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Recombinant Human MMP16 protein (His tag)
SKU: PDEH100384-100
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Recombinant Human MMP16 protein (His tag)
| SKU # | PDEH100384 |
| Expression Host | E. coli |
Description
| Synonyms | Matrix metalloproteinase-16;MMP16; |
| Species | Human |
| Expression_host | E.coli |
| Sequence | Ala 151-Lys 450 |
| Accession | P51512 |
| Mol_Mass | 32.9 kDa |
| AP_Mol_Mass | 35 kDa |
| Tag | N-His & C-His |
| Bio_Activity | Not validated for activity |
Propertie
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin level | Please contact us for more information. |
| Storage | 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. |
| 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 | 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 |
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 (ECM). MMP-16 (MT3-MMP) is found in brain, lung, placenta, smooth muscle cells, and malignant tumor tissues including oral melanoma and renal carcinoma . MMP-16 has been shown to activate proMMP-2 and degrade various ECM components including native collagens. MMP-16 has been proposed to possess the potential to directly enhance the growth and invasiveness of cells in vivo, two critical processes for development and carcinogenesis . Structurally, MMP-16 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail . The structure of the catalytic domain in complex with a hydroxamate inhibitor has been solved . The rhMMP-16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.