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Neutrophil collagenase, EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL collagenase, PMNL-CL, HNC, CLG1.
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.
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.
Escherichia Coli.
Sterile Filtered clear solution.
The protein Solution (100 units/ml) in 0.05M Tris-HCl buffer, pH 7.6, containing 0.2M NaCl, 5mM CaCl2, 0.0025% NaN3 and 0.1% BSA.
MMP-8 although stable at 14°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles.
Greater than 90% as determined by SDS-PAGE.
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.
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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