CN104169301A - 人生长激素受体拮抗剂抗体及其使用方法 - Google Patents
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- C07K2317/00—Immunoglobulins specific features
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
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| US201161579618P | 2011-12-22 | 2011-12-22 | |
| US61/579,618 | 2011-12-22 | ||
| PCT/IB2012/057151 WO2013093707A1 (en) | 2011-12-22 | 2012-12-10 | Human growth hormone receptor antagonist antibodies and methods of use thereof |
Publications (1)
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| CN104169301A true CN104169301A (zh) | 2014-11-26 |
Family
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Family Applications (1)
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| CN201280070288.9A Pending CN104169301A (zh) | 2011-12-22 | 2012-12-10 | 人生长激素受体拮抗剂抗体及其使用方法 |
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| EP (1) | EP2794659A1 (enExample) |
| JP (1) | JP2015502975A (enExample) |
| KR (1) | KR20140102710A (enExample) |
| CN (1) | CN104169301A (enExample) |
| AU (1) | AU2012356206A1 (enExample) |
| BR (1) | BR112014014824A2 (enExample) |
| CA (1) | CA2859472A1 (enExample) |
| HK (1) | HK1204328A1 (enExample) |
| IL (1) | IL233119A0 (enExample) |
| IN (1) | IN2014CN04652A (enExample) |
| MX (1) | MX2014007644A (enExample) |
| RU (1) | RU2014123030A (enExample) |
| SG (1) | SG11201402828XA (enExample) |
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| ZA (1) | ZA201404735B (enExample) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN119080929A (zh) * | 2023-06-05 | 2024-12-06 | 东莞市朋志生物科技有限公司 | 抗白介素6抗体、检测白介素6的试剂和试剂盒 |
| WO2025146121A1 (zh) * | 2024-01-05 | 2025-07-10 | 长春金赛药业有限责任公司 | Ghr激动型抗体及其应用 |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9353189B2 (en) | 2014-01-24 | 2016-05-31 | William R Church | Antibody specific to Staphylococcus aureus, therapeutic method and detection method using same |
| WO2016130901A2 (en) * | 2015-02-12 | 2016-08-18 | University Of Southern California | Blockers of the growth hormone receptor in disease prevention and treatment |
| US11473088B2 (en) * | 2016-12-02 | 2022-10-18 | Ohio University | Method of treating cancer and method of sensitizing cancer cells to the action of chemotherapeutic agents via growth hormone receptor antagonists or knock down |
| CN112272677B (zh) * | 2018-02-26 | 2024-10-29 | 米纳瓦生物技术公司 | 使用抗muc1＊抗体的诊断方法 |
| WO2020069208A1 (en) * | 2018-09-27 | 2020-04-02 | The Regents Of The University Of California | Prevention and treatment of osteoarthritis by inhibition of insulin growth factor-1 signaling |
| US11345744B2 (en) | 2019-05-07 | 2022-05-31 | William R Church | Antibody specific to Staphylococcus aureus, therapeutic method and detection method using same |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
Family Cites Families (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3773919A (en) | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| FR2413974A1 (fr) | 1978-01-06 | 1979-08-03 | David Bernard | Sechoir pour feuilles imprimees par serigraphie |
| US4485045A (en) | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4544545A (en) | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US4754065A (en) | 1984-12-18 | 1988-06-28 | Cetus Corporation | Precursor to nucleic acid probe |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US4777127A (en) | 1985-09-30 | 1988-10-11 | Labsystems Oy | Human retrovirus-related products and methods of diagnosing and treating conditions associated with said retrovirus |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US4800159A (en) | 1986-02-07 | 1989-01-24 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences |
| GB8702816D0 (en) | 1987-02-07 | 1987-03-11 | Al Sumidaie A M K | Obtaining retrovirus-containing fraction |
| US5219740A (en) | 1987-02-13 | 1993-06-15 | Fred Hutchinson Cancer Research Center | Retroviral gene transfer into diploid fibroblasts for gene therapy |
| US5057417A (en) | 1987-06-12 | 1991-10-15 | Genentech, Inc. | Compositions and methods for the synthesis of growth hormone receptor and growth hormone binding protein |
| US5422120A (en) | 1988-05-30 | 1995-06-06 | Depotech Corporation | Heterovesicular liposomes |
| AP129A (en) | 1988-06-03 | 1991-04-17 | Smithkline Biologicals S A | Expression of retrovirus gag protein eukaryotic cells |
| US5047335A (en) | 1988-12-21 | 1991-09-10 | The Regents Of The University Of Calif. | Process for controlling intracellular glycosylation of proteins |
| EP0454781B1 (en) | 1989-01-23 | 1998-12-16 | Chiron Corporation | Recombinant cells for therapies of infection and hyperproliferative disorders and preparation thereof |
| DE69034168T3 (de) | 1989-03-21 | 2013-04-11 | Vical, Inc. | Expression von exogenen Polynukleotidsequenzen in Wirbeltieren |
| US6673776B1 (en) | 1989-03-21 | 2004-01-06 | Vical Incorporated | Expression of exogenous polynucleotide sequences in a vertebrate, mammal, fish, bird or human |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| ATE144793T1 (de) | 1989-06-29 | 1996-11-15 | Medarex Inc | Bispezifische reagenzien für die aids-therapie |
| EP1645635A3 (en) | 1989-08-18 | 2010-07-07 | Oxford Biomedica (UK) Limited | Replication defective recombinant retroviruses expressing a palliative |
| US5585362A (en) | 1989-08-22 | 1996-12-17 | The Regents Of The University Of Michigan | Adenovirus vectors for gene therapy |
| US5013556A (en) | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| NZ237464A (en) | 1990-03-21 | 1995-02-24 | Depotech Corp | Liposomes with at least two separate chambers encapsulating two separate biologically active substances |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5278299A (en) | 1991-03-18 | 1994-01-11 | Scripps Clinic And Research Foundation | Method and composition for synthesizing sialylated glycosyl compounds |
| WO1992020373A1 (en) | 1991-05-14 | 1992-11-26 | Repligen Corporation | Heteroconjugate antibodies for treatment of hiv infection |
| GB9115364D0 (en) | 1991-07-16 | 1991-08-28 | Wellcome Found | Antibody |
| DE69233013T2 (de) | 1991-08-20 | 2004-03-04 | The Government Of The United States Of America As Represented By The Secretary Of National Institute Of Health, Office Of Technology Transfer | Adenovirus vermittelter gentransfer in den gastrointestinaltrakt |
| AU669124B2 (en) | 1991-09-18 | 1996-05-30 | Kyowa Hakko Kirin Co., Ltd. | Process for producing humanized chimera antibody |
| JP3540315B2 (ja) | 1991-09-23 | 2004-07-07 | メディカル リサーチ カウンシル | キメラ抗体の製造−組合せアプローチ |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| WO1993010218A1 (en) | 1991-11-14 | 1993-05-27 | The United States Government As Represented By The Secretary Of The Department Of Health And Human Services | Vectors including foreign genes and negative selective markers |
| AU3144193A (en) | 1991-11-21 | 1993-06-15 | Board Of Trustees Of The Leland Stanford Junior University | Controlling degradation of glycoprotein oligosaccharides by extracellular glycosisases |
| GB9125623D0 (en) | 1991-12-02 | 1992-01-29 | Dynal As | Cell modification |
| FR2688514A1 (fr) | 1992-03-16 | 1993-09-17 | Centre Nat Rech Scient | Adenovirus recombinants defectifs exprimant des cytokines et medicaments antitumoraux les contenant. |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| JPH07507689A (ja) | 1992-06-08 | 1995-08-31 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 特定組織のターゲティング方法及び組成物 |
| JPH09507741A (ja) | 1992-06-10 | 1997-08-12 | アメリカ合衆国 | ヒト血清による不活性化に耐性のあるベクター粒子 |
| GB2269175A (en) | 1992-07-31 | 1994-02-02 | Imperial College | Retroviral vectors |
| ATE149570T1 (de) | 1992-08-17 | 1997-03-15 | Genentech Inc | Bispezifische immunoadhesine |
| CA2592997A1 (en) | 1992-12-03 | 1994-06-09 | Genzyme Corporation | Pseudo-adenovirus vectors |
| US5981568A (en) | 1993-01-28 | 1999-11-09 | Neorx Corporation | Therapeutic inhibitor of vascular smooth muscle cells |
| AU6818094A (en) | 1993-04-22 | 1994-11-08 | Depotech Corporation | Cyclodextrin liposomes encapsulating pharmacologic compounds and methods for their use |
| JP3532566B2 (ja) | 1993-06-24 | 2004-05-31 | エル． グラハム，フランク | 遺伝子治療のためのアデノウイルスベクター |
| EP0694070B1 (en) | 1993-09-15 | 2002-04-10 | Chiron Corporation | Recombinant alphavirus vectors |
| US6015686A (en) | 1993-09-15 | 2000-01-18 | Chiron Viagene, Inc. | Eukaryotic layered vector initiation systems |
| JP3875990B2 (ja) | 1993-10-25 | 2007-01-31 | カンジ，インコーポレイテッド | 組換えアデノウイルスベクターおよび使用方法 |
| NZ276305A (en) | 1993-11-16 | 1997-10-24 | Depotech Corp | Controlled release vesicle compositions |
| US6436908B1 (en) | 1995-05-30 | 2002-08-20 | Duke University | Use of exogenous β-adrenergic receptor and β-adrenergic receptor kinase gene constructs to enhance myocardial function |
| WO1995030763A2 (en) | 1994-05-09 | 1995-11-16 | Chiron Viagene, Inc. | Retroviral vectors having a reduced recombination rate |
| WO1996017072A2 (en) | 1994-11-30 | 1996-06-06 | Chiron Viagene, Inc. | Recombinant alphavirus vectors |
| US6265150B1 (en) | 1995-06-07 | 2001-07-24 | Becton Dickinson & Company | Phage antibodies |
| AU2998597A (en) | 1996-05-06 | 1997-11-26 | Chiron Corporation | Crossless retroviral vectors |
| AU9692198A (en) | 1997-10-10 | 1999-05-03 | Kevin J. Donahue | Gene delivery compositions and methods |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| CA2341029A1 (en) | 1998-08-17 | 2000-02-24 | Abgenix, Inc. | Generation of modified molecules with increased serum half-lives |
| AU3734900A (en) | 1999-03-09 | 2000-09-28 | University Of Southern California | Method of promoting myocyte proliferation and myocardial tissue repair |
| CN101014364B (zh) | 2002-12-24 | 2012-01-18 | 里纳特神经系统学公司 | 抗ngf抗体及其使用方法 |
| AU2006236508B2 (en) | 2005-04-15 | 2012-02-02 | Precision Biologics, Inc. | Recombinant monoclonal antibodies and corresponding antigens for colon and pancreatic cancers |
| US20070243192A1 (en) | 2006-02-21 | 2007-10-18 | Regents Of The University Of Michigan | Growth hormone receptor antagonist cancer treatment |
| SG170799A1 (en) * | 2006-03-28 | 2011-05-30 | Biogen Idec Inc | Anti-igf-ir antibodies and uses thereof |
-
2012
- 2012-12-10 WO PCT/IB2012/057151 patent/WO2013093707A1/en not_active Ceased
- 2012-12-10 AU AU2012356206A patent/AU2012356206A1/en not_active Abandoned
- 2012-12-10 SG SG11201402828XA patent/SG11201402828XA/en unknown
- 2012-12-10 RU RU2014123030A patent/RU2014123030A/ru not_active Application Discontinuation
- 2012-12-10 MX MX2014007644A patent/MX2014007644A/es unknown
- 2012-12-10 HK HK15104823.8A patent/HK1204328A1/xx unknown
- 2012-12-10 JP JP2014548270A patent/JP2015502975A/ja active Pending
- 2012-12-10 BR BR112014014824A patent/BR112014014824A2/pt not_active IP Right Cessation
- 2012-12-10 US US14/367,483 patent/US9249224B2/en not_active Expired - Fee Related
- 2012-12-10 IN IN4652CHN2014 patent/IN2014CN04652A/en unknown
- 2012-12-10 CN CN201280070288.9A patent/CN104169301A/zh active Pending
- 2012-12-10 EP EP12806702.2A patent/EP2794659A1/en not_active Withdrawn
- 2012-12-10 KR KR1020147017014A patent/KR20140102710A/ko not_active Ceased
- 2012-12-10 CA CA2859472A patent/CA2859472A1/en not_active Abandoned
-
2014
- 2014-06-12 IL IL233119A patent/IL233119A0/en unknown
- 2014-06-26 ZA ZA2014/04735A patent/ZA201404735B/en unknown
Non-Patent Citations (3)
| Title |
|---|
| CHHABRA Y等: "Role of the growth hormone-IGF-1 axis in cancer", 《EXPERT REVIEW OF ENDOCRINOLOGY AND METABOLISM》 * |
| JIANG J等: "Inhibitory GH receptor extracellular domain monoclonal antibodies:Three-dimensional epitope mapping", 《ENDOCRINOLOGY》 * |
| LATTUADA D等: "Monoclonal antibody against human growth hormone receptor", 《HYBRIDOMA》 * |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN119080929A (zh) * | 2023-06-05 | 2024-12-06 | 东莞市朋志生物科技有限公司 | 抗白介素6抗体、检测白介素6的试剂和试剂盒 |
| CN119080929B (zh) * | 2023-06-05 | 2025-08-12 | 东莞市朋志生物科技有限公司 | 抗白介素6抗体、检测白介素6的试剂和试剂盒 |
| WO2025146121A1 (zh) * | 2024-01-05 | 2025-07-10 | 长春金赛药业有限责任公司 | Ghr激动型抗体及其应用 |
Also Published As
| Publication number | Publication date |
|---|---|
| BR112014014824A2 (pt) | 2019-09-24 |
| JP2015502975A (ja) | 2015-01-29 |
| WO2013093707A1 (en) | 2013-06-27 |
| RU2014123030A (ru) | 2016-02-20 |
| SG11201402828XA (en) | 2014-10-30 |
| ZA201404735B (en) | 2016-10-26 |
| KR20140102710A (ko) | 2014-08-22 |
| US9249224B2 (en) | 2016-02-02 |
| IN2014CN04652A (enExample) | 2015-09-18 |
| CA2859472A1 (en) | 2013-06-27 |
| AU2012356206A1 (en) | 2014-06-26 |
| US20140356359A1 (en) | 2014-12-04 |
| IL233119A0 (en) | 2014-07-31 |
| MX2014007644A (es) | 2014-09-26 |
| HK1204328A1 (en) | 2015-11-13 |
| EP2794659A1 (en) | 2014-10-29 |
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