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Human MMP16 Recombinant Protein (His tag) (RPES5643)

SKU:
RPES5643
Product Type:
Recombinant Protein
Species:
Human
€149

Description

Product Name:Human MMP16 Recombinant Protein (His tag)
Product Code:RPES5643
Size:20µg
Species:Human
Expression Host:E.coli
Synonyms:Matrix metalloproteinase-16, MMP16,
Mol Mass:32.89 kDa
AP Mol Mass:35 kDa
Tag:N-His & C-His
Purity:> 95 % as determined by reducing SDS-PAGE.
Endotoxin Level:Please contact us for more information.
Bio Activity:Testing in progress
Sequence:Ala 151-Lys 450
Accession:P51512
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 (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.

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