Recombinant Human MMP8/Matrix metalloproteinase 8

Full-length Recombinant Human Matrix Metalloproteinase 8 (MMP-8) degrades interstitial collagens by acting preferentially on collagen type I. Increased MMP-8 protein is associated with infiltration of neutrophils into the skin, which are the major cell type that expresses MMP-8. MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation. Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes. Recombinant Human Matrix Metalloproteinase-8 produced in, E. coli, is a single, non-glycosylated, polypeptide chain having a MW = 75 kDa and purified by proprietary chromatographic techniques.

75 kDa