GM 6001, MMP inhibitor
GM 6001, MMP inhibitor
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(21 Publications)
GM 6001 (ab120845) is a broad spectrum, cell-permeable, potent matrix metalloprotease (MMP) inhibitor for MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-14 and MMP-26. Moleculr weight: 388.5
- Pharmacologically active in vivo
- Available in different sizes to fit your experimental needs
查看别名
27 kDa interstitial collagenase, 72 kDa gelatinase, 72kD type IV collagenase, 82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, AI503551, C8orf57, CHDS6, CLG, CLG 1, CLG 3, CLG 4, CLG 4A, CLG 4B, Collagenase 1, Collagenase 1 neutrophil, Collagenase 3, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, DKFZp761D112, EC 3.4.24.35, EC 3.4.24.65, Endometase, Fibroblast collagenase, GELB, Gelatinase 92 KD, Gelatinase A, Gelatinase B, Gelatinase alpha, Gelatinase beta, Gelatinase neutrophil, HME, HNC, Interstitial collagenase, MANDP1, MANDP2, ME, MGC126102, MGC126103, MGC126104, MGC138506, MME, MMP II, MMP-X1, MMP-X2, MMP12_HUMAN, MMP13_HUMAN, MMP14_HUMAN, MMP15_HUMAN, MMP16_HUMAN, MMP17_HUMAN, MMP1_HUMAN, MMP2_HUMAN, MMP3_HUMAN, MMP7_HUMAN, MMP8_HUMAN, MMP9_HUMAN, MONA, MPSL1, MT-MMP 1, MT-MMP 2, MT-MMP 3, MT-MMP 4, MT1-MMP, MT2-MMP, MT3-MMP, MT4-MMP, Macrophage elastase, Macrophage gelatinase, Macrophage metalloelastase, Macrophage metaloelastase, Matrilysin, Matrilysin 2, Matrin, Matrix Metalloproteinase 26, Matrix Metalloproteinase 9, Matrix metallopeptidase 1 (interstitial collagenase), Matrix metallopeptidase 12 (macrophage elastase), Matrix metallopeptidase 13 (collagenase 3), Matrix metallopeptidase 14 (membrane inserted), Matrix metallopeptidase 15 membrane inserted, Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase, Matrix metallopeptidase 8 (neutrophil collagenase), Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase), Matrix metalloprotease 1, Matrix metalloprotease 12, Matrix metalloprotease 8, Matrix metalloproteinase 17 membrane inserted, Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), Matrix metalloproteinase 3 preproprotein, Matrix metalloproteinase II, Matrix metalloproteinase-1, Matrix metalloproteinase-12, Matrix metalloproteinase-13, Matrix metalloproteinase-14, Matrix metalloproteinase-15, Matrix metalloproteinase-16, Matrix metalloproteinase-17, Matrix metalloproteinase-2, Matrix metalloproteinase-3, Matrix metalloproteinase-7, Matrix metalloproteinase-8, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type matrix metalloproteinase 2, Membrane-type matrix metalloproteinase 3, Membrane-type matrix metalloproteinase 4, Membrane-type-1 matrix metalloproteinase, Membrane-type-2 matrix metalloproteinase, Membrane-type-3 matrix metalloproteinase, Membrane-type-4 matrix metalloproteinase, Neutrophil collagenase, Neutrophil gelatinase, OTTHUMP00000045866, PEX, PMNL collagenase, PMNL-CL, PUMP 1, Proteoglycanase, Pump-1 protease, Putative transmembrane protein C8orf57, SL-1, SMCP-2, STMY, STMY1, Stromelisin 1, Stromelysin 1 progelatinase, Stromelysin-1, TBE-1, Transin-1, Type V collagenase, Uterine matrilysin, Uterine metalloproteinase, collagenase, fibroblast, collagenase, interstitial
- Chemical Structure
Lab
Chemical Structure - GM 6001, MMP inhibitor (AB120845)
2D chemical structure image of ab120845, GM 6001, MMP inhibitor
产品详情
性能和储存信息
运输条件
推荐的短期储存条件
推荐的长期储存条件
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Pathways
MMPs operate within significant biological processes like the inflammatory response and cellular signaling pathways including the MAPK and NF-kB pathways. They interact with other proteins such as integrins and cytokines to modulate cellular and inflammatory responses. Such interactions impact the balance between matrix formation and degradation exemplifying their involvement in tissue homeostasis and response to injury or disease.
Biological function summary
MMPs facilitate the breakdown of extracellular matrix components impacting processes such as angiogenesis wound healing and embryonic development. They often work in concert with other proteins in the extracellular space potentially forming complexes with tissue inhibitors of metalloproteinases (TIMPs) which regulate their activity. MMPs not only maintain normal physiological function but also reactivate and remodel tissue structure during pathological conditions providing grounds for cellular migration and proliferation.
文献 (21)
Recent publications for all applications. Explore the full list and refine your search
Scientific reports 14:26248 PubMed39482373
2024
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Nature communications 15:2861 PubMed38570505
2024
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Development, growth & differentiation 66:133-144 PubMed38281811
2024
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iScience 26:108211 PubMed37942007
2023
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Scientific reports 13:15508 PubMed37726363
2023
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Journal of molecular cell biology 14: PubMed36271843
2023
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Science advances 9:eadd9275 PubMed36989370
2023
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Acta biomaterialia 155:167-181 PubMed36371004
2022
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Journal of biomedical materials research. Part A 111:389-403 PubMed36210776
2022
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Nature communications 13:1151 PubMed35241668
2022
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