MMP25 antibody

Matrix Metalloproteinase 25, also known as membrane type matrix metalloproteinase 6 and leukolysin, was initially cloned from human leukocytes and found to be specifically expressed by peripheral blood leukocytes. The expression of MMP25 (leukolysin) at the mRNA level appears to be localized to neutrophils. MMP25 was also found in lung, spleen, brain tumors, and several tumor cell lines. Like the other membrane-type metalloproteinases, MMP25 is associated with the cell membrane, but is anchored to the cell surface via a GPI (glycosyl-phosphatidyl inositol) attachment, rather than through a transmembrane domain. MMP25 is proteolytically active and truncated forms digest gelatin in zymograms. Like the other MT MMPs, MMP25 has a furin cleavage site, where prohormone convertases can activate the zymogen. MMP25 can be shed from the from the cell surface, into the culture media under stimulatory conditions. MMP25 is expressed in brain tumors and may facilitate tumor progression through its ability to activate progelatinase A at the cell membrane in colon carcinomas or brain tumors. MMP25 may also play a role in the cellular migration and invasion of the extracellular matrix and basement membranes. The MMP25 gene maps to human chromosome 16p13.3.