Enzo BML-SE540-0010 MMP-20 (catalytic domain) (human), (recombinant) (10 µg)

Preincubation of MMP-20 catalytic domain at 0.4nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 0.1nM for 1 hour completely inhibits enzymatic activity.

Matrix metalloproteinase 20, Enamelysin

Useful tool to study 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.

19.9 kDa

≥95% (SDS-PAGE)

Purified by multi-step chromatography.

Produced in E. coli. Active recombinant matrix metalloproteinase-20 (MMP-20, enamelysin) cloned from human cDNA. The enzyme consists of residues Tyr¹⁰⁸-Phe²⁷⁶ (NM_004771), which comprises the catalytic domain of human MMP-20, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-20 which lacks the C-terminal hemopexin domain.

≥ 10000pmol/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.

O60882

-80°C

Dry Ice