KR102311761B1 - 항-Siglec-8 항체 및 그의 사용 방법 - Google Patents
항-Siglec-8 항체 및 그의 사용 방법 Download PDFInfo
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- KR102311761B1 KR102311761B1 KR1020167018130A KR20167018130A KR102311761B1 KR 102311761 B1 KR102311761 B1 KR 102311761B1 KR 1020167018130 A KR1020167018130 A KR 1020167018130A KR 20167018130 A KR20167018130 A KR 20167018130A KR 102311761 B1 KR102311761 B1 KR 102311761B1
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| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
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| US20190338027A1 (en) * | 2017-01-06 | 2019-11-07 | Allakos Inc. | Methods and compositions for treating chronic obstructive pulmonary disorder |
| EA201992626A1 (ru) | 2017-05-05 | 2020-04-24 | Аллакос Инк. | Способы и композиции для лечения аллергических заболеваний глаз |
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| KR20200105494A (ko) | 2017-12-29 | 2020-09-07 | 코넬 유니버시티 | 호산구성 장애에 대한 유전자 요법 |
| US20210246205A1 (en) * | 2018-05-04 | 2021-08-12 | Allakos Inc. | Methods and compositions for treating chronic urticaria |
| BR112021015009A2 (pt) * | 2019-02-15 | 2021-10-05 | Allakos Inc. | Métodos e composições para o tratamento da gastrite mastocística, esofagite mastocística, enterite mastocística, duodenite mastocística e/ou gastroenterite mastocística |
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| EP4048698A4 (en) * | 2019-10-24 | 2023-12-06 | Allakos Inc. | Methods and compositions for treating irritable bowel syndrome and functional dyspepsia |
| EP4061840A4 (en) * | 2019-11-19 | 2024-05-15 | The Trustees of The University of Pennsylvania | ANTI-ALPHA-SYNUCLEIN MONOCLONAL ANTIBODIES, AND CORRESPONDING METHODS OF USE |
| WO2021247821A1 (en) * | 2020-06-03 | 2021-12-09 | The Wistar Institute Of Anatomy And Biology | Monoclonal antibodies against human siglec-9 and use thereof for immunotherapy |
| WO2022061032A1 (en) * | 2020-09-17 | 2022-03-24 | Allakos Inc. | Methods and compositions for treating viral infection |
| WO2022215566A1 (ja) * | 2021-04-05 | 2022-10-13 | 国立大学法人筑波大学 | アレルギー性疾患の予防又は治療剤 |
| EP4518897A1 (en) * | 2022-05-06 | 2025-03-12 | Seattle Children's Hospital d/b/a Seattle Children's Research Institute | Inhibiting mast cell activation by binding sialic acid-binding immunoglobulin-like lectin-9 (siglec-9) |
| WO2024043940A1 (en) * | 2022-08-25 | 2024-02-29 | Allakos Inc. | Methods and compositions for treating atopic dermatitis |
| WO2024254441A1 (en) * | 2023-06-08 | 2024-12-12 | Allakos Inc. | Bispecific antibodies to siglec-6 and siglec-8 and methods of use thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001066126A1 (en) | 2000-03-07 | 2001-09-13 | Smithkline Beecham Corporation | Sialoadhesin factor-2 antibodies |
| US20030092091A1 (en) * | 2000-03-07 | 2003-05-15 | Abrahamson Julie A. | Sialoadhesin factor-2 antibodies |
Family Cites Families (89)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
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| US4601978A (en) | 1982-11-24 | 1986-07-22 | The Regents Of The University Of California | Mammalian metallothionein promoter system |
| US4560655A (en) | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4767704A (en) | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US4965199A (en) | 1984-04-20 | 1990-10-23 | Genentech, Inc. | Preparation of functional human factor VIII in mammalian cells using methotrexate based selection |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| 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 |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| US4927762A (en) | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| 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 |
| US5677425A (en) | 1987-09-04 | 1997-10-14 | Celltech Therapeutics Limited | Recombinant antibody |
| EP0435911B1 (en) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Cell culture medium for enhanced cell growth, culture longevity and product expression |
| 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 |
| US5891693A (en) | 1990-01-25 | 1999-04-06 | Alusuisse Holdings A.G. | Recombinant DNA methods vectors and host cells |
| US5122469A (en) | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| US5508192A (en) | 1990-11-09 | 1996-04-16 | Board Of Regents, The University Of Texas System | Bacterial host strains for producing proteolytically sensitive polypeptides |
| US5264365A (en) | 1990-11-09 | 1993-11-23 | Board Of Regents, The University Of Texas System | Protease-deficient bacterial strains for production of proteolytically sensitive polypeptides |
| 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 |
| 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 |
| EP0605522B1 (en) | 1991-09-23 | 1999-06-23 | Medical Research Council | Methods for the production of humanized antibodies |
| 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 |
| EP1997894B1 (en) | 1992-02-06 | 2011-03-30 | Novartis Vaccines and Diagnostics, Inc. | Biosynthetic binding protein for cancer marker |
| CA2118508A1 (en) | 1992-04-24 | 1993-11-11 | Elizabeth S. Ward | Recombinant production of immunoglobulin-like domains in prokaryotic cells |
| PT752248E (pt) | 1992-11-13 | 2001-01-31 | Idec Pharma Corp | Aplicacao terapeutica de anticorpos quimericos e marcados radioactivamente contra antigenios de diferenciacao restrita de linfocitos b humanos para o tratamento do linfoma de celulas b |
| US5885573A (en) | 1993-06-01 | 1999-03-23 | Arch Development Corporation | Methods and materials for modulation of the immunosuppressive activity and toxicity of monoclonal antibodies |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| US5639635A (en) | 1994-11-03 | 1997-06-17 | 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 |
| US5641870A (en) | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US6121022A (en) | 1995-04-14 | 2000-09-19 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| GB9603256D0 (en) | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US6027888A (en) | 1996-04-05 | 2000-02-22 | Board Of Regents, The University Of Texas System | Methods for producing soluble, biologically-active disulfide-bond containing eukaryotic proteins in bacterial cells |
| US5834597A (en) | 1996-05-20 | 1998-11-10 | Protein Design Labs, Inc. | Mutated nonactivating IgG2 domains and anti CD3 antibodies incorporating the same |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US6083715A (en) | 1997-06-09 | 2000-07-04 | Board Of Regents, The University Of Texas System | Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells |
| JP2002506353A (ja) | 1997-06-24 | 2002-02-26 | ジェネンテック・インコーポレーテッド | ガラクトシル化糖タンパク質の方法及び組成物 |
| WO1999022764A1 (en) | 1997-10-31 | 1999-05-14 | Genentech, Inc. | Methods and compositions comprising glycoprotein glycoforms |
| ATE531812T1 (de) | 1997-12-05 | 2011-11-15 | Scripps Research Inst | Humanisierung von nager-antikörpern |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| DK1068241T3 (da) | 1998-04-02 | 2008-02-04 | Genentech Inc | Antistofvarianter og fragmenter deraf |
| 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 |
| US7504256B1 (en) | 1999-10-19 | 2009-03-17 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing polypeptide |
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| ES2649037T3 (es) | 2000-12-12 | 2018-01-09 | Medimmune, Llc | Moléculas con semividas prolongadas, composiciones y usos de las mismas |
| CA2838062C (en) | 2001-08-03 | 2015-12-22 | Roche Glycart Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| NZ532526A (en) * | 2001-10-25 | 2007-01-26 | Genentech Inc | Compositions comprising a glycoprotein having a Fc region |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| US7317091B2 (en) | 2002-03-01 | 2008-01-08 | Xencor, Inc. | Optimized Fc variants |
| AU2003236019A1 (en) | 2002-04-09 | 2003-10-20 | Kyowa Hakko Kirin Co., Ltd. | Drug containing antibody composition appropriate for patient suffering from Fc Gamma RIIIa polymorphism |
| WO2003084569A1 (en) | 2002-04-09 | 2003-10-16 | Kyowa Hakko Kogyo Co., Ltd. | Drug containing antibody composition |
| US20040259150A1 (en) | 2002-04-09 | 2004-12-23 | Kyowa Hakko Kogyo Co., Ltd. | Method of enhancing of binding activity of antibody composition to Fcgamma receptor IIIa |
| MXPA04009924A (es) | 2002-04-09 | 2005-07-01 | Kyowa Hakko Kogyo Kk | Celulas de genoma modificado. |
| JP4628679B2 (ja) | 2002-04-09 | 2011-02-09 | 協和発酵キリン株式会社 | Ｇｄｐ−フコースの輸送に関与する蛋白質の活性が低下または欠失した細胞 |
| JPWO2003085118A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物の製造方法 |
| 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 |
| AU2004279742A1 (en) | 2003-10-08 | 2005-04-21 | Kyowa Hakko Kirin Co., Ltd. | Fused protein composition |
| AU2004280065A1 (en) | 2003-10-09 | 2005-04-21 | Kyowa Hakko Kirin Co., Ltd. | Process for producing antibody composition by using RNA inhibiting the function of alpha1,6-fucosyltransferase |
| TR201809892T4 (tr) | 2003-11-05 | 2018-07-23 | Roche Glycart Ag | Fc reseptörüne bağlanma afinitesi ve artırılmış efektör fonksiyonu bulunan antijen bağlayan moleküller. |
| WO2005053742A1 (ja) | 2003-12-04 | 2005-06-16 | Kyowa Hakko Kogyo Co., Ltd. | 抗体組成物を含有する医薬 |
| AU2005207003C1 (en) | 2004-01-20 | 2013-06-13 | Humanigen, Inc. | Antibody specificity transfer using minimal essential binding determinants |
| US7745421B2 (en) | 2004-05-25 | 2010-06-29 | The Johns Hopkins University | Methods and compositions for treating diseases and disorders associated with Siglec-8 expressing cells |
| AU2005306502B2 (en) | 2004-11-16 | 2012-11-15 | Humanigen, Inc. | Immunoglobulin variable region cassette exchange |
| WO2007056525A2 (en) | 2005-11-10 | 2007-05-18 | James Paulson | High affinity siglec ligands |
| WO2007056870A1 (en) | 2005-11-21 | 2007-05-24 | The Governors Of The University Of Alberta | Methods and compositions for pharmacologically controlled targeted immunotherapy |
| US20080226635A1 (en) | 2006-12-22 | 2008-09-18 | Hans Koll | Antibodies against insulin-like growth factor I receptor and uses thereof |
| CA2723197C (en) | 2008-05-02 | 2017-09-19 | Seattle Genetics, Inc. | Methods and compositions for making antibodies and antibody derivatives with reduced core fucosylation |
| BR112012004387A2 (pt) * | 2009-08-28 | 2015-09-08 | Vlst Corp | anticorpos anticinas que se l igam a múltiplas quimiocinas cc. |
| SG178925A1 (en) | 2009-09-22 | 2012-04-27 | Volker Sandig | Process for producing molecules containing specialized glycan structures |
| US8586044B2 (en) | 2010-05-28 | 2013-11-19 | Northwestern University | Treatment of chronic pelvic pain syndrome |
| EP2465873A1 (en) | 2010-12-16 | 2012-06-20 | Deutsches Rheuma-Forschungszentrum Berlin | Eosinophils as a therapeutic target |
| EP2683821B1 (en) * | 2011-03-06 | 2018-07-25 | Merck Serono SA | Low fucose cell lines and uses thereof |
| CN104220603B (zh) * | 2012-02-10 | 2017-06-06 | 马里兰大学，巴尔的摩 | 抗体及其Fc片段的化学酶法糖基化工程 |
| WO2015131155A1 (en) * | 2014-02-28 | 2015-09-03 | Allakos Inc. | Methods and compositions for treating siglec-8 associated diseases |
| US10604577B2 (en) * | 2015-10-22 | 2020-03-31 | Allakos Inc. | Methods and compositions for treating systemic mastocytosis |
| EA201992626A1 (ru) * | 2017-05-05 | 2020-04-24 | Аллакос Инк. | Способы и композиции для лечения аллергических заболеваний глаз |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001066126A1 (en) | 2000-03-07 | 2001-09-13 | Smithkline Beecham Corporation | Sialoadhesin factor-2 antibodies |
| US20030092091A1 (en) * | 2000-03-07 | 2003-05-15 | Abrahamson Julie A. | Sialoadhesin factor-2 antibodies |
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