||Progelatinase B complex is isolated from human blood.
||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 enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
||The proenzyme is solubilized in 50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 5 mM CaCl2, 1 μM ZnCl2, 0.05 % Brij-35, 0.05 % NaN3.
||>1400 mU/mg (upon trypsin activation)
||Gelatinase B displays three bands on SDS-PAGE at 220, 130 and 92 kDa. The 92 and the 220 kDa represent the monomer and the disufide-bridged homodimer of progelatinase B. The 130 kDa form could be identified as a disulfide bridge complex of the monomer and
||≥95 % of total protein by SDS-PAGE
||Purified progelatinase B monomer can serve as antigen standard in immunochemical analyses. Active gelatinase B is used to study the degradation of extracellular matrix proteins, to screen inhibitors of matrix metalloproteinases and to characterize inhibitor actions.