CN118772278A - Flt3的特异性抗体及其用途 - Google Patents
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- 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
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
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Landscapes
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| JP7054924B2 (ja) | 2015-09-23 | 2022-04-15 | サイトイミューン セラピューティクス， インコーポレイテッド | 免疫療法のためのｆｌｔ３指向ｃａｒ細胞 |
| US11623958B2 (en) | 2016-05-20 | 2023-04-11 | Harpoon Therapeutics, Inc. | Single chain variable fragment CD3 binding proteins |
| BR112018073739A2 (pt) | 2016-05-20 | 2019-02-26 | Harpoon Therapeutics, Inc. | proteína de ligação de albumina sérica de domínio único |
| WO2018119279A1 (en) | 2016-12-21 | 2018-06-28 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Human monoclonal antibodies specific for flt3 and uses thereof |
| US11535668B2 (en) | 2017-02-28 | 2022-12-27 | Harpoon Therapeutics, Inc. | Inducible monovalent antigen binding protein |
| CA3063359A1 (en) | 2017-05-12 | 2018-11-15 | Harpoon Therapeutics, Inc. | Mesothelin binding proteins |
| EP3630841A1 (en) | 2017-06-02 | 2020-04-08 | Pfizer Inc. | Antibodies specific for flt3 and their uses |
| MY201327A (en) * | 2017-06-02 | 2024-02-16 | Pfizer | Chimeric antigen receptors targeting flt3 |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| UA129446C2 (uk) | 2017-10-13 | 2025-04-30 | Гарпун Терап'Ютікс, Інк. | Триспецифічні білки і способи їх застосування |
| KR20240067985A (ko) | 2018-02-27 | 2024-05-17 | 화이자 인코포레이티드 | 항체 정제 |
| KR20200128116A (ko) | 2018-02-28 | 2020-11-11 | 화이자 인코포레이티드 | Il-15 변이체 및 이의 용도 |
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| DK3797121T3 (da) | 2018-05-23 | 2024-07-08 | Pfizer | Antistoffer, der er specifikke for CD3, og anvendelser deraf |
| KR20230146098A (ko) | 2018-05-23 | 2023-10-18 | 화이자 인코포레이티드 | GUCY2c에 특이적인 항체 및 이의 용도 |
| US12195544B2 (en) | 2018-09-21 | 2025-01-14 | Harpoon Therapeutics, Inc. | EGFR binding proteins and methods of use |
| EP3856771A4 (en) | 2018-09-25 | 2022-06-29 | Harpoon Therapeutics, Inc. | Dll3 binding proteins and methods of use |
| EP3902836A4 (en) * | 2018-12-18 | 2022-08-31 | Boehringer Ingelheim IO Canada Inc. | FLT3 AGONISTIC ANTIBODIES AND THEIR USES |
| WO2020128893A1 (en) | 2018-12-21 | 2020-06-25 | Pfizer Inc. | Combination treatments of cancer comprising a tlr agonist |
| CA3144617A1 (en) * | 2019-06-26 | 2020-12-30 | Ap Biosciences, Inc. | Antibodies for t-cell activation |
| US11339159B2 (en) | 2019-07-17 | 2022-05-24 | Pfizer Inc. | Toll-like receptor agonists |
| BR112022006817A2 (pt) * | 2019-10-15 | 2022-07-05 | Dragonfly Therapeutics Inc | Anticorpos direcionados a flt3 e uso dos mesmos |
| PE20230160A1 (es) | 2019-12-17 | 2023-02-01 | Pfizer | Anticuerpos especificos para cd47, pd-l1 y sus usos |
| CA3164804A1 (en) | 2019-12-18 | 2021-06-24 | Pfizer Inc. | Once daily cancer treatment regimen with a prmt5 inhibitor |
| WO2021146383A1 (en) * | 2020-01-17 | 2021-07-22 | BioLegend, Inc. | Anti-tlr7 agents and compositions and methods for making and using the same |
| IL295448A (en) | 2020-02-21 | 2022-10-01 | Harpoon Therapeutics Inc | flt3 binding proteins and methods of use |
| CA3174908A1 (en) | 2020-03-09 | 2021-09-16 | Pfizer Inc. | Fusion proteins and uses thereof |
| KR20220167331A (ko) | 2020-04-14 | 2022-12-20 | 르 라보레또레 쎄르비에르 | 항-flt3 항체 및 조성물 |
| WO2021212069A1 (en) | 2020-04-17 | 2021-10-21 | City Of Hope | Flt3-targeted chimeric antigen receptor modified cells for treatment of flt3-positive malignancies |
| MX2022014180A (es) | 2020-05-13 | 2022-12-02 | Pfizer | Metodos, terapias y usos para tratar cancer. |
| CN111808821B (zh) * | 2020-06-24 | 2022-06-14 | 南方医科大学珠江医院 | Flt3-nkg2d双靶点car-t的构建与制备 |
| JP2023533793A (ja) * | 2020-07-17 | 2023-08-04 | ファイザー・インク | 治療用抗体およびそれらの使用 |
| JP2023540795A (ja) | 2020-09-14 | 2023-09-26 | ファイザー・インク | がんを処置するための方法、治療、および使用 |
| CN116419688A (zh) * | 2020-11-24 | 2023-07-11 | 菲利普莫里斯生产公司 | 具有囊部分的气溶胶生成制品 |
| WO2022153161A1 (en) | 2021-01-14 | 2022-07-21 | Pfizer Inc. | Treatment of cancer using a prmt5 inhibitor |
| CN113621068B (zh) * | 2021-10-11 | 2022-01-07 | 上海恒润达生生物科技股份有限公司 | 一种特异性结合cd276的抗体或其抗原结合片段及其制备方法和应用 |
| CN114316060B (zh) * | 2021-12-15 | 2023-06-13 | 北京市肿瘤防治研究所 | 抗人cd19与cd206双特异性抗体及其制备方法和应用 |
| CN113980907B (zh) * | 2021-12-24 | 2022-03-15 | 山东兴瑞生物科技有限公司 | 一种抗flt3嵌合抗原受体修饰的t细胞及其在制备治疗aml药物中的应用 |
| US11945785B2 (en) | 2021-12-30 | 2024-04-02 | Biomea Fusion, Inc. | Pyrazine compounds as inhibitors of FLT3 |
| WO2023165514A1 (zh) * | 2022-03-01 | 2023-09-07 | 江苏恒瑞医药股份有限公司 | 特异性结合flt3和cd3的抗原结合分子及其医药用途 |
| WO2023218320A1 (en) | 2022-05-11 | 2023-11-16 | Pfizer Inc. | Anti-lymphotoxin beta receptor antibodies and methods of use thereof |
| JP2025520411A (ja) | 2022-06-17 | 2025-07-03 | ファイザー・インク | Ｉｌ－１２バリアント、抗ｐｄ１抗体、融合タンパク質、およびその使用 |
| WO2024003773A1 (en) | 2022-07-01 | 2024-01-04 | Pfizer Inc. | 2,7-naphthyridine compounds as mastl inhibitors |
| CA3261000A1 (en) | 2022-07-05 | 2024-01-11 | Pfizer | PYRIDO[4,3-D]PYRIMIDINES COMPOUNDS |
| WO2024030888A2 (en) * | 2022-08-01 | 2024-02-08 | Yale University | Tnfr2 antibodies and methods of using the same |
| WO2024074977A1 (en) | 2022-10-04 | 2024-04-11 | Pfizer Inc. | Substituted 1 h-pyrazolo-pyridine and-pyrimidine compounds |
| CN120379671A (zh) | 2022-10-18 | 2025-07-25 | 辉瑞公司 | 用于治疗癌症的化合物 |
| WO2024102693A2 (en) | 2022-11-07 | 2024-05-16 | Xencor, Inc. | Il-18-fc fusion proteins |
| WO2024105563A1 (en) | 2022-11-16 | 2024-05-23 | Pfizer Inc. | Substituted bicyclic pyridone derivatives |
| WO2024108163A2 (en) * | 2022-11-18 | 2024-05-23 | University Of Pittsburgh - Of The Commonwealth System Of Higher Education | Molecules that bind to cd135 polypeptides |
| US20250141023A1 (en) | 2022-12-02 | 2025-05-01 | Lg Energy Solution, Ltd. | Battery Pack |
| AU2024253142A1 (en) | 2023-04-05 | 2025-10-16 | Pfizer Inc. | Pyrido[4,3-d]pyrimidine compounds |
| WO2024213979A1 (en) | 2023-04-10 | 2024-10-17 | Pfizer Inc. | Pyrido[4,3-d]pyrimidine compounds |
| WO2024218686A1 (en) | 2023-04-20 | 2024-10-24 | Pfizer Inc. | Pyrido[4,3-d]pyrimidine compounds |
| WO2025032521A1 (en) | 2023-08-10 | 2025-02-13 | Pfizer Inc. | Methods, therapies and uses for treating cancer |
| WO2025094035A1 (en) | 2023-11-01 | 2025-05-08 | Pfizer Inc. | Toll-like receptor agonists and conjugates thereof |
| CN120040594B (zh) * | 2025-02-21 | 2025-09-23 | 四川大学 | 一种靶向flt3基因编辑通用型car-t细胞的制备方法和应用 |
Family Cites Families (130)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2413974A1 (fr) | 1978-01-06 | 1979-08-03 | David Bernard | Sechoir pour feuilles imprimees par serigraphie |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US4754065A (en) | 1984-12-18 | 1988-06-28 | Cetus Corporation | Precursor to nucleic acid probe |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| 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 |
| US4777127A (en) | 1985-09-30 | 1988-10-11 | Labsystems Oy | Human retrovirus-related products and methods of diagnosing and treating conditions associated with said retrovirus |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US4800159A (en) | 1986-02-07 | 1989-01-24 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences |
| 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 |
| GB8702816D0 (en) | 1987-02-07 | 1987-03-11 | Al Sumidaie A M K | Obtaining retrovirus-containing fraction |
| US5219740A (en) | 1987-02-13 | 1993-06-15 | Fred Hutchinson Cancer Research Center | Retroviral gene transfer into diploid fibroblasts for gene therapy |
| US5422120A (en) | 1988-05-30 | 1995-06-06 | Depotech Corporation | Heterovesicular liposomes |
| AP129A (en) | 1988-06-03 | 1991-04-17 | Smithkline Biologicals S A | Expression of retrovirus gag protein eukaryotic cells |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5047335A (en) | 1988-12-21 | 1991-09-10 | The Regents Of The University Of Calif. | Process for controlling intracellular glycosylation of proteins |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| EP0454781B1 (en) | 1989-01-23 | 1998-12-16 | Chiron Corporation | Recombinant cells for therapies of infection and hyperproliferative disorders and preparation thereof |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US6673776B1 (en) | 1989-03-21 | 2004-01-06 | Vical Incorporated | Expression of exogenous polynucleotide sequences in a vertebrate, mammal, fish, bird or human |
| DE69034168T3 (de) | 1989-03-21 | 2013-04-11 | Vical, Inc. | Expression von exogenen Polynukleotidsequenzen in Wirbeltieren |
| ATE144793T1 (de) | 1989-06-29 | 1996-11-15 | Medarex Inc | Bispezifische reagenzien für die aids-therapie |
| EP1645635A3 (en) | 1989-08-18 | 2010-07-07 | Oxford Biomedica (UK) Limited | Replication defective recombinant retroviruses expressing a palliative |
| US5585362A (en) | 1989-08-22 | 1996-12-17 | The Regents Of The University Of Michigan | Adenovirus vectors for gene therapy |
| NZ237464A (en) | 1990-03-21 | 1995-02-24 | Depotech Corp | Liposomes with at least two separate chambers encapsulating two separate biologically active substances |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| JPH06500011A (ja) | 1990-06-29 | 1994-01-06 | ラージ スケール バイオロジー コーポレイション | 形質転換された微生物によるメラニンの製造 |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| KR100272077B1 (ko) | 1990-08-29 | 2000-11-15 | 젠팜인터내셔날,인코포레이티드 | 이종 항체를 생산할 수 있는 전이유전자를 가진 인간이외의 동물 |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| US5278299A (en) | 1991-03-18 | 1994-01-11 | Scripps Clinic And Research Foundation | Method and composition for synthesizing sialylated glycosyl compounds |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| GB9115364D0 (en) | 1991-07-16 | 1991-08-28 | Wellcome Found | Antibody |
| DE69233013T2 (de) | 1991-08-20 | 2004-03-04 | The Government Of The United States Of America As Represented By The Secretary Of National Institute Of Health, Office Of Technology Transfer | Adenovirus vermittelter gentransfer in den gastrointestinaltrakt |
| AU669124B2 (en) | 1991-09-18 | 1996-05-30 | Kyowa Hakko Kirin Co., Ltd. | Process for producing humanized chimera antibody |
| JP3540315B2 (ja) | 1991-09-23 | 2004-07-07 | メディカル リサーチ カウンシル | キメラ抗体の製造−組合せアプローチ |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| WO1993010218A1 (en) | 1991-11-14 | 1993-05-27 | The United States Government As Represented By The Secretary Of The Department Of Health And Human Services | Vectors including foreign genes and negative selective markers |
| AU3144193A (en) | 1991-11-21 | 1993-06-15 | Board Of Trustees Of The Leland Stanford Junior University | Controlling degradation of glycoprotein oligosaccharides by extracellular glycosisases |
| GB9125623D0 (en) | 1991-12-02 | 1992-01-29 | Dynal As | Cell modification |
| US5714350A (en) | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
| FR2688514A1 (fr) | 1992-03-16 | 1993-09-17 | Centre Nat Rech Scient | Adenovirus recombinants defectifs exprimant des cytokines et medicaments antitumoraux les contenant. |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| JPH07507689A (ja) | 1992-06-08 | 1995-08-31 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 特定組織のターゲティング方法及び組成物 |
| JPH09507741A (ja) | 1992-06-10 | 1997-08-12 | アメリカ合衆国 | ヒト血清による不活性化に耐性のあるベクター粒子 |
| GB2269175A (en) | 1992-07-31 | 1994-02-02 | Imperial College | Retroviral vectors |
| ATE149570T1 (de) | 1992-08-17 | 1997-03-15 | Genentech Inc | Bispezifische immunoadhesine |
| US6210671B1 (en) | 1992-12-01 | 2001-04-03 | Protein Design Labs, Inc. | Humanized antibodies reactive with L-selectin |
| CA2592997A1 (en) | 1992-12-03 | 1994-06-09 | Genzyme Corporation | Pseudo-adenovirus vectors |
| AU6818094A (en) | 1993-04-22 | 1994-11-08 | Depotech Corporation | Cyclodextrin liposomes encapsulating pharmacologic compounds and methods for their use |
| US6180377B1 (en) | 1993-06-16 | 2001-01-30 | Celltech Therapeutics Limited | Humanized antibodies |
| JP3532566B2 (ja) | 1993-06-24 | 2004-05-31 | エル． グラハム，フランク | 遺伝子治療のためのアデノウイルスベクター |
| EP0694070B1 (en) | 1993-09-15 | 2002-04-10 | Chiron Corporation | Recombinant alphavirus vectors |
| US6015686A (en) | 1993-09-15 | 2000-01-18 | Chiron Viagene, Inc. | Eukaryotic layered vector initiation systems |
| JP3875990B2 (ja) | 1993-10-25 | 2007-01-31 | カンジ，インコーポレイテッド | 組換えアデノウイルスベクターおよび使用方法 |
| NZ276305A (en) | 1993-11-16 | 1997-10-24 | Depotech Corp | Controlled release vesicle compositions |
| US5635388A (en) | 1994-04-04 | 1997-06-03 | Genentech, Inc. | Agonist antibodies against the flk2/flt3 receptor and uses thereof |
| US6436908B1 (en) | 1995-05-30 | 2002-08-20 | Duke University | Use of exogenous β-adrenergic receptor and β-adrenergic receptor kinase gene constructs to enhance myocardial function |
| WO1995030763A2 (en) | 1994-05-09 | 1995-11-16 | Chiron Viagene, Inc. | Retroviral vectors having a reduced recombination rate |
| WO1996017072A2 (en) | 1994-11-30 | 1996-06-06 | Chiron Viagene, Inc. | Recombinant alphavirus vectors |
| US6265150B1 (en) | 1995-06-07 | 2001-07-24 | Becton Dickinson & Company | Phage antibodies |
| AU2998597A (en) | 1996-05-06 | 1997-11-26 | Chiron Corporation | Crossless retroviral vectors |
| AU9692198A (en) | 1997-10-10 | 1999-05-03 | Kevin J. Donahue | Gene delivery compositions and methods |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| AU5301499A (en) | 1998-08-20 | 2000-03-14 | Chugai Seiyaku Kabushiki Kaisha | Method for screening candidate compounds for drug against tumor |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US6849425B1 (en) | 1999-10-14 | 2005-02-01 | Ixsys, Inc. | Methods of optimizing antibody variable region binding affinity |
| GB0205395D0 (en) | 2002-03-07 | 2002-04-24 | Univ Southampton | Materials and methods relating to the treatment of lymphoma |
| CN101014364B (zh) | 2002-12-24 | 2012-01-18 | 里纳特神经系统学公司 | 抗ngf抗体及其使用方法 |
| PL1713806T3 (pl) | 2004-02-14 | 2013-09-30 | Irm Llc | Związki i kompozycje jako inhibitory kinaz białkowych |
| WO2005110392A1 (en) | 2004-05-14 | 2005-11-24 | The University Of Melbourne | Methods of modulating flt3 activity |
| KR20120133403A (ko) * | 2004-06-01 | 2012-12-10 | 도만티스 리미티드 | 증강된 혈청 반감기를 가지는 이특이성 융합 항체 |
| AU2005274852B2 (en) | 2004-07-19 | 2011-12-08 | The Johns Hopkins University | FLT3 inhibitors for immune suppression |
| WO2006017538A2 (en) | 2004-08-03 | 2006-02-16 | Dyax Corp. | Hk1-binding proteins |
| WO2006045120A2 (en) | 2004-10-19 | 2006-04-27 | Teva Pharmaceutical Industries Ltd. | Purification of tegaserod maleate |
| AU2006236508B2 (en) | 2005-04-15 | 2012-02-02 | Precision Biologics, Inc. | Recombinant monoclonal antibodies and corresponding antigens for colon and pancreatic cancers |
| US20060281755A1 (en) | 2005-06-10 | 2006-12-14 | Baumann Christian A | Synergistic modulation of flt3 kinase using aminopyrimidines kinase modulators |
| US20060281771A1 (en) | 2005-06-10 | 2006-12-14 | Baumann Christian A | Synergistic modulation of flt3 kinase using aminoquinoline and aminoquinazoline kinase modulators |
| EA200801118A1 (ru) | 2005-10-18 | 2008-10-30 | Янссен Фармацевтика Н.В. | Способ ингибирования flt3 киназы |
| EA016717B1 (ru) | 2006-06-06 | 2012-07-30 | Круселл Холланд Б.В. | Моноклональное антитело человека, обладающее опсонизирующей фагоцитарной киллерной активностью в отношении enterococcus и staphylococcus aureus, и его применение |
| JP5346820B2 (ja) | 2007-03-13 | 2013-11-20 | エイチユーエムエイビーエス・リミテッド・ライアビリティ・カンパニー | Ｈ５ｎ１亜型ａ型インフルエンザウィルスに対する抗体 |
| AU2009221915A1 (en) | 2008-03-03 | 2009-09-11 | Dyax Corp. | Metalloproteinase 12 binding proteins |
| AR071891A1 (es) * | 2008-05-30 | 2010-07-21 | Imclone Llc | Anticuerpos humanos anti-flt3 (receptor tirosina cinasa 3 tipo fms humano) |
| US8632774B2 (en) | 2008-07-02 | 2014-01-21 | Emergent Product Development Seattle, Llc | Antagonists of IL-6 |
| US20110152173A1 (en) | 2008-07-02 | 2011-06-23 | Emergent Product Development Seattle ,LLC | TNF-a ANTAGONIST MULTI-TARGET BINDING PROTEINS |
| US20110275094A1 (en) | 2008-11-06 | 2011-11-10 | Gunawardane Ruwanthi N | Phosphorylated fms-related tyrosine kinase 3 biomarker assay |
| US9023996B2 (en) | 2009-12-23 | 2015-05-05 | Synimmune Gmbh | Anti-FLT3 antibodies |
| HUE045270T2 (hu) | 2010-01-05 | 2019-12-30 | Inst Nat Sante Rech Med | FLT3 receptor anatgonisták fájdalom rendellenességek kezelésére |
| ES2905545T3 (es) | 2010-01-06 | 2022-04-11 | Takeda Pharmaceuticals Co | Proteínas de unión a calicreína plasmática |
| WO2011113041A2 (en) | 2010-03-12 | 2011-09-15 | The Johns Hopkins University | Neutralization of flt3 ligand as a leukemia therapy |
| WO2013040142A2 (en) | 2011-09-16 | 2013-03-21 | Iogenetics, Llc | Bioinformatic processes for determination of peptide binding |
| EP2569337A1 (en) | 2010-05-14 | 2013-03-20 | Rinat Neuroscience Corp. | Heterodimeric proteins and methods for producing and purifying them |
| EP2575880B1 (en) | 2010-05-27 | 2019-01-16 | Genmab A/S | Monoclonal antibodies against her2 epitope |
| WO2012009568A2 (en) | 2010-07-16 | 2012-01-19 | Adimab, Llc | Antibody libraries |
| NZ604510A (en) | 2010-08-17 | 2013-10-25 | Csl Ltd | Dilutable biocidal compositions and methods of use |
| CA2813411C (en) | 2010-11-05 | 2016-08-02 | Rinat Neuroscience Corporation | Engineered polypeptide conjugates and methods for making thereof using transglutaminase |
| WO2012094115A1 (en) | 2010-12-17 | 2012-07-12 | Arrowhead Research Corporation | Compositions and methods for inhibiting expression of flt3 genes |
| WO2012084895A2 (en) | 2010-12-20 | 2012-06-28 | Universiteit Gent | Crystal structure of flt3 ligand-receptor complex |
| JP2014514314A (ja) | 2011-04-20 | 2014-06-19 | ゲンマブ エー／エス | Ｈｅｒ２およびｃｄ３に対する二重特異性抗体 |
| WO2012166978A2 (en) | 2011-05-31 | 2012-12-06 | The Regents Of The University Of California | Fertilization and fruit size |
| CA2857721C (en) | 2011-12-05 | 2022-05-31 | X-Body, Inc. | Pdgf receptor beta binding polypeptides |
| DK2794658T3 (en) | 2011-12-19 | 2017-06-19 | Synimmune Gmbh | BISPECIFIC ANTIBODY MOLECULE |
| WO2013166453A2 (en) | 2012-05-03 | 2013-11-07 | La Jolla Institute For Allergy And Immunology | T cell epitopes from cockroach and methods of making and using same |
| AU2013265336A1 (en) | 2012-05-22 | 2014-12-04 | Novartis Ag | Meningococcus serogroup X conjugate |
| CN104583230A (zh) | 2012-07-13 | 2015-04-29 | 宾夕法尼亚大学董事会 | 通过共同引入双特异性抗体增强car t细胞的活性 |
| CA2919583C (en) | 2013-07-31 | 2018-09-11 | Rinat Neuroscience Corp. | Engineered polypeptide conjugates |
| EP3131927B8 (en) | 2014-04-14 | 2020-12-23 | Cellectis | Bcma (cd269) specific chimeric antigen receptors for cancer immunotherapy |
| CN104288765A (zh) | 2014-07-03 | 2015-01-21 | 成都中联生科基因科技有限公司 | 一种利用具有中和FLT3生物学活性的McAb应用于肿瘤的靶向治疗的新方法 |
| DE102014116708A1 (de) | 2014-07-23 | 2016-01-28 | Physik Instrumente (Pi) Gmbh & Co. Kg | Aktorvorrichtung |
| CA2956471C (en) | 2014-07-31 | 2024-09-10 | Amgen Res Munich Gmbh | OPTIMIZED CONSTRUCTIONS OF SINGLE-CATENAL, BI-SPECIFIC, AND CROSS-SPECIFIC ANTIBODY |
| EP3029067A1 (en) | 2014-12-01 | 2016-06-08 | Deutsches Krebsforschungszentrum | Use of blocking-reagents for reducing unspecific T cell-activation |
| US9974865B2 (en) * | 2015-03-09 | 2018-05-22 | Agensys, Inc. | Antibody drug conjugates (ADC) that bind to FLT3 proteins |
| MX2017011644A (es) | 2015-03-13 | 2017-12-04 | Cytomx Therapeutics Inc | Anticuerpos anti-pdl1, anticuerpos anti-pdl1 activables y metodos de uso de los mismos. |
| LT3280441T (lt) | 2015-04-07 | 2021-11-25 | Alector Llc | Anti-sortilino antikūnai ir jų naudojimo būdai |
| IL254817B2 (en) | 2015-04-08 | 2023-12-01 | Novartis Ag | Cd20 therapies, cd22 therapies, and combination therapies with a cd19 chimeric antigen receptor (car) - expressing cell |
| WO2016164656A1 (en) | 2015-04-08 | 2016-10-13 | Sorrento Therapeutics, Inc. | Antibody therapeutics that bind cd38 |
| ES3012402T3 (en) | 2015-04-13 | 2025-04-09 | Pfizer | Therapeutic antibodies and their uses |
| JP6921001B2 (ja) | 2015-04-13 | 2021-08-18 | ファイザー・インク | Ｂ細胞成熟抗原を標的にするキメラ抗原受容体 |
| TWI829617B (zh) | 2015-07-31 | 2024-01-21 | 德商安美基研究（慕尼黑）公司 | Ｆｌｔ３及ｃｄ３抗體構築體 |
| TWI717375B (zh) | 2015-07-31 | 2021-02-01 | 德商安美基研究（慕尼黑）公司 | Ｃｄ７０及ｃｄ３抗體構築體 |
| JP7054924B2 (ja) | 2015-09-23 | 2022-04-15 | サイトイミューン セラピューティクス， インコーポレイテッド | 免疫療法のためのｆｌｔ３指向ｃａｒ細胞 |
| US10358497B2 (en) | 2015-09-29 | 2019-07-23 | Amgen Inc. | Methods of treating cardiovascular disease with an ASGR inhibitor |
| MY201327A (en) | 2017-06-02 | 2024-02-16 | Pfizer | Chimeric antigen receptors targeting flt3 |
| EP3630841A1 (en) | 2017-06-02 | 2020-04-08 | Pfizer Inc. | Antibodies specific for flt3 and their uses |
-
2018
- 2018-05-31 EP EP18734624.2A patent/EP3630841A1/en active Pending
- 2018-05-31 CN CN202410785323.XA patent/CN118772278A/zh active Pending
- 2018-05-31 KR KR1020197038745A patent/KR102356984B1/ko active Active
- 2018-05-31 CA CA3006798A patent/CA3006798A1/en active Pending
- 2018-05-31 PE PE2019002483A patent/PE20191846A1/es unknown
- 2018-05-31 PE PE2024001738A patent/PE20242042A1/es unknown
- 2018-05-31 TW TW111105166A patent/TWI790120B/zh active
- 2018-05-31 MX MX2019014465A patent/MX2019014465A/es unknown
- 2018-05-31 AU AU2018275359A patent/AU2018275359C1/en not_active Ceased
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