JP6202774B1 - 抗ｃ５抗体および使用方法 - Google Patents
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| CN107551270A (zh) | 2008-04-11 | 2018-01-09 | 中外制药株式会社 | 与多个分子的抗原反复结合的抗原结合分子 |
| RU2658504C9 (ru) | 2010-11-30 | 2018-08-21 | Чугаи Сейяку Кабусики Кайся | Антигенсвязывающая молекула, способная многократно связываться с множеством антигенных молекул |
| TW201809008A (zh) | 2014-12-19 | 2018-03-16 | 日商中外製藥股份有限公司 | 抗ｃ５抗體及使用方法 |
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| JP2021506241A (ja) | 2017-12-13 | 2021-02-22 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドＲｅｇｅｎｅｒｏｎ Ｐｈａｒｍａｃｅｕｔｉｃａｌｓ， Ｉｎｃ． | 抗ｃ５抗体組み合わせ物およびその使用 |
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| CA3137907A1 (en) * | 2019-04-24 | 2020-10-29 | The Trustees Of The University Of Pennsylvania | Bi-functional humanized anti-c5 antibodies and factor h fusion proteins and uses thereof |
| CN113563467A (zh) * | 2020-04-28 | 2021-10-29 | 上海普铭生物科技有限公司 | 针对人补体蛋白c5的抗体及其应用 |
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Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995029697A1 (en) * | 1994-05-02 | 1995-11-09 | Alexion Pharmaceuticals, Inc. | Methods and compositions for the treatment of glomerulonephritis and other inflammatory diseases |
| WO2009125825A1 (ja) * | 2008-04-11 | 2009-10-15 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
| WO2010015608A1 (en) * | 2008-08-05 | 2010-02-11 | Novartis Ag | Compositions and methods for antibodies targeting complement protein c5 |
| WO2011111007A2 (en) * | 2010-03-11 | 2011-09-15 | Rinat Neuroscience Corporation | ANTIBODIES WITH pH DEPENDENT ANTIGEN BINDING |
| WO2014119969A1 (ko) * | 2013-01-31 | 2014-08-07 | 서울대학교 산학협력단 | 보체 관련 질환의 예방 및 치료를 위한 c5 항체 및 방법 |
| WO2014160958A1 (en) * | 2013-03-29 | 2014-10-02 | Alexion Pharmaceuticals, Inc. | Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 |
| WO2015134894A1 (en) * | 2014-03-07 | 2015-09-11 | Alexion Pharmaceuticals, Inc. | Anti-c5 antibodies having improved pharmacokinetics |
| WO2016098356A1 (en) * | 2014-12-19 | 2016-06-23 | Chugai Seiyaku Kabushiki Kaisha | Anti-c5 antibodies and methods of use |
| JP6088703B1 (ja) * | 2015-12-18 | 2017-03-01 | 中外製薬株式会社 | 抗ｃ５抗体および使用方法 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0230985Y2 (uk) | 1985-07-08 | 1990-08-21 | ||
| US7738506B1 (en) | 2001-06-12 | 2010-06-15 | Telefonaktiebolaget Lm Ericsson | Method and system for communication |
| US7432356B2 (en) | 2001-08-17 | 2008-10-07 | Genentech, Inc. | Complement pathway inhibitors binding to C5 and C5a without preventing formation of C5b |
| JP4333939B2 (ja) | 2001-08-27 | 2009-09-16 | ロード・コーポレーション | トロリ線の吊架装置 |
| DE10253331A1 (de) | 2002-11-14 | 2004-06-03 | Symrise Gmbh & Co. Kg | Verwendung von trans-Pellitori als Aromastoff |
| US7267849B2 (en) | 2004-03-02 | 2007-09-11 | Nitto Denko Corporation | Compensator for liquid crystal display |
| KR20080069889A (ko) | 2007-03-20 | 2008-07-29 | (주)화도 | 폴리에틸렌 관 |
| EP2129681A2 (en) * | 2007-03-22 | 2009-12-09 | Novartis Ag | C5 antigens and uses thereof |
| KR101515650B1 (ko) | 2007-04-11 | 2015-04-27 | 세키스이가가쿠 고교가부시키가이샤 | 가교 폴리비닐아세탈 수지의 제조 방법 및 가교 폴리비닐아세탈 수지 |
| KR20100054403A (ko) | 2008-11-14 | 2010-05-25 | 삼성전자주식회사 | 온라인 공동 작문 장치 및 방법 |
| TW201206466A (en) * | 2010-03-11 | 2012-02-16 | Rinat Neuroscience Corp | Antibodies with pH dependent antigen binding |
| KR20110111007A (ko) | 2010-04-02 | 2011-10-10 | 이화여자대학교 산학협력단 | Ｌ／ｄ 광학변환 및 광학분할을 위한 옥타하이드로-바이나프톨 유도체 |
| KR20110122011A (ko) | 2010-05-03 | 2011-11-09 | 황보철종 | 매장 포인트 통합 관리 시스템 및 그 방법 |
| EA028244B1 (ru) * | 2012-08-13 | 2017-10-31 | Ридженерон Фармасьютикалз, Инк. | АНТИТЕЛА К PCSK9 C pH-ЗАВИСИМЫМИ ХАРАКТЕРИСТИКАМИ СВЯЗЫВАНИЯ |
| MX2018015030A (es) * | 2016-06-17 | 2019-04-22 | Chugai Pharmaceutical Co Ltd | Anticuerpos anti-c5 y metodos de uso. |
-
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Patent Citations (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995029697A1 (en) * | 1994-05-02 | 1995-11-09 | Alexion Pharmaceuticals, Inc. | Methods and compositions for the treatment of glomerulonephritis and other inflammatory diseases |
| WO2009125825A1 (ja) * | 2008-04-11 | 2009-10-15 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
| WO2010015608A1 (en) * | 2008-08-05 | 2010-02-11 | Novartis Ag | Compositions and methods for antibodies targeting complement protein c5 |
| WO2011111007A2 (en) * | 2010-03-11 | 2011-09-15 | Rinat Neuroscience Corporation | ANTIBODIES WITH pH DEPENDENT ANTIGEN BINDING |
| WO2014119969A1 (ko) * | 2013-01-31 | 2014-08-07 | 서울대학교 산학협력단 | 보체 관련 질환의 예방 및 치료를 위한 c5 항체 및 방법 |
| WO2014160958A1 (en) * | 2013-03-29 | 2014-10-02 | Alexion Pharmaceuticals, Inc. | Compositions and methods for increasing the serum half-life of a therapeutic agent targeting complement c5 |
| WO2015134894A1 (en) * | 2014-03-07 | 2015-09-11 | Alexion Pharmaceuticals, Inc. | Anti-c5 antibodies having improved pharmacokinetics |
| WO2016098356A1 (en) * | 2014-12-19 | 2016-06-23 | Chugai Seiyaku Kabushiki Kaisha | Anti-c5 antibodies and methods of use |
| JP6088703B1 (ja) * | 2015-12-18 | 2017-03-01 | 中外製薬株式会社 | 抗ｃ５抗体および使用方法 |
| JP2017113013A (ja) * | 2015-12-18 | 2017-06-29 | 中外製薬株式会社 | 抗ｃ５抗体および使用方法 |
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