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. Human recombinant Matrix Metalloproteinase-8 produced in E. coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.
Human MMP8 expressed in E.coli
CAT# CSC-CTK0372-10 (1 unit); CAT# CSC-CTK0372-50 (5 unit)
Greater than 90% as determined by SDS-PAGE analysis.
100 units/ml after activation with APMA by solution assay method. One unit of collagenolytic activity is defined as the cleavage of 1 μg of collagen per minute by the solution method.
Sterile-filtered, clear solution (100 units/ml) in 0.05 M Tris-HCl buffer (pH 7.6), containing 0.2 M NaCl, 5 mM CaCl ? , 0.0025% NaN ? and 0.1% BSA.
Please centrifuge product briefly before opening vial. The dissolved protein can be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
Store at 4°C if entire vial will be used within 1 week. Store frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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