CN113372443A - Il-8-结合抗体及其应用 - Google Patents
Il-8-结合抗体及其应用 Download PDFInfo
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- CN113372443A CN113372443A CN202110827885.2A CN202110827885A CN113372443A CN 113372443 A CN113372443 A CN 113372443A CN 202110827885 A CN202110827885 A CN 202110827885A CN 113372443 A CN113372443 A CN 113372443A
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| TWI895351B (zh) | 2020-02-12 | 2025-09-01 | 日商中外製藥股份有限公司 | 用於癌症之治療的抗cd137抗原結合分子 |
| WO2021165417A1 (en) * | 2020-02-19 | 2021-08-26 | Adivo Gmbh | Modified fc regions |
| PE20230108A1 (es) * | 2020-04-17 | 2023-01-25 | Zoetis Services Llc | Variantes de anticuerpos caninos |
| GB2595299B (en) | 2020-05-21 | 2022-08-03 | Mabsolve Ltd | Modified immunoglobulin FC regions |
| US20240382692A1 (en) * | 2020-07-28 | 2024-11-21 | Chugai Seiyaku Kabushiki Kaisha | Prefilled syringe formulation with needle with needle shield containing novel modified antibody |
| CN116847887A (zh) * | 2020-08-27 | 2023-10-03 | 伊诺西治疗公司 | 治疗自身免疫性疾病和癌症的方法和组合物 |
| EP4342984A4 (en) | 2021-05-19 | 2025-04-23 | Chugai Seiyaku Kabushiki Kaisha | Method for predicting in vivo pharmacokinetics of molecule |
| CN117500829A (zh) | 2021-06-18 | 2024-02-02 | 豪夫迈·罗氏有限公司 | 双特异性抗ccl2抗体 |
Family Cites Families (129)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| 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 |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| US5959177A (en) | 1989-10-27 | 1999-09-28 | The Scripps Research Institute | Transgenic plants expressing assembled secretory antibodies |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| WO1993012227A1 (en) | 1991-12-17 | 1993-06-24 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| JP2938569B2 (ja) | 1990-08-29 | 1999-08-23 | ジェンファーム インターナショナル，インコーポレイティド | 異種免疫グロブリンを作る方法及びトランスジェニックマウス |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| US5571894A (en) | 1991-02-05 | 1996-11-05 | Ciba-Geigy Corporation | Recombinant antibodies specific for a growth factor receptor |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| GB9114948D0 (en) | 1991-07-11 | 1991-08-28 | Pfizer Ltd | Process for preparing sertraline intermediates |
| JP3951062B2 (ja) | 1991-09-19 | 2007-08-01 | ジェネンテック・インコーポレーテッド | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、２官能性Ｆ（ａｂ’）２抗体の産生のための使用 |
| FI941572L (fi) | 1991-10-07 | 1994-05-27 | Oncologix Inc | Anti-erbB-2-monoklonaalisten vasta-aineiden yhdistelmä ja käyttömenetelmä |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| EP1136556B1 (en) | 1991-11-25 | 2005-06-08 | Enzon, Inc. | Method of producing multivalent antigen-binding proteins |
| EP1997894B1 (en) | 1992-02-06 | 2011-03-30 | Novartis Vaccines and Diagnostics, Inc. | Biosynthetic binding protein for cancer marker |
| SG48760A1 (en) | 1992-07-24 | 2003-03-18 | Abgenix Inc | Generation of xenogenetic antibodies |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| FR2707189B1 (fr) | 1993-07-09 | 1995-10-13 | Gradient Ass | Procédé de traitement de résidus de combustion et installation de mise en Óoeuvre dudit procédé. |
| CN1156460A (zh) * | 1994-07-13 | 1997-08-06 | 中外制药株式会社 | 抗人白细胞介素-8的重构人抗体 |
| JP3865418B2 (ja) * | 1994-07-13 | 2007-01-10 | 中外製薬株式会社 | ヒトインターロイキン−８に対する再構成ヒト抗体 |
| TW416960B (en) * | 1994-07-13 | 2001-01-01 | Chugai Pharmaceutical Co Ltd | Reshaped human antibody to human interleukin-8 |
| US6048972A (en) * | 1994-07-13 | 2000-04-11 | Chugai Pharmaceutical Co., Ltd. | Recombinant materials for producing humanized anti-IL-8 antibodies |
| DE69535243T2 (de) * | 1994-07-13 | 2007-05-10 | Chugai Seiyaku K.K. | Gegen menschliches interleukin-8 gerichteter, rekonstituierter menschlicher antikörper |
| US5789199A (en) | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US5840523A (en) | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous polypeptides |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| DE69637481T2 (de) | 1995-04-27 | 2009-04-09 | Amgen Fremont Inc. | Aus immunisierten Xenomäusen stammende menschliche Antikörper gegen IL-8 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| US6267958B1 (en) | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
| US6903194B1 (en) | 1996-09-26 | 2005-06-07 | Chungai Seiyaku Kabushiki Kaisha | Antibody against human parathormone related peptides |
| US6025158A (en) * | 1997-02-21 | 2000-02-15 | Genentech, Inc. | Nucleic acids encoding humanized anti-IL-8 monoclonal antibodies |
| FR2761994B1 (fr) | 1997-04-11 | 1999-06-18 | Centre Nat Rech Scient | Preparation de recepteurs membranaires a partir de baculovirus extracellulaires |
| US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
| US6610833B1 (en) | 1997-11-24 | 2003-08-26 | The Institute For Human Genetics And Biochemistry | Monoclonal human natural antibodies |
| ATE531812T1 (de) | 1997-12-05 | 2011-11-15 | Scripps Research Inst | Humanisierung von nager-antikörpern |
| US6458355B1 (en) * | 1998-01-22 | 2002-10-01 | Genentech, Inc. | Methods of treating inflammatory disease with anti-IL-8 antibody fragment-polymer conjugates |
| PT1071700E (pt) | 1998-04-20 | 2010-04-23 | Glycart Biotechnology Ag | Modificação por glicosilação de anticorpos para melhorar a citotoxicidade celular dependente de anticorpos |
| ES2694002T3 (es) | 1999-01-15 | 2018-12-17 | Genentech, Inc. | Polipéptido que comprende una región Fc de IgG1 humana variante |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| WO2000061739A1 (fr) | 1999-04-09 | 2000-10-19 | Kyowa Hakko Kogyo Co., Ltd. | Methode de regulation de l'activite d'une molecule immunologiquement fonctionnelle |
| EP1222292B1 (en) | 1999-10-04 | 2005-08-31 | Medicago Inc. | Method for regulating transcription of foreign genes in the presence of nitrogen |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| EP1240319A1 (en) | 1999-12-15 | 2002-09-18 | Genentech, Inc. | Shotgun scanning, a combinatorial method for mapping functional protein epitopes |
| PT2857516T (pt) | 2000-04-11 | 2017-08-28 | Genentech Inc | Anticorpos multivalentes e utilizações dos mesmos |
| JP5291279B2 (ja) | 2000-09-08 | 2013-09-18 | ウニヴェルジテート・チューリッヒ | 反復モジュールを含む反復タンパク質の集合体 |
| MXPA03002974A (es) | 2000-10-06 | 2004-05-05 | Kyowa Hakko Kogyo Kk | Celulas que producen composiciones de anticuerpo. |
| WO2002032925A2 (en) | 2000-10-16 | 2002-04-25 | Phylos, Inc. | Protein scaffolds for antibody mimics and other binding proteins |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| KR100857943B1 (ko) | 2000-11-30 | 2008-09-09 | 메다렉스, 인코포레이티드 | 인간 항체의 제조를 위한 형질전환 트랜스염색체 설치류 |
| AU2002307037B2 (en) | 2001-04-02 | 2008-08-07 | Biogen Idec Inc. | Recombinant antibodies coexpressed with GnTIII |
| US20030157561A1 (en) | 2001-11-19 | 2003-08-21 | Kolkman Joost A. | Combinatorial libraries of monomer domains |
| WO2003029462A1 (en) | 2001-09-27 | 2003-04-10 | Pieris Proteolab Ag | Muteins of human neutrophil gelatinase-associated lipocalin and related proteins |
| JP2005512044A (ja) * | 2001-12-03 | 2005-04-28 | アブジェニックス・インコーポレーテッド | 結合特性に基づく抗体分類 |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| JP4468803B2 (ja) * | 2002-05-31 | 2010-05-26 | ジーイー・ヘルスケア・バイオ−サイエンシーズ・アーベー | 結合剤を基板表面にカップリングさせる方法 |
| CA2488441C (en) | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
| US20060141456A1 (en) | 2002-06-12 | 2006-06-29 | Cynthia Edwards | Methods and compositions for milieu-dependent binding of a targeted agent to a target |
| EP3321282A1 (en) | 2002-09-27 | 2018-05-16 | Xencor, Inc. | Optimized fc variants and methods for their generation |
| US7361740B2 (en) | 2002-10-15 | 2008-04-22 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| AR042485A1 (es) | 2002-12-16 | 2005-06-22 | Genentech Inc | Anticuerpo humanizado que se une al cd20 humano |
| WO2004065416A2 (en) | 2003-01-16 | 2004-08-05 | Genentech, Inc. | Synthetic antibody phage libraries |
| US7871607B2 (en) | 2003-03-05 | 2011-01-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminoglycanases |
| US20060104968A1 (en) | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| NZ544486A (en) | 2003-06-13 | 2009-04-30 | Biogen Idec Inc | Aglycosyl anti-cd154 (cd40 ligand) antibodies and uses thereof |
| AU2003271174A1 (en) | 2003-10-10 | 2005-04-27 | Chugai Seiyaku Kabushiki Kaisha | Double specific antibodies substituting for functional protein |
| WO2005040229A2 (en) | 2003-10-24 | 2005-05-06 | Avidia, Inc. | Ldl receptor class a and egf domain monomers and multimers |
| EP2275448A3 (en) | 2003-12-19 | 2013-02-06 | Genentech, Inc. | Monovalent antibody fragments useful as therapeutics |
| ATE437184T1 (de) | 2004-01-12 | 2009-08-15 | Applied Molecular Evolution | Varianten der fc-region |
| US20050260711A1 (en) | 2004-03-30 | 2005-11-24 | Deepshikha Datta | Modulating pH-sensitive binding using non-natural amino acids |
| WO2005097832A2 (en) | 2004-03-31 | 2005-10-20 | Genentech, Inc. | Humanized anti-tgf-beta antibodies |
| US7785903B2 (en) | 2004-04-09 | 2010-08-31 | Genentech, Inc. | Variable domain library and uses |
| CA2885854C (en) | 2004-04-13 | 2017-02-21 | F. Hoffmann-La Roche Ag | Anti-p-selectin antibodies |
| DK2471813T3 (en) * | 2004-07-15 | 2015-03-02 | Xencor Inc | Optimized Fc variants |
| DK2213683T3 (da) | 2004-08-04 | 2013-09-02 | Mentrik Biotech Llc | VARIANT-Fc-REGIONER |
| CA2577370A1 (en) | 2004-08-16 | 2006-03-02 | Medimmune, Inc. | Integrin antagonists with enhanced antibody dependent cell-mediated cytotoxicity activity |
| KR20070057839A (ko) | 2004-08-19 | 2007-06-07 | 제넨테크, 인크. | 변경된 이펙터 기능을 갖는 폴리펩티드 변이체 |
| TWI309240B (en) | 2004-09-17 | 2009-05-01 | Hoffmann La Roche | Anti-ox40l antibodies |
| JO3000B1 (ar) | 2004-10-20 | 2016-09-05 | Genentech Inc | مركبات أجسام مضادة . |
| US7632497B2 (en) | 2004-11-10 | 2009-12-15 | Macrogenics, Inc. | Engineering Fc Antibody regions to confer effector function |
| US20090061485A1 (en) | 2004-12-22 | 2009-03-05 | Chugai Seiyaku Kabushiki Kaisha | Method of Producing an Antibody Using a Cell in Which the Function of Fucose Transporter Is Inhibited |
| CA2602663A1 (en) | 2005-03-31 | 2006-10-05 | Xencor, Inc. | Fc variants with optimized properties |
| US8008443B2 (en) | 2005-04-26 | 2011-08-30 | Medimmune, Llc | Modulation of antibody effector function by hinge domain engineering |
| PL1919503T3 (pl) | 2005-08-10 | 2015-04-30 | Macrogenics Inc | Identyfikacja i inżynieria przeciwciał ze zmiennymi regionami FC oraz sposoby ich stosowania |
| EP1931709B1 (en) | 2005-10-03 | 2016-12-07 | Xencor, Inc. | Fc variants with optimized fc receptor binding properties |
| ES2577292T3 (es) | 2005-11-07 | 2016-07-14 | Genentech, Inc. | Polipéptidos de unión con secuencias hipervariables de VH/VL diversificadas y consenso |
| US20070237764A1 (en) | 2005-12-02 | 2007-10-11 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| WO2007092772A2 (en) | 2006-02-03 | 2007-08-16 | Medimmune, Inc. | Protein formulations |
| EP3056568B1 (en) | 2006-03-31 | 2021-09-15 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| EP2016101A2 (en) | 2006-05-09 | 2009-01-21 | Genentech, Inc. | Binding polypeptides with optimized scaffolds |
| CA2659574C (en) | 2006-08-02 | 2017-04-25 | The Uab Research Foundation | Methods and compositions related to soluble monoclonal variable lymphocyte receptors of defined antigen specificity |
| PL2059533T3 (pl) | 2006-08-30 | 2013-04-30 | Genentech Inc | Przeciwciała wieloswoiste |
| MX2009002414A (es) * | 2006-09-08 | 2009-05-20 | Medimmune Llc | Anticuerpos anti-cd19 humanizados y su uso en el tratamiento de oncologia, transplante y enfermedad autoinmunitaria. |
| WO2008092117A2 (en) | 2007-01-25 | 2008-07-31 | Xencor, Inc. | Immunoglobulins with modifications in the fcr binding region |
| AU2008234248C1 (en) | 2007-03-29 | 2015-01-22 | Genmab A/S | Bispecific antibodies and methods for production thereof |
| EP2144931A2 (en) | 2007-04-04 | 2010-01-20 | The Government Of The U.S.A, As Represented By The Secretary, Dept. Of Health And Human Services | Monoclonal antibodies against dengue and other viruses with deletion in fc region |
| CN100592373C (zh) | 2007-05-25 | 2010-02-24 | 群康科技(深圳)有限公司 | 液晶显示面板驱动装置及其驱动方法 |
| WO2009026117A2 (en) * | 2007-08-16 | 2009-02-26 | Glaxo Group Limited | Novel compounds |
| CN101874042B9 (zh) | 2007-09-26 | 2019-01-01 | 中外制药株式会社 | 利用cdr的氨基酸取代来改变抗体等电点的方法 |
| HRP20150279T1 (hr) | 2007-12-26 | 2015-05-08 | Xencor, Inc. | Fc inaäśice s promijenjenim vezanjem na fcrn |
| AU2009204501B2 (en) | 2008-01-07 | 2015-02-12 | Amgen Inc. | Method for making antibody Fc-heterodimeric molecules using electrostatic steering effects |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| TWI667346B (zh) * | 2010-03-30 | 2019-08-01 | 中外製藥股份有限公司 | 促進抗原消失之具有經修飾的FcRn親和力之抗體 |
| CN103052649B (zh) | 2010-07-29 | 2015-12-16 | Xencor公司 | 具有修改的等电点的抗体 |
| KR101962483B1 (ko) | 2010-11-17 | 2019-03-29 | 추가이 세이야쿠 가부시키가이샤 | 혈액응고 제viii 인자의 기능을 대체하는 기능을 갖는 다중특이성 항원 결합 분자 |
| CN103328632A (zh) | 2010-11-30 | 2013-09-25 | 中外制药株式会社 | 与多分子的抗原重复结合的抗原结合分子 |
| JP6043629B2 (ja) | 2011-01-07 | 2016-12-14 | 中外製薬株式会社 | 抗体の物性を改善させる方法 |
| CN112812184A (zh) | 2011-02-25 | 2021-05-18 | 中外制药株式会社 | FcγRIIb特异性Fc抗体 |
| TW201817745A (zh) | 2011-09-30 | 2018-05-16 | 日商中外製藥股份有限公司 | 具有促進抗原清除之ＦｃＲｎ結合域的治療性抗原結合分子 |
| MX366269B (es) * | 2011-09-30 | 2019-07-04 | Chugai Pharmaceutical Co Ltd | Biblioteca de moleculas de union dependientes de la concentracion ionica. |
| CA2850194C (en) | 2011-09-30 | 2023-03-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule for promoting elimination of antigens |
| KR20230143201A (ko) | 2011-11-30 | 2023-10-11 | 추가이 세이야쿠 가부시키가이샤 | 면역 복합체를 형성하는 세포내로의 운반체（캐리어）를 포함하는 의약 |
| EP4624490A3 (en) | 2012-02-09 | 2025-11-05 | Chugai Seiyaku Kabushiki Kaisha | Modified fc region of antibody |
| KR20220136441A (ko) | 2012-02-24 | 2022-10-07 | 추가이 세이야쿠 가부시키가이샤 | ＦｃγＲＩＩＢ를 매개로 항원의 소실을 촉진하는 항원 결합 분자 |
| WO2014030750A1 (ja) | 2012-08-24 | 2014-02-27 | 中外製薬株式会社 | マウスFcγRII特異的Fc抗体 |
| WO2014030728A1 (ja) | 2012-08-24 | 2014-02-27 | 中外製薬株式会社 | FcγRIIb特異的Fc領域改変体 |
| EP2970508A4 (en) | 2013-03-15 | 2016-12-14 | Permeon Biologics Inc | GENETICALLY MODIFIED LOADING ANTIBODIES OR ENHANCED ENHANCEMENT ENHANCEMENT TARGETING PROTEIN COMPOSITIONS AND METHODS OF USE |
| CN113621057A (zh) | 2013-04-02 | 2021-11-09 | 中外制药株式会社 | Fc区变体 |
| SG10201907215QA (en) * | 2015-02-05 | 2019-09-27 | Chugai Pharmaceutical Co Ltd | Antibodies Comprising An Ion Concentration Dependent Antigen-Binding Domain, Fc Region Variants, Il-8-Binding Antibodies, And Uses Therof |
| MY203894A (en) * | 2015-09-18 | 2024-07-23 | Chugai Pharmaceutical Co Ltd | Il-8-binding antibodies and uses thereof |
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