BRPI0715115A2 - anticorpo monoclonal isolado, molÉcula de Ácido nucleico isolada, vetor de expressço, cÉlula hospedeira, mÉtodos para tratar uma doenÇa, e para produzir um anticorpo monoclonal isolado, uso do anticorpo monoclonal isolado, e, composiÇço farmacÊutica - Google Patents
anticorpo monoclonal isolado, molÉcula de Ácido nucleico isolada, vetor de expressço, cÉlula hospedeira, mÉtodos para tratar uma doenÇa, e para produzir um anticorpo monoclonal isolado, uso do anticorpo monoclonal isolado, e, composiÇço farmacÊutica Download PDFInfo
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Classifications
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C—CHEMISTRY; METALLURGY
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- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
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- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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Landscapes
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| US8062864B2 (en) | 2007-05-21 | 2011-11-22 | Alderbio Holdings Llc | Nucleic acids encoding antibodies to IL-6, and recombinant production of anti-IL-6 antibodies |
| US7906117B2 (en) | 2007-05-21 | 2011-03-15 | Alderbio Holdings Llc | Antagonists of IL-6 to prevent or treat cachexia, weakness, fatigue, and/or fever |
| US8404235B2 (en) | 2007-05-21 | 2013-03-26 | Alderbio Holdings Llc | Antagonists of IL-6 to raise albumin and/or lower CRP |
| US9701747B2 (en) | 2007-05-21 | 2017-07-11 | Alderbio Holdings Llc | Method of improving patient survivability and quality of life by anti-IL-6 antibody administration |
| US20090238825A1 (en) * | 2007-05-21 | 2009-09-24 | Kovacevich Brian R | Novel rabbit antibody humanization methods and humanized rabbit antibodies |
| US8252286B2 (en) | 2007-05-21 | 2012-08-28 | Alderbio Holdings Llc | Antagonists of IL-6 to prevent or treat thrombosis |
| CN105001332B (zh) | 2007-05-21 | 2018-12-04 | 奥尔德生物控股有限责任公司 | 针对il-6的抗体及其用途 |
| US8034344B2 (en) | 2008-05-13 | 2011-10-11 | Novimmune S.A. | Anti-IL-6/IL-6R antibodies and methods of use thereof |
| US8188235B2 (en) * | 2008-06-18 | 2012-05-29 | Pfizer Inc. | Antibodies to IL-6 and their uses |
| JP2012503490A (ja) * | 2008-09-26 | 2012-02-09 | ワイス・エルエルシー | 単鎖抗体ライブラリー設計 |
| WO2010056948A2 (en) * | 2008-11-13 | 2010-05-20 | Femta Pharmaceuticals, Inc. | Humanized anti-il-6 antibodies |
| US9452227B2 (en) | 2008-11-25 | 2016-09-27 | Alderbio Holdings Llc | Methods of treating or diagnosing conditions associated with elevated IL-6 using anti-IL-6 antibodies or fragments |
| KR20110112307A (ko) * | 2008-11-25 | 2011-10-12 | 앨더 바이오파마슈티컬즈, 인코포레이티드 | 알부민을 상승시키고 및／또는 ｃｒｐ를 낮추는 ｉｌ６의 길항제 |
| US8337847B2 (en) | 2008-11-25 | 2012-12-25 | Alderbio Holdings Llc | Methods of treating anemia using anti-IL-6 antibodies |
| US8323649B2 (en) | 2008-11-25 | 2012-12-04 | Alderbio Holdings Llc | Antibodies to IL-6 and use thereof |
| US8992920B2 (en) | 2008-11-25 | 2015-03-31 | Alderbio Holdings Llc | Anti-IL-6 antibodies for the treatment of arthritis |
| US9212223B2 (en) | 2008-11-25 | 2015-12-15 | Alderbio Holdings Llc | Antagonists of IL-6 to prevent or treat thrombosis |
| US8420089B2 (en) | 2008-11-25 | 2013-04-16 | Alderbio Holdings Llc | Antagonists of IL-6 to raise albumin and/or lower CRP |
| US8911722B2 (en) | 2009-09-14 | 2014-12-16 | The Regents Of The University Of Colorado, A Body Corporate | Modulation of yeast-based immunotherapy products and responses |
| US9775921B2 (en) | 2009-11-24 | 2017-10-03 | Alderbio Holdings Llc | Subcutaneously administrable composition containing anti-IL-6 antibody |
| US20120294852A1 (en) | 2009-11-24 | 2012-11-22 | Smith Jeffrey T L | Antagonists of il-6 to raise albumin and/or lower crp |
| SMT201900549T1 (it) | 2010-03-12 | 2019-11-13 | Debiopharm Int Sa | Molecole leganti il cd37 e loro immunoconiugati |
| CA2818813C (en) | 2010-11-23 | 2020-10-06 | Alder Biopharmaceuticals, Inc. | Anti-il-6 antibodies for the treatment of oral mucositis |
| WO2012098238A1 (en) | 2011-01-21 | 2012-07-26 | Novimmune S.A. | Combination therapies and methods using anti-cd3 modulating agents and anti-il-6 antagonists |
| EA201391342A1 (ru) * | 2011-04-01 | 2014-11-28 | Иммьюноджен, Инк. | Cd37-связывающие молекулы и их иммуноконъюгаты |
| WO2013175276A1 (en) * | 2012-05-23 | 2013-11-28 | Argen-X B.V | Il-6 binding molecules |
| CA2889181C (en) * | 2012-10-22 | 2021-12-07 | Fountain Biopharma Inc. | Antibodies to interleukin-6 and uses thereof |
| CN104903349B (zh) * | 2012-11-08 | 2018-10-19 | 十一生物治疗股份有限公司 | Il-6拮抗剂及其应用 |
| MX392539B (es) | 2015-06-08 | 2025-03-24 | Debiopharm Int Sa | Combinaciones de inmunoconjugado anti-cd37 y anticuerpo anti-cd20. |
| US20170029499A1 (en) | 2015-07-31 | 2017-02-02 | Astrazeneca Pharmaceuticals Lp | Methods for treating hepcidin-mediated disorders |
| UA129489C2 (uk) | 2015-08-28 | 2025-05-14 | Дебіофарм Інтернаціонал, С.А. | Антитіло до cd37 |
| CN109310755A (zh) * | 2016-02-02 | 2019-02-05 | 卡德门企业有限公司 | Pd-l1和kdr的双特异性结合蛋白 |
| SG11201809786TA (en) * | 2016-05-05 | 2018-12-28 | Univ Pennsylvania | Dna monoclonal antibodies targeting il-6 and cd126 |
| US11278629B2 (en) | 2016-11-02 | 2022-03-22 | Debiopharm International, S.A. | Methods for improving anti-CD37 immunoconjugate therapy |
| TW202444416A (zh) | 2017-02-01 | 2024-11-16 | 耶魯大學 | 心臟衰竭及心腎症候群之精準治療 |
| KR20230047223A (ko) | 2018-01-05 | 2023-04-06 | 노보 노르디스크 에이/에스 | 면역억제 없이 il-6 매개 염증을 치료하기 위한 방법 |
| CN112218662A (zh) | 2018-05-30 | 2021-01-12 | 德彪发姆国际有限公司 | 抗cd37免疫缀合物给药方案 |
| CN109517064B (zh) * | 2018-10-10 | 2020-05-08 | 北京汇智和源生物技术有限公司 | 白介素-6的人源化单克隆抗体、其编码基因及应用 |
| US20200405883A1 (en) | 2019-06-20 | 2020-12-31 | Baxalta Incorporated | Method of treatment with viral-based gene therapy |
| CN112279913B (zh) * | 2020-10-30 | 2022-05-03 | 上海百英生物科技有限公司 | 一种抗人il-6单克隆抗体及应用 |
| EP4252243A2 (en) | 2020-11-30 | 2023-10-04 | Enigma Biointelligence, Inc. | Non-invasive assessment of alzheimer's disease |
| CN113980129B (zh) * | 2021-01-15 | 2023-07-28 | 东大生物技术(苏州)有限公司 | 一组il-11单克隆抗体及其医药用途 |
| CN115925792B (zh) * | 2022-08-19 | 2025-06-27 | 浙江农林大学 | 一种香榧活性肽及其在制备降血压产品中的应用 |
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| 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 |
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| ATE552012T1 (de) | 1994-10-07 | 2012-04-15 | Chugai Pharmaceutical Co Ltd | Hemmung des abnormalen wachstums von synovialzellen durch il-6-antagonisten als wirkstoff |
| EP0800829B2 (en) | 1994-12-29 | 2012-07-25 | Chugai Seiyaku Kabushiki Kaisha | Use of a pm-1 antibody or of a mh 166 antibody for enhancing the anti-tumor effect of cisplatin or carboplatin |
| GB9702944D0 (en) | 1997-02-13 | 1997-04-02 | Univ Manchester | Reducing fibrosis |
| KR100838862B1 (ko) | 1997-03-21 | 2008-06-16 | 츄가이 세이야꾸 가부시키가이샤 | 아이엘-6 안타고니스트를 유효성분으로 함유하는 감작 티 세포 관여 질환의 예방 또는 치료제 |
| CA2324115C (en) | 1998-03-17 | 2008-12-23 | Chugai Seiyaku Kabushiki Kaisha | A preventive or therapeutic agent for inflammatory bowel disease comprising il-6 antagonist as an active ingredient |
| US7494652B1 (en) | 1998-06-10 | 2009-02-24 | Promega Corporation | Treatment of sepsis |
| DK1108435T3 (da) | 1998-08-24 | 2007-02-05 | Chugai Pharmaceutical Co Ltd | Forebyggende midler eller midler mod pancreatitis indeholdende anti-IL-6-receptor-antistoffer som den aktive bestanddel |
| US7083950B2 (en) | 1998-09-25 | 2006-08-01 | Regeneron Pharmaceuticals, Inc. | High affinity fusion proteins and therapeutic and diagnostic methods for use |
| WO2000044774A2 (en) | 1999-01-27 | 2000-08-03 | The University Of South Florida | Inhibition of stat3 signal transduction for human cancer therapy |
| US6846486B1 (en) | 2000-02-24 | 2005-01-25 | Advanced Biotherapy Concepts, Inc. | Method of treating allergy by administering an anti-histamine antibody |
| DE60141274D1 (de) | 2000-05-03 | 2010-03-25 | Medimmune Inc | Kombinationstherapie zur behandlung respiratorischer krankheiten mittels antikörper und anti-entzündungs wirkstoffe |
| AU1095202A (en) | 2000-10-25 | 2002-05-06 | Chugai Pharmaceutical Co Ltd | Preventives or remedies for psoriasis containing as the active ingredient il-6 antagonist |
| WO2002036165A1 (fr) | 2000-10-27 | 2002-05-10 | Chugai Seiyaku Kabushiki Kaisha | Agent à base d'antagoniste d'il-6, faisant baisser le niveau des mmp-3 dans le sang |
| DE60126130T2 (de) * | 2000-11-17 | 2007-10-18 | The University Of Rochester | In-vitro verfahren zur herstellung und identifizierung von immunglobulin moleküle in eukaryotischen zellen |
| US20050196755A1 (en) | 2000-11-17 | 2005-09-08 | Maurice Zauderer | In vitro methods of producing and identifying immunoglobulin molecules in eukaryotic cells |
| WO2002069904A2 (en) | 2001-03-02 | 2002-09-12 | Medimmune, Inc. | Cd2 antagonists for treatment of autoimmune or inflammatory disease |
| US20020168360A1 (en) | 2001-03-02 | 2002-11-14 | Christine Dingivan | Methods of preventing or treating inflammatory or autoimmune disorders by administering integrin alphanubeta3 antagonists in combination with other prophylactic or therapeutic agents |
| UA80091C2 (en) | 2001-04-02 | 2007-08-27 | Chugai Pharmaceutical Co Ltd | Remedies for infant chronic arthritis-relating diseases and still's disease which contain an interleukin-6 (il-6) antagonist |
| DK1562968T3 (da) * | 2001-11-14 | 2013-10-28 | Janssen Biotech Inc | Anti-il-6-antistoffer, sammensætninger, fremgangsmåder og anvendelser |
| WO2003054016A2 (en) | 2001-12-21 | 2003-07-03 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw | Method for cloning of variable domain sequences |
| US20060275294A1 (en) | 2002-08-22 | 2006-12-07 | Omoigui Osemwota S | Method of prevention and treatment of aging, age-related disorders and/or age-related manifestations including atherosclerosis, peripheral vascular disease, coronary artery disease, osteoporosis, arthritis, type 2 diabetes, dementia, alzheimers disease and cancer |
| CN1678744B (zh) | 2002-08-30 | 2010-05-26 | 财团法人化学及血清疗法研究所 | 人的抗人白细胞介素-6抗体以及所述抗体的片段 |
| CA2506230A1 (en) | 2002-11-15 | 2004-06-03 | Centocor, Inc. | Anti-angiogenic uses of il-6 antagonists |
| EP1594897A4 (en) | 2003-02-04 | 2006-11-08 | Centocor Inc | USE OF IL-6 ANTAGONISTS IN COMBINATION WITH STEROIDS FOR INCREASED APOPTOSIS |
| EP1444989A1 (en) | 2003-02-07 | 2004-08-11 | Giorgio Dr. Stassi | Sensitizing cells for apoptosis by selectively blocking cytokines |
| JP4555924B2 (ja) | 2003-02-24 | 2010-10-06 | 中外製薬株式会社 | インターロイキン−６アンタゴニストを含有する脊髄損傷治療剤 |
| GB2401040A (en) | 2003-04-28 | 2004-11-03 | Chugai Pharmaceutical Co Ltd | Method for treating interleukin-6 related diseases |
| WO2005023193A2 (en) | 2003-09-04 | 2005-03-17 | Interleukin Genetics, Inc. | Methods of treating endometriosis |
| JP2007526022A (ja) | 2003-10-24 | 2007-09-13 | メドトロニック・インコーポレーテッド | 炎症誘発性媒介物質の産生を減弱することによって神経性障害を処置する技法 |
| US20050100550A1 (en) | 2003-11-10 | 2005-05-12 | Mohit Trikha | Anti-angiogenic uses of IL-6 antagonists |
| JP2008505054A (ja) | 2004-02-11 | 2008-02-21 | ワーナー−ランバート カンパニー リミテッド ライアビリティー カンパニー | Ｉｌ−６アンタゴニストで骨関節炎を治療する方法 |
| JP2008524242A (ja) | 2004-12-16 | 2008-07-10 | ジェネンテック・インコーポレーテッド | 自己免疫障害を治療する方法 |
| WO2006105665A1 (en) | 2005-04-06 | 2006-10-12 | Bioartificial Gel Technologies Inc. | Hydrogel composition for modulation of topical inflammatory response |
| EP1712241A1 (en) | 2005-04-15 | 2006-10-18 | Centre National De La Recherche Scientifique (Cnrs) | Composition for treating cancer adapted for intra-tumoral administration and uses thereof |
| PA8672101A1 (es) | 2005-04-29 | 2006-12-07 | Centocor Inc | Anticuerpos anti-il-6, composiciones, métodos y usos |
| EP1888629B1 (en) | 2005-05-10 | 2013-04-24 | Neoloch Aps | Neuritogenic peptides |
-
2007
- 2007-08-03 AU AU2007282023A patent/AU2007282023B2/en not_active Ceased
- 2007-08-03 US US11/882,751 patent/US7919095B2/en not_active Expired - Fee Related
- 2007-08-03 EP EP07811042.6A patent/EP2064241B1/en active Active
- 2007-08-03 JP JP2009522880A patent/JP2009545319A/ja active Pending
- 2007-08-03 CA CA2657763A patent/CA2657763C/en not_active Expired - Fee Related
- 2007-08-03 KR KR20097003512A patent/KR101479537B1/ko not_active Expired - Fee Related
- 2007-08-03 CN CN2007800289537A patent/CN101563365B/zh not_active Expired - Fee Related
- 2007-08-03 EA EA200900037A patent/EA200900037A1/ru unknown
- 2007-08-03 WO PCT/US2007/017337 patent/WO2008019061A2/en not_active Ceased
- 2007-08-03 BR BRPI0715115-2A patent/BRPI0715115A2/pt not_active Application Discontinuation
- 2007-08-03 MX MX2009001110A patent/MX2009001110A/es not_active Application Discontinuation
-
2009
- 2009-01-15 CR CR10563A patent/CR10563A/es unknown
- 2009-01-15 NO NO20090224A patent/NO20090224L/no not_active Application Discontinuation
- 2009-01-15 IL IL196550A patent/IL196550A0/en unknown
- 2009-01-22 ZA ZA200900514A patent/ZA200900514B/xx unknown
- 2009-01-28 CO CO09007783A patent/CO6150192A2/es unknown
- 2009-02-17 MA MA31649A patent/MA30653B1/fr unknown
Also Published As
| Publication number | Publication date |
|---|---|
| WO2008019061A3 (en) | 2008-10-09 |
| KR20090039801A (ko) | 2009-04-22 |
| CA2657763A1 (en) | 2008-02-14 |
| KR101479537B1 (ko) | 2015-01-07 |
| CN101563365B (zh) | 2012-10-31 |
| US20080075726A1 (en) | 2008-03-27 |
| EA200900037A1 (ru) | 2009-10-30 |
| WO2008019061A2 (en) | 2008-02-14 |
| MA30653B1 (fr) | 2009-08-03 |
| CR10563A (es) | 2009-04-14 |
| IL196550A0 (en) | 2011-08-01 |
| MX2009001110A (es) | 2009-05-11 |
| CN101563365A (zh) | 2009-10-21 |
| JP2009545319A (ja) | 2009-12-24 |
| NO20090224L (no) | 2009-03-31 |
| AU2007282023A1 (en) | 2008-02-14 |
| CA2657763C (en) | 2016-05-31 |
| EP2064241A2 (en) | 2009-06-03 |
| ZA200900514B (en) | 2010-04-28 |
| EP2064241B1 (en) | 2015-10-07 |
| CO6150192A2 (es) | 2010-04-20 |
| AU2007282023B2 (en) | 2012-09-13 |
| US7919095B2 (en) | 2011-04-05 |
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