UA81114C2 - Novel antibodies to tissue factor as anticoagulants - Google Patents
Novel antibodies to tissue factor as anticoagulants Download PDFInfo
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- UA81114C2 UA81114C2 UA20041109787A UA20041109787A UA81114C2 UA 81114 C2 UA81114 C2 UA 81114C2 UA 20041109787 A UA20041109787 A UA 20041109787A UA 20041109787 A UA20041109787 A UA 20041109787A UA 81114 C2 UA81114 C2 UA 81114C2
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/485—Epidermal growth factor [EGF], i.e. urogastrone
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/7455—Thrombomodulin
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
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- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/32—Immunoglobulins specific features characterized by aspects of specificity or valency specific for a neo-epitope on a complex, e.g. antibody-antigen or ligand-receptor
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
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- Transplantation (AREA)
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- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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US37656602P | 2002-05-01 | 2002-05-01 | |
PCT/US2003/013521 WO2003093422A2 (en) | 2002-05-01 | 2003-04-30 | Novel tissue factor targeted antibodies as anticoagulants |
Publications (1)
Publication Number | Publication Date |
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UA81114C2 true UA81114C2 (en) | 2007-12-10 |
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Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
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UA20041109787A UA81114C2 (en) | 2002-05-01 | 2003-04-30 | Novel antibodies to tissue factor as anticoagulants |
UA20041109788A UA85996C2 (ru) | 2002-05-01 | 2003-04-30 | Слитый антикоагулянтный белок тромбомодулина, который обеспечивает направленное перенесение к тканевому фактору |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
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UA20041109788A UA85996C2 (ru) | 2002-05-01 | 2003-04-30 | Слитый антикоагулянтный белок тромбомодулина, который обеспечивает направленное перенесение к тканевому фактору |
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US (3) | US7250168B2 (ko) |
EP (2) | EP1503785B1 (ko) |
JP (2) | JP4567437B2 (ko) |
KR (2) | KR101080587B1 (ko) |
CN (2) | CN100563709C (ko) |
AR (1) | AR039515A1 (ko) |
AT (2) | ATE484524T1 (ko) |
AU (2) | AU2003225255B2 (ko) |
BR (2) | BR0304659A (ko) |
CA (2) | CA2483909A1 (ko) |
CR (1) | CR7584A (ko) |
DE (2) | DE60334538D1 (ko) |
DK (2) | DK1549341T3 (ko) |
EC (2) | ECSP045468A (ko) |
ES (2) | ES2354419T3 (ko) |
HK (1) | HK1080372A1 (ko) |
IL (3) | IL164733A0 (ko) |
MX (2) | MXPA04010795A (ko) |
NO (2) | NO20035848L (ko) |
NZ (2) | NZ536243A (ko) |
PE (1) | PE20040597A1 (ko) |
PL (2) | PL373945A1 (ko) |
PT (2) | PT1503785E (ko) |
RS (2) | RS102404A (ko) |
RU (2) | RU2320366C2 (ko) |
TW (1) | TWI343388B (ko) |
UA (2) | UA81114C2 (ko) |
WO (2) | WO2003093422A2 (ko) |
ZA (2) | ZA200409692B (ko) |
Families Citing this family (39)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DK1188830T3 (da) | 1999-06-02 | 2010-04-26 | Chugai Pharmaceutical Co Ltd | Nyt hæmopoietinreceptorprotein NR10 |
WO2001023556A1 (fr) | 1999-09-27 | 2001-04-05 | Chugai Seiyaku Kabushiki Kaisha | Nouvelle proteine receptrice d'hemopoietine (nr12) |
US7312325B2 (en) | 2000-09-26 | 2007-12-25 | Duke University | RNA aptamers and methods for identifying the same |
US7579000B2 (en) | 2002-05-01 | 2009-08-25 | Bayer Schering Pharma Ag | Tissue factor targeted antibodies as anticoagulants |
AU2003225255B2 (en) * | 2002-05-01 | 2008-07-31 | Bayer Schering Pharma Aktiengesellschaft | Novel tissue factor targeted antibodies as anticoagulants |
EP1539235A2 (en) | 2002-07-01 | 2005-06-15 | Human Genome Sciences, Inc. | Antibodies that specifically bind to reg iv |
US7425328B2 (en) | 2003-04-22 | 2008-09-16 | Purdue Pharma L.P. | Tissue factor antibodies and uses thereof |
US7833978B2 (en) * | 2004-02-20 | 2010-11-16 | Emory University | Thrombomodulin derivatives and conjugates |
JP4718541B2 (ja) | 2004-04-22 | 2011-07-06 | リガド・バイオサイエンシーズ・インコーポレーテツド | 改良された凝固因子調節剤 |
CN103665168A (zh) | 2005-06-03 | 2014-03-26 | 持田制药株式会社 | 抗cd14抗体融合蛋白质 |
US20090130104A1 (en) * | 2005-10-05 | 2009-05-21 | The Trustees Of The University Of Pennsylvania | Fusion proteins for inhibition and dissolution of coagulation |
US20110040073A1 (en) * | 2006-04-07 | 2011-02-17 | Novo Nordisk Healthcare A/G | Covalent Factor VII-Tissue Factor Complex |
CN101500608A (zh) | 2006-06-08 | 2009-08-05 | 中外制药株式会社 | 炎性疾病的预防或治疗药 |
BRPI0720158A2 (pt) * | 2006-10-06 | 2014-05-20 | Asahi Kasei Pharma Corp | Agentes para terapia e/ou melhora de coagulação intravascular disseminada, para reduzir a probabilidade de morte em pacientes sofrendo da mesma, métodos para selecionar pacientes, e, para tratar e/ou melhorar coagulação intravascular disseminada |
US9649499B2 (en) * | 2007-03-28 | 2017-05-16 | Medtronic ATS Medical, Inc. | Method for inhibiting platelet interaction with biomaterial surfaces |
US20100316563A1 (en) * | 2007-09-20 | 2010-12-16 | Bracco Imaging S.P.A. | Method For The Preparation Of New Oligoclonal Antibodies |
CA2708065C (en) | 2007-12-05 | 2015-02-24 | Chugai Seiyaku Kabushiki Kaisha | Therapeutic agent for pruritus |
WO2009086552A1 (en) * | 2008-01-02 | 2009-07-09 | The Trustees Of The University Of Pennsylvania | Targeting recombinant therapeutics to circulating red blood cells |
UA112050C2 (uk) * | 2008-08-04 | 2016-07-25 | БАЄР ХЕЛСКЕР ЛЛСі | Терапевтична композиція, що містить моноклональне антитіло проти інгібітора шляху тканинного фактора (tfpi) |
JP5529869B2 (ja) * | 2008-08-14 | 2014-06-25 | メルク・シャープ・アンド・ドーム・コーポレーション | プロテインaアフィニティークロマトグラフィーを用いる抗体の精製方法 |
US20110262466A1 (en) * | 2008-10-16 | 2011-10-27 | The Trustees Of The University Of Pennsylvania | Compositions containing thrombomodulin domains and uses thereof |
US20120165244A1 (en) * | 2008-10-30 | 2012-06-28 | Hua-Lin Wu | Methods for binding lewis y antigen |
UA109633C2 (uk) | 2008-12-09 | 2015-09-25 | Антитіло людини проти тканинного фактора | |
EP2230251A1 (en) * | 2009-03-19 | 2010-09-22 | Bracco Imaging S.p.A | Antibodies specifically active in the coronary plaque and method for their identification |
CA2771328A1 (en) * | 2009-08-28 | 2011-03-03 | Bayer Healthcare Llc | Cofactors for thrombin activation of factor vii and uses thereof |
GB201007356D0 (en) | 2010-04-30 | 2010-06-16 | Leverton Licence Holdings Ltd | Conjugated factor VIIa |
KR101331101B1 (ko) | 2010-06-04 | 2013-11-19 | 에스케이케미칼주식회사 | 인자 vii 활성을 갖는 융합 단백질 |
US9168314B2 (en) | 2010-06-15 | 2015-10-27 | Genmab A/S | Human antibody drug conjugates against tissue factor |
AU2011287360A1 (en) * | 2010-08-05 | 2013-02-21 | Council Of Scientific & Industrial Research | Protein fusion constructs possessing thrombolytic and anticoagulant properties |
RU2445365C1 (ru) * | 2010-11-03 | 2012-03-20 | Общество с ограниченной ответственностью "Инновационный Центр "Новые Технологии и Материалы" (ООО "ИЦ Новтехмат") | Штамм гибридных культивируемых клеток mus musculus - продуцент моноклональных антител, специфичных к протеину с человека (варианты) |
BR112017022101A2 (pt) | 2015-04-14 | 2018-07-31 | Chugai Seiyaku Kabushiki Kaisha | composição farmacêutica para prevenção e/ou tratamento de dermatite atópica contendo antagonista de il-31 como ingrediente ativo |
WO2016176440A2 (en) * | 2015-04-28 | 2016-11-03 | Saint Louis University | Thrombin-thrombomodulin fusion proteins as protein c activators |
US11085031B2 (en) | 2016-04-28 | 2021-08-10 | Saint Louis University | Thrombin-thrombomodulin fusion proteins as a powerful anticoagulant |
RU2019118427A (ru) * | 2016-11-16 | 2020-12-17 | БАЙЕР ХелсКер ЛЛСи | Нацеленный на эритроциты фактор viii и способ его применения |
BR102017005783A2 (pt) * | 2017-03-21 | 2018-10-02 | Fund Butantan | processo de obtenção de esculptina e seus fragmentos, esculptina recombinante e seus usos |
US20210318338A1 (en) * | 2018-10-04 | 2021-10-14 | Thrombosis And Coagulation Ab | Method for the determination of protein s levels |
BR112022006590A2 (pt) | 2019-11-20 | 2022-06-28 | Chugai Pharmaceutical Co Ltd | Preparação contendo anticorpos |
CN114686443B (zh) * | 2020-12-31 | 2023-11-03 | 广州万孚生物技术股份有限公司 | 杂交瘤细胞、抗血栓调节蛋白单克隆抗体及其制备方法和应用 |
CN114686444B (zh) * | 2020-12-31 | 2024-05-31 | 广州万孚生物技术股份有限公司 | 杂交瘤细胞、抗血栓调节蛋白单克隆抗体及其制备方法和应用 |
Family Cites Families (27)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4208479A (en) * | 1977-07-14 | 1980-06-17 | Syva Company | Label modified immunoassays |
ZA862768B (en) * | 1985-04-17 | 1986-12-30 | Zymogenetics Inc | Expression of factor vii and ix activities in mammalian cells |
US5589173A (en) * | 1986-11-04 | 1996-12-31 | Genentech, Inc. | Method and therapeutic compositions for the treatment of myocardial infarction |
US5223427A (en) * | 1987-03-31 | 1993-06-29 | The Scripps Research Institute | Hybridomas producing monoclonal antibodies reactive with human tissue-factor glycoprotein heavy chain |
US5437864A (en) * | 1987-03-31 | 1995-08-01 | The Scripps Research Institute | Method of inhibiting blood coagulation in extracorporeal circulation by inhibiting human tissue factor |
US4912207A (en) * | 1987-05-06 | 1990-03-27 | Washington University | DNA clone of human thrombomodulin and portions thereof |
DK299087D0 (da) | 1987-06-12 | 1987-06-12 | Novo Industri As | Proteins and derivatives thereof |
US5298599A (en) * | 1988-12-30 | 1994-03-29 | Oklahoma Medical Research Foundation | Expression and purification of recombinant soluble tissue factor |
AU646633B2 (en) * | 1989-02-17 | 1994-03-03 | Codon | Soluble analogs of thrombomodulin |
US6063763A (en) * | 1989-04-28 | 2000-05-16 | Schering Aktiengesellschaft | Protease-resistant thrombomodulin analogs |
US5466668A (en) * | 1989-04-28 | 1995-11-14 | Schering Aktiengesellschaft | Superior thrombomodulin analogs for pharmaceutical use |
US5256770A (en) * | 1990-04-09 | 1993-10-26 | Schering Ag | Oxidation resistant thrombomodulin analogs |
KR930008093B1 (ko) * | 1990-08-03 | 1993-08-25 | 아사히가세이고오교 가부시끼가이샤 | 신규 폴리펩티드 및 이를 유효성분으로 하는 의약조성물 |
US5843442A (en) * | 1990-10-22 | 1998-12-01 | Corvas International, Inc. | Blood coagulation protein antagonists and uses therefor |
US5506134A (en) | 1990-10-22 | 1996-04-09 | Corvas International, Inc. | Hypridoma and monoclonal antibody which inhibits blood coagulation tissue factor/factor VIIa complex |
JPH0578397A (ja) * | 1991-01-29 | 1993-03-30 | Sumitomo Pharmaceut Co Ltd | 血栓溶解タンパク質 |
JPH06133780A (ja) * | 1992-10-23 | 1994-05-17 | Sumitomo Pharmaceut Co Ltd | 新規なt−PA改変体 |
US5916874A (en) * | 1994-04-20 | 1999-06-29 | Asahi Kasei Kogyo Kabushiki Kaisha | Method for treating liver injury |
US5736364A (en) * | 1995-12-04 | 1998-04-07 | Genentech, Inc. | Factor viia inhibitors |
US5986065A (en) * | 1997-03-10 | 1999-11-16 | Sunol Molecular Corporation | Antibodies for inhibiting blood coagulation and methods of use thereof |
CA2325346A1 (en) * | 1998-04-03 | 1999-10-14 | Chugai Seiyaku Kabushiki Kaisha | Humanized antibody against human tissue factor (tf) and process for constructing humanized antibody |
AU2001250814B2 (en) * | 2000-03-16 | 2007-02-15 | Genentech, Inc. | Anti-tissue factor antibodies with enhanced anticoagulant potency |
US6632791B1 (en) | 2000-06-21 | 2003-10-14 | Schering Aktiengesellschaft | Thrombomodulin analogs for pharmaceutical use |
TWI338009B (en) * | 2001-10-29 | 2011-03-01 | Genentech Inc | Antibodies for inhibiting blood coagulation and methods of use thereof |
EP1978108A3 (en) | 2002-01-08 | 2009-01-07 | Siemens Healthcare Diagnostics GmbH | Single nucleotide polymorphisms predicting cardiovascular disease and medication efficacy |
US7579000B2 (en) | 2002-05-01 | 2009-08-25 | Bayer Schering Pharma Ag | Tissue factor targeted antibodies as anticoagulants |
AU2003225255B2 (en) * | 2002-05-01 | 2008-07-31 | Bayer Schering Pharma Aktiengesellschaft | Novel tissue factor targeted antibodies as anticoagulants |
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