MMP-12 (catalytic domain) (human), (recombinant)

Preincubation of MMP-12 catalytic domain at 4nM with the inhibitor NNGH (Prod. No. BML-PI115) at 20nM, or with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 5nM, for 1 hour completely inhibits enzymatic activity.

Matrix metalloproteinase 12, Metalloelastase, Macrophage elastase

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

Liquid. In 50mM TRIS, pH 9.5, containing 5mM calcium chloride, 500mM sodium chloride, 20µM zinc chloride, 0.5% Brij-35, and 30% glycerol.

20.3 kDa

≥95% (SDS-PAGE)

Purified by multi-step chromatography.

Produced in E. coli. Active Matrix Metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase; often confused with neutrophil elastase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-12 (Phe⁹⁹-Leu²⁷¹, NM_002426) with a C-terminal purification tag.

≥2000 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.

In an SDS-PAGE gel, the enzyme runs as a doublet (~20 kDa). The higher band represents the polypeptide described above, while spontaneous cleavage of the tag results in the lower band. Both species possess identical enzymatic activities.

P39900