MMP-10 (catalytic domain) (human), (recombinant)

Preincubation of MMP-10 catalytic domain at 22nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 100nM for 1 hour inhibits enzymatic activity by 95%.

Matrix metalloproteinase 10, Stromelysin-2

Useful tool to study of enzyme kinetics, cleave target substrates, and screen for inhibitors.

Liquid. In 50mM TRIS, 5mM CaCl₂, 300mM NaCl, 20µM ZnCl₂, 0.5% Brij-35, and 30% glycerol.

19.4 kDa

Partially purified by single-step affinity chromatography and gel filtration.

Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe⁹⁹-Glu²⁷¹, NM_2425) with a C-terminal purification tag. 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.

≥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.

P09238