Product Name :
MMP-10 (catalytic domain) (human), (recombinant)
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Molecular Weight:
19.4 kDa
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Additional Information :
| Activity Preincubation of MMP-10 catalytic domain at 22nM with the broad-spectrum inhibitor GM6001 at 100nM for 1 hour inhibits enzymatic activity by 95%.{{477775-14-7} web|{477775-14-7} Biological Activity|{477775-14-7} In stock|{477775-14-7} custom synthesis} | Alternative Name Matrix metalloproteinase 10, Stromelysin-2 | Application Notes Useful tool to study of enzyme kinetics, cleave target substrates, and screen for inhibitors. | Formulation Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. | MW 19.4 kDa | Purity Detail Partially purified by single-step affinity chromatography and gel filtration. | Source Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA.{{1194396-71-8} medchemexpress|{1194396-71-8} Purity & Documentation|{1194396-71-8} In Vitro|{1194396-71-8} custom synthesis} The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag.PMID:27809446 This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. | Specific Activity ≥200 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. | UniProt ID P09238
