ES2546943T3 - Polipéptidos, dominios variables de anticuerpo y antagonistas - Google Patents
Polipéptidos, dominios variables de anticuerpo y antagonistas Download PDFInfo
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- ES2546943T3 ES2546943T3 ES08750800.8T ES08750800T ES2546943T3 ES 2546943 T3 ES2546943 T3 ES 2546943T3 ES 08750800 T ES08750800 T ES 08750800T ES 2546943 T3 ES2546943 T3 ES 2546943T3
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Classifications
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- 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
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Landscapes
- Health & Medical Sciences (AREA)
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Applications Claiming Priority (5)
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| US93363207P | 2007-06-06 | 2007-06-06 | |
| US933632P | 2007-06-06 | ||
| GB0724331 | 2007-12-13 | ||
| GBGB0724331.4A GB0724331D0 (en) | 2007-12-13 | 2007-12-13 | Compositions for pulmonary delivery |
| PCT/GB2008/050405 WO2008149148A2 (en) | 2007-06-06 | 2008-06-04 | Polypeptides, antibody variable domains and antagonists |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2546943T3 true ES2546943T3 (es) | 2015-09-30 |
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| ES08750800.8T Active ES2546943T3 (es) | 2007-06-06 | 2008-06-04 | Polipéptidos, dominios variables de anticuerpo y antagonistas |
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| EP (5) | EP2162468A2 (OSRAM) |
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| BR (3) | BRPI0812268A2 (OSRAM) |
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| CR (2) | CR11195A (OSRAM) |
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| CN103254309B (zh) | 2005-05-18 | 2017-09-26 | 埃博灵克斯股份有限公司 | 针对肿瘤坏死因子α的改进的纳米体TM |
| DE102005023617A1 (de) | 2005-05-21 | 2006-11-23 | Aspre Ag | Verfahren zum Mischen von Farben in einem Display |
| GB0724331D0 (en) | 2007-12-13 | 2008-01-23 | Domantis Ltd | Compositions for pulmonary delivery |
| JP2010528647A (ja) * | 2007-06-06 | 2010-08-26 | ドマンティス リミテッド | ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
| MX2009013137A (es) | 2007-06-06 | 2010-04-30 | Domantis Ltd | Metodos para seleccionar polipeptidos resistentes a la proteasa. |
| BRPI0819932A2 (pt) * | 2007-12-13 | 2019-07-30 | Glaxo Group Ltd | composição, uso de uma composição, dispositivo nebulizador, inalador ou intranasal, processos para produzir uma composição farmacêutica e uma composição polipeptídica, e, uso de um tampão fisiologicamente aceitável. |
| CN102089325A (zh) | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | 能够结合血清白蛋白的肽，以及包含其的化合物、构建体和多肽 |
| LT3216803T (lt) | 2008-06-25 | 2020-06-10 | Novartis Ag | Stabilūs ir tirpūs antikūnai, slopinantys vegf |
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| KR20110091777A (ko) * | 2008-11-26 | 2011-08-12 | 글락소 그룹 리미티드 | 폴리펩티드, 항체 가변 도메인 및 길항제 |
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| JP2012532620A (ja) | 2009-07-16 | 2012-12-20 | グラクソ グループ リミテッド | 改良型抗血清アルブミン結合単一可変ドメイン |
| WO2011047215A1 (en) * | 2009-10-14 | 2011-04-21 | Aileron Therapeutics, Inc. | Improved peptidomimetic macrocycles |
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| EP2531523A1 (en) | 2010-02-05 | 2012-12-12 | Ablynx N.V. | Peptides capable of binding to serum albumin and compounds, constructs and polypeptides comprising the same |
| KR20130109977A (ko) | 2010-05-20 | 2013-10-08 | 글락소 그룹 리미티드 | 개선된 항-혈청 알부민 결합 변이체 |
| US9012609B2 (en) * | 2010-08-13 | 2015-04-21 | Glaxosmithkline Intellectual Property Development Limited | Anti-serum albumin binding variants |
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| CA2810465C (en) | 2010-09-16 | 2018-10-02 | Baliopharm Ag | Anti-hutnfr1 antibody |
| JP2014501515A (ja) | 2010-12-01 | 2014-01-23 | グラクソ グループ リミテッド | 改良された抗血清アルブミン結合単一可変ドメイン |
| JP2014505698A (ja) * | 2011-02-02 | 2014-03-06 | グラクソ グループ リミテッド | 新規抗原結合タンパク質 |
| US9527925B2 (en) | 2011-04-01 | 2016-12-27 | Boehringer Ingelheim International Gmbh | Bispecific binding molecules binding to VEGF and ANG2 |
| RU2642310C2 (ru) | 2011-06-28 | 2018-01-24 | ИНХИБРКС ЭлЭлСи | Слитые серпиновые полипептиды и способы их применения |
| US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
| CA2842099A1 (en) * | 2011-07-27 | 2013-01-31 | Glaxo Group Limited | Antigen binding constructs |
| UA118833C2 (uk) * | 2011-08-17 | 2019-03-25 | Ґлаксо Ґруп Лімітед | Одиничний варіабельний домен імуноглобуліну, який зв'язується з tnfr1 |
| GB2497138A (en) * | 2011-12-02 | 2013-06-05 | Randox Lab Ltd | Biomarkers for stroke and stroke subtype diagnosis. |
| US9695233B2 (en) | 2012-07-13 | 2017-07-04 | Roche Glycart Ag | Bispecific anti-VEGF/anti-ANG-2 antibodies and their use in the treatment of ocular vascular diseases |
| WO2014111550A1 (en) | 2013-01-17 | 2014-07-24 | Glaxosmithkline Intellectual Property Development Limited | Modified anti-serum albumin binding proteins |
| TW201514193A (zh) * | 2013-01-31 | 2015-04-16 | Glaxo Group Ltd | 製備蛋白質之方法 |
| US9840553B2 (en) | 2014-06-28 | 2017-12-12 | Kodiak Sciences Inc. | Dual PDGF/VEGF antagonists |
| AR103173A1 (es) | 2014-12-22 | 2017-04-19 | Novarits Ag | Productos farmacéuticos y composiciones líquidas estables de anticuerpos il-17 |
| MA41374A (fr) * | 2015-01-20 | 2017-11-28 | Cytomx Therapeutics Inc | Substrats clivables par métalloprotéase matricielle et clivables par sérine protéase et procédés d'utilisation de ceux-ci |
| JP7088454B2 (ja) | 2015-12-30 | 2022-06-21 | コディアック サイエンシーズ インコーポレイテッド | 抗体および抗体複合体 |
| GB201617622D0 (en) * | 2016-10-18 | 2016-11-30 | VIB VZW and Universiteit Gent | Means and methods to treat inflammation |
| RU2625010C1 (ru) * | 2016-11-10 | 2017-07-11 | Илья Петрович Приколаб | Экспрессионный плазмидный вектор для экспрессии активной формы TNFR1-Fc и способ получения рекомбинантного белка |
| MX2019005947A (es) | 2016-11-28 | 2019-08-26 | Chugai Pharmaceutical Co Ltd | Molecula de union a ligando que tiene actividad de union a ligando ajustable. |
| AU2017364817B2 (en) | 2016-11-28 | 2023-11-09 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding domain, and polypeptide including conveying section |
| UY37651A (es) * | 2017-03-31 | 2018-10-31 | Swedish Orphan Biovitrum Ab Publ | Polipéptido de unión al il-1r-i |
| EP3703689A1 (en) * | 2017-11-01 | 2020-09-09 | Allogene Therapeutics, Inc. | Modified caspase-9 polypeptides and methods of use thereof |
| KR20200089312A (ko) | 2017-11-28 | 2020-07-24 | 추가이 세이야쿠 가부시키가이샤 | 리간드 결합 활성을 조정 가능한 리간드 결합 분자 |
| KR20250134208A (ko) | 2017-11-28 | 2025-09-09 | 추가이 세이야쿠 가부시키가이샤 | 항원 결합 도메인 및 운반 부분을 포함하는 폴리펩티드 |
| CN112203679A (zh) | 2018-03-02 | 2021-01-08 | 科达制药股份有限公司 | Il-6抗体及其融合构建体和缀合物 |
| US20210155701A1 (en) * | 2018-05-30 | 2021-05-27 | Chugai Seiyaku Kabushiki Kaisha | Polypeptide comprising il-1r1 binding domain and carrying moiety |
| WO2019230867A1 (en) | 2018-05-30 | 2019-12-05 | Chugai Seiyaku Kabushiki Kaisha | Polypeptide comprising aggrecan binding domain and carrying moiety |
| PL3623798T3 (pl) * | 2018-09-13 | 2022-03-28 | Euroimmun Medizinische Labordiagnostika Ag | Sposób i urządzenie do wykrywania i przedstawiania obrazu immunofluorescencyjnego próbki biologicznej |
| CN112955240B (zh) * | 2018-10-25 | 2022-09-16 | 豪夫迈·罗氏有限公司 | 抗体FcRn结合的修饰 |
| AU2019394972A1 (en) | 2018-12-06 | 2021-06-03 | Cytomx Therapeutics, Inc. | Matrix metalloprotease-cleavable and serine or cysteine protease-cleavable substrates and methods of use thereof |
| CN111454366B (zh) * | 2019-01-21 | 2023-06-16 | 中国科学院深圳先进技术研究院 | 一种融合蛋白及其应用 |
| EP3919903B1 (en) * | 2019-01-31 | 2025-01-08 | Sekisui Medical Co., Ltd. | Method for immunological analysis of free aim in biological sample, and measurement kit |
| WO2021072265A1 (en) | 2019-10-10 | 2021-04-15 | Kodiak Sciences Inc. | Methods of treating an eye disorder |
| JP7473398B2 (ja) * | 2020-05-28 | 2024-04-23 | シスメックス株式会社 | キャリブレータ、複合体、及びＩｇＡ凝集体を測定する方法 |
| IL300930A (en) * | 2020-08-27 | 2023-04-01 | Enosi Therapeutics Corp | Methods and compositions for the treatment of autoimmune diseases and cancer |
| WO2022117569A1 (en) | 2020-12-02 | 2022-06-09 | Oncurious Nv | A ccr8 antagonist antibody in combination with a lymphotoxin beta receptor agonist antibody in therapy against cancer |
| CN115181751A (zh) * | 2021-04-02 | 2022-10-14 | 苏州博腾生物制药有限公司 | 靶向白蛋白的嵌合抗原受体及其使用方法 |
| CN114657162B (zh) * | 2022-03-04 | 2023-06-16 | 华南理工大学 | 一种具有血管内皮细胞保护功能的抗氧化五肽及其应用 |
| CN115112704B (zh) * | 2022-06-21 | 2025-07-15 | 中特检验集团有限公司 | 一种光热发电有机热载体热稳定性检测方法 |
| TWI850016B (zh) | 2022-07-08 | 2024-07-21 | 丹麥商諾佛 儂迪克股份有限公司 | 能夠取代fviii(a)之高效isvd化合物 |
| WO2025049818A1 (en) | 2023-08-29 | 2025-03-06 | Enosi Therapeutics Corporation | Tnfr1 antagonists lacking agonist activity and uses thereof |
| CN119909772B (zh) * | 2025-04-01 | 2025-06-20 | 安徽一帆新材料科技有限公司 | 用于净水的再生阴树脂及其制备方法 |
Family Cites Families (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2148299B (en) * | 1983-09-01 | 1988-01-06 | Hybritech Inc | Antibody compositions of therapeutic agents having an extended serum half-life |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| JP3095168B2 (ja) | 1988-02-05 | 2000-10-03 | エル． モリソン，シェリー | ドメイン‐変性不変部を有する抗体 |
| DE68927933T2 (de) | 1988-09-02 | 1997-08-14 | Dyax Corp | Herstellung und auswahl von rekombinantproteinen mit verschiedenen bindestellen |
| FI903489A0 (fi) | 1988-11-11 | 1990-07-10 | Medical Res Council | Ligander med en enda sektion, receptorer innehaollande naemnda ligander, foerfaranden foer deras framstaellning samt anvaendning av liganderna och receptorerna. |
| ATE92107T1 (de) | 1989-04-29 | 1993-08-15 | Delta Biotechnology Ltd | N-terminale fragmente von menschliches serumalbumin enthaltenden fusionsproteinen. |
| CA2016842A1 (en) | 1989-05-16 | 1990-11-16 | Richard A. Lerner | Method for tapping the immunological repertoire |
| US5143854A (en) | 1989-06-07 | 1992-09-01 | Affymax Technologies N.V. | Large scale photolithographic solid phase synthesis of polypeptides and receptor binding screening thereof |
| US5977307A (en) | 1989-09-07 | 1999-11-02 | Alkermes, Inc. | Transferrin receptor specific ligand-neuropharmaceutical agent fusion proteins |
| US6172197B1 (en) | 1991-07-10 | 2001-01-09 | Medical Research Council | Methods for producing members of specific binding pairs |
| 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 |
| WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| JPH06504997A (ja) | 1990-12-06 | 1994-06-09 | アフィメトリックス， インコーポレイテッド | 非常に大きい規模の固定化されたポリマーの合成 |
| DE69233745D1 (de) | 1991-12-02 | 2008-10-23 | Cambridge Antibody Tech | Herstellung von Autoantikörpern auf Phagenoberflächen ausgehend von Antikörpersegmentbibliotheken |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| CA2163345A1 (en) | 1993-06-16 | 1994-12-22 | Susan Adrienne Morgan | Antibodies |
| US5702892A (en) | 1995-05-09 | 1997-12-30 | The United States Of America As Represented By The Department Of Health And Human Services | Phage-display of immunoglobulin heavy chain libraries |
| DK1143006T3 (da) | 1995-08-18 | 2008-07-14 | Morphosys Ip Gmbh | Vektorer/DNA-sekvenser fra humane kombinatoriske antistofbiblioteker |
| BRPI9707379B8 (pt) * | 1996-02-09 | 2015-07-07 | Abbvie Biotechnology Ltd | Composições farmacêuticas compreendendo anticorpo humano recombinante geneticamente engenheirado, e anticorpo humano recombinante geneticamente engenheirado. |
| EP1908832B1 (en) | 1997-07-07 | 2012-12-26 | Medical Research Council | A method for increasing the concentration of a nucleic acid molecule |
| GB9722131D0 (en) | 1997-10-20 | 1997-12-17 | Medical Res Council | Method |
| AU762814B2 (en) | 1998-05-13 | 2003-07-03 | Domantis Limited | Selection system |
| IL127127A0 (en) | 1998-11-18 | 1999-09-22 | Peptor Ltd | Small functional units of antibody heavy chain variable regions |
| GB2375112A (en) | 2000-02-03 | 2002-11-06 | Domantis Ltd | Combinatorial protein domains |
| CA2399388A1 (en) | 2000-02-11 | 2001-08-16 | Michael J. Lenardo | Identification of a domain in the tumor necrosis factor receptor family that mediates pre-ligand receptor assembly and function |
| US7164009B2 (en) * | 2000-09-15 | 2007-01-16 | Genentech, Inc. | Pro9821 polypeptides |
| TWI327599B (en) | 2000-11-28 | 2010-07-21 | Medimmune Llc | Methods of administering/dosing anti-rsv antibodies for prophylaxis and treatment |
| US20060073141A1 (en) * | 2001-06-28 | 2006-04-06 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| CA2447851C (en) | 2001-06-28 | 2012-08-28 | Domantis Limited | Dual-specific ligand and its use |
| GB0118689D0 (en) * | 2001-08-01 | 2001-09-19 | Psimedica Ltd | Pharmaceutical formulation |
| WO2003076567A2 (en) | 2002-03-05 | 2003-09-18 | Eli Lilly And Company | Heterologous g-csf fusion proteins |
| DK1517921T3 (da) * | 2002-06-28 | 2006-10-09 | Domantis Ltd | Immunglobulin-enkeltvariable antigen-bindende domæner og dobbeltspecifikke konstruktioner deraf |
| US20060002935A1 (en) | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| US7696320B2 (en) | 2004-08-24 | 2010-04-13 | Domantis Limited | Ligands that have binding specificity for VEGF and/or EGFR and methods of use therefor |
| NZ538384A (en) | 2002-09-06 | 2009-04-30 | Alexion Pharma Inc | Treatment for asthma using a compound which binds to or otherwise blocks the generation and/or activity of one or more complement components reptors, such as, C5a receptors |
| NZ538569A (en) | 2002-09-06 | 2009-02-28 | Amgen Inc | Therapeutic human anti-IL-1R1 monoclonal antibody |
| EP3299393A1 (en) | 2002-11-08 | 2018-03-28 | Ablynx N.V. | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| AU2003290330A1 (en) | 2002-12-27 | 2004-07-22 | Domantis Limited | Dual specific single domain antibodies specific for a ligand and for the receptor of the ligand |
| GB0230203D0 (en) * | 2002-12-27 | 2003-02-05 | Domantis Ltd | Fc fusion |
| US20060104968A1 (en) * | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| AU2004220325B2 (en) * | 2003-06-30 | 2011-05-12 | Domantis Limited | Polypeptides |
| EP1729795B1 (en) | 2004-02-09 | 2016-02-03 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1737962B1 (en) | 2004-03-24 | 2010-09-01 | Domantis Limited | Gas1 universal leader |
| PL1802334T3 (pl) * | 2004-10-21 | 2013-01-31 | Genentech Inc | Sposób leczenia wewnątrzgałkowych chorób neowaskularnych |
| MX2007006593A (es) * | 2004-12-02 | 2008-03-04 | Domantis Ltd | Anticuerpos de dominio simple anti-il 1r1 y sus usos terapeuticos. |
| GB0521621D0 (en) * | 2005-10-24 | 2005-11-30 | Domantis Ltd | Tumor necrosis factor receptor 1 antagonists for treating respiratory diseases |
| EP1957536A2 (en) * | 2005-12-01 | 2008-08-20 | Domantis Limited | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007063311A2 (en) | 2005-12-01 | 2007-06-07 | Domantis Limited | Competitive domain antibody formats that bind interleukin 1 receptor type 1 |
| US8940683B2 (en) | 2006-08-10 | 2015-01-27 | Roy C. Levitt | Localized therapy of lower airways inflammatory disorders with proinflammatory cytokine inhibitors |
| WO2008049897A1 (en) * | 2006-10-27 | 2008-05-02 | Ablynx N.V. | Intranasal delivery of polypeptides and proteins |
| MX2009013137A (es) | 2007-06-06 | 2010-04-30 | Domantis Ltd | Metodos para seleccionar polipeptidos resistentes a la proteasa. |
| JP2010528647A (ja) | 2007-06-06 | 2010-08-26 | ドマンティス リミテッド | ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
-
2008
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