CN103764677A - 抗神经生长因子抗体及其制备和使用方法 - Google Patents
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
- C07K16/467—Igs with modifications in the FR-residues only
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- C07K—PEPTIDES
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- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/74—Inducing cell proliferation
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
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- Veterinary Medicine (AREA)
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- Peptides Or Proteins (AREA)
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- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104774265A (zh) * | 2015-02-12 | 2015-07-15 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体11f1及其杂交瘤细胞株 |
| CN104910274A (zh) * | 2015-02-12 | 2015-09-16 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体12c11及其杂交瘤细胞株 |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9067988B2 (en) | 2010-12-01 | 2015-06-30 | Alderbio Holdings Llc | Methods of preventing or treating pain using anti-NGF antibodies |
| US9539324B2 (en) | 2010-12-01 | 2017-01-10 | Alderbio Holdings, Llc | Methods of preventing inflammation and treating pain using anti-NGF compositions |
| US11214610B2 (en) | 2010-12-01 | 2022-01-04 | H. Lundbeck A/S | High-purity production of multi-subunit proteins such as antibodies in transformed microbes such as Pichia pastoris |
| US9884909B2 (en) | 2010-12-01 | 2018-02-06 | Alderbio Holdings Llc | Anti-NGF compositions and use thereof |
| WO2012075340A2 (en) | 2010-12-01 | 2012-06-07 | Alderbio Holdings Llc | Anti-ngf compositions and use thereof |
| US9078878B2 (en) | 2010-12-01 | 2015-07-14 | Alderbio Holdings Llc | Anti-NGF antibodies that selectively inhibit the association of NGF with TrkA, without affecting the association of NGF with p75 |
| AU2012252153B2 (en) * | 2011-05-06 | 2016-07-07 | Zoetis Services Llc | Anti-nerve growth factor antibodies and methods of preparing and using the same |
| CA2932515C (en) | 2013-12-20 | 2023-08-01 | Intervet International B.V. | Caninized antibodies |
| ES2853823T3 (es) | 2014-09-30 | 2021-09-17 | Intervet Int Bv | Anticuerpos de PD-L1 que se unen a PD-L1 canino |
| BR112017025029A2 (pt) * | 2015-05-22 | 2018-08-07 | Astellas Pharma Inc. | ?novo fragmento fab de anticorpo ngf anti- humano?. |
| JP7008020B2 (ja) | 2015-12-18 | 2022-01-25 | インターベット インターナショナル ベー． フェー． | ヒトおよびイヌｉｌ－４ｒアルファに対するイヌ化ヒト抗体 |
| US11091556B2 (en) | 2015-12-18 | 2021-08-17 | Intervet Inc. | Caninized human antibodies to human IL-4R alpha |
| CN119390821A (zh) | 2017-08-15 | 2025-02-07 | 伊兰科美国公司 | 兽药用IgG Fc变体 |
| GB2578867A (en) * | 2018-10-09 | 2020-06-03 | Genome Res Ltd | Animal models and therapeutic molecules |
| AU2019250128A1 (en) | 2018-10-15 | 2020-04-30 | Avent Inc. | Compositions, systems, kits, and methods for neural ablation |
| CA3199234A1 (en) * | 2020-10-22 | 2022-04-28 | Scout Bio, Inc. | Method of suppressing immune response to vector-delivered therapeutic protein |
| TW202306990A (zh) | 2021-05-12 | 2023-02-16 | 大陸商江蘇恆瑞醫藥股份有限公司 | 特異性結合ｒａｎｋｌ和ｎｇｆ的抗原結合分子及其醫藥用途 |
| KR20240107201A (ko) | 2021-08-31 | 2024-07-08 | 스카우트 바이오, 인코포레이티드 | 항원-결합 분자 및 이의 용도 |
| WO2025036564A1 (de) * | 2023-08-17 | 2025-02-20 | Gottfried Wilhelm Leibniz Universität Hannover (Luh) | Nukleinsäuresequenz, vektor, screening-verfahren und verfahren zur herstellung von rekombinanten antikörpern |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2138512A1 (en) * | 2003-12-24 | 2009-12-30 | PanGenetics B.V. | Humanized anti-NGF antibodies |
| WO2010027488A2 (en) * | 2008-09-04 | 2010-03-11 | Vet Therapeutics, Inc. | Monoclonal antibodies |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4376110A (en) | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
| 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 |
| US6291158B1 (en) | 1989-05-16 | 2001-09-18 | Scripps Research Institute | Method for tapping the immunological repertoire |
| AU632843B2 (en) * | 1989-08-10 | 1993-01-14 | Juridical Foundation The Chemo-Sero-Therapeutic Research Institute | Cat-mouse heterohybridoma and gene fragment coding for constant region of feline immunoglobulin |
| WO1992022324A1 (en) | 1991-06-14 | 1992-12-23 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| SE9400088D0 (sv) | 1994-01-14 | 1994-01-14 | Kabi Pharmacia Ab | Bacterial receptor structures |
| DE19742706B4 (de) | 1997-09-26 | 2013-07-25 | Pieris Proteolab Ag | Lipocalinmuteine |
| EP1332209B1 (en) | 2000-09-08 | 2009-11-11 | Universität Zürich | Collections of repeat proteins comprising repeat modules |
| US20030157561A1 (en) | 2001-11-19 | 2003-08-21 | Kolkman Joost A. | Combinatorial libraries of monomer domains |
| US20050053973A1 (en) | 2001-04-26 | 2005-03-10 | Avidia Research Institute | Novel proteins with targeted binding |
| EP3372614B1 (en) * | 2004-04-07 | 2022-06-08 | Rinat Neuroscience Corp. | Methods for treating bone cancer pain by administering a nerve growth factor antagonist |
| ITRM20050290A1 (it) * | 2005-06-07 | 2006-12-08 | Lay Line Genomics Spa | Uso di molecole in grado di inibire il legame tra ngf e il suo recettore trka come analgesici ad effetto prolungato. |
| US20070212703A1 (en) | 2005-09-27 | 2007-09-13 | Stemmer Willem P | Proteinaceous pharmaceuticals and uses thereof |
| US8435523B2 (en) | 2009-05-04 | 2013-05-07 | Abbott Research B.V. | Antibodies against nerve growth factor (NGF) with enhanced in vivo stability |
| BR112012022342A2 (pt) * | 2010-03-04 | 2017-02-14 | Vet Therapeutics Inc | anticorpos monoclonais dirigidos a cd52 |
| JP5911813B2 (ja) * | 2010-03-04 | 2016-04-27 | ベット・セラピューティクス・インコーポレイテッドＶｅｔ Ｔｈｅｒａｐｅｕｔｉｃｓ Ｉｎｃ． | Ｃｄ２０に対するモノクローナル抗体 |
| CA2808577C (en) * | 2010-08-19 | 2018-09-25 | Abbott Laboratories | Anti-ngf antibodies and their use |
| AU2012252153B2 (en) * | 2011-05-06 | 2016-07-07 | Zoetis Services Llc | Anti-nerve growth factor antibodies and methods of preparing and using the same |
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2012
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- 2012-05-08 CA CA2834983A patent/CA2834983C/en active Active
- 2012-05-08 BR BR112013028652A patent/BR112013028652A8/pt not_active Application Discontinuation
- 2012-05-08 WO PCT/GB2012/051004 patent/WO2012153123A1/en not_active Ceased
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- 2012-05-08 RU RU2013154307A patent/RU2640252C2/ru not_active Application Discontinuation
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2138512A1 (en) * | 2003-12-24 | 2009-12-30 | PanGenetics B.V. | Humanized anti-NGF antibodies |
| WO2010027488A2 (en) * | 2008-09-04 | 2010-03-11 | Vet Therapeutics, Inc. | Monoclonal antibodies |
Non-Patent Citations (2)
| Title |
|---|
| COVACEUSZACH S等: "Dissecting NGF interactions with TrkA and p75 Receptor by Structural and Functional Studies of an Anti-NGF Neutralizing Antibody", 《JOURNAL OF MOLECULAR BIOLOGY 》, vol. 381, no. 4, 12 September 2008 (2008-09-12), pages 881 - 896, XP023611489, DOI: doi:10.1016/j.jmb.2008.06.008 * |
| PELAT THIBAUT等: "Obtention and engineering of non-human primate (NHP) antibodies for therapeutics", 《MINI REVIEWS IN MEDICINAL CHEMISTRY》, vol. 9, no. 14, 31 December 2009 (2009-12-31), pages 1663 - 1638, XP008134866, DOI: doi:10.2174/138955709791012283 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104774265A (zh) * | 2015-02-12 | 2015-07-15 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体11f1及其杂交瘤细胞株 |
| CN104910274A (zh) * | 2015-02-12 | 2015-09-16 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体12c11及其杂交瘤细胞株 |
| CN104774265B (zh) * | 2015-02-12 | 2018-05-04 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体11f1及其杂交瘤细胞株 |
| CN104910274B (zh) * | 2015-02-12 | 2018-05-04 | 北京华安科创生物技术有限公司 | 抗人神经生长因子的中和性单克隆抗体12c11及其杂交瘤细胞株 |
Also Published As
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|---|---|
| MY160884A (en) | 2017-03-31 |
| AU2012252153A1 (en) | 2013-11-14 |
| RU2640252C2 (ru) | 2017-12-27 |
| EP2705056B1 (en) | 2018-11-14 |
| NZ617448A (en) | 2015-01-30 |
| WO2012153123A1 (en) | 2012-11-15 |
| JP6181043B2 (ja) | 2017-08-16 |
| BR112013028652A8 (pt) | 2017-12-26 |
| SG10201500957QA (en) | 2015-04-29 |
| GB201320050D0 (en) | 2013-12-25 |
| GB2504888B (en) | 2016-02-03 |
| RU2013154307A (ru) | 2015-06-20 |
| KR20140041532A (ko) | 2014-04-04 |
| EP3502136A1 (en) | 2019-06-26 |
| BR112013028652A2 (pt) | 2016-11-29 |
| GB2504888A (en) | 2014-02-12 |
| EP2705056A1 (en) | 2014-03-12 |
| ES2704007T3 (es) | 2019-03-13 |
| JP2017123870A (ja) | 2017-07-20 |
| SG194795A1 (en) | 2013-12-30 |
| CA2834983C (en) | 2020-11-17 |
| AU2012252153A8 (en) | 2013-12-19 |
| KR101833465B1 (ko) | 2018-02-28 |
| AU2012252153B2 (en) | 2016-07-07 |
| CA2834983A1 (en) | 2012-11-15 |
| JP6526089B2 (ja) | 2019-06-05 |
| US20190276525A1 (en) | 2019-09-12 |
| JP2014519318A (ja) | 2014-08-14 |
| US20140170136A1 (en) | 2014-06-19 |
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