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Protein Tag: N-His & C-His
Uniprot: P51512
Accession: P51512
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.
Bio Acitivity: Not validated for activity
Sequence: Ala 151-Lys 450
Purity: > 95% as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4.
Normally 5%-8% trehalose, mannitol and 0.01% Tween 80 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.
Endotoxin: < 10 EU/mg of the protein as determined by the LAL method.
Calculated MW: 32.9 kDa
Observed MW: 35 kDa
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