||Recombinant Human MMP17 produced in E.coli was fused to a His-tag at the C-terminus. The catalytic domain of human MMP-17 is produced by tryptic activation of a recombinant soluble proform.
||Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP"s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP"s in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage.
||Liquid. 50mM TRIS-HCl, pH 7.5 containing 150mM NaCl, 5mM CaCl2, 1% glycerol and 0.1% Triton X-100.
||≥6mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 per min. at 37℃, pH 7.5.
||Store at -80°C.