TWI596108B - 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 - Google Patents
包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 Download PDFInfo
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- TWI596108B TWI596108B TW101119728A TW101119728A TWI596108B TW I596108 B TWI596108 B TW I596108B TW 101119728 A TW101119728 A TW 101119728A TW 101119728 A TW101119728 A TW 101119728A TW I596108 B TWI596108 B TW I596108B
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Classifications
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- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/30—Processes for preparing, regenerating, or reactivating
- B01J20/32—Impregnating or coating ; Solid sorbent compositions obtained from processes involving impregnating or coating
- B01J20/3231—Impregnating or coating ; Solid sorbent compositions obtained from processes involving impregnating or coating characterised by the coating or impregnating layer
- B01J20/3242—Layers with a functional group, e.g. an affinity material, a ligand, a reactant or a complexing group
- B01J20/3268—Macromolecular compounds
- B01J20/3272—Polymers obtained by reactions otherwise than involving only carbon to carbon unsaturated bonds
- B01J20/3274—Proteins, nucleic acids, polysaccharides, antibodies or antigens
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3804—Affinity chromatography
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- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3804—Affinity chromatography
- B01D15/3809—Affinity chromatography of the antigen-antibody type, e.g. protein A, G or L chromatography
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- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/281—Sorbents specially adapted for preparative, analytical or investigative chromatography
- B01J20/286—Phases chemically bonded to a substrate, e.g. to silica or to polymers
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/30—Processes for preparing, regenerating, or reactivating
- B01J20/32—Impregnating or coating ; Solid sorbent compositions obtained from processes involving impregnating or coating
- B01J20/3231—Impregnating or coating ; Solid sorbent compositions obtained from processes involving impregnating or coating characterised by the coating or impregnating layer
- B01J20/3242—Layers with a functional group, e.g. an affinity material, a ligand, a reactant or a complexing group
- B01J20/3268—Macromolecular compounds
- B01J20/3272—Polymers obtained by reactions otherwise than involving only carbon to carbon unsaturated bonds
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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
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1271—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Micrococcaceae (F), e.g. Staphylococcus
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Analytical Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161494701P | 2011-06-08 | 2011-06-08 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| TW201305191A TW201305191A (zh) | 2013-02-01 |
| TWI596108B true TWI596108B (zh) | 2017-08-21 |
Family
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Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW101119728A TWI596108B (zh) | 2011-06-08 | 2012-06-07 | 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 |
| TW104122522A TWI570134B (zh) | 2011-06-08 | 2012-06-07 | 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 |
| TW105142237A TWI638828B (zh) | 2011-06-08 | 2012-06-07 | 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
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| TW104122522A TWI570134B (zh) | 2011-06-08 | 2012-06-07 | 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 |
| TW105142237A TWI638828B (zh) | 2011-06-08 | 2012-06-07 | 包含新穎之基於金黃色葡萄球菌蛋白質ａ之配位子的層析基質 |
Country Status (13)
| Country | Link |
|---|---|
| US (5) | US8754196B2 (OSRAM) |
| EP (2) | EP2532672B1 (OSRAM) |
| JP (4) | JP5756428B2 (OSRAM) |
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| CN (2) | CN102895960B (OSRAM) |
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Families Citing this family (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040067532A1 (en) | 2002-08-12 | 2004-04-08 | Genetastix Corporation | High throughput generation and affinity maturation of humanized antibody |
| CA3187687A1 (en) | 2007-09-14 | 2009-03-19 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| US8592555B2 (en) | 2008-08-11 | 2013-11-26 | Emd Millipore Corporation | Immunoglobulin-binding proteins with improved specificity |
| SG195555A1 (en) | 2008-12-24 | 2013-12-30 | Emd Millipore Corp | Caustic stable chromatography ligands |
| SG186552A1 (en) * | 2011-06-08 | 2013-01-30 | Emd Millipore Corp | Chromatography matrices including novel staphylococcus aureus protein a based ligands |
| WO2013081540A1 (en) * | 2011-11-30 | 2013-06-06 | Ge Healthcare Bio-Sciences Ab | Affinity chromatography matrix |
| EP2682168A1 (en) | 2012-07-02 | 2014-01-08 | Millipore Corporation | Purification of biological molecules |
| JP6182210B2 (ja) | 2012-06-29 | 2017-08-16 | イー・エム・デイー・ミリポア・コーポレイシヨン | タンパク質精製プロセス中のウイルスの不活性化方法 |
| MY178616A (en) | 2012-09-17 | 2020-10-19 | Grace W R & Co | Chromatography media and devices |
| CN104768536B (zh) | 2012-09-17 | 2019-03-29 | 格雷斯公司 | 官能化微粒状载体材料和其制备和使用方法 |
| ES2735354T3 (es) | 2013-03-14 | 2019-12-18 | Emd Millipore Corp | Métodos para aumentar la pureza de proteínas utilizando la cromatografía basada en proteína A |
| CN105377880B (zh) * | 2013-07-10 | 2020-08-07 | 通用电气医疗集团生物工艺研发股份公司 | 突变的免疫球蛋白结合多肽 |
| ES2737078T3 (es) * | 2013-09-04 | 2020-01-10 | Emd Millipore Corp | Cromatografía de Proteína A |
| PL3094390T3 (pl) | 2014-01-16 | 2021-12-06 | W.R. Grace & Co. - Conn. | Nośniki do chromatografii powinowactwa i urządzenia do chromatografii |
| PL3137209T3 (pl) | 2014-05-02 | 2023-01-02 | W.R. Grace & Co. - Conn. | Funkcjonalizowany materiał nośnikowy i sposoby wytwarzania oraz stosowania funkcjonalizowanego materiału nośnikowego |
| ES2920381T3 (es) * | 2014-08-15 | 2022-08-03 | Merck Patent Gmbh | Purificación de inmunoglobulinas a partir de plasma |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| CN104399283B (zh) * | 2014-12-04 | 2016-02-17 | 江西省农业科学院农产品质量安全与标准研究所 | 黄曲霉毒素b1适配体亲和柱的制备方法 |
| CN104645949B (zh) * | 2015-02-04 | 2017-01-25 | 浙江大学 | 一种以四肽为功能配基的亲和层析介质及其制备方法 |
| JP6805831B2 (ja) | 2015-02-05 | 2020-12-23 | 三菱ケミカル株式会社 | 免疫グロブリンに親和性を有するタンパク質、およびそれを用いたアフィニティ分離剤、液体クロマトグラフィー用カラム |
| DK3253785T3 (da) | 2015-02-06 | 2019-07-08 | Navigo Proteins Gmbh | Hidtil ukendte egfr-bindingsproteiner |
| GB201503578D0 (en) * | 2015-03-03 | 2015-04-15 | Ge Healthcare Bio Sciences Ab | Sanitization method for affinity chromatography matrices |
| CN107429244A (zh) * | 2015-03-26 | 2017-12-01 | Jsr株式会社 | 免疫球蛋白结合蛋白质和使用其的亲和载体 |
| KR20170121746A (ko) * | 2015-04-13 | 2017-11-02 | 후지필름 가부시키가이샤 | 단쇄 펩타이드 고정화 담체의 제조 방법 및 단쇄 펩타이드 고정화 담체 |
| US10695744B2 (en) | 2015-06-05 | 2020-06-30 | W. R. Grace & Co.-Conn. | Adsorbent biprocessing clarification agents and methods of making and using the same |
| ES2916101T3 (es) | 2015-07-16 | 2022-06-28 | Navigo Proteins Gmbh | Nuevas proteínas de unión a inmunoglobulina y su uso en la purificación por afinidad |
| JP2018520675A (ja) | 2015-07-20 | 2018-08-02 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツングＮａｖｉｇｏ Ｐｒｏｔｅｉｎｓ ＧｍｂＨ | ジユビキチン変異タンパク質をベースとした新規結合タンパク質及びその生成方法 |
| GB201515339D0 (en) * | 2015-08-28 | 2015-10-14 | Ge Healthcare Bio Sciences Ab | A seperation matrix and a method of seperating antibodies |
| US10697982B2 (en) | 2015-09-08 | 2020-06-30 | Merck Patent Gmbh | Methods of evaluating quality of a chromatography media which binds anti-A or anti-B antibodies |
| US10697983B2 (en) * | 2015-09-08 | 2020-06-30 | Merck Patent Gmbh | Methods of evaluating quality of media suitable for removing anti-A or anti-B antibodies |
| US20170066839A1 (en) | 2015-09-08 | 2017-03-09 | Merck Patent Gmbh | Novel affinity chromatography media for removal of anti-a and/or anti-b antibodies |
| CN105413644A (zh) * | 2015-12-02 | 2016-03-23 | 南昌大学 | 基于特异结合黄曲霉毒素单域重链抗体的亲和吸附材料 |
| KR101993845B1 (ko) * | 2016-02-18 | 2019-06-28 | (주)에이피테크놀로지 | 알칼리 저항성이 증대된 항체 친화성 리간드 |
| AU2017260274A1 (en) | 2016-05-04 | 2018-11-01 | Navigo Proteins Gmbh | Targeted compounds for the site-specific coupling of chemical moieties comprising a peptide linker |
| CN109311949B (zh) | 2016-05-11 | 2022-09-16 | 思拓凡生物工艺研发有限公司 | 储存分离基质的方法 |
| ES2914278T3 (es) * | 2016-05-11 | 2022-06-08 | Cytiva Bioprocess R & D Ab | Polipéptidos de unión a inmunoglobulina mutados |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| EP3455243B1 (en) | 2016-05-11 | 2021-03-24 | Cytiva BioProcess R&D AB | Separation matrix |
| ES2909833T3 (es) | 2016-05-11 | 2022-05-10 | Cytiva Bioprocess R & D Ab | Método de limpieza y/o desinfección de una matriz de separación |
| JP7031934B2 (ja) | 2016-05-11 | 2022-03-08 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックス |
| KR101857953B1 (ko) * | 2016-07-06 | 2018-05-16 | 아미코젠주식회사 | 알칼리 내성이 증가된 변이 면역글로불린 결합 단백질 |
| AU2017311542B2 (en) | 2016-08-11 | 2021-06-24 | Repligen Corporation | Alkaline stable Fc—binding proteins for affinity chromatography |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| EP3551646A1 (en) | 2016-12-12 | 2019-10-16 | HurraH S.à r.l. | Compositions and methods for increasing the immunoglobulin binding capacities of immunoglobulin-binding polypeptides and oligopeptides |
| CN106596822B (zh) * | 2016-12-16 | 2018-01-19 | 南京市产品质量监督检验院 | 一种食品中金黄色葡萄球菌苯酚可溶性调控蛋白的检测方法 |
| GB201708277D0 (en) | 2017-05-24 | 2017-07-05 | Ge Healthcare | A Recombinant protein |
| EP4491268A3 (en) | 2017-08-07 | 2025-04-09 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| EP3521304B9 (en) | 2018-02-01 | 2023-10-04 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| WO2019091918A1 (en) | 2017-11-07 | 2019-05-16 | Navigo Proteins Gmbh | Fusion proteins with specificity for ed-b and long serum half-life for diagnosis or treatment of cancer |
| WO2019093439A1 (ja) | 2017-11-09 | 2019-05-16 | 東ソー株式会社 | 免疫グロブリン結合性タンパク質 |
| US20210130395A1 (en) * | 2018-05-11 | 2021-05-06 | William Marsh Rice University | Proximity induced site-specific antibody conjugation |
| KR102055708B1 (ko) | 2018-06-26 | 2019-12-13 | 동일플랜트 주식회사 | 스팀 배기관에 삽입된 히트파이프를 이용한 드래프트 방식 복수기 |
| EP3842536A4 (en) | 2018-08-24 | 2023-01-18 | JSR Corporation | IMMUNOGLOBULIN BINDING PROTEIN AND AFFINITY SUPPORT USING THE SAME |
| GB201904125D0 (en) | 2019-03-26 | 2019-05-08 | Ge Healthcare Bio Sciences Ab | Method for sanitization of a chromatography column |
| CN112210013A (zh) * | 2019-07-03 | 2021-01-12 | 拜奥普罗塞亚科技有限责任公司 | 碱耐受性亲和色谱配体 |
| CN114667450B (zh) * | 2019-09-24 | 2025-05-02 | 里珍纳龙药品有限公司 | 用于色谱介质的使用和再生的系统及方法 |
| EP3875472A1 (en) * | 2020-03-06 | 2021-09-08 | Navigo Proteins Gmbh | Novel immunoglobulin binding polypeptides |
| GB202113626D0 (en) | 2021-09-24 | 2021-11-10 | Cytiva Bioprocess R & D Ab | FC binding polypeptides |
| GB202203478D0 (en) | 2022-03-14 | 2022-04-27 | Cytiva Bioprocess R & D Ab | Vh3 binding polypeptides |
| CN115850408A (zh) * | 2022-09-01 | 2023-03-28 | 西安蓝晓科技新材料股份有限公司 | 一种多肽、融合型多聚体蛋白质及其用途 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101522278A (zh) * | 2006-09-29 | 2009-09-02 | 通用电气健康护理生物科学股份公司 | 用于抗体分离的包含来自金黄色葡萄球菌a蛋白的结构域c的层析配体 |
| CN101704879A (zh) * | 2008-08-11 | 2010-05-12 | 米利波尔公司 | 具有改进的特异性的新型免疫球蛋白结合蛋白 |
Family Cites Families (67)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE462046C (sv) | 1982-08-23 | 1998-04-27 | Pharmacia Biotech Ab | Hybrid-DNA-vektor innehållande DNA-sekvens från Staphylococcus aureus, förfarande för dess framställning och bakterie innehållande densamma |
| US5151350A (en) | 1982-10-27 | 1992-09-29 | Repligen Corporation | Cloned genes encoding recombinant protein a |
| US4617266A (en) | 1983-04-28 | 1986-10-14 | Genex Corporation | Production of Protein A |
| NZ218050A (en) | 1985-11-13 | 1989-05-29 | Wistar Inst | Test for the presence of htlv-1v |
| SE8505922D0 (sv) | 1985-12-13 | 1985-12-13 | Kabigen Ab | Construction of an igg binding protein to facilitate downstream processing using protein engineering |
| US5260373A (en) | 1987-03-13 | 1993-11-09 | Repligen Corporation | Immobilized immunoglobulin-binding proteins |
| US5084559A (en) | 1987-03-27 | 1992-01-28 | Repligen Corporation | Protein a domain mutants |
| US5089473A (en) | 1988-08-29 | 1992-02-18 | Monsanto Company | Somatotropin variants and their use |
| GB8902770D0 (en) | 1989-02-08 | 1989-03-30 | Bioprocessing Ltd | Improvements in or relating to supports for immunoaffinity separations |
| US4879378A (en) | 1989-03-30 | 1989-11-07 | Union Carbide Chemicals And Plastics Company Inc. | Polysiloxanes with pendant sterically hindered phenol moiety connected to the silicon atom via a carbonylyoxy-containing link |
| US5401650A (en) | 1990-10-24 | 1995-03-28 | The Mount Sinai School Of Medicine Of The City University Of New York | Cloning and expression of biologically active α-galactosidase A |
| US5198531A (en) | 1991-06-14 | 1993-03-30 | Research Diagnostic Antibodies | Polymeric resin for peptide synthesis |
| EP0863210A3 (en) | 1991-07-25 | 1999-09-22 | Oriental Yeast Co., Ltd. | Immunoglobulin-binding artificial protein |
| US5240680A (en) | 1991-12-19 | 1993-08-31 | Chiron Corporation | Automated apparatus for use in peptide synthesis |
| US5573905A (en) | 1992-03-30 | 1996-11-12 | The Scripps Research Institute | Encoded combinatorial chemical libraries |
| SE9400088D0 (sv) | 1994-01-14 | 1994-01-14 | Kabi Pharmacia Ab | Bacterial receptor structures |
| SE9503925D0 (sv) | 1995-11-07 | 1995-11-07 | Pharmacia Biotech Ab | Separationsmedium för IgG |
| WO1997036614A1 (en) | 1996-03-29 | 1997-10-09 | Terman David S | Polymerized staphylococcal protein a for treatment of diseases |
| US6013763A (en) | 1996-06-04 | 2000-01-11 | Genentech, Inc. | Peptide variants of protein A |
| US5856452A (en) | 1996-12-16 | 1999-01-05 | Sembiosys Genetics Inc. | Oil bodies and associated proteins as affinity matrices |
| US7026446B1 (en) | 1997-12-24 | 2006-04-11 | Diatech Pty Ltd. | Bifunctional molecules |
| GB9823071D0 (en) | 1998-10-21 | 1998-12-16 | Affibody Technology Ab | A method |
| US6589529B1 (en) | 1998-10-30 | 2003-07-08 | Children's Hospital Medical Center | Rotavirus subunit vaccine |
| SE9901379D0 (sv) | 1999-04-19 | 1999-04-19 | Pharmacia & Upjohn Ab | Receptor structures |
| US6602977B1 (en) | 1999-04-19 | 2003-08-05 | Biovitrum Ab | Receptor structures |
| EP2017343A3 (en) | 1999-05-15 | 2009-01-28 | University of California, San Diego | Protein A based binding domains with desirable activities |
| US7163686B1 (en) | 1999-05-15 | 2007-01-16 | The Regents Of The University Of California | Protein A based binding domains with desirable activities |
| EP3960855A1 (en) | 2001-12-28 | 2022-03-02 | Chugai Seiyaku Kabushiki Kaisha | Method for stabilizing proteins |
| US7709209B2 (en) | 2002-03-25 | 2010-05-04 | Ge Healthcare Bio-Sciences Ab | Protein ligands |
| SE0200943D0 (sv) | 2002-03-25 | 2002-03-25 | Amersham Biosciences Ab | Mutant protein |
| US7083948B1 (en) | 2002-12-24 | 2006-08-01 | Immunex Corporation | Polypeptide purification reagents and methods for their use |
| CA2516518A1 (en) | 2003-02-28 | 2004-09-10 | Lonza Biologics Plc. | Antibody purification by protein a and ion exchange chromatography |
| GB0304576D0 (en) | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
| JP4871126B2 (ja) | 2003-07-04 | 2012-02-08 | アフィボディ・アーベー | Ｈｅｒ２に対する結合親和性を有するポリペプチド |
| US7956165B2 (en) | 2003-07-24 | 2011-06-07 | Affisink Biotechnology Ltd. | Compositions and methods for purifying and crystallizing molecules of interest |
| AU2004278311A1 (en) | 2003-10-03 | 2005-04-14 | Genentech, Inc. | IGF binding proteins |
| EP1564286A1 (en) * | 2004-02-11 | 2005-08-17 | Université de Liège | Hybrid proteins of beta-lactamase class A |
| US8597908B2 (en) | 2004-07-06 | 2013-12-03 | Kaneka Corporation | Process for producing protein A-like protein with use of Brevibacillus genus bacterium |
| US8728828B2 (en) | 2004-12-22 | 2014-05-20 | Ge Healthcare Bio-Sciences Ab | Purification of immunoglobulins |
| US20080254551A1 (en) | 2004-12-30 | 2008-10-16 | Achsel Tilmann | Immunoprecipitaion-Based Method to Purify and Characterise Biological Macromolecular Complexes |
| EP1869071B1 (en) | 2005-03-01 | 2010-12-01 | Affibody AB | Tnf-alpha binding polypeptide, uses thereof and methods employing it |
| JP2006304633A (ja) | 2005-04-26 | 2006-11-09 | Apro Life Science Institute Inc | イムノグロブリン結合タンパク質 |
| CN101213211A (zh) * | 2005-06-17 | 2008-07-02 | 惠氏公司 | 纯化含Fc区蛋白的方法 |
| WO2007014591A1 (de) | 2005-08-03 | 2007-02-08 | Merck Patent Gmbh | Hydrophiles vernetztes polymer |
| CN102989018A (zh) | 2005-08-03 | 2013-03-27 | Rq生物科技有限公司 | 用于诊断IgA和IgM介导的肾脏疾病的方法和组合物 |
| US8440191B2 (en) | 2005-11-18 | 2013-05-14 | Tufts Medical Center | Clearance of abnormal IGA1 in IGA1 deposition diseases |
| CN103028380B (zh) | 2006-01-06 | 2015-08-19 | Emd密理博公司 | 亲和层析基质及其制备和使用方法 |
| EP1992692B1 (en) | 2006-02-21 | 2013-01-09 | Protenova Co., Ltd. | Immunoglobulin affinity ligand |
| US20080096819A1 (en) | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| GB0610776D0 (en) | 2006-05-31 | 2006-07-12 | Univ Bath | Novel applications for staphylococcus aureus Sbi protein |
| JP5004165B2 (ja) | 2006-10-10 | 2012-08-22 | 独立行政法人産業技術総合研究所 | タンパク質の配向制御固定化に適したタンパク質 |
| US7691608B2 (en) | 2006-12-06 | 2010-04-06 | Repligen Corporation | Nucleic acids encoding recombinant protein A |
| US8362217B2 (en) | 2006-12-21 | 2013-01-29 | Emd Millipore Corporation | Purification of proteins |
| KR101431856B1 (ko) | 2007-01-22 | 2014-08-27 | 제넨테크, 인크. | 항체의 고분자전해질 침전 및 정제 |
| JP2008266221A (ja) | 2007-04-20 | 2008-11-06 | National Institute Of Advanced Industrial & Technology | アミノ末端１箇所で配向制御固定化された固定化タンパク質 |
| JP5522723B2 (ja) | 2007-05-21 | 2014-06-18 | ノマディックバイオサイエンス株式会社 | 新規ポリペプチド，アフィニティークロマトグラフィー用材，及びイムノグロブリンの分離及び／又は精製方法 |
| SG149759A1 (en) | 2007-07-10 | 2009-02-27 | Millipore Corp | Media for affinity chromatography |
| JP2009071766A (ja) | 2007-09-18 | 2009-04-02 | Panasonic Corp | 受信端末装置 |
| JP2011523408A (ja) | 2008-05-15 | 2011-08-11 | ノボ・ノルデイスク・エー／エス | 抗体精製方法 |
| JP5677943B2 (ja) | 2008-06-05 | 2015-02-25 | アフィボディ・アーベーＡｆｆｉｂｏｄｙ Ａｂ | ポリペプチド |
| SG195555A1 (en) * | 2008-12-24 | 2013-12-30 | Emd Millipore Corp | Caustic stable chromatography ligands |
| US20120149875A1 (en) | 2009-01-12 | 2012-06-14 | Ge Healthcare Bio-Sciences Ab | Affinity chromatography matrix |
| EP2412809B1 (en) | 2009-03-24 | 2017-08-09 | Kaneka Corporation | Protein having affinity for immunoglobulin, and immunoglobulin-binding affinity ligand |
| EP2646126A4 (en) * | 2010-11-29 | 2014-12-17 | Ge Healthcare Bio Sciences Ab | affinity chromatography |
| WO2012087230A1 (en) | 2010-12-20 | 2012-06-28 | Ge Healthcare Bio-Sciences Ab | Affinity chromatography matrix |
| EP2690173B1 (en) * | 2011-03-25 | 2019-07-03 | Kaneka Corporation | Protein for affinity-separation matrix |
| SG186552A1 (en) | 2011-06-08 | 2013-01-30 | Emd Millipore Corp | Chromatography matrices including novel staphylococcus aureus protein a based ligands |
-
2012
- 2012-05-29 SG SG2012039533A patent/SG186552A1/en unknown
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN101522278A (zh) * | 2006-09-29 | 2009-09-02 | 通用电气健康护理生物科学股份公司 | 用于抗体分离的包含来自金黄色葡萄球菌a蛋白的结构域c的层析配体 |
| CN101704879A (zh) * | 2008-08-11 | 2010-05-12 | 米利波尔公司 | 具有改进的特异性的新型免疫球蛋白结合蛋白 |
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