RU2425054C2 - Антитела против il2 - Google Patents
Антитела против il2 Download PDFInfo
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- RU2425054C2 RU2425054C2 RU2007143996/10A RU2007143996A RU2425054C2 RU 2425054 C2 RU2425054 C2 RU 2425054C2 RU 2007143996/10 A RU2007143996/10 A RU 2007143996/10A RU 2007143996 A RU2007143996 A RU 2007143996A RU 2425054 C2 RU2425054 C2 RU 2425054C2
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Cited By (2)
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| RU2745451C1 (ru) * | 2017-05-25 | 2021-03-25 | Инститьют Фор Бейсик Сайенс | Антитела к человеческому интерлейкину-2 и их применение |
| RU2832154C2 (ru) * | 2019-03-18 | 2024-12-19 | Бионтех Сел Энд Джин Терепиз Гмбх | Варианты рецептора интерлейкина-2 (il2r) и интерлейкина-2 (il2) для специфической активации иммунных эффекторных клеток |
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| EP2408820A4 (en) * | 2009-03-16 | 2013-01-23 | Cephalon Australia Pty Ltd | HUMANIZED ANTIBODIES WITH ANTITUMOR EFFECT |
| WO2011054030A1 (en) * | 2009-11-05 | 2011-05-12 | Cephalon Australia Pty Ltd | Treatment of cancer involving mutated kras or braf genes |
| WO2013152024A1 (en) * | 2012-04-03 | 2013-10-10 | Novelmed Therapeutics, Inc | Humanized and chimeric anti-factor c3 antibodies and uses thereof |
| BR112016013641A2 (pt) * | 2013-12-12 | 2017-08-08 | Umc Utrecht Holding Bv | Moléculas tipo imunoglobulina direcionadas contra fibronectina-eda |
| KR102400060B1 (ko) | 2013-12-26 | 2022-05-19 | 미쓰비시 타나베 파마 코퍼레이션 | 인간 항 il-33 중화 단일클론 항체 |
| WO2016005950A1 (en) * | 2014-07-10 | 2016-01-14 | Novartis Ag | Immune-stimulating monoclonal antibodies against human interleukin-2 |
| CN115636880A (zh) * | 2015-10-23 | 2023-01-24 | 辉瑞有限公司 | 抗il-2抗体及其组合物和用途 |
| WO2017122130A1 (en) | 2016-01-11 | 2017-07-20 | Novartis Ag | Immune-stimulating humanized monoclonal antibodies against human interleukin-2, and fusion proteins thereof |
| AU2017292752B2 (en) | 2016-07-06 | 2023-07-27 | Celgene Corporation | Antibodies with low immunogenicity and uses thereof |
| BR112019005944A2 (pt) * | 2016-09-28 | 2019-06-11 | Musc Foudation For Res Development | anticorpos que se ligam à interleucina 2 e usos dos mesmos |
| CN115920041A (zh) | 2017-08-31 | 2023-04-07 | 田边三菱制药株式会社 | 含有il-33拮抗剂的子宫内膜异位症治疗剂 |
| JP7245358B2 (ja) | 2019-06-10 | 2023-03-23 | 山東博安生物技術股▲ふん▼有限公司 | 抗cd25抗体及びその適用 |
| CN117157312A (zh) | 2021-03-30 | 2023-12-01 | 豪夫迈·罗氏有限公司 | 蛋白酶活化的多肽 |
| CN113248610B (zh) * | 2021-05-14 | 2022-08-16 | 厦门柏慈生物科技有限公司 | 白细胞介素2结合分子、其衍生物、试剂盒及其生产方法和用途 |
| WO2024068705A1 (en) | 2022-09-29 | 2024-04-04 | F. Hoffmann-La Roche Ag | Protease-activated polypeptides |
| CN115850471A (zh) * | 2022-10-13 | 2023-03-28 | 深圳市百士通科技开发有限公司 | 一种抗人il-2单克隆抗体及其应用 |
| CN119661706B (zh) * | 2024-01-31 | 2025-11-28 | 康立泰生物医药(青岛)有限公司 | 一种抗人白介素2抗体及其应用 |
| CN118515762B (zh) * | 2024-07-23 | 2024-11-01 | 北京百普赛斯生物科技股份有限公司 | 特异性结合il-2的抗体及其应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2197993C2 (ru) * | 1996-12-11 | 2003-02-10 | Авентис Фарма Дойчланд Гмбх | Самоусиливающиеся фармакологически контролируемые экспрессионные системы |
| RU2004114882A (ru) * | 2001-11-14 | 2005-04-20 | Сентокор, Инк. (Us) | Антитела против il-6, композиции, способы и применение |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2001274939A1 (en) * | 2000-05-24 | 2001-12-03 | Smith Kline Beecham Corporation | Sialoadhesin factor-3 antibodies |
| GB0013810D0 (en) * | 2000-06-06 | 2000-07-26 | Celltech Chiroscience Ltd | Biological products |
| WO2004045512A2 (en) * | 2002-11-15 | 2004-06-03 | Genmab A/S | Human monoclonal antibodies against cd25 |
| EP1653844B1 (en) * | 2003-08-13 | 2012-12-12 | Novartis Vaccines and Diagnostics, Inc. | Prion-specific peptide reagents |
-
2006
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- 2006-05-31 RU RU2007143996/10A patent/RU2425054C2/ru not_active IP Right Cessation
- 2006-05-31 EP EP06743094A patent/EP1888644A1/en not_active Withdrawn
- 2006-05-31 JP JP2008514011A patent/JP5414271B2/ja not_active Expired - Fee Related
- 2006-05-31 MX MX2007014565A patent/MX2007014565A/es active IP Right Grant
- 2006-05-31 WO PCT/EP2006/005194 patent/WO2006128690A1/en not_active Ceased
- 2006-05-31 NZ NZ563213A patent/NZ563213A/en not_active IP Right Cessation
- 2006-05-31 US US11/916,017 patent/US7964707B2/en active Active
- 2006-05-31 BR BRPI0610912-8A patent/BRPI0610912A2/pt not_active Application Discontinuation
- 2006-05-31 AU AU2006254333A patent/AU2006254333B2/en not_active Ceased
- 2006-05-31 CN CN2006800197422A patent/CN101189265B/zh not_active Expired - Fee Related
- 2006-05-31 CA CA2609234A patent/CA2609234C/en not_active Expired - Fee Related
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2007
- 2007-10-31 ZA ZA200709456A patent/ZA200709456B/xx unknown
- 2007-11-12 IL IL187316A patent/IL187316A0/en unknown
- 2007-12-19 NO NO20076568A patent/NO20076568L/no not_active Application Discontinuation
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2197993C2 (ru) * | 1996-12-11 | 2003-02-10 | Авентис Фарма Дойчланд Гмбх | Самоусиливающиеся фармакологически контролируемые экспрессионные системы |
| RU2004114882A (ru) * | 2001-11-14 | 2005-04-20 | Сентокор, Инк. (Us) | Антитела против il-6, композиции, способы и применение |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2745451C1 (ru) * | 2017-05-25 | 2021-03-25 | Инститьют Фор Бейсик Сайенс | Антитела к человеческому интерлейкину-2 и их применение |
| RU2832154C2 (ru) * | 2019-03-18 | 2024-12-19 | Бионтех Сел Энд Джин Терепиз Гмбх | Варианты рецептора интерлейкина-2 (il2r) и интерлейкина-2 (il2) для специфической активации иммунных эффекторных клеток |
Also Published As
| Publication number | Publication date |
|---|---|
| NO20076568L (no) | 2008-02-19 |
| AU2006254333B2 (en) | 2011-02-17 |
| EP1888644A1 (en) | 2008-02-20 |
| CA2609234C (en) | 2014-04-22 |
| KR20080032046A (ko) | 2008-04-14 |
| JP5414271B2 (ja) | 2014-02-12 |
| US20080317746A1 (en) | 2008-12-25 |
| BRPI0610912A2 (pt) | 2008-12-02 |
| CN101189265B (zh) | 2012-07-04 |
| CA2609234A1 (en) | 2006-12-07 |
| ZA200709456B (en) | 2008-08-27 |
| MX2007014565A (es) | 2008-02-11 |
| JP2008542321A (ja) | 2008-11-27 |
| NZ563213A (en) | 2009-07-31 |
| AU2006254333A1 (en) | 2006-12-07 |
| RU2007143996A (ru) | 2009-07-20 |
| US7964707B2 (en) | 2011-06-21 |
| IL187316A0 (en) | 2008-04-13 |
| KR101340559B1 (ko) | 2013-12-11 |
| WO2006128690A1 (en) | 2006-12-07 |
| CN101189265A (zh) | 2008-05-28 |
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