014-05-06 KR KR1020157032904A patent/KR102272851B1/ko active Active
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- 2014-05-06 CN CN202310118200.6A patent/CN116003579A/zh active Pending
- 2014-05-06 NO NO14722194A patent/NO2994485T3/no unknown
- 2014-05-06 EP EP14722194.9A patent/EP2994485B1/en active Active
- 2014-05-06 ES ES17200909T patent/ES2905675T3/es active Active
- 2014-05-06 HU HUE17200909A patent/HUE057119T2/hu unknown
-
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- 2015-11-02 IL IL242408A patent/IL242408B/en active IP Right Grant
-
2019
- 2019-01-10 JP JP2019002288A patent/JP2019104735A/ja active Pending
-
2022
- 2022-02-09 CY CY20221100113T patent/CY1125281T1/el unknown
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070259453A1 (en) * | 2004-10-21 | 2007-11-08 | Ge Healthcare Bio-Sciences Ab | Method of Antibody Purification |
| WO2009099829A1 (en) * | 2008-01-30 | 2009-08-13 | Genentech, Inc. | Composition comprising antibody that binds to domain ii of her2 and acidic variants thereof |
| WO2009111347A1 (en) * | 2008-02-29 | 2009-09-11 | Biogen Idec Ma Inc. | Purified immunoglobulin fusion proteins and methods of their purification |
| WO2011090719A2 (en) * | 2009-12-29 | 2011-07-28 | Dr. Reddy's Laboratories Ltd. | Protein purification by ion exchange |
| WO2013075849A1 (en) * | 2011-11-23 | 2013-05-30 | Sanofi | Protein purification using bis-tris buffer |
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