MMP-7;MPSL1;PUMP-1

E.coli

Tyr95-Lys267

P09237

Human

18.9 kDa

20 kDa

N-His

Not validated for activity

> 95% as determined by reducing SDS-PAGE.

< 10 EU/mg of the protein as determined by the LAL method

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.

It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.

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.