CA2735279A1 - Anti-cd5 antibodies - Google Patents
Anti-cd5 antibodies Download PDFInfo
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- CA2735279A1 CA2735279A1 CA2735279A CA2735279A CA2735279A1 CA 2735279 A1 CA2735279 A1 CA 2735279A1 CA 2735279 A CA2735279 A CA 2735279A CA 2735279 A CA2735279 A CA 2735279A CA 2735279 A1 CA2735279 A1 CA 2735279A1
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- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2896—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against molecules with a "CD"-designation, not provided for elsewhere
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- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
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| US61/093,700 | 2008-09-02 | ||
| PCT/DK2009/050218 WO2010022737A1 (en) | 2008-08-29 | 2009-08-28 | Anti-cd5 antibodies |
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| WO2012122514A1 (en) * | 2011-03-09 | 2012-09-13 | Centrose, Llc | Extracellular targeted drug conjugates |
| WO2013023162A2 (en) * | 2011-08-10 | 2013-02-14 | Genus Oncology, Llc | Anti-muc1 antibodies for cancer diagnostics |
| MX350335B (es) | 2011-08-17 | 2017-09-04 | Univ California | Anticuerpos que enlazan alfa-v beta-8 integrina. |
| US12466897B2 (en) | 2011-10-10 | 2025-11-11 | Xencor, Inc. | Heterodimeric human IgG1 polypeptides with isoelectric point modifications |
| CN102786595B (zh) * | 2012-08-03 | 2014-04-23 | 无锡傲锐东源生物科技有限公司 | 抗cd5蛋白单克隆抗体及其用途 |
| US9708404B2 (en) | 2012-12-21 | 2017-07-18 | Seattle Genetics, Inc. | Anti-NTB-A antibodies and related compositions and methods |
| ES2871816T3 (es) * | 2012-12-27 | 2021-11-02 | Sanofi Sa | Anticuerpos anti-LAMP1 y conjugados anticuerpo-fármaco, y usos de los mismos |
| DK2943511T3 (da) | 2013-01-14 | 2019-10-21 | Xencor Inc | Nye heterodimeriske proteiner |
| US10858417B2 (en) | 2013-03-15 | 2020-12-08 | Xencor, Inc. | Heterodimeric proteins |
| WO2015123777A1 (en) * | 2014-02-19 | 2015-08-27 | Cangene Corporation | Methods of modulating an immune response |
| US10259887B2 (en) | 2014-11-26 | 2019-04-16 | Xencor, Inc. | Heterodimeric antibodies that bind CD3 and tumor antigens |
| CN107406512A (zh) | 2014-11-26 | 2017-11-28 | Xencor公司 | 结合cd3和cd38的异二聚体抗体 |
| KR102689285B1 (ko) | 2014-11-26 | 2024-07-31 | 젠코어 인코포레이티드 | Ｃｄ3 및 종양 항원과 결합하는 이종이량체 항체 |
| US20170151281A1 (en) | 2015-02-19 | 2017-06-01 | Batu Biologics, Inc. | Chimeric antigen receptor dendritic cell (car-dc) for treatment of cancer |
| US10786549B2 (en) | 2015-04-23 | 2020-09-29 | Baylor College Of Medicine | CD5 chimeric antigen receptor for adoptive T cell therapy |
| WO2017214285A1 (en) * | 2016-06-07 | 2017-12-14 | Eynav Klechevsky | Detection of cd5 and methods and compositions for modulating cd5 |
| KR20190020341A (ko) | 2016-06-28 | 2019-02-28 | 젠코어 인코포레이티드 | 소마토스타틴 수용체 2에 결합하는 이종이량체 항체 |
| WO2018017864A2 (en) * | 2016-07-20 | 2018-01-25 | Oncomed Pharmaceuticals, Inc. | Pvrig-binding agents and uses thereof |
| MY199683A (en) * | 2016-09-16 | 2023-11-16 | Shanghai Henlius Biotech Inc | Anti-pd-1 antibodies |
| US20180128545A1 (en) | 2016-11-08 | 2018-05-10 | Berry Metal Company | Modular furnace cooling wall |
| AU2018366199A1 (en) | 2017-11-08 | 2020-05-28 | Xencor, Inc. | Bispecific and monospecific antibodies using novel anti-PD-1 sequences |
| BR112020010662A2 (pt) | 2017-11-29 | 2020-11-10 | Magenta Therapeutics, Inc. | composições e métodos para a depleção de células cd5+ |
| AU2019247415A1 (en) | 2018-04-04 | 2020-10-22 | Xencor, Inc. | Heterodimeric antibodies that bind fibroblast activation protein |
| IL316074A (en) * | 2018-04-18 | 2024-12-01 | Biomadison Inc | Compounds for determining vaccine potency |
| WO2020097193A1 (en) | 2018-11-06 | 2020-05-14 | The Regents Of The University Of California | Chimeric antigen receptors for phagocytosis |
| CN121059792A (zh) | 2018-12-19 | 2025-12-05 | 宾夕法尼亚大学董事会 | Cd2/5/7敲除抗-cd2/5/7嵌合抗原受体t细胞针对t细胞淋巴瘤和白血病的用途 |
| EP3947406A4 (en) | 2019-04-05 | 2022-12-28 | Academia Sinica | SIALIDASE RESISTANT SACCHARIDE, METHOD FOR PRODUCTION AND USE |
| KR20220003572A (ko) | 2019-04-24 | 2022-01-10 | 하이델베르크 파마 리서치 게엠베하 | 아마톡신 항체-약물 결합체 및 이의 용도 |
| US11026973B2 (en) | 2019-04-30 | 2021-06-08 | Myeloid Therapeutics, Inc. | Engineered phagocytic receptor compositions and methods of use thereof |
| GB2628935B (en) | 2019-09-03 | 2025-03-05 | Myeloid Therapeutics Inc | Methods and compositions for genomic integration |
| US10980836B1 (en) | 2019-12-11 | 2021-04-20 | Myeloid Therapeutics, Inc. | Therapeutic cell compositions and methods of manufacturing and use thereof |
| KR20230038416A (ko) | 2020-05-08 | 2023-03-20 | 아카데미아 시니카 | 키메릭 인플루엔자 백신 |
| US11919956B2 (en) | 2020-05-14 | 2024-03-05 | Xencor, Inc. | Heterodimeric antibodies that bind prostate specific membrane antigen (PSMA) and CD3 |
| US20230340089A1 (en) * | 2020-05-14 | 2023-10-26 | City Of Hope | Smc1a antibodies and uses thereof |
| EP3915641A1 (en) * | 2020-05-27 | 2021-12-01 | International-Drug-Development-Biotech | Anti-cd5 antibodies and methods of use thereof |
| US20230340141A1 (en) * | 2020-08-21 | 2023-10-26 | City Of Hope | Anti-cd5 antibody compositions and uses thereof |
| EP4211245A1 (en) | 2020-09-14 | 2023-07-19 | Vor Biopharma Inc. | Compositions and methods for cd5 modification |
| WO2022098905A2 (en) | 2020-11-04 | 2022-05-12 | Myeloid Therapeutics, Inc. | Engineered chimeric fusion protein compositions and methods of use thereof |
| WO2022099090A1 (en) * | 2020-11-06 | 2022-05-12 | Xencor, Inc. | Heterodimeric antibodies that bind tgfbrii |
| CN116801905A (zh) * | 2020-12-17 | 2023-09-22 | 先声再明医药有限公司 | Cd5抗体及其应用 |
| US20240050568A1 (en) * | 2021-01-12 | 2024-02-15 | Nanjing IASO Biotechnology Co., Ltd. | Fully human single-domain tandem chimeric antigen receptor (car) targeting cd5, and use thereof |
| MX2023009100A (es) | 2021-02-03 | 2023-09-25 | Mozart Therapeutics Inc | Agentes aglutinantes y métodos para usar los mismos. |
| WO2022192403A1 (en) | 2021-03-09 | 2022-09-15 | Xencor, Inc. | Heterodimeric antibodies that bind cd3 and cldn6 |
| JP2024509274A (ja) | 2021-03-10 | 2024-02-29 | ゼンコア インコーポレイテッド | Ｃｄ３及びｇｐｃ３に結合するヘテロ二量体抗体 |
| MX2023000578A (es) | 2021-04-12 | 2023-04-26 | Academia Sinica | Vacuna mejorada contra el coronavirus. |
| EP4332118A1 (en) * | 2021-04-29 | 2024-03-06 | Korea Research Institute of Bioscience and Biotechnology | Novel anti-cd5 chimeric antigen receptor and immune cell expressing same |
| AU2022272235A1 (en) | 2021-05-11 | 2023-12-21 | Myeloid Therapeutics, Inc. | Methods and compositions for genomic integration |
| CN113105547B (zh) * | 2021-05-18 | 2022-04-08 | 福州迈新生物技术开发有限公司 | 抗cd5蛋白单克隆抗体及其细胞株、制备方法和应用 |
| TW202334429A (zh) | 2021-10-01 | 2023-09-01 | 中央研究院 | Sars-cov-2棘蛋白特異性抗體及其用途 |
| WO2023076876A1 (en) | 2021-10-26 | 2023-05-04 | Mozart Therapeutics, Inc. | Modulation of immune responses to viral vectors |
| US12077597B2 (en) | 2021-11-24 | 2024-09-03 | International-Drug-Development-Biotech | Anti-CD5 antibodies and methods of use thereof |
| US20230279080A1 (en) * | 2021-12-27 | 2023-09-07 | Academia Sinica | Antibody specific to spike protein of sars-cov-2 and uses thereof |
| WO2024039683A1 (en) * | 2022-08-15 | 2024-02-22 | Myeloid Therapeutics, Inc. | Compositions and methods for conditioning patients for cell therapy |
| WO2024040194A1 (en) | 2022-08-17 | 2024-02-22 | Capstan Therapeutics, Inc. | Conditioning for in vivo immune cell engineering |
| TW202502301A (zh) | 2023-04-08 | 2025-01-16 | 磐石醫藥生技股份有限公司 | 透過聚合物囊泡進行標的遞送之方法及組合物 |
| WO2024249954A1 (en) | 2023-05-31 | 2024-12-05 | Capstan Therapeutics, Inc. | Lipid nanoparticle formulations and compositions |
| WO2024258967A1 (en) * | 2023-06-13 | 2024-12-19 | Synthis Therapeutics, Inc. | Anti-cd5 antibodies and their uses |
| WO2025076127A1 (en) | 2023-10-05 | 2025-04-10 | Capstan Therapeutics, Inc. | Constrained ionizable cationic lipids and lipid nanoparticles |
| WO2025076113A1 (en) | 2023-10-05 | 2025-04-10 | Capstan Therapeutics, Inc. | Ionizable cationic lipids with conserved spacing and lipid nanoparticles |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
| US20250302763A1 (en) | 2024-02-22 | 2025-10-02 | Capstan Therapeutics, Inc. | Immune engineering amplification |
| WO2025217452A1 (en) | 2024-04-11 | 2025-10-16 | Capstan Therapeutics, Inc. | Constrained ionizable cationic lipids and lipid nanoparticles |
| WO2025217454A2 (en) | 2024-04-11 | 2025-10-16 | Capstan Therapeutics, Inc. | Ionizable cationic lipids and lipid nanoparticles |
Family Cites Families (1)
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| DE4312916C2 (de) * | 1993-04-14 | 1995-03-23 | Fresenius Ag | Arzneimittel zur Behandlung von Immunreaktionen |
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- 2009-08-28 KR KR1020117007230A patent/KR20110050541A/ko not_active Withdrawn
- 2009-08-28 BR BRPI0917148A patent/BRPI0917148A2/pt not_active IP Right Cessation
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| ZA201100300B (en) | 2012-01-25 |
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| CN102137873A (zh) | 2011-07-27 |
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| AU2009287164A1 (en) | 2010-03-04 |
| IL209975A0 (en) | 2011-02-28 |
| BRPI0917148A2 (pt) | 2015-12-01 |
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