MMP-14 (catalytic domain) (human), (recombinant)

Preincubation of MMP-14 catalytic domain at 13.6nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity.

Matrix metalloproteinase 14, Membrane type matrix metalloproteinase 1, MT-1 MMP

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

Liquid. In 50mM TRIS, pH 7.5, containing 5mM calcium chloride, 300mM sodium chloride, 20µM zinc chloride, 0.5% Brij-35, and 30% glycerol.

22.5 kDa

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

Produced in E.coli. Active Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase 1, MT1-MMP) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-14 (Tyr¹¹²-Arg²⁹⁸, NM_004995) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-14 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.

≥1000 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.

P50281