EA015148B1 - СПОСОБЫ ОЧИСТКИ Aβ-СВЯЗЫВАЮЩЕГО БЕЛКА, СОДЕРЖАЩЕГО ОБЛАСТЬ FC - Google Patents
СПОСОБЫ ОЧИСТКИ Aβ-СВЯЗЫВАЮЩЕГО БЕЛКА, СОДЕРЖАЩЕГО ОБЛАСТЬ FC Download PDFInfo
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- EA015148B1 EA015148B1 EA200800083A EA200800083A EA015148B1 EA 015148 B1 EA015148 B1 EA 015148B1 EA 200800083 A EA200800083 A EA 200800083A EA 200800083 A EA200800083 A EA 200800083A EA 015148 B1 EA015148 B1 EA 015148B1
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Classifications
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- 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
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
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- Molecular Biology (AREA)
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- Pathology (AREA)
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- Cell Biology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Mycology (AREA)
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- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US69182105P | 2005-06-17 | 2005-06-17 | |
| PCT/US2006/024026 WO2006138737A2 (en) | 2005-06-17 | 2006-06-16 | Methods of purifying anti a beta antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA200800083A1 EA200800083A1 (ru) | 2008-06-30 |
| EA015148B1 true EA015148B1 (ru) | 2011-06-30 |
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| Application Number | Title | Priority Date | Filing Date |
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| EA201100177A EA201100177A1 (ru) | 2005-06-17 | 2006-06-16 | СПОСОБЫ ОЧИСТКИ АНТИТЕЛ К β-АМИЛОИДУ |
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Families Citing this family (113)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI239847B (en) * | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US7588766B1 (en) | 2000-05-26 | 2009-09-15 | Elan Pharma International Limited | Treatment of amyloidogenic disease |
| US7964192B1 (en) | 1997-12-02 | 2011-06-21 | Janssen Alzheimer Immunotherapy | Prevention and treatment of amyloidgenic disease |
| US20080050367A1 (en) * | 1998-04-07 | 2008-02-28 | Guriq Basi | Humanized antibodies that recognize beta amyloid peptide |
| US7790856B2 (en) * | 1998-04-07 | 2010-09-07 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize beta amyloid peptide |
| US6761888B1 (en) | 2000-05-26 | 2004-07-13 | Neuralab Limited | Passive immunization treatment of Alzheimer's disease |
| US6787523B1 (en) * | 1997-12-02 | 2004-09-07 | Neuralab Limited | Prevention and treatment of amyloidogenic disease |
| US7700751B2 (en) | 2000-12-06 | 2010-04-20 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize β-amyloid peptide |
| MY139983A (en) * | 2002-03-12 | 2009-11-30 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| DE10303974A1 (de) | 2003-01-31 | 2004-08-05 | Abbott Gmbh & Co. Kg | Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung |
| JP2006516639A (ja) * | 2003-02-01 | 2006-07-06 | ニユーララブ・リミテツド | 可溶性A−βに対する抗体を生成させるための能動免疫 |
| TWI306458B (en) * | 2003-05-30 | 2009-02-21 | Elan Pharma Int Ltd | Humanized antibodies that recognize beta amyloid peptide |
| EP1797182A2 (en) * | 2004-10-05 | 2007-06-20 | Wyeth a Corporation of the State of Delaware | Methods and compositions for improving recombinant protein production |
| SG156672A1 (en) * | 2004-10-22 | 2009-11-26 | Amgen Inc | Methods for refolding of recombinant antibodies |
| ES2396555T3 (es) | 2004-12-15 | 2013-02-22 | Janssen Alzheimer Immunotherapy | Anticuerpos que reconocen péptido beta amiloide |
| EP1838348B1 (en) | 2004-12-15 | 2013-06-26 | Janssen Alzheimer Immunotherapy | Humanized amyloid beta antibodies for use in improving cognition |
| GT200600031A (es) * | 2005-01-28 | 2006-08-29 | Formulacion anticuerpo anti a beta | |
| CN101213211A (zh) | 2005-06-17 | 2008-07-02 | 惠氏公司 | 纯化含Fc区蛋白的方法 |
| EP1954718B1 (en) | 2005-11-30 | 2014-09-03 | AbbVie Inc. | Anti-a globulomer antibodies, antigen-binding moieties thereof, corresponding hybridomas, nucleic acids, vectors, host cells, methods of producing said antibodies, compositions comprising said antibodies, uses of said antibodies and methods of using said antibodies |
| RU2432362C2 (ru) | 2005-11-30 | 2011-10-27 | Эбботт Лэборетриз | Моноклональные антитела и их применения |
| KR101591223B1 (ko) | 2005-12-12 | 2016-02-04 | 에이씨 이뮨 에스.에이. | 치료적 특성을 갖는 베타 1-42 특이적인 단일클론성 항체 |
| US8784810B2 (en) * | 2006-04-18 | 2014-07-22 | Janssen Alzheimer Immunotherapy | Treatment of amyloidogenic diseases |
| WO2010044803A1 (en) * | 2008-10-17 | 2010-04-22 | Elan Pharma International Limited | Treatment of amyloidogenic diseases |
| SG173385A1 (en) * | 2006-07-14 | 2011-08-29 | Ac Immune S A Ch | Humanized antibody against amyloid beta |
| ZA200900836B (en) * | 2006-08-28 | 2010-05-26 | Ares Trading Sa | Process for the purification of FC-fusion proteins |
| LT2061803T (lt) * | 2006-08-28 | 2019-11-25 | Ares Trading Sa | Fc turinčių baltymų gryninimo būdas |
| MX345141B (es) | 2006-09-13 | 2017-01-18 | Abbvie Inc * | Mejoras de cultivos celulares. |
| US8911964B2 (en) | 2006-09-13 | 2014-12-16 | Abbvie Inc. | Fed-batch method of making human anti-TNF-alpha antibody |
| US8455626B2 (en) | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
| EP2486928A1 (en) * | 2007-02-27 | 2012-08-15 | Abbott GmbH & Co. KG | Method for the treatment of amyloidoses |
| US8003097B2 (en) * | 2007-04-18 | 2011-08-23 | Janssen Alzheimer Immunotherapy | Treatment of cerebral amyloid angiopathy |
| JP2011526240A (ja) * | 2007-04-18 | 2011-10-06 | ヤンセン アルツハイマー イミュノセラピー | 脳アミロイド血管症の予防および治療 |
| JP2010528583A (ja) * | 2007-06-11 | 2010-08-26 | エーシー イミューン ソシエテ アノニム | アミロイドβに対するヒト化抗体 |
| US8613923B2 (en) | 2007-06-12 | 2013-12-24 | Ac Immune S.A. | Monoclonal antibody |
| US8048420B2 (en) | 2007-06-12 | 2011-11-01 | Ac Immune S.A. | Monoclonal antibody |
| US20090155249A1 (en) * | 2007-06-12 | 2009-06-18 | Ac Immune S.A. | Humanized antibody igg1 |
| DK2182983T3 (da) | 2007-07-27 | 2014-07-14 | Janssen Alzheimer Immunotherap | Behandling af amyloidogene sygdomme med humaniserede anti-abeta antistoffer |
| NZ585110A (en) * | 2007-10-05 | 2012-09-28 | Genentech Inc | Method and compositions for diagnosis and treatment of amyloidosis |
| PL2238166T3 (pl) * | 2007-10-05 | 2014-07-31 | Genentech Inc | Zastosowanie przeciwciała anty-Beta amyloidowego w chorobach oczu |
| EP2650308A3 (en) * | 2007-10-05 | 2014-11-12 | Genentech, Inc. | Use of anti-amyloid beta antibody in ocular diseases |
| JO3076B1 (ar) * | 2007-10-17 | 2017-03-15 | Janssen Alzheimer Immunotherap | نظم العلاج المناعي المعتمد على حالة apoe |
| DK2211904T3 (en) | 2007-10-19 | 2016-10-24 | Seattle Genetics Inc | Cd19-binding agents and uses thereof |
| RU2498991C2 (ru) * | 2007-10-30 | 2013-11-20 | Дженентек, Инк. | Очистка антител с помощью катионообменной хроматографии |
| WO2009064424A1 (en) * | 2007-11-13 | 2009-05-22 | Rational Affinity Devices, L.L.C. | Tunable affinity ligands for the separation and detection of target substances |
| KR101247374B1 (ko) * | 2008-06-26 | 2013-03-26 | 한국생명공학연구원 | 면역글로불린 G의 Fc 부위에 선택적으로 결합하는 신규펩타이드 및 그의 제조방법 |
| US8592555B2 (en) | 2008-08-11 | 2013-11-26 | Emd Millipore Corporation | Immunoglobulin-binding proteins with improved specificity |
| CN104974251A (zh) | 2008-10-20 | 2015-10-14 | Abbvie公司 | 在抗体纯化过程中的病毒灭活 |
| MX2011004199A (es) * | 2008-10-20 | 2011-05-24 | Abbott Lab | Anticuerpos que unen a il-18 y metodos para purificar los mismos. |
| TWI610936B (zh) * | 2008-10-20 | 2018-01-11 | 艾伯維有限公司 | 使用蛋白質a親和性層析進行抗體之分離及純化 |
| CN118324847A (zh) | 2008-10-29 | 2024-07-12 | 阿布林克斯公司 | 单域抗原结合性分子的纯化方法 |
| US9393304B2 (en) | 2008-10-29 | 2016-07-19 | Ablynx N.V. | Formulations of single domain antigen binding molecules |
| US9067981B1 (en) | 2008-10-30 | 2015-06-30 | Janssen Sciences Ireland Uc | Hybrid amyloid-beta antibodies |
| KR20110086184A (ko) | 2008-12-22 | 2011-07-27 | 에프. 호프만-라 로슈 아게 | 면역글로불린 정제 |
| SG195555A1 (en) | 2008-12-24 | 2013-12-30 | Emd Millipore Corp | Caustic stable chromatography ligands |
| US8268820B2 (en) * | 2009-03-26 | 2012-09-18 | Hoffmann-La Roche Inc. | 2,3-diaryl- or heteroaryl-substituted 1,1,1-trifluoro-2-hydroxypropyl compounds |
| EP2982690B1 (en) | 2009-04-30 | 2021-01-27 | Ablynx N.V. | Method for the production of domain antibodies |
| CN102686738A (zh) | 2009-09-01 | 2012-09-19 | 弗·哈夫曼-拉罗切有限公司 | 通过改进的a蛋白洗脱增强的蛋白质纯化 |
| KR101632312B1 (ko) | 2009-11-03 | 2016-06-21 | 삼성전자주식회사 | 항체 불변 영역에 특이적으로 결합하는 융합 단백질, 그의 제조 방법 및 이를 이용한 항체 분리 방법 |
| EP2918574A1 (en) * | 2009-12-31 | 2015-09-16 | Groupe Novasep SAS | Purification of succinic acid from the fermentation broth containing ammonium succinate |
| EP2542567B1 (de) * | 2010-03-05 | 2020-02-12 | Boehringer Ingelheim International Gmbh | Selektive anreicherung von antikörpern |
| WO2011110598A1 (en) * | 2010-03-10 | 2011-09-15 | F. Hoffmann-La Roche Ag | Method for purifying immunoglobulin solutions |
| WO2011130377A2 (en) | 2010-04-15 | 2011-10-20 | Abbott Laboratories | Amyloid-beta binding proteins |
| MX341369B (es) | 2010-07-30 | 2016-08-17 | Genentech Inc * | Anticuerpo anti-beta-amiloide humanizado seguro y funcional. |
| EP3533803B1 (en) | 2010-08-14 | 2021-10-27 | AbbVie Inc. | Anti-amyloid-beta antibodies |
| WO2012099576A1 (en) * | 2011-01-18 | 2012-07-26 | Baxter International Inc. | Measurement of anti-amyloid antibodies in human blood |
| KR102058254B1 (ko) | 2011-03-29 | 2019-12-20 | 글락소스미스클라인 엘엘씨 | 단백질 정제용 완충제 시스템 |
| SG10201604554WA (en) * | 2011-06-08 | 2016-07-28 | Emd Millipore Corp | Chromatography matrices including novel staphylococcus aureus protein a based ligands |
| WO2013013193A1 (en) * | 2011-07-20 | 2013-01-24 | Zepteon, Incorporated | Polypeptide separation methods |
| US9994610B2 (en) * | 2011-10-19 | 2018-06-12 | Roche Glycart Ag | Separation method for fucosylated antibodies |
| AU2013322710A1 (en) * | 2012-09-25 | 2015-04-16 | Glenmark Pharmaceuticals S.A. | Purification of hetero-dimeric immunoglobulins |
| TWI596107B (zh) | 2013-06-25 | 2017-08-21 | 卡地拉保健有限公司 | 單株抗體之新穎純化方法 |
| MX384222B (es) | 2013-07-05 | 2025-03-14 | Lab Francais Du Fractionnement | Matriz de cromatografia de afinidad. |
| NZ718144A (en) | 2013-09-13 | 2022-05-27 | Genentech Inc | Methods and compositions comprising purified recombinant polypeptides |
| AR100716A1 (es) * | 2014-06-02 | 2016-10-26 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Producción de fragmentos fc |
| JP6451118B2 (ja) * | 2014-07-17 | 2019-01-16 | 東ソー株式会社 | 抗体の分離方法 |
| AR101262A1 (es) * | 2014-07-26 | 2016-12-07 | Regeneron Pharma | Plataforma de purificación para anticuerpos biespecíficos |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| FR3038517B1 (fr) | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
| CN105175548B (zh) * | 2015-08-13 | 2019-02-05 | 齐鲁制药有限公司 | 重组人血管内皮生长因子受体-抗体融合蛋白的纯化方法 |
| KR102691585B1 (ko) | 2015-08-21 | 2024-08-05 | 에프. 호프만-라 로슈 아게 | 친화성 크로마토그래피에서의 숙주 세포 단백질 감소 방법 |
| CN107849122B (zh) * | 2015-08-21 | 2022-01-25 | 豪夫迈·罗氏有限公司 | 用低电导率洗涤缓冲液进行亲和层析纯化 |
| SI3337817T1 (sl) * | 2015-08-21 | 2021-12-31 | F. Hoffmann - La Roche Ag | Postopek za redukcijo beljakovin gostiteljske celice pri afinitetni kromatografiji |
| EP3344643B1 (en) * | 2015-09-04 | 2025-07-02 | Qiagen Sciences LLC | Methods for co-isolation of nucleic acids and proteins |
| GB201600154D0 (en) * | 2016-01-05 | 2016-02-17 | Bayer As | Isotope preparation method |
| GB201600161D0 (en) * | 2016-01-05 | 2016-02-17 | Bayer As | Isotope purification method |
| HUE067896T2 (hu) | 2016-04-27 | 2024-11-28 | Abbvie Mfg Management Unlimited Company | Olyan betegségek kezelési módszerei az anti-IL-13 antitestek alkalmazásával, amelyekben az IL-13 aktivitás káros |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| JP7106187B2 (ja) | 2016-05-11 | 2022-07-26 | 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 | 分離マトリックスを保存する方法 |
| 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 |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| CN109071613A (zh) | 2016-05-11 | 2018-12-21 | 通用电气医疗集团生物工艺研发股份公司 | 分离基质 |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| WO2017194593A1 (en) | 2016-05-11 | 2017-11-16 | Ge Healthcare Bioprocess R&D Ab | Method of cleaning and/or sanitizing a separation matrix |
| WO2018018011A2 (en) * | 2016-07-22 | 2018-01-25 | Amgen Inc. | Methods of purifying fc-containing proteins |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| CN106519029B (zh) * | 2016-10-31 | 2020-03-17 | 山东泰邦生物制品有限公司 | 一种Aβ寡聚体抗体的制备工艺 |
| US10941178B2 (en) * | 2017-03-17 | 2021-03-09 | Gilead Sciences, Inc. | Method of purifying an antibody |
| JP2018167260A (ja) * | 2017-03-29 | 2018-11-01 | 三菱ケミカル株式会社 | イオン交換体の保存方法、生理活性物質の精製装置及び生理活性物質の精製方法 |
| ES2887046T3 (es) * | 2017-08-17 | 2021-12-21 | Just Evotec Biologics Inc | Método de purificación de proteína glicosilada a partir de galectinas de las células hospedadoras y otros contaminantes |
| US11447547B1 (en) | 2017-12-13 | 2022-09-20 | Amgen Inc. | Method of antigen-binding protein production |
| CN109929038B (zh) * | 2017-12-15 | 2020-10-09 | 山东博安生物技术有限公司 | Vegf捕获剂融合蛋白的纯化方法 |
| CN108048477A (zh) * | 2017-12-15 | 2018-05-18 | 南京理工大学 | 基于大肠杆菌表达系统的制备多肽的方法 |
| EP3727629A1 (en) | 2017-12-22 | 2020-10-28 | Regeneron Pharmaceuticals, Inc. | System and method for characterizing drug product impurities |
| WO2019183334A1 (en) | 2018-03-21 | 2019-09-26 | Waters Technologies Corporation | Non-antibody high-affinity-based sample preparation, sorbents, devices and methods |
| JP7496316B2 (ja) | 2018-04-24 | 2024-06-06 | キアゲン サイエンシーズ, エルエルシー | 複雑な試料からの核酸の単離および阻害物質の除去 |
| US20220314142A1 (en) * | 2019-07-01 | 2022-10-06 | Pfizer Inc. | Improvements to wash solutions for protein a chromatography in an antibody purification process |
| CN112409477B (zh) * | 2019-08-21 | 2022-11-08 | 广东菲鹏生物有限公司 | IgM纯化方法 |
| 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 |
| EP4142792A4 (en) * | 2020-05-01 | 2024-11-27 | Kashiv Biosciences, LLC | An improved process of purification of protein |
| CN113968909A (zh) * | 2020-07-22 | 2022-01-25 | 信达生物制药(苏州)有限公司 | 一种双特异性抗体的纯化方法 |
| UY39337A (es) | 2020-07-23 | 2022-02-25 | Othair Prothena Ltd | Anticuerpos anti-abeta |
| TW202504919A (zh) | 2023-05-30 | 2025-02-01 | 美商派拉岡醫療公司 | α4β7整合素抗體組合物及使用方法 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0323027A2 (en) * | 1987-12-30 | 1989-07-05 | Bioprobe International, Inc. | Monoclonal antibody purification process |
| WO2002046237A2 (en) * | 2000-12-06 | 2002-06-13 | Neuralab Limited | Humanized antibodies that recognize beta amyloid peptide |
| US20040229330A1 (en) * | 2003-02-27 | 2004-11-18 | Bayer Pharmaceuticals Corporation | Integrated method for capture and purification of tagged proteins |
Family Cites Families (73)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| JPS61134325A (ja) | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| WO1987002671A1 (en) | 1985-11-01 | 1987-05-07 | International Genetic Engineering, Inc. | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5225539A (en) * | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4851341A (en) * | 1986-12-19 | 1989-07-25 | Immunex Corporation | Immunoaffinity purification system |
| US5336603A (en) * | 1987-10-02 | 1994-08-09 | Genentech, Inc. | CD4 adheson variants |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| DE68927933T2 (de) | 1988-09-02 | 1997-08-14 | Dyax Corp | Herstellung und auswahl von rekombinantproteinen mit verschiedenen bindestellen |
| US5116964A (en) | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US5225538A (en) | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| DE69133566T2 (de) * | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| AU665190B2 (en) | 1990-07-10 | 1995-12-21 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5112952A (en) * | 1990-09-28 | 1992-05-12 | Pierce Chemical Company | Composition and method for isolation and purification of Immunoglobulin M |
| DK0564531T3 (da) | 1990-12-03 | 1998-09-28 | Genentech Inc | Berigelsesfremgangsmåde for variantproteiner med ændrede bindingsegenskaber |
| DK1279731T3 (da) | 1991-03-01 | 2007-09-24 | Dyax Corp | Fremgangsmåde til udvikling af bindende miniproteiner |
| DK1471142T3 (da) | 1991-04-10 | 2009-03-09 | Scripps Research Inst | Heterodimere receptor-biblioteker under anvendelse af fagemider |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| US5786180A (en) * | 1995-02-14 | 1998-07-28 | Bayer Corporation | Monoclonal antibody 369.2B specific for β A4 peptide |
| SI0950067T1 (sl) * | 1996-11-27 | 2007-12-31 | Genentech Inc | Afinitetno čiščenje polipeptida na proteinskemA matriksu |
| WO1998047343A2 (en) * | 1997-04-04 | 1998-10-29 | Biosite Diagnostics, Inc. | Antibodies or binding protein libraries displayed on phage, cells, or other replicatable genetic packages |
| US6913745B1 (en) * | 1997-12-02 | 2005-07-05 | Neuralab Limited | Passive immunization of Alzheimer's disease |
| US6750324B1 (en) * | 1997-12-02 | 2004-06-15 | Neuralab Limited | Humanized and chimeric N-terminal amyloid beta-antibodies |
| US6787523B1 (en) | 1997-12-02 | 2004-09-07 | Neuralab Limited | Prevention and treatment of amyloidogenic disease |
| US7588766B1 (en) | 2000-05-26 | 2009-09-15 | Elan Pharma International Limited | Treatment of amyloidogenic disease |
| TWI239847B (en) * | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US7790856B2 (en) * | 1998-04-07 | 2010-09-07 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize beta amyloid peptide |
| US6761888B1 (en) | 2000-05-26 | 2004-07-13 | Neuralab Limited | Passive immunization treatment of Alzheimer's disease |
| US6905686B1 (en) | 1997-12-02 | 2005-06-14 | Neuralab Limited | Active immunization for treatment of alzheimer's disease |
| US20080050367A1 (en) | 1998-04-07 | 2008-02-28 | Guriq Basi | Humanized antibodies that recognize beta amyloid peptide |
| US6710226B1 (en) * | 1997-12-02 | 2004-03-23 | Neuralab Limited | Transgenic mouse assay to determine the effect of Aβ antibodies and Aβ Fragments on alzheimer's disease characteristics |
| US7964192B1 (en) | 1997-12-02 | 2011-06-21 | Janssen Alzheimer Immunotherapy | Prevention and treatment of amyloidgenic disease |
| US7179892B2 (en) * | 2000-12-06 | 2007-02-20 | Neuralab Limited | Humanized antibodies that recognize beta amyloid peptide |
| US20050059802A1 (en) * | 1998-04-07 | 2005-03-17 | Neuralab Ltd | Prevention and treatment of amyloidogenic disease |
| US6787637B1 (en) | 1999-05-28 | 2004-09-07 | Neuralab Limited | N-Terminal amyloid-β antibodies |
| SI1481992T1 (sl) | 2000-02-24 | 2017-01-31 | Washington University St. Louis | Humanizirana protitelesa, ki vežejo amiloidni peptid beta |
| US7700751B2 (en) | 2000-12-06 | 2010-04-20 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize β-amyloid peptide |
| EP1385545B1 (en) | 2001-04-30 | 2009-01-07 | Eli Lilly And Company | Humanized antibodies recognizing the beta-amyloid peptide |
| ATE409047T1 (de) * | 2001-04-30 | 2008-10-15 | Lilly Co Eli | Humanisierte antikörper |
| WO2003015691A2 (en) | 2001-08-17 | 2003-02-27 | Eli Lilly And Company | RAPID IMPROVEMENT OF COGNITION IN CONDITIONS RELATED TO A$g(b) |
| WO2003016466A2 (en) | 2001-08-17 | 2003-02-27 | Eli Lilly And Company | ANTI-Aβ ANTIBODIES |
| EP2048154B2 (en) | 2002-02-05 | 2015-06-03 | Genentech, Inc. | Protein purification |
| AR038568A1 (es) | 2002-02-20 | 2005-01-19 | Hoffmann La Roche | Anticuerpos anti-a beta y su uso |
| MY139983A (en) | 2002-03-12 | 2009-11-30 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| JP2006516639A (ja) | 2003-02-01 | 2006-07-06 | ニユーララブ・リミテツド | 可溶性A−βに対する抗体を生成させるための能動免疫 |
| GB0304576D0 (en) | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
| EP1601697B1 (en) | 2003-02-28 | 2007-05-30 | Lonza Biologics plc | Antibody purification by Protein A and ion exchange chromatography |
| TWI306458B (en) | 2003-05-30 | 2009-02-21 | Elan Pharma Int Ltd | Humanized antibodies that recognize beta amyloid peptide |
| DK2336172T3 (en) | 2003-10-27 | 2015-01-26 | Wyeth Llc | The removal of aggregates of high molecular weight by hydroxylapatite chromatography |
| PL1701968T3 (pl) * | 2003-12-17 | 2015-11-30 | Wyeth Llc | Koniugaty nośników z peptydami immunogennymi i sposoby ich wytwarzania |
| EP2479184A3 (en) * | 2003-12-17 | 2013-09-04 | Janssen Alzheimer Immunotherapy | Beta immunogenic peptide carrier conjugates and methods of producing the same |
| WO2005077981A2 (en) * | 2003-12-22 | 2005-08-25 | Xencor, Inc. | Fc POLYPEPTIDES WITH NOVEL Fc LIGAND BINDING SITES |
| EP1767217A1 (en) | 2004-07-14 | 2007-03-28 | Astellas Pharma Inc. | Agent for promoting the recovery from dysfunction after the onset of central neurological disease |
| EP1797182A2 (en) | 2004-10-05 | 2007-06-20 | Wyeth a Corporation of the State of Delaware | Methods and compositions for improving recombinant protein production |
| ES2396555T3 (es) | 2004-12-15 | 2013-02-22 | Janssen Alzheimer Immunotherapy | Anticuerpos que reconocen péptido beta amiloide |
| PE20061401A1 (es) | 2004-12-15 | 2006-12-23 | Neuralab Ltd | ANTICUERPOS Aß PARA MEJORAR LA COGNICION |
| EP1838348B1 (en) | 2004-12-15 | 2013-06-26 | Janssen Alzheimer Immunotherapy | Humanized amyloid beta antibodies for use in improving cognition |
| GT200600031A (es) * | 2005-01-28 | 2006-08-29 | Formulacion anticuerpo anti a beta | |
| PA8661401A1 (es) | 2005-01-28 | 2006-09-08 | Wyeth Corp | Formulaciones del liquido polipeptido estabilizado |
| CN101213211A (zh) | 2005-06-17 | 2008-07-02 | 惠氏公司 | 纯化含Fc区蛋白的方法 |
| US8003097B2 (en) * | 2007-04-18 | 2011-08-23 | Janssen Alzheimer Immunotherapy | Treatment of cerebral amyloid angiopathy |
| JP2011526240A (ja) | 2007-04-18 | 2011-10-06 | ヤンセン アルツハイマー イミュノセラピー | 脳アミロイド血管症の予防および治療 |
| DK2182983T3 (da) | 2007-07-27 | 2014-07-14 | Janssen Alzheimer Immunotherap | Behandling af amyloidogene sygdomme med humaniserede anti-abeta antistoffer |
| JO3076B1 (ar) | 2007-10-17 | 2017-03-15 | Janssen Alzheimer Immunotherap | نظم العلاج المناعي المعتمد على حالة apoe |
| IT1395574B1 (it) | 2009-09-14 | 2012-10-16 | Guala Dispensing Spa | Dispositivo di erogazione |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0323027A2 (en) * | 1987-12-30 | 1989-07-05 | Bioprobe International, Inc. | Monoclonal antibody purification process |
| WO2002046237A2 (en) * | 2000-12-06 | 2002-06-13 | Neuralab Limited | Humanized antibodies that recognize beta amyloid peptide |
| US20040229330A1 (en) * | 2003-02-27 | 2004-11-18 | Bayer Pharmaceuticals Corporation | Integrated method for capture and purification of tagged proteins |
Non-Patent Citations (1)
| Title |
|---|
| "Antibody purification", ANTIBODY PURIFICATION HANDBOOK, AMERSHAM BIOSCIENCES, UPPSALA, SE, 2002, page complete, XP002357261, the whole document * |
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