Product Details
Alternative Name: | Matrix metalloproteinase 7, Matrilysin, Pump |
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MW: | 20.4 kDa |
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Source: | Produced in E. coli. Active Matrix Metalloproteinase-7 (MMP-7, matrilysin, pump) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-7 (Tyr95-Lys267, NM_002423) with a C-terminal purification tag. |
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UniProt ID: | P09237 |
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Formulation: | Liquid. In 50 mM Tris-HCl pH 7.5, 5 mM CaCl2, 300 mM NaCl, 20 µM ZnCl2, 0.5% Brij-35, and 30% glycerol. |
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Purity: | ≥95% (SDS-PAGE) |
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Purity Detail: | Purified by multi-step chromatography. |
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Activity: | Preincubation of MMP-7 catalytic domain at 19nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 100nM for 1 hour completely inhibits enzymatic activity. |
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Specific Activity: | ≥500 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate. |
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Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors. |
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Shipping: | Dry Ice |
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Long Term Storage: | -80°C |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14: U. Eckhard, et al.; Data Brief
7, 299 (2016),
Application(s): Quenched fluorescence protease activity assay,
Abstract;
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The Dendritic Cell Major Histocompatibility Complex II (MHC II) Peptidome Derives from a Variety of Processing Pathways and Includes Peptides with a Broad Spectrum of HLA-DM Sensitivity: C.C. Clement, et al.; J. Biol. Chem.
291, 5576 (2016),
Abstract;
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The in vitro resistance of IgG2 to proteolytic attack concurs with a comparative paucity of autoantibodies against peptide analogs of the IgG2 hinge: R.J. Brezski, et al.; Mabs
3, 558 (2011),
Abstract;
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