MMP-8 (catalytic domain) (human), (recombinant)

Preincubation of MMP-8 catalytic domain at 13.6 nM with the broad-spectrum inhibitor GM6001 (Prod #BML-EI300) at 20nM for 1 hour completely inhibits enzymatic activity.

Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2

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.

20.3 kDa

≥90% (SDS-PAGE)

Purified by multi-step chromatography.

Produced in E. coli. Active Matrix Metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-8 (Phe⁹⁹-Gln²⁶⁹, NM_002424) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-8 which lacks the C-terminal hemopexin domain1. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.

≥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.

P22894