CN104395345A - 抗基质金属蛋白酶9抗体 - Google Patents
抗基质金属蛋白酶9抗体 Download PDFInfo
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- CN104395345A CN104395345A CN201280072749.6A CN201280072749A CN104395345A CN 104395345 A CN104395345 A CN 104395345A CN 201280072749 A CN201280072749 A CN 201280072749A CN 104395345 A CN104395345 A CN 104395345A
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/54—Medicinal preparations containing antigens or antibodies characterised by the route of administration
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/545—Medicinal preparations containing antigens or antibodies characterised by the dose, timing or administration schedule
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
- G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
- G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
- G01N2333/9643—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general with EC number
- G01N2333/96486—Metalloendopeptidases (3.4.24)
- G01N2333/96491—Metalloendopeptidases (3.4.24) with definite EC number
- G01N2333/96494—Matrix metalloproteases, e. g. 3.4.24.7
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Food Science & Technology (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (1)
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|---|---|---|---|
| PCT/US2012/027160 WO2013130078A1 (en) | 2012-02-29 | 2012-02-29 | Antibodies to matrix metalloproteinase 9 |
Publications (1)
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| CN104395345A true CN104395345A (zh) | 2015-03-04 |
Family
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| CN201280072749.6A Pending CN104395345A (zh) | 2012-02-29 | 2012-02-29 | 抗基质金属蛋白酶9抗体 |
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| JP (1) | JP6067756B2 (enExample) |
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| WO (1) | WO2013130078A1 (enExample) |
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Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ701444A (en) | 2010-08-27 | 2016-06-24 | Gilead Biologics Inc | Antibodies to matrix metalloproteinase 9 |
| WO2013130905A1 (en) * | 2012-02-29 | 2013-09-06 | Gilead Biologics, Inc. | Antibodies to matrix metalloproteinase 9 |
| MD20140107A2 (ro) | 2012-02-29 | 2015-03-31 | Gilead Biologics, Inc. | Anticorpi împotriva metaloproteinazei 9 din matrice |
| WO2015130813A1 (en) * | 2014-02-27 | 2015-09-03 | Gilead Biologics, Inc. | Antibodies to matrix metalloproteinase 9 and methods of use thereof |
| EP2985295A1 (en) * | 2014-08-13 | 2016-02-17 | Calypso Biotech SA | Antibodies specific for MMP9 |
| EP2985296A1 (en) * | 2014-08-13 | 2016-02-17 | Calypso Biotech SA | Antibodies specific for MMP9 |
| CN105037553B (zh) * | 2015-08-20 | 2018-04-17 | 内蒙古蒙元生物基因科技有限公司 | 一种能够检测癌症的免疫球蛋白 |
| EP3440113A1 (en) | 2016-04-08 | 2019-02-13 | Gilead Sciences, Inc. | Compositions and methods for treating cancer, inflammatory diseases and autoimmune diseases |
| US10326830B1 (en) * | 2016-09-02 | 2019-06-18 | Amazon Technologies, Inc. | Multipath tunneling to a service offered at several datacenters |
| EP3555138A1 (en) | 2016-12-16 | 2019-10-23 | Université de Bordeaux | Mmp9 inhibitors and uses thereof in the prevention or treatment of a depigmenting disorder |
| US10941178B2 (en) | 2017-03-17 | 2021-03-09 | Gilead Sciences, Inc. | Method of purifying an antibody |
| JP7109440B2 (ja) | 2017-07-18 | 2022-07-29 | 第一三共株式会社 | 活性型mmp-9結合ペプチド |
| CN110885375B (zh) * | 2019-12-20 | 2021-07-02 | 南京融捷康生物科技有限公司 | 特异性针对mmp-9蛋白锌离子结合结构域的单域抗体及产品与应用 |
| CN111785321B (zh) * | 2020-06-12 | 2022-04-05 | 浙江工业大学 | 一种基于深度卷积神经网络的dna绑定残基预测方法 |
| CN117327186B (zh) * | 2023-07-12 | 2024-03-12 | 北京达成生物科技有限公司 | 结合mmp3蛋白的双特异性抗体及其用途 |
| WO2025076280A1 (en) | 2023-10-05 | 2025-04-10 | Ashibio, Inc. | Methods and compositions for treating mmp-9 mediated disorders |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1459505A (zh) * | 2002-05-21 | 2003-12-03 | 赵平 | 中国汉族人基质金属蛋白酶-9基因重构、表达、纯化及其医学应用 |
| WO2009111450A2 (en) * | 2008-03-03 | 2009-09-11 | Dyax Corp. | Metalloproteinase 9 binding proteins |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| US5859205A (en) * | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| JP2938569B2 (ja) | 1990-08-29 | 1999-08-23 | ジェンファーム インターナショナル,インコーポレイティド | 異種免疫グロブリンを作る方法及びトランスジェニックマウス |
| GB9022788D0 (en) | 1990-10-19 | 1990-12-05 | Cortecs Ltd | Pharmaceutical formulations |
| EP1136556B1 (en) | 1991-11-25 | 2005-06-08 | Enzon, Inc. | Method of producing multivalent antigen-binding proteins |
| AU783019B2 (en) * | 1999-07-13 | 2005-09-15 | University Of Southern California | Novel method and composition for inhibition of angiogenesis using antagonists based on MMP-9 and beta1 integrins |
| CA2496834C (en) * | 2002-09-06 | 2014-03-18 | Alexion Pharmaceuticals, Inc. | Method of treatment of asthma using antibodies to complement component c5 |
| RU2470941C2 (ru) * | 2005-12-02 | 2012-12-27 | Дженентек, Инк. | Связывающие полипептиды и их применения |
| WO2008154439A1 (en) * | 2007-06-08 | 2008-12-18 | Irm Llc | Methods and compositions for inducing apoptosis in cancer cells |
| EP2262840A4 (en) * | 2008-03-03 | 2012-08-08 | Dyax Corp | METALLOPROTEINASE 9 AND METALLOPROTEINASE 2 BINDING PROTEINS |
| AU2009308369A1 (en) * | 2008-10-22 | 2010-04-29 | Dyax Corp. | Combination treatments comprising protease binding proteins for inflammatory disorders |
| US20110286916A1 (en) * | 2008-11-20 | 2011-11-24 | Jose Miguel Aste-Amezaga | Generation and characterization of anti-notch antibodies for therapeutic and diagnostic use |
| CN102822202B (zh) * | 2010-01-27 | 2015-07-22 | 耶达研究及发展有限公司 | 抑制金属蛋白的抗体 |
| NZ701444A (en) | 2010-08-27 | 2016-06-24 | Gilead Biologics Inc | Antibodies to matrix metalloproteinase 9 |
| WO2013130905A1 (en) | 2012-02-29 | 2013-09-06 | Gilead Biologics, Inc. | Antibodies to matrix metalloproteinase 9 |
| MD20140107A2 (ro) | 2012-02-29 | 2015-03-31 | Gilead Biologics, Inc. | Anticorpi împotriva metaloproteinazei 9 din matrice |
-
2012
- 2012-02-29 MD MDA20140107A patent/MD20140107A2/ro not_active Application Discontinuation
- 2012-02-29 KR KR1020147026786A patent/KR20140130724A/ko not_active Ceased
- 2012-02-29 BR BR112014021477A patent/BR112014021477A2/pt not_active IP Right Cessation
- 2012-02-29 SG SG11201405305PA patent/SG11201405305PA/en unknown
- 2012-02-29 US US14/382,301 patent/US9550836B2/en active Active
- 2012-02-29 ES ES12708473T patent/ES2731441T3/es active Active
- 2012-02-29 IN IN8011DEN2014 patent/IN2014DN08011A/en unknown
- 2012-02-29 EP EP12708473.9A patent/EP2820048B1/en active Active
- 2012-02-29 AU AU2012318302A patent/AU2012318302C1/en not_active Ceased
- 2012-02-29 EA EA201491575A patent/EA201491575A1/ru unknown
- 2012-02-29 CN CN201280072749.6A patent/CN104395345A/zh active Pending
- 2012-02-29 CA CA2865530A patent/CA2865530C/en not_active Expired - Fee Related
- 2012-02-29 AP AP2014007907A patent/AP2014007907A0/xx unknown
- 2012-02-29 HK HK15108571.3A patent/HK1208036A1/xx unknown
- 2012-02-29 WO PCT/US2012/027160 patent/WO2013130078A1/en not_active Ceased
- 2012-02-29 JP JP2014559872A patent/JP6067756B2/ja not_active Expired - Fee Related
- 2012-02-29 MX MX2014010449A patent/MX2014010449A/es unknown
-
2014
- 2014-08-27 ZA ZA2014/06319A patent/ZA201406319B/en unknown
- 2014-08-27 PH PH12014501931A patent/PH12014501931A1/en unknown
- 2014-08-28 CL CL2014002282A patent/CL2014002282A1/es unknown
- 2014-08-29 CO CO14190943A patent/CO7061040A2/es unknown
- 2014-09-24 CR CR20140443A patent/CR20140443A/es unknown
- 2014-09-26 EC ECIEPI201420504A patent/ECSP14020504A/es unknown
-
2015
- 2015-10-13 AU AU2015242967A patent/AU2015242967B2/en not_active Ceased
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2016
- 2016-12-12 US US15/376,232 patent/US20170183421A1/en not_active Abandoned
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2017
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2019
- 2019-01-10 US US16/245,169 patent/US10800857B2/en active Active
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2020
- 2020-09-10 US US17/017,491 patent/US11634505B2/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1459505A (zh) * | 2002-05-21 | 2003-12-03 | 赵平 | 中国汉族人基质金属蛋白酶-9基因重构、表达、纯化及其医学应用 |
| WO2009111450A2 (en) * | 2008-03-03 | 2009-09-11 | Dyax Corp. | Metalloproteinase 9 binding proteins |
Non-Patent Citations (1)
| Title |
|---|
| CARTER P J. ET AL.: "Potent antibody therapeutics by design", 《NATURE REVIEWS IMMUNOLOGY》 * |
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