CN105658666A - 抗garp蛋白及其用途 - Google Patents
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- CN105658666A CN105658666A CN201480043607.6A CN201480043607A CN105658666A CN 105658666 A CN105658666 A CN 105658666A CN 201480043607 A CN201480043607 A CN 201480043607A CN 105658666 A CN105658666 A CN 105658666A
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Abstract
Description
Claims (19)
Priority Applications (1)
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CN202110765205.9A CN113583128A (zh) | 2013-08-01 | 2014-08-01 | 抗garp蛋白及其用途 |
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Cited By (2)
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WO2022152285A1 (zh) * | 2021-01-18 | 2022-07-21 | 上海济煜医药科技有限公司 | Garp蛋白抗体及其应用 |
Families Citing this family (46)
Publication number | Priority date | Publication date | Assignee | Title |
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Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1333274A (zh) * | 2000-07-07 | 2002-01-30 | 上海博德基因开发有限公司 | 一种新的多肽——人garp蛋白12.98和编码这种多肽的多核苷酸 |
Family Cites Families (23)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
US5892019A (en) | 1987-07-15 | 1999-04-06 | The United States Of America, As Represented By The Department Of Health And Human Services | Production of a single-gene-encoded immunoglobulin |
DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
DK1136556T3 (da) | 1991-11-25 | 2005-10-03 | Enzon Inc | Fremgangsmåde til fremstilling af multivalente antigen-bindende proteiner |
NZ298145A (en) * | 1994-12-29 | 1998-08-26 | Yamanouchi Pharma Co Ltd | Monoclonal antibodies having inhibitory effect on type ii phospholipase a2, proteins forming part thereof, cells producing them, dna encoding them, recombinant vector comprising the dna and medicament |
US7709610B2 (en) * | 2003-05-08 | 2010-05-04 | Facet Biotech Corporation | Therapeutic use of anti-CS1 antibodies |
US20070048785A1 (en) * | 2004-06-09 | 2007-03-01 | Lin Laura L | Anti-IL-13 antibodies and complexes |
US8815526B2 (en) | 2005-03-31 | 2014-08-26 | Case Western Reserve University | Methods and reagents for identifying/isolating T regulatory (Treg) cells and for treating individuals |
WO2007113301A1 (en) | 2006-04-03 | 2007-10-11 | Medizinische Hochschule Hannover | Pharmaceuticals for influencing the reaction of the human immune system |
US20100291677A1 (en) * | 2007-08-24 | 2010-11-18 | Keio University | Reducer of immunosuppression by tumor cell and antitumor agent using the same |
JP5581490B2 (ja) * | 2007-10-25 | 2014-09-03 | ザ スクリプス リサーチ インスティテュート | 抗体媒介による細菌のクオラムセンシングの破壊 |
WO2009073163A1 (en) * | 2007-12-03 | 2009-06-11 | American Type Culture Collection (Atcc) | Avian influenza antibodies, compositions, and methods thereof |
WO2009095478A1 (en) * | 2008-01-31 | 2009-08-06 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Antibodies against human cd39 and use thereof for inhibiting t regulatory cells activity |
GB2461546B (en) * | 2008-07-02 | 2010-07-07 | Argen X Bv | Antigen binding polypeptides |
WO2010022341A1 (en) | 2008-08-21 | 2010-02-25 | The United State Of America, As Represented By The Secretary, Department Of Health And Human Services | Methods of enriching and using regulatory t cells |
US20150203840A1 (en) | 2012-08-31 | 2015-07-23 | Argen-X N.V. | Method for producing antibody molecules having inter-species, intra-target cross-reactivity |
RS61778B1 (sr) | 2013-05-06 | 2021-06-30 | Scholar Rock Inc | Kompozicije i postupci za modulaciju faktora rasta |
EP2832747A1 (en) | 2013-08-01 | 2015-02-04 | Université Catholique de Louvain | Anti-GARP protein and uses thereof |
EP3027650B1 (en) * | 2013-08-01 | 2021-01-13 | Université catholique de Louvain | Antibody binding a complex of human glycoprotein a repetitions predominant (garp) and latent tgf-beta-1 |
EP3253796A1 (en) | 2015-02-03 | 2017-12-13 | Université Catholique de Louvain | Anti-garp protein and uses thereof |
TWI836305B (zh) | 2015-09-24 | 2024-03-21 | 日商第一三共股份有限公司 | 抗garp抗體及其製造方法及用途 |
WO2018013939A1 (en) | 2016-07-14 | 2018-01-18 | Scholar Rock, Inc. | Tgfb antibodies, methods, and uses |
-
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Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1333274A (zh) * | 2000-07-07 | 2002-01-30 | 上海博德基因开发有限公司 | 一种新的多肽——人garp蛋白12.98和编码这种多肽的多核苷酸 |
Non-Patent Citations (6)
Title |
---|
A. X. ZHOU等: "GARP-TGF- Complexes Negatively Regulate Regulatory T Cell Development and Maintenance of Peripheral CD4+ T Cells In Vivo", 《J. IMMUNOL.》 * |
D. Q. TRAN等: "GARP (LRRC32) is essential for the surface expression of latent TGF- on platelets and activated FOXP3+ regulatory T cells", 《PROC. NATL. ACAD. SCI.》 * |
J. P. EDWARDS等: "Regulation of the Expression of GARP/Latent TGF- 1 Complexes on Mouse T Cells and Their Role in Regulatory T Cell and Th17 Differentiation", 《J. IMMUNOL》 * |
JULIE STOCKIS等: "Membrane protein GARP is a receptor for latent TGF-β on the surface of activated human Treg", 《EUROPEAN JOURANAL OF IMMUNOLOGY》 * |
ROSEMARY J等: "Targeting the TGFβ signaling pathway in disease", 《NATURE REVIEW DRUG DISCOVERY》 * |
RUI WANG等: "GARP regulates the bioavailability and activation of TGF-β", 《MOLECULAR BIOLOGY OF THE CELL》 * |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN111971053A (zh) * | 2018-02-12 | 2020-11-20 | 综合医院公司 | 靶向肿瘤微环境的嵌合抗原受体 |
WO2022152285A1 (zh) * | 2021-01-18 | 2022-07-21 | 上海济煜医药科技有限公司 | Garp蛋白抗体及其应用 |
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