MMP-7,Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican. MMP-7 is implicated in the activation of other proteinases such as plasminogen, MMP-1, MMP-2, and MMP-9. In addition to its roles in connective tissue remodeling and cancer, MMP-7 also regulates intestinal alpha -defensin activation in innate host defense, releases tumor necrosis factor-alpha in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site.
Lyophilized from 0.22 µm filtered solution in 10mM HEPES,5mM CaCl2,150mM NaCl (pH 7.5). Normally 8% trehalose is added as protectant before lyophilization.
Lyophilized from 0.22 µm filtered solution in 10mM HEPES,5mM CaCl2,150mM NaCl (pH 7.5). Normally 8% trehalose is added as protectant before lyophilization.
Anwendungsbeschreibung:
Cross-Reactivity: Centrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage,it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA,5% HSA,10% FBS or 5% Trehalose),and aliquot the reconstituted protein solution to minimize free-thaw cycles., ResearchArea: Other Recombinant Protein
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