TW212184B - - Google Patents
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- TW212184B TW212184B TW080102180A TW80102180A TW212184B TW 212184 B TW212184 B TW 212184B TW 080102180 A TW080102180 A TW 080102180A TW 80102180 A TW80102180 A TW 80102180A TW 212184 B TW212184 B TW 212184B
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- Prior art keywords
- antibody
- moab
- fusion
- bispecific
- hybrid
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Landscapes
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| JP8898590 | 1990-04-02 | ||
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| HU (1) | HUT63203A (OSRAM) |
| IE (1) | IE76288B1 (OSRAM) |
| TW (1) | TW212184B (OSRAM) |
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| US6001355A (en) * | 1982-12-14 | 1999-12-14 | Dowdle; Eugene Bernard Davey | Pro-tPA for the treatment of thrombosis, embolism and related conditions |
| US6017512A (en) * | 1992-06-23 | 2000-01-25 | Diatide, Inc. | Radiolabeled peptides |
| US5620675A (en) | 1992-06-23 | 1997-04-15 | Diatech, Inc. | Radioactive peptides |
| DK0771216T3 (da) * | 1994-07-11 | 2001-02-05 | Scripps Research Inst | Fremgangsmåder og præparater til specifik koagulering af tumorvaskulatur |
| US5869274A (en) * | 1995-08-09 | 1999-02-09 | Zymed Laboratories, Inc. | Immuno-histochemical method that reduces background staining |
| US6537520B1 (en) | 1998-03-31 | 2003-03-25 | Bristol-Myers Squibb Pharma Company | Pharmaceuticals for the imaging of angiogenic disorders |
| US6524553B2 (en) | 1998-03-31 | 2003-02-25 | Bristol-Myers Squibb Pharma Company | Quinolone vitronectin receptor antagonist pharmaceuticals |
| US6548663B1 (en) | 1998-03-31 | 2003-04-15 | Bristol-Myers Squibb Pharma Company | Benzodiazepine vitronectin receptor antagonist pharmaceuticals |
| US6312689B1 (en) | 1998-07-23 | 2001-11-06 | Millennium Pharmaceuticals, Inc. | Anti-CCR2 antibodies and methods of use therefor |
| US6794518B1 (en) | 1998-12-18 | 2004-09-21 | Bristol-Myers Squibb Pharma Company | Vitronectin receptor antagonist pharmaceuticals |
| US6511649B1 (en) | 1998-12-18 | 2003-01-28 | Thomas D. Harris | Vitronectin receptor antagonist pharmaceuticals |
| WO2000035887A2 (en) | 1998-12-18 | 2000-06-22 | Du Pont Pharm Co | Vitronectin receptor antagonist pharmaceuticals |
| US6569402B1 (en) | 1998-12-18 | 2003-05-27 | Bristol-Myers Squibb Pharma Company | Vitronectin receptor antagonist pharmaceuticals |
| BR9917079A (pt) | 1998-12-18 | 2001-10-30 | Du Pont Pharm Co | Compostos antagonistas de receptor devitronectina, kit, composição metalofarmacêuticade diagnóstico ou terapêutica, composição deagente de contraste para ultra-som, composiçãoradiofarmacêutica terapêutica, composiçãofarmacêutica de diagnóstico, método detratamento da artrite reumatóide, do cancêr e darestenose em um paciente, método de formação deimagem da angiogênese terapêutica, do câncer, denovos vasos sanguìneos, da arteriosclerose, darestenose, da isquemia e da lesão por reperfusãodo miocárdio em um paciente |
| US7660415B2 (en) * | 2000-08-03 | 2010-02-09 | Selinfreund Richard H | Method and apparatus for controlling access to storage media |
| UA81743C2 (uk) | 2000-08-07 | 2008-02-11 | Центокор, Инк. | МОНОКЛОНАЛЬНЕ АНТИТІЛО ЛЮДИНИ, ЩО СПЕЦИФІЧНО ЗВ'ЯЗУЄТЬСЯ З ФАКТОРОМ НЕКРОЗУ ПУХЛИН АЛЬФА (ФНПα), ФАРМАЦЕВТИЧНА КОМПОЗИЦІЯ, ЩО ЙОГО МІСТИТЬ, ТА СПОСІБ ЛІКУВАННЯ РЕВМАТОЇДНОГО АРТРИТУ |
| US6902734B2 (en) | 2000-08-07 | 2005-06-07 | Centocor, Inc. | Anti-IL-12 antibodies and compositions thereof |
| US7288390B2 (en) | 2000-08-07 | 2007-10-30 | Centocor, Inc. | Anti-dual integrin antibodies, compositions, methods and uses |
| AU2002346369B2 (en) | 2001-11-14 | 2009-08-27 | Recordati Uk Ltd | Anti-IL-6 antibodies, compositions, methods and uses |
| US9708410B2 (en) | 2003-05-30 | 2017-07-18 | Janssen Biotech, Inc. | Anti-tissue factor antibodies and compositions |
| AU2003271174A1 (en) * | 2003-10-10 | 2005-04-27 | Chugai Seiyaku Kabushiki Kaisha | Double specific antibodies substituting for functional protein |
| US20080075712A1 (en) * | 2003-10-14 | 2008-03-27 | Kunihiro Hattori | Double Specific Antibodies Substituting For Functional Proteins |
| JP2007521248A (ja) | 2003-12-10 | 2007-08-02 | ミレニアム ファーマシューティカルズ， インコーポレイテッド | ヒト化抗ｃｃｒ２抗体および該抗体を使用する方法 |
| US10011858B2 (en) | 2005-03-31 | 2018-07-03 | Chugai Seiyaku Kabushiki Kaisha | Methods for producing polypeptides by regulating polypeptide association |
| DK1876236T3 (da) * | 2005-04-08 | 2014-10-20 | Chugai Pharmaceutical Co Ltd | Antistof som funktionel erstatning for blodkoagulationsfaktor VIII |
| JO3058B1 (ar) | 2005-04-29 | 2017-03-15 | Applied Molecular Evolution Inc | الاجسام المضادة لمضادات -اي ال-6,تركيباتها طرقها واستعمالاتها |
| EP2364998A1 (en) | 2005-06-16 | 2011-09-14 | The Feinstein Institute for Medical Research | Antibodies against HMGB1 and fragments thereof |
| CN101252951B (zh) | 2005-06-30 | 2011-12-21 | 森托科尔公司 | 抗il-23抗体、组合物、方法和用途 |
| HUE049832T2 (hu) | 2005-12-29 | 2020-10-28 | Janssen Biotech Inc | Humán anti-IL-23 ellenanyagok, készítmények, eljárás és alkalmazások |
| EP4218801A3 (en) | 2006-03-31 | 2023-08-23 | Chugai Seiyaku Kabushiki Kaisha | Antibody modification method for purifying bispecific antibody |
| WO2007114319A1 (ja) | 2006-03-31 | 2007-10-11 | Chugai Seiyaku Kabushiki Kaisha | 抗体の血中動態を制御する方法 |
| SI2202245T1 (sl) | 2007-09-26 | 2016-10-28 | Chugai Seiyaku Kabushiki Kaisha | Postopek modificiranja izoelektrične točke protitelesa preko aminokislinske substitucije v CDR |
| AU2011215900A1 (en) | 2010-02-10 | 2012-07-26 | Immunogen, Inc. | CD20 antibodies and uses thereof |
| MX2012011479A (es) | 2010-03-30 | 2012-12-17 | Janssen Biotech Inc | Anticuerpos de interleucina-25 humanizados. |
| EP4269563A3 (en) | 2010-06-19 | 2024-01-10 | Memorial Sloan-Kettering Cancer Center | Anti-gd2 antibodies |
| US9334331B2 (en) | 2010-11-17 | 2016-05-10 | Chugai Seiyaku Kabushiki Kaisha | Bispecific antibodies |
| CA2903576C (en) | 2013-03-15 | 2021-06-08 | Nai-Kong V. Cheung | High affinity anti-gd2 antibodies |
| TW201536810A (zh) | 2013-07-15 | 2015-10-01 | Novo Nordisk As | 結合尿激酶纖維蛋白溶酶原活化物之抗體 |
| AU2014325063B2 (en) | 2013-09-27 | 2019-10-31 | Chugai Seiyaku Kabushiki Kaisha | Method for producing polypeptide heteromultimer |
| US10273301B2 (en) | 2013-12-24 | 2019-04-30 | Janssen Pharmaceutica Nv | Anti-vista antibodies and fragments |
| MA40764A (fr) | 2014-09-26 | 2017-08-01 | Chugai Pharmaceutical Co Ltd | Agent thérapeutique induisant une cytotoxicité |
| TWI701435B (zh) | 2014-09-26 | 2020-08-11 | 日商中外製藥股份有限公司 | 測定ｆｖｉｉｉ的反應性之方法 |
| TWI700300B (zh) | 2014-09-26 | 2020-08-01 | 日商中外製藥股份有限公司 | 中和具有第ｖｉｉｉ凝血因子（ｆｖｉｉｉ）機能替代活性的物質之抗體 |
| WO2016159213A1 (ja) | 2015-04-01 | 2016-10-06 | 中外製薬株式会社 | ポリペプチド異種多量体の製造方法 |
| CN107849142B (zh) | 2015-05-15 | 2022-04-26 | 综合医院公司 | 拮抗性抗肿瘤坏死因子受体超家族抗体 |
| CN107922497B (zh) | 2015-06-24 | 2022-04-12 | 詹森药业有限公司 | 抗vista抗体和片段 |
| JP6954842B2 (ja) | 2015-12-25 | 2021-10-27 | 中外製薬株式会社 | 増強された活性を有する抗体及びその改変方法 |
| MX2018007781A (es) | 2015-12-28 | 2018-09-05 | Chugai Pharmaceutical Co Ltd | Metodo para promover la eficiencia de purificacion del polipeptido que contiene la region de fragmento cristalizable (fc). |
| US10899836B2 (en) | 2016-02-12 | 2021-01-26 | Janssen Pharmaceutica Nv | Method of identifying anti-VISTA antibodies |
| AU2017241776B2 (en) | 2016-03-29 | 2024-06-20 | Janssen Biotech, Inc. | Treating psoriasis with increased interval dosing of anti-IL12 and/or -23 antibody |
| WO2017175058A1 (en) | 2016-04-07 | 2017-10-12 | Janssen Pharmaceutica Nv | Anti-vista antibodies and fragments, uses thereof, and methods of identifying same |
| MY200833A (en) | 2016-04-28 | 2024-01-17 | Chugai Pharmaceutical Co Ltd | Antibody-Containing Preparation |
| CA3035081A1 (en) | 2016-09-02 | 2018-03-08 | Dana-Farber Cancer Institute, Inc. | Composition and methods of treating b cell disorders |
| KR20230117462A (ko) | 2016-09-06 | 2023-08-08 | 추가이 세이야쿠 가부시키가이샤 | 응고 제 ix 인자 및/또는 활성화 응고 제 ix 인자 및응고 제 x 인자 및/또는 활성화 응고 제 x 인자를 인식하는 이중특이성 항체의 사용법 |
| MA46366A (fr) | 2016-09-30 | 2019-08-07 | Janssen Biotech Inc | Procédé sûr et efficace de traitement du psoriasis avec un anticorps spécifique contre l'il-23 |
| KR20190078648A (ko) | 2016-11-16 | 2019-07-04 | 얀센 바이오테크 인코포레이티드 | 항-il23 특이적 항체로 건선을 치료하는 방법 |
| TW201825515A (zh) | 2017-01-04 | 2018-07-16 | 美商伊繆諾金公司 | Ｍｅｔ抗體以及其免疫結合物及用途 |
| EP3573658A4 (en) | 2017-01-30 | 2021-07-21 | Janssen Biotech, Inc. | ANTI-TNF ANTIBODIES, COMPOSITIONS AND METHODS FOR THE TREATMENT OF ACTIVE PSORIASIC RHEUMATISM |
| KR20190115042A (ko) | 2017-02-07 | 2019-10-10 | 얀센 바이오테크 인코포레이티드 | 활성 강직성 척추염의 치료를 위한 항-tnf 항체, 조성물, 및 방법 |
| AU2018338859B2 (en) | 2017-09-29 | 2025-06-26 | Chugai Seiyaku Kabushiki Kaisha | Multispecific antigen-binding molecule having blood coagulation factor VIII (FVIII) cofactor function-substituting activity, and pharmaceutical formulation containing said molecule as active ingredient |
| CR20200229A (es) | 2017-11-01 | 2020-07-12 | Chugai Pharmaceutical Co Ltd | Variantes e isoformas de anticuerpos con actividad biológica reducida |
| KR20240170590A (ko) | 2017-11-06 | 2024-12-03 | 얀센 바이오테크 인코포레이티드 | 항-il23 특이적 항체로 건선성 관절염을 치료하는 안전하고 유효한 방법 |
| US20190269757A1 (en) | 2018-03-05 | 2019-09-05 | Janssen Biotech, Inc. | Methods of Treating Crohn's Disease with Anti-IL23 Specific Antibody |
| EP3790587A4 (en) | 2018-05-11 | 2022-01-26 | Janssen Biotech, Inc. | Methods of treating depression using il-23 antibodies |
| WO2019246494A1 (en) | 2018-06-21 | 2019-12-26 | Yumanity Therapeutics, Inc. | Compositions and methods for the treatment and prevention of neurological disorders |
| WO2020014306A1 (en) | 2018-07-10 | 2020-01-16 | Immunogen, Inc. | Met antibodies and immunoconjugates and uses thereof |
| US20200025776A1 (en) | 2018-07-18 | 2020-01-23 | Janssen Biotech, Inc. | Sustained Response Predictors After Treatment With Anti-IL23 Specific Antibody |
| CA3120237A1 (en) | 2018-11-20 | 2020-05-28 | Janssen Biotech, Inc. | Safe and effective method of treating psoriasis with anti-il-23 specific antibody |
| MA55705A (fr) | 2019-04-17 | 2022-02-23 | Novo Nordisk As | Anticorps bispécifiques |
| US11780911B2 (en) | 2019-05-23 | 2023-10-10 | Janssen Biotech, Inc. | Method of treating inflammatory bowel disease with a combination therapy of antibodies to IL-23 and TNF alpha |
| US20220324959A1 (en) | 2019-06-03 | 2022-10-13 | Janssen Biotech, Inc. | Anti-tnf antibodies, compositions, and methods for the treatment of active ankylosing spondylitis |
| EP3980065A4 (en) | 2019-06-04 | 2023-07-05 | Janssen Biotech, Inc. | SAFE AND EFFECTIVE METHOD OF TREATING PSORIATIC ARTHRITIS WITH A SPECIFIC ANTI-IL23 ANTIBODY |
| WO2021028752A1 (en) | 2019-08-15 | 2021-02-18 | Janssen Biotech, Inc. | Anti-tfn antibodies for treating type i diabetes |
| CA3181949A1 (en) | 2020-05-05 | 2021-11-11 | Janssen Biotech, Inc. | Methods of treating crohn's disease with anti-il23 specific antibody |
| US12258393B2 (en) | 2020-05-21 | 2025-03-25 | Janssen Biotech, Inc. | Method of treating inflammatory bowel disease with a combination therapy of antibodies to IL-23 and TNF alpha |
| EP4178616A4 (en) | 2020-07-13 | 2024-07-24 | Janssen Biotech, Inc. | SAFE AND EFFECTIVE METHOD FOR TREATING PSORIATIC ARTHRITIS USING A SPECIFIC ANTI-IL23 ANTIBODY |
| IL305836A (en) | 2021-03-12 | 2023-11-01 | Janssen Biotech Inc | A method for treating psoriatic arthritis patients with insufficient response to TNF therapy with a specific anti-IL23 antibody |
| JP2024510744A (ja) | 2021-03-12 | 2024-03-11 | ヤンセン バイオテツク，インコーポレーテツド | 抗ｉｌ２３特異的抗体で乾癬性関節炎を治療する安全かつ有効な方法 |
| MX2024005197A (es) | 2021-10-29 | 2024-07-24 | Janssen Biotech Inc | Métodos para tratar la enfermedad de crohn con el anticuerpo específico anti-il23. |
| CA3238377A1 (en) | 2021-11-15 | 2023-05-19 | Janssen Biotech, Inc. | Methods of treating crohn's disease with anti-il23 specific antibody |
| WO2023095000A1 (en) | 2021-11-23 | 2023-06-01 | Janssen Biotech, Inc. | Method of treating ulcerative colitis with anti-il23 specific antibody |
| JP2025512860A (ja) | 2022-03-30 | 2025-04-22 | ヤンセン バイオテツク，インコーポレーテツド | Ｉｌ－２３に特異的な抗体によって軽度から中等度の乾癬を治療する方法 |
| WO2023215498A2 (en) | 2022-05-05 | 2023-11-09 | Modernatx, Inc. | Compositions and methods for cd28 antagonism |
| CN119768427A (zh) | 2022-05-18 | 2025-04-04 | 詹森生物科技公司 | 用于评估il23抗体以及用il23抗体治疗银屑病关节炎的方法 |
| WO2024097639A1 (en) | 2022-10-31 | 2024-05-10 | Modernatx, Inc. | Hsa-binding antibodies and binding proteins and uses thereof |
| CN120569403A (zh) | 2022-11-22 | 2025-08-29 | 詹森生物科技公司 | 用抗il23特异性抗体治疗溃疡性结肠炎的方法 |
| WO2024118866A1 (en) | 2022-12-01 | 2024-06-06 | Modernatx, Inc. | Gpc3-specific antibodies, binding domains, and related proteins and uses thereof |
| WO2024206126A1 (en) | 2023-03-27 | 2024-10-03 | Modernatx, Inc. | Cd16-binding antibodies and uses thereof |
| US20250296998A1 (en) | 2024-03-20 | 2025-09-25 | Janssen Biotech, Inc. | Methods of Treating Crohn's Disease with Anti-IL23 Specific Antibody |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4714681A (en) * | 1981-07-01 | 1987-12-22 | The Board Of Reagents, The University Of Texas System Cancer Center | Quadroma cells and trioma cells and methods for the production of same |
| US4474893A (en) * | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| JP3177776B2 (ja) * | 1988-09-27 | 2001-06-18 | 武田薬品工業株式会社 | ハイブリッドモノクローナル抗体，抗体産生ポリドーマおよび抗体含有薬剤 |
| ES521370A0 (es) * | 1982-04-12 | 1985-04-16 | Hybritech Inc | Un procedimiento para obtener un polidoma. |
| WO1985004811A1 (en) * | 1984-04-23 | 1985-11-07 | Boston Biomedical Research Institute, Inc. | Bispecific antibody determinants |
| DE3426903A1 (de) * | 1984-07-20 | 1986-01-23 | Biotest Pharma GmbH, 6000 Frankfurt | Eine immunglobulinpraeparation in kombination mit einer anderen pharmakologisch wirksamen praeparation zur verwendung bei der behandlung von krankheiten |
| WO1987006240A1 (en) * | 1986-04-14 | 1987-10-22 | The General Hospital Corporation | Heterobifunctional antibodies and method of use |
| US4889922A (en) * | 1986-08-13 | 1989-12-26 | Monsanto Co. | Monoclonal antibody specific for human colon fibroblast-derived T-PA |
| DE3909708A1 (de) * | 1989-03-23 | 1990-09-27 | Boehringer Mannheim Gmbh | Verfahren zur herstellung bispezifischer antikoerper |
-
1991
- 1991-03-20 TW TW080102180A patent/TW212184B/zh active
- 1991-03-27 EP EP91104844A patent/EP0450479B1/en not_active Expired - Lifetime
- 1991-03-27 CA CA002039259A patent/CA2039259A1/en not_active Abandoned
- 1991-03-27 DE DE69121272T patent/DE69121272T2/de not_active Expired - Fee Related
- 1991-03-27 AT AT91104844T patent/ATE141285T1/de not_active IP Right Cessation
- 1991-03-28 IE IE107991A patent/IE76288B1/en not_active IP Right Cessation
- 1991-03-28 HU HU911027A patent/HUT63203A/hu unknown
- 1991-04-02 KR KR1019910005314A patent/KR910018039A/ko not_active Ceased
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1994
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| EP0450479B1 (en) | 1996-08-14 |
| CA2039259A1 (en) | 1991-10-03 |
| DE69121272D1 (de) | 1996-09-19 |
| HUT63203A (en) | 1993-07-28 |
| KR910018039A (ko) | 1991-11-30 |
| HU911027D0 (en) | 1991-10-28 |
| US5496549A (en) | 1996-03-05 |
| DE69121272T2 (de) | 1997-01-09 |
| IE911079A1 (en) | 1991-10-09 |
| IE76288B1 (en) | 1997-10-08 |
| ATE141285T1 (de) | 1996-08-15 |
| EP0450479A1 (en) | 1991-10-09 |
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