Marimastat, Matrix metalloprotease (MMP) inhibitor
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(2 Publications)
MW 331.41 Da, Purity >98%. Potent matrix metalloproteinase inhibitor. Broad-spectrum inhibitor of all major MMPs. Prevents or reduces spread and growth of tumors.
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27 kDa interstitial collagenase, 72 kDa gelatinase, 72kD type IV collagenase, 82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, A disintegrin and metalloprotease domain 10, A disintegrin and metalloproteinase domain 10, A disintegrin and metalloproteinase domain 17, A disintegrin and metalloproteinase domain 17 (tumor necrosis factor, alpha, converting enzyme), AD 10, AD18, ADA10_HUMAN, ADA17_HUMAN, ADAM 17, ADAM metallopeptidase domain 10, ADAM metallopeptidase domain 17, ADAM17 protein, APC1 protein, CD 156b, CD 156c, CD156b antigen, CD156c antigen, CDw156, CHDS6, CLG, CLG 1, CLG 3, CLG 4, CLG 4A, CLG 4B, CSVP, Cachectin, Collagenase 1, Collagenase 1 neutrophil, Collagenase 3, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, DIF, Differentiation inducing factor, Disintegrin and metalloproteinase domain-containing protein 10, Disintegrin and metalloproteinase domain-containing protein 17, EC 3.4.24.35, EC 3.4.24.65, Fibroblast collagenase, GELB, Gelatinase 92 KD, Gelatinase A, Gelatinase B, Gelatinase alpha, Gelatinase beta, Gelatinase neutrophil, HME, HNC, HsT 18717, Interstitial collagenase, Kuz, Kuzbanian, Kuzbanian protein homolog, Kuzbanian, Drosophila, homolog of, MANDP1, MANDP2, ME, MGC126102, MGC126103, MGC126104, MGC138506, MGC71942, MME, MMP II, MMP-X1, MMP12_HUMAN, MMP13_HUMAN, MMP14_HUMAN, MMP1_HUMAN, MMP2_HUMAN, MMP3_HUMAN, MMP7_HUMAN, MMP8_HUMAN, MMP9_HUMAN, MONA, MPSL1, MT-MMP 1, MT1-MMP, Macrophage cytotoxic factor, Macrophage elastase, Macrophage gelatinase, Macrophage metalloelastase, Macrophage metaloelastase, Mammalian disintegrin-metalloprotease, Matrilysin, Matrin, 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 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 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-2, Matrix metalloproteinase-3, Matrix metalloproteinase-7, Matrix metalloproteinase-8, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, NISBD, NISBD1, Neutrophil collagenase, Neutrophil gelatinase, OTTHUMP00000045866, PEX, PMNL collagenase, PMNL-CL, PUMP 1, Proteoglycanase, Pump-1 protease, RAK, SL-1, STMY, STMY1, Snake venom-like protease, Stromelisin 1, Stromelysin 1 progelatinase, Stromelysin-1, TACE, TBE-1, TNF superfamily member 2, TNF, macrophage derived, TNF, monocyte derived, TNF-alpha, TNF-alpha convertase, TNF-alpha-converting enzyme, TNFA_HUMAN, TNFSF2, Tnf, Transin-1, Tumor Necrosis Factor Alpha Converting Enzyme, Tumor Necrosis Factor, Membrane Form, Tumor necrosis factor, Tumor necrosis factor (TNF superfamily member 2), Tumor necrosis factor alpha, Tumor necrosis factor ligand superfamily member 2, Tumor necrosis factor, soluble form, Type V collagenase, Uterine matrilysin, Uterine metalloproteinase, collagenase, fibroblast, collagenase, interstitial
- Chemical Structure
Lab
Chemical Structure - Marimastat, Matrix metalloprotease (MMP) inhibitor (AB141276)
2D chemical structure image of ab141276, Marimastat, Matrix metalloprotease (MMP) inhibitor
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MMPs participate in remodeling tissues during various physiological processes like wound healing angiogenesis and normal tissue maintenance. These proteases do not act alone; they often form complexes with other proteins facilitating processes like the activation of latent forms of MMPs. ADAM (A Disintegrin and Metalloproteinase) family members such as ADAM10 and ADAM17 act alongside MMPs especially in activities related to cell signaling and shedding of membrane proteins. TNF alpha a pro-inflammatory cytokine often interacts with MMPs modulating their activity during inflammatory responses.
Pathways
These metalloproteases embed themselves within significant systems notably the Wnt signaling and TGF-beta pathways. In these pathways MMPs work in tandem with proteins such as integrins and growth factors to regulate cellular behavior and extracellular matrix composition. MMP inhibitors chemical compounds like marimastat restrain MMP activity demonstrating importance in research and potential therapeutic applications for conditions involving excessive matrix degradation.
Publications (2)
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Developmental cell 58:1414-1428.e4 PubMed37321214
2023
Applications
Unspecified application
Species
Unspecified reactive species
Immunity 47:710-722.e6 PubMed29045902
2017
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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