MMP-11 (catalytic domain) (human), (recombinant)

Matrix metalloproteinase 11, Stromelysin-3

Useful 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.

19.3 kDa

≥95% (SDS-PAGE)

Purified by multi-step chromatography.

Produced in E. coli. Active Matrix Metalloproteinase-11 (MMP-11, Stromelysin-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-11 (Phe⁹⁸-Ser²⁶⁶, NM_005940) with a C-terminal purification tag. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. It may be an important link between obesity and cancer.

Due to its unusual substrate preferences [A(A/Q)(N/A)~(L/Y)(T/V/M/R)(R/K), or G(G/A)E~LR5], MMP-11 cleaves MMP peptide substrates such as Prod. No. BML-P125, BML-P126, and BML-P132 extremely slowly (several hours yield very little product). Therefore, the activity of each lot of MMP-11 is verified by digestion of macromolecules.

P24347