||Recombinant Human Matrix Metalloproteinase-8 produced inE.Coliis 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.
||Sterile Filtered clear solution.
||Greater than 90% as determined by SDS-PAGE.
||The protein Solution (100 units/ml) in 0.05 M Tris-HCl buffer, pH 7.6, containing 0.2 M NaCl, 5 mM CaCl2, 0.0025% NaN3 and 0.1% BSA.
||100 units/ml after activation with APMA by solution assay method. One unit of collagenolytic activity is defined as the cleavage of 1µg of collagen per minute by the solution method.
||Used as a standard for analyzing mammalian collagenase activity.
||MMP-8 although stable at 14°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.