RU2603743C2 - Иммуноглобулины k cd52 человека - Google Patents
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- RU2603743C2 RU2603743C2 RU2011150516/10A RU2011150516A RU2603743C2 RU 2603743 C2 RU2603743 C2 RU 2603743C2 RU 2011150516/10 A RU2011150516/10 A RU 2011150516/10A RU 2011150516 A RU2011150516 A RU 2011150516A RU 2603743 C2 RU2603743 C2 RU 2603743C2
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Families Citing this family (39)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2300022A2 (en) | 2008-04-25 | 2011-03-30 | Duke University | Regulatory b cells and their uses |
| BRPI1013927A2 (pt) | 2009-05-13 | 2016-04-05 | Genzyme Corp | métodos e composições para o tratamento de lúpus |
| TWI614267B (zh) * | 2009-05-13 | 2018-02-11 | 建新公司 | 抗人類cd52免疫球蛋白 |
| US9814740B2 (en) * | 2010-12-21 | 2017-11-14 | Duke University | Methods and compositions combining immunotherapy with monocyte activation |
| EP2700652B1 (en) * | 2011-04-18 | 2018-12-19 | The University of Tokyo | Diagnosis and treatment of cancer using anti-itm2a antibody |
| GB201109238D0 (en) * | 2011-06-01 | 2011-07-13 | Antitope Ltd | Antibodies |
| BR112014009925B1 (pt) | 2011-10-28 | 2022-09-20 | Teva Pharmaceuticals Australia Pty Ltd | Construtores de polipeptídeos e seus usos |
| WO2013185165A1 (en) * | 2012-06-14 | 2013-12-19 | The Walter And Eliza Hall Institute Of Medical Research | Cd-52 antibodies and their use in determining and enhancing an immune response in a subject |
| US10017739B2 (en) | 2012-09-06 | 2018-07-10 | Duke University | Methods of expanding and assessing B cells and using expanded B cells to treat disease |
| WO2014066271A1 (en) * | 2012-10-22 | 2014-05-01 | Becton, Dickinson And Company | Non-b-lineage cells capable of producing antibody |
| CA2903817A1 (en) | 2013-03-12 | 2014-10-09 | Institute of Arthritis Research, LLC | Immunologically active polypeptide |
| CU24446B1 (es) | 2013-03-13 | 2019-10-04 | Prothena Biosciences Ltd | Un anticuerpo monoclonal humanizado que se une a tau |
| AR095199A1 (es) * | 2013-03-15 | 2015-09-30 | Genzyme Corp | Anticuerpos anti-cd52 |
| KR102042174B1 (ko) | 2013-03-29 | 2019-11-08 | 삼성전자주식회사 | 인간화 및 친화도 성숙된 항 c-Met 항체 및 그의 용도 |
| KR102060540B1 (ko) * | 2013-04-03 | 2019-12-31 | 삼성전자주식회사 | 항 c-Met 항체 및 항 Ang2 항체를 포함하는 병용 투여용 약학 조성물 |
| MX2015014181A (es) | 2013-04-09 | 2016-05-24 | Boston Biomedical Inc | 2-acetilnafto [2,3-b]furano -4,9-diona para uso en el tratamiento del cáncer. |
| KR102186363B1 (ko) * | 2013-09-06 | 2020-12-04 | 삼성전자주식회사 | c-Met 저해제 및 베타-카테닌 저해제를 포함하는 병용 투여용 약학 조성물 |
| KR102192591B1 (ko) * | 2013-09-09 | 2020-12-18 | 삼성전자주식회사 | c-Met 저해제 및 c-Myc 저해제를 포함하는 병용 투여용 약학 조성물 |
| WO2016196935A1 (en) | 2015-06-03 | 2016-12-08 | Boston Biomedical, Inc. | Compositions comprising a cancer stemness inhibitor and an immunotherapeutic agent for use in treating cancer |
| US10752679B2 (en) | 2016-05-02 | 2020-08-25 | Prothena Biosciences Limited | Tau immunotherapy |
| AU2017259039B2 (en) | 2016-05-02 | 2024-05-09 | Prothena Biosciences Limited | Antibodies recognizing tau |
| EA201892417A1 (ru) | 2016-05-02 | 2019-05-31 | Протена Биосайенсис Лимитед | Антитела, распознающие тау |
| US11299469B2 (en) | 2016-11-29 | 2022-04-12 | Sumitomo Dainippon Pharma Oncology, Inc. | Naphthofuran derivatives, preparation, and methods of use thereof |
| CN110248668B (zh) | 2016-12-15 | 2023-05-30 | 杜克大学 | 用于消耗调节性b10细胞的抗体和方法以及与免疫检查点抑制剂的联用 |
| EP3612564A2 (en) | 2017-04-21 | 2020-02-26 | Genzyme Corporation | Treatment of multiple sclerosis with anti-cd52 antibodies |
| CN110881274B (zh) * | 2017-05-02 | 2024-11-15 | 普罗塞纳生物科学有限公司 | 识别tau的抗体 |
| US10646464B2 (en) | 2017-05-17 | 2020-05-12 | Boston Biomedical, Inc. | Methods for treating cancer |
| GB201710836D0 (en) * | 2017-07-05 | 2017-08-16 | Ucl Business Plc | ROR1 Car T-Cells |
| EP3728301A4 (en) * | 2017-12-20 | 2021-10-06 | Radimmune Therapeutics, Inc. | ANTIBODIES DIRECTED AGAINST CENTRIN-1, THEIR MANUFACTURING PROCESSES AND THEIR USES |
| KR102880569B1 (ko) * | 2018-12-19 | 2025-11-06 | 후맙스 바이오메드 에스에이 | B형 간염 바이러스를 중화하는 항체 및 이의 용도 |
| PL3897672T3 (pl) | 2018-12-20 | 2024-10-07 | Vir Biotechnology, Inc. | Terapia skojarzona hbv |
| JP7630834B2 (ja) | 2019-03-03 | 2025-02-18 | プロセナ バイオサイエンシーズ リミテッド | タウ認識抗体 |
| CN109929835A (zh) * | 2019-03-27 | 2019-06-25 | 中国人民解放军第四军医大学 | 一种鼠单克隆抗体功能轻链可变区基因的扩增方法 |
| EP3972998A1 (en) | 2019-05-21 | 2022-03-30 | Novartis AG | Cd19 binding molecules and uses thereof |
| AU2020299024A1 (en) * | 2019-07-02 | 2022-01-20 | Telix Pharmaceuticals (Innovations) Pty Ltd | Antibodies against CAIX with reduced affinity for the neonatal Fc receptor |
| TWI800824B (zh) * | 2020-05-08 | 2023-05-01 | 大陸商亘喜生物科技(上海)有限公司 | 一種抗cd19抗體的抗體及其製備和應用 |
| IL302786A (en) * | 2020-11-19 | 2023-07-01 | Genzyme Corp | Flow cytometry attenuated reporter expression (flare) multiple reporter system and methods of use thereof |
| WO2022133169A1 (en) | 2020-12-18 | 2022-06-23 | Century Therapeutics, Inc. | Chimeric antigen receptor systems with adaptable receptor specificity |
| WO2025031965A1 (en) * | 2023-08-04 | 2025-02-13 | Cimeio Therapeutics Ag | Discernible cell surface protein variants of cd52 for use in cell therapy |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2006126068A2 (en) * | 2005-05-24 | 2006-11-30 | Avestha Gengraine Technologies Pvt Ltd | Recombinant method for the production of a monoclonal antibody to cd52 for the treatment of chronic lymphocytic leukemia |
Family Cites Families (74)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US6054561A (en) * | 1984-02-08 | 2000-04-25 | Chiron Corporation | Antigen-binding sites of antibody molecules specific for cancer antigens |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| US4970198A (en) | 1985-10-17 | 1990-11-13 | American Cyanamid Company | Antitumor antibiotics (LL-E33288 complex) |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| EP0271581B1 (en) | 1986-04-17 | 1993-01-13 | Kyowa Hakko Kogyo Co., Ltd. | Novel compounds dc-88a and dc-89a1 and process for their preparation |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| JP3101690B2 (ja) | 1987-03-18 | 2000-10-23 | エス・ビィ・2・インコーポレイテッド | 変性抗体の、または変性抗体に関する改良 |
| WO1988009344A1 (en) | 1987-05-21 | 1988-12-01 | Creative Biomolecules, Inc. | Targeted multifunctional proteins |
| WO1989007142A1 (en) | 1988-02-05 | 1989-08-10 | Morrison Sherie L | Domain-modified constant region antibodies |
| DE10199051I2 (de) * | 1988-02-12 | 2005-05-04 | Btg Int Ltd | Modifizierte Antik¦rper. |
| JP2598116B2 (ja) | 1988-12-28 | 1997-04-09 | 協和醗酵工業株式会社 | 新規物質dc113 |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| JP2510335B2 (ja) | 1989-07-03 | 1996-06-26 | 協和醗酵工業株式会社 | Dc―88a誘導体 |
| US5187186A (en) | 1989-07-03 | 1993-02-16 | Kyowa Hakko Kogyo Co., Ltd. | Pyrroloindole derivatives |
| US5208020A (en) | 1989-10-25 | 1993-05-04 | Immunogen Inc. | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| ES2246502T3 (es) | 1990-08-29 | 2006-02-16 | Genpharm International, Inc. | Animales no humanos transgenicos capaces de producir anticuerpos heterologos. |
| GB9022547D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Purified immunoglobulin |
| GB9022543D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Antibody production |
| GB9108056D0 (en) * | 1991-04-16 | 1991-06-05 | Hale Geoffrey | Synthetic antigen |
| EP0519596B1 (en) | 1991-05-17 | 2005-02-23 | Merck & Co. Inc. | A method for reducing the immunogenicity of antibody variable domains |
| JP4124480B2 (ja) | 1991-06-14 | 2008-07-23 | ジェネンテック・インコーポレーテッド | 免疫グロブリン変異体 |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| US5264586A (en) | 1991-07-17 | 1993-11-23 | The Scripps Research Institute | Analogs of calicheamicin gamma1I, method of making and using the same |
| US5269388A (en) | 1991-11-12 | 1993-12-14 | Stress-Tek, Inc. | Weighing bed |
| GB9125768D0 (en) | 1991-12-04 | 1992-02-05 | Hale Geoffrey | Therapeutic method |
| CA2076465C (en) | 1992-03-25 | 2002-11-26 | Ravi V. J. Chari | Cell binding agent conjugates of analogues and derivatives of cc-1065 |
| WO1994026087A2 (en) | 1993-05-14 | 1994-11-24 | Connor Kim C O | Recombinant protein production and insect cell culture and process |
| AU691811B2 (en) | 1993-06-16 | 1998-05-28 | Celltech Therapeutics Limited | Antibodies |
| US7119248B1 (en) | 1994-04-12 | 2006-10-10 | Miltenyi Biotec Gmbh | Antibodies against epitopes with homology to self antigens, methods of preparation and applications thereof |
| PT705833E (pt) | 1994-04-22 | 2004-11-30 | Kyowa Hakko Kogyo Kk | Derivado de dc-89 |
| US5550246A (en) | 1994-09-07 | 1996-08-27 | The Scripps Research Institute | Calicheamicin mimics |
| US5712374A (en) | 1995-06-07 | 1998-01-27 | American Cyanamid Company | Method for the preparation of substantiallly monomeric calicheamicin derivative/carrier conjugates |
| US5714586A (en) | 1995-06-07 | 1998-02-03 | American Cyanamid Company | Methods for the preparation of monomeric calicheamicin derivative/carrier conjugates |
| GB9603507D0 (en) | 1996-02-20 | 1996-04-17 | Isis Innovation | Antibody variants |
| US7147851B1 (en) | 1996-08-15 | 2006-12-12 | Millennium Pharmaceuticals, Inc. | Humanized immunoglobulin reactive with α4β7 integrin |
| GB2339430A (en) | 1997-05-21 | 2000-01-26 | Biovation Ltd | Method for the production of non-immunogenic proteins |
| CA2342967A1 (en) | 1998-12-08 | 2000-06-15 | Biovation Limited | Modifying protein immunogenicity |
| ES2276708T3 (es) | 1999-11-24 | 2007-07-01 | Immunogen, Inc. | Agentes citotoxicos que comprenden taxanos y su uso terapeutico. |
| IL151499A0 (en) | 2000-03-03 | 2003-04-10 | Cambridge Antibody Tech | Human antibodies against eotaxin and their use |
| US6333410B1 (en) | 2000-08-18 | 2001-12-25 | Immunogen, Inc. | Process for the preparation and purification of thiol-containing maytansinoids |
| US7465790B2 (en) | 2000-10-09 | 2008-12-16 | Isis Innovation, Inc. | Therapeutic antibodies |
| US20020132983A1 (en) | 2000-11-30 | 2002-09-19 | Junghans Richard P. | Antibodies as chimeric effector cell receptors against tumor antigens |
| CA2467633C (en) | 2001-12-03 | 2012-03-27 | Abgenix, Inc. | Antibody categorization based on binding characteristics |
| AU2003217912A1 (en) * | 2002-03-01 | 2003-09-16 | Xencor | Antibody optimization |
| AU2003291281A1 (en) | 2002-11-01 | 2004-06-07 | The Ohio State University Research Foundation | Cytogenetic abnormalities that are predictive of response to therapy for chronic lymphocytic leukemia |
| CN1225480C (zh) * | 2002-12-18 | 2005-11-02 | 马菁 | 抗cd52单克隆抗体、其编码序列及应用 |
| US7534427B2 (en) | 2002-12-31 | 2009-05-19 | Immunomedics, Inc. | Immunotherapy of B cell malignancies and autoimmune diseases using unconjugated antibodies and conjugated antibodies and antibody combinations and fusion proteins |
| AU2004226492A1 (en) | 2003-03-31 | 2004-10-14 | Kirin Beer Kabushiki Kaisha | Method of inducing differentiation and proliferating regulatory T cell by anti-CD52 antibody and medicinal composition therefor |
| CA2526120A1 (en) | 2003-06-03 | 2005-02-24 | Cell Genesys, Inc. | Compositions and methods for enhanced expression of recombinant polypeptides from a single vector using a peptide cleavage site |
| CN1898267B (zh) | 2003-11-01 | 2012-05-23 | 默克专利股份有限公司 | 修饰的抗cd52抗体 |
| US20060204496A1 (en) * | 2003-11-28 | 2006-09-14 | Tetsuo Kojima | Agonist antibody against heteroreceptor |
| ITRM20030601A1 (it) | 2003-12-24 | 2005-06-25 | Lay Line Genomics Spa | Metodo per l'umanizzazione di anticorpi e anticorpi umanizzati con esso ottenuti. |
| AU2005282720B2 (en) * | 2004-09-02 | 2011-08-04 | Genentech, Inc. | Anti-FC-gamma RIIB receptor antibody and uses therefor |
| US7655229B2 (en) * | 2004-09-02 | 2010-02-02 | Chan Andrew C | Anti-FC-gamma RIIB receptor antibody and uses therefor |
| MX2007009545A (es) | 2005-02-08 | 2008-03-11 | Genzyme Corp | Anticuerpos para tgfbeta. |
| JP5175181B2 (ja) | 2005-05-27 | 2013-04-03 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | Tweak結合抗体 |
| PT1966244E (pt) * | 2005-12-30 | 2012-05-17 | Merck Patent Gmbh | Anticorpos anti-il-6 impedindo a ligação da il-6 complexada com il-6ralfa a gp130 |
| CA2649440A1 (en) * | 2006-04-12 | 2007-10-25 | Genzyme Corporation | Methods of treating autoimmune diseases |
| HUE026740T2 (en) | 2006-09-13 | 2016-07-28 | Alcafleu Man Gmbh & Co Kg | Treatment of Multiple Sclerosis (MS) with Campath-1H |
| CN101668531B (zh) | 2007-02-28 | 2014-05-07 | 默沙东公司 | 用于治疗免疫病症的联合治疗 |
| EP2160408A1 (en) * | 2007-06-22 | 2010-03-10 | Bayer Schering Pharma Aktiengesellschaft | Use of antibodies against the cd52 antigen for the treatment of neurological disorders, particularly transmissible spongiform encephalopathy and alzheimer's disease |
| TWI614267B (zh) | 2009-05-13 | 2018-02-11 | 建新公司 | 抗人類cd52免疫球蛋白 |
| EP2429584A4 (en) | 2009-05-13 | 2013-02-20 | Genzyme Corp | TREATMENT PROCEDURE AND COMPOSITIONS |
| BRPI1013927A2 (pt) | 2009-05-13 | 2016-04-05 | Genzyme Corp | métodos e composições para o tratamento de lúpus |
| EA031447B1 (ru) | 2009-07-15 | 2019-01-31 | Аимм Терапьютикс Б.В. | Антитела, которые связываются с sdr белками, и способы их использования |
| US9354228B2 (en) | 2010-07-16 | 2016-05-31 | Adimab, Llc | Antibody libraries |
| ITMI20110376A1 (it) | 2011-03-10 | 2012-09-11 | Wilic Sarl | Aerogeneratore raffreddato a fluido |
| GB201109238D0 (en) | 2011-06-01 | 2011-07-13 | Antitope Ltd | Antibodies |
| AR095199A1 (es) | 2013-03-15 | 2015-09-30 | Genzyme Corp | Anticuerpos anti-cd52 |
| EP3204425B1 (en) | 2014-10-09 | 2020-09-16 | Genzyme Corporation | Glycoengineered antibody drug conjugates |
| EP3612564A2 (en) | 2017-04-21 | 2020-02-26 | Genzyme Corporation | Treatment of multiple sclerosis with anti-cd52 antibodies |
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2006126068A2 (en) * | 2005-05-24 | 2006-11-30 | Avestha Gengraine Technologies Pvt Ltd | Recombinant method for the production of a monoclonal antibody to cd52 for the treatment of chronic lymphocytic leukemia |
Non-Patent Citations (2)
| Title |
|---|
| GRIBBEN J.G., HALLEK M., Rediscovering alemtuzumab: current and emerging therapeutic roles, BRITISH JOURNAL OF HAEMATOLOGY, March 2009, vol.144, no.6, pp.818-831;. * |
| РОЙТ А., БРОСТОФФФ ДЖ., МЕЙЛ Д. Иммунология. Пер. с англ. - М.:Мир, 2000 - 592с., ил. * |
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