Description
Product Name: | Human MMP-7 Recombinant Protein (His tag) |
Product Code: | RPES5442 |
Size: | 20µg |
Species: | Human |
Expression Host: | E.coli |
Synonyms: | MMP-7, MPSL1, PUMP-1 |
Mol Mass: | 18.92 kDa |
AP Mol Mass: | 20 kDa |
Tag: | N-His |
Purity: | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin Level: | Please contact us for more information. |
Bio Activity: | Testing in progress |
Sequence: | Tyr 95-Lys 267 |
Accession: | P09237 |
Storage: | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
Shipping: | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation: | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution: | Please refer to the printed manual for detailed information. |
Background: | 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. |