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Overview
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Matrix Metalloproteinase-8 Human Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa. The MMP-8 is purified by proprietary chromatographic techniques. Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form. Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I. Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, 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.
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- Properties
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Overview