MMP-24, Catalytic Domain Liquid. In 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl2, pH 7.5. AVOID FREEZE/THAW CYCLES. Recombinant, human pro-MT5-MMP fused to a His•Tag® sequence, expressed in E. coli and activated to yield the active catalytic domain. Two isoforms are produced, one with an N-terminal Tyr156, the other with an N-terminal Leu158. Useful for the study of the activation of progelatinase A and the degradation of extracellular matrix proteins. MT5-MMP is a member of the Zn2+- and Ca2+-dependent endopeptidases that functions in the degradation of extracellular matrix components such as gelatin, chondroitin sulfate, and dermatan sulfate. It has a tendency to be shed from cell surface membranes and appears to undergo rapid autocatalytic destruction into smaller fragments. Specific activity: ≥100 mU/mg protein. One unit is defined as the amount of enzyme necessary to hydrolyze 1.0 mmol of the substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg (Cat. No. 03-32-5032) per minute at 37°C, pH 7.5. Purity: ≥95% by SDS-PAGE. Ref.: Llano, E., et al. 1999. Cancer Res. 59, 2570. Pei, D. 1999. J. Biol. Chem. 274, 8925. |
