Key Product Details
Structure / Form
N-terminal Sequence Analysis
Predicted Molecular Mass
The specific activity is >2000 pmol/min/µg, as measured under the described conditions.
Formulation, Preparation and Storage
|Formulation||Supplied as a 0.2 μm filtered solution in MES, NaCl, CaCl2 and Glycerol.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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 (1). 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.
Product Specific Notices for Recombinant Mouse MMP-7 Protein, CF
For research use only