MX2007009091A - Formulaciones de polipeptido liquidas estabilizadas. - Google Patents
Formulaciones de polipeptido liquidas estabilizadas.Info
- Publication number
- MX2007009091A MX2007009091A MX2007009091A MX2007009091A MX2007009091A MX 2007009091 A MX2007009091 A MX 2007009091A MX 2007009091 A MX2007009091 A MX 2007009091A MX 2007009091 A MX2007009091 A MX 2007009091A MX 2007009091 A MX2007009091 A MX 2007009091A
- Authority
- MX
- Mexico
- Prior art keywords
- formulation
- antibody
- antigen
- polypeptide
- binding polypeptide
- Prior art date
Links
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Families Citing this family (77)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7790856B2 (en) | 1998-04-07 | 2010-09-07 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize beta amyloid peptide |
| US7588766B1 (en) | 2000-05-26 | 2009-09-15 | Elan Pharma International Limited | Treatment of amyloidogenic disease |
| US7964192B1 (en) | 1997-12-02 | 2011-06-21 | Janssen Alzheimer Immunotherapy | Prevention and treatment of amyloidgenic disease |
| TWI239847B (en) | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US20080050367A1 (en) | 1998-04-07 | 2008-02-28 | Guriq Basi | Humanized antibodies that recognize beta amyloid peptide |
| US6761888B1 (en) | 2000-05-26 | 2004-07-13 | Neuralab Limited | Passive immunization treatment of Alzheimer's disease |
| US7700751B2 (en) | 2000-12-06 | 2010-04-20 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize β-amyloid peptide |
| MY139983A (en) | 2002-03-12 | 2009-11-30 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| UA87453C2 (ru) * | 2003-02-01 | 2009-07-27 | Вайет | Применения фрагмента ав для лечения болезни альцгеймера |
| TWI374893B (en) | 2003-05-30 | 2012-10-21 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| EP1797182A2 (en) * | 2004-10-05 | 2007-06-20 | Wyeth a Corporation of the State of Delaware | Methods and compositions for improving recombinant protein production |
| WO2006066089A1 (en) | 2004-12-15 | 2006-06-22 | Neuralab Limited | Humanized amyloid beta antibodies for use in improving cognition |
| TW200636066A (en) | 2004-12-15 | 2006-10-16 | Elan Pharm Inc | Humanized antibodies that recognize beta amyloid peptide |
| GT200600031A (es) | 2005-01-28 | 2006-08-29 | Formulacion anticuerpo anti a beta | |
| CN101213211A (zh) * | 2005-06-17 | 2008-07-02 | 惠氏公司 | 纯化含Fc区蛋白的方法 |
| TW200806317A (en) * | 2006-03-20 | 2008-02-01 | Wyeth Corp | Methods for reducing protein aggregation |
| US8784810B2 (en) | 2006-04-18 | 2014-07-22 | Janssen Alzheimer Immunotherapy | Treatment of amyloidogenic diseases |
| TW200806315A (en) * | 2006-04-26 | 2008-02-01 | Wyeth Corp | Novel formulations which stabilize and inhibit precipitation of immunogenic compositions |
| CA2671968A1 (en) * | 2006-12-11 | 2008-06-19 | F. Hoffmann-La Roche Ag | Abeta antibody parenteral formulation |
| EP2104682B1 (en) | 2007-01-11 | 2016-09-21 | Michael Bacher | Diagnosis and treatment of alzheimer's and other neurodementing diseases |
| RU2476442C2 (ru) * | 2007-03-29 | 2013-02-27 | Эббот Лэборетриз | Кристаллические антитела против il-12 человека |
| US8003097B2 (en) | 2007-04-18 | 2011-08-23 | Janssen Alzheimer Immunotherapy | Treatment of cerebral amyloid angiopathy |
| ES2498040T3 (es) | 2007-07-27 | 2014-09-24 | Janssen Alzheimer Immunotherapy | Tratamiento de enfermedades amiloidogénicas con anticuerpos anti-beta humanizados |
| JO3076B1 (ar) | 2007-10-17 | 2017-03-15 | Janssen Alzheimer Immunotherap | نظم العلاج المناعي المعتمد على حالة apoe |
| EP2219602A1 (en) * | 2007-11-15 | 2010-08-25 | Amgen, Inc | Aqueous formulation of erythropoiesis stimulating protein stablised by antioxidants for parenteral administration |
| KR20150080038A (ko) * | 2007-11-30 | 2015-07-08 | 애브비 바이오테크놀로지 리미티드 | 단백질 제형 및 이의 제조방법 |
| US8883146B2 (en) | 2007-11-30 | 2014-11-11 | Abbvie Inc. | Protein formulations and methods of making same |
| PE20091174A1 (es) | 2007-12-27 | 2009-08-03 | Chugai Pharmaceutical Co Ltd | Formulacion liquida con contenido de alta concentracion de anticuerpo |
| EP2993186B1 (en) | 2008-03-14 | 2019-09-04 | Biocon Limited | A monoclonal antibody and a method thereof |
| US9067981B1 (en) | 2008-10-30 | 2015-06-30 | Janssen Sciences Ireland Uc | Hybrid amyloid-beta antibodies |
| EP2196476A1 (en) * | 2008-12-10 | 2010-06-16 | Novartis Ag | Antibody formulation |
| WO2010100135A1 (en) * | 2009-03-05 | 2010-09-10 | Ablynx N.V. | Novel antigen binding dimer-complexes, methods of making/avoiding and uses thereof |
| CA2765220A1 (en) * | 2009-07-14 | 2011-01-20 | Biogen Idec Ma Inc. | Methods for inhibiting yellow color and peroxide formation in a composition |
| US9345661B2 (en) * | 2009-07-31 | 2016-05-24 | Genentech, Inc. | Subcutaneous anti-HER2 antibody formulations and uses thereof |
| AR078161A1 (es) | 2009-09-11 | 2011-10-19 | Hoffmann La Roche | Formulaciones farmaceuticas muy concentradas de un anticuerpo anti cd20. uso de la formulacion. metodo de tratamiento. |
| EP2519539A4 (en) * | 2009-12-28 | 2013-11-13 | Ligocyte Pharmaceuticals Inc | METHODS FOR STABILIZING VIRUS-LIKE PARTICULATE SOLUTIONS BASED ON INFLUENZA-INFLUENZA-VIRUSED VIRUSES |
| EP2519262A2 (en) * | 2009-12-29 | 2012-11-07 | F. Hoffmann-La Roche AG | Antibody formulation |
| EA201892184A1 (ru) | 2010-03-01 | 2019-03-29 | БАЙЕР ХЕЛЬСКЕР ЛЛСи | Оптимизированные моноклональные антитела против ингибитора пути тканевого фактора |
| JP6023696B2 (ja) | 2010-03-31 | 2016-11-09 | スタビリテック リミテッド | ミョウバンアジュバントおよびミョウバンアジュバント化ワクチンの保存方法 |
| EP2552478B1 (en) | 2010-03-31 | 2016-12-21 | Stabilitech Ltd. | Excipients for stabilising viral particles |
| HUE026885T2 (en) | 2010-03-31 | 2016-08-29 | Stabilitech Ltd | Stabilize virus fragments |
| RU2607024C2 (ru) | 2010-06-04 | 2017-01-10 | УАЙТ ЭлЭлСи | Вакцины streptococcus pneumoniae |
| US8821865B2 (en) | 2010-11-11 | 2014-09-02 | Abbvie Biotechnology Ltd. | High concentration anti-TNFα antibody liquid formulations |
| EP2471554A1 (en) * | 2010-12-28 | 2012-07-04 | Hexal AG | Pharmaceutical formulation comprising a biopharmaceutical drug |
| EP2500035A1 (en) * | 2011-03-15 | 2012-09-19 | Icon Genetics GmbH | Pharmaceutical formulation containing immunglobulin |
| KR102031020B1 (ko) | 2011-03-31 | 2019-10-14 | 머크 샤프 앤드 돔 코포레이션 | 인간 프로그램화된 사멸 수용체 pd-1에 대한 항체의 안정한 제제 및 관련된 치료 |
| GB201117233D0 (en) | 2011-10-05 | 2011-11-16 | Stabilitech Ltd | Stabilisation of polypeptides |
| JP2015526409A (ja) * | 2012-07-03 | 2015-09-10 | ヤンセン・サイエンシズ・アイルランド・ユーシー | Ｃ−末端及び中心エピトープａ−ベータ抗体 |
| US9592297B2 (en) * | 2012-08-31 | 2017-03-14 | Bayer Healthcare Llc | Antibody and protein formulations |
| EP3936148A1 (en) | 2013-07-23 | 2022-01-12 | Biocon Limited | Use of a cd6 binding partner and method based thereon |
| IL312865B2 (en) | 2013-09-11 | 2025-06-01 | Eagle Biologics Inc | Liquid protein formulations containing viscosity-lowering agents |
| GB201320660D0 (en) * | 2013-11-22 | 2014-01-08 | Qualasept Ltd | Method |
| GB201406569D0 (en) | 2014-04-11 | 2014-05-28 | Stabilitech Ltd | Vaccine compositions |
| AR103173A1 (es) | 2014-12-22 | 2017-04-19 | Novarits Ag | Productos farmacéuticos y composiciones líquidas estables de anticuerpos il-17 |
| AR104847A1 (es) * | 2015-06-17 | 2017-08-16 | Lilly Co Eli | Formulación de anticuerpo anti-cgrp |
| IL302486A (en) | 2015-06-24 | 2023-06-01 | Hoffmann La Roche | Antibodies against the transnephrine receptor with adapted affinity |
| AR106189A1 (es) | 2015-10-02 | 2017-12-20 | Hoffmann La Roche | ANTICUERPOS BIESPECÍFICOS CONTRA EL A-b HUMANO Y EL RECEPTOR DE TRANSFERRINA HUMANO Y MÉTODOS DE USO |
| CN114057885A (zh) | 2015-10-02 | 2022-02-18 | 豪夫迈·罗氏有限公司 | 双特异性抗人cd20/人转铁蛋白受体抗体及使用方法 |
| GB201604124D0 (en) * | 2016-03-10 | 2016-04-27 | Ucb Biopharma Sprl | Pharmaceutical formulation |
| CN107446044B (zh) * | 2016-05-30 | 2021-04-30 | 越海百奥药业(绍兴)有限公司 | 一种纯化抗体的方法及所用缓冲液 |
| KR102387287B1 (ko) * | 2016-08-02 | 2022-04-14 | 암바 아이피 리미티드 | 안정한 이부프로펜 주사용 조성물 |
| EP3529274B1 (en) | 2016-10-21 | 2024-04-17 | Biocon Limited | A monoclonal antibody and a method of use for the treatment of lupus |
| GB201703063D0 (en) | 2017-02-24 | 2017-04-12 | Arecor Ltd | Stabilized antibody protein solutions |
| US11608357B2 (en) | 2018-08-28 | 2023-03-21 | Arecor Limited | Stabilized antibody protein solutions |
| EP3372241A1 (en) | 2017-03-06 | 2018-09-12 | Ares Trading S.A. | Liquid pharmaceutical composition |
| EP3372242A1 (en) | 2017-03-06 | 2018-09-12 | Ares Trading S.A. | Liquid pharmaceutical composition |
| JOP20190260A1 (ar) | 2017-05-02 | 2019-10-31 | Merck Sharp & Dohme | صيغ ثابتة لأجسام مضادة لمستقبل الموت المبرمج 1 (pd-1) وطرق استخدامها |
| WO2018204374A1 (en) | 2017-05-02 | 2018-11-08 | Merck Sharp & Dohme Corp. | Formulations of anti-lag3 antibodies and co-formulations of anti-lag3 antibodies and anti-pd-1 antibodies |
| GB2562241B (en) | 2017-05-08 | 2022-04-06 | Stabilitech Biopharma Ltd | Vaccine compositions |
| KR20250053967A (ko) * | 2017-08-22 | 2025-04-22 | 바이오젠 엠에이 인코포레이티드 | 항-베타 아밀로이드 항체를 함유하는 약제학적 조성물 |
| JP7422659B2 (ja) | 2017-12-08 | 2024-01-26 | アルジェニクス ビーブイ | 全身型重症筋無力症治療のためのＦｃＲｎアンタゴニストの使用 |
| MX2020013195A (es) * | 2018-06-08 | 2021-02-26 | Argenx Bvba | Composiciones y metodos para el tratamiento de la trombocitopenia inmunitaria. |
| KR20210089215A (ko) | 2018-11-07 | 2021-07-15 | 머크 샤프 앤드 돔 코포레이션 | 항-lag3 항체 및 항-pd-1 항체의 공동-제제 |
| GB201906917D0 (en) * | 2019-05-16 | 2019-07-03 | Intract Pharma Ltd | Novel compositions |
| FI4087875T3 (fi) | 2020-01-08 | 2024-10-25 | argenx BV | Vastasyntyneen ihmisen Fc-reseptorin (FcRn) antagonisteja pemfigus-häiriöiden hoitoon |
| CN114404575A (zh) * | 2020-12-07 | 2022-04-29 | 苏州智核生物医药科技有限公司 | 一种重组人促甲状腺素注射液 |
| WO2023242372A1 (en) | 2022-06-15 | 2023-12-21 | argenx BV | Fcrn/hsa binding molecules and methods of use |
Family Cites Families (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5358708A (en) * | 1993-01-29 | 1994-10-25 | Schering Corporation | Stabilization of protein formulations |
| US5385887A (en) * | 1993-09-10 | 1995-01-31 | Genetics Institute, Inc. | Formulations for delivery of osteogenic proteins |
| US6270757B1 (en) * | 1994-04-21 | 2001-08-07 | Genetics Institute, Inc. | Formulations for IL-11 |
| US6372716B1 (en) * | 1994-04-26 | 2002-04-16 | Genetics Institute, Inc. | Formulations for factor IX |
| ATE216590T1 (de) * | 1995-02-06 | 2002-05-15 | Genetics Inst | Arzneimittelformulierungen für il-12 |
| US5786180A (en) * | 1995-02-14 | 1998-07-28 | Bayer Corporation | Monoclonal antibody 369.2B specific for β A4 peptide |
| US6267958B1 (en) * | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
| US5770700A (en) * | 1996-01-25 | 1998-06-23 | Genetics Institute, Inc. | Liquid factor IX formulations |
| JP3919235B2 (ja) * | 1997-06-13 | 2007-05-23 | ジェネンテク，インコーポレイテッド | 抗体製剤 |
| US5994511A (en) * | 1997-07-02 | 1999-11-30 | Genentech, Inc. | Anti-IgE antibodies and methods of improving polypeptides |
| TWI239847B (en) * | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US7179892B2 (en) * | 2000-12-06 | 2007-02-20 | Neuralab Limited | Humanized antibodies that recognize beta amyloid peptide |
| PE20020574A1 (es) * | 2000-12-06 | 2002-07-02 | Wyeth Corp | Anticuerpos humanizados que reconocen el peptido amiloideo beta |
| GB0113179D0 (en) * | 2001-05-31 | 2001-07-25 | Novartis Ag | Organic compounds |
| IL161677A0 (en) * | 2001-11-08 | 2004-09-27 | Protein Design Labs | Stable liquid pharmaceutical formulation of igg antibodies |
| US20030171556A1 (en) * | 2001-12-13 | 2003-09-11 | Chi-Bom Chae | Beta-amyloid binding factors and inhibitors thereof |
| MY139983A (en) * | 2002-03-12 | 2009-11-30 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| US7132100B2 (en) * | 2002-06-14 | 2006-11-07 | Medimmune, Inc. | Stabilized liquid anti-RSV antibody formulations |
| US20040191243A1 (en) * | 2002-12-13 | 2004-09-30 | Bei Chen | System and method for stabilizing antibodies with histidine |
| DK2335725T3 (en) * | 2003-04-04 | 2017-01-23 | Genentech Inc | Highly concentrated antibody and protein formulations |
| TWI374893B (en) * | 2003-05-30 | 2012-10-21 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
-
2006
- 2006-01-27 AU AU2006207901A patent/AU2006207901A1/en not_active Abandoned
- 2006-01-27 CN CNA200680003387XA patent/CN101111264A/zh active Pending
- 2006-01-27 US US11/342,252 patent/US20060210557A1/en not_active Abandoned
- 2006-01-27 RU RU2007124933/13A patent/RU2007124933A/ru not_active Application Discontinuation
- 2006-01-27 TW TW095103327A patent/TW200638943A/zh unknown
- 2006-01-27 EP EP06734749A patent/EP1841456A2/en not_active Withdrawn
- 2006-01-27 SV SV2006002394A patent/SV2008002394A/es not_active Application Discontinuation
- 2006-01-27 GT GT200600033A patent/GT200600033A/es unknown
- 2006-01-27 KR KR1020077019697A patent/KR20070107079A/ko not_active Withdrawn
- 2006-01-27 MX MX2007009091A patent/MX2007009091A/es not_active Application Discontinuation
- 2006-01-27 DO DO2006000022A patent/DOP2006000022A/es unknown
- 2006-01-27 CA CA002595380A patent/CA2595380A1/en not_active Abandoned
- 2006-01-27 BR BRPI0606867-7A patent/BRPI0606867A2/pt not_active IP Right Cessation
- 2006-01-27 JP JP2007553395A patent/JP2008528638A/ja not_active Withdrawn
- 2006-01-27 PE PE2006000113A patent/PE20061201A1/es not_active Application Discontinuation
- 2006-01-27 AR ARP060100314A patent/AR052469A1/es not_active Application Discontinuation
- 2006-01-27 PA PA20068661401A patent/PA8661401A1/es unknown
- 2006-01-27 UY UY29350A patent/UY29350A1/es not_active Application Discontinuation
- 2006-01-27 WO PCT/US2006/004741 patent/WO2006081587A2/en not_active Ceased
-
2007
- 2007-07-02 IL IL184341A patent/IL184341A0/en unknown
- 2007-07-17 NO NO20073666A patent/NO20073666L/no not_active Application Discontinuation
- 2007-07-27 ZA ZA2007/06256A patent/ZA200706256B/en unknown
- 2007-08-07 CR CR9294A patent/CR9294A/es not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| ZA200706256B (en) | 2009-12-30 |
| AR052469A1 (es) | 2007-03-21 |
| NO20073666L (no) | 2007-10-25 |
| IL184341A0 (en) | 2007-10-31 |
| JP2008528638A (ja) | 2008-07-31 |
| TW200638943A (en) | 2006-11-16 |
| CA2595380A1 (en) | 2006-08-03 |
| CN101111264A (zh) | 2008-01-23 |
| US20060210557A1 (en) | 2006-09-21 |
| SV2008002394A (es) | 2008-02-08 |
| AU2006207901A1 (en) | 2006-08-03 |
| WO2006081587A2 (en) | 2006-08-03 |
| BRPI0606867A2 (pt) | 2009-07-21 |
| DOP2006000022A (es) | 2006-08-15 |
| CR9294A (es) | 2008-01-21 |
| WO2006081587A3 (en) | 2006-10-12 |
| UY29350A1 (es) | 2006-08-31 |
| PE20061201A1 (es) | 2006-11-03 |
| RU2007124933A (ru) | 2009-03-10 |
| PA8661401A1 (es) | 2006-09-08 |
| EP1841456A2 (en) | 2007-10-10 |
| GT200600033A (es) | 2006-10-25 |
| KR20070107079A (ko) | 2007-11-06 |
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| FA | Abandonment or withdrawal |