MMP-14 proenzyme (soluble) (human), (recombinant) (His-tag) | Enzo Life Sciences ALX-201-100-C010 product information

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product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

protein

product name :

MMP-14 proenzyme (soluble) (human), (recombinant) (His-tag)

catalog :

ALX-201-100-C010

quantity :

10 µg

citations: 2

Reference
d Ortho M, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J, et al. Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur J Biochem. 1997;250:751-7 pubmed
Butler G, Butler M, Atkinson S, Will H, Tamura T, Schade van Westrum S, et al. The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study. J Biol Chem. 1998;273:871-80 pubmed

product information

Product ID :

ALX-201-100

Catalog Number :

ALX-201-100-C010

Product Name :

MMP-14 proenzyme (soluble) (human), (recombinant) (His-tag)

Product Type :

Protein

Size :

10 µg

list of Pubmed id :

9461298, 9422744

Product Description :

Active soluble MMP-14 is used to study the activation of MMP-2 (progelatinase A) and the degradations of proteins of the extracellular matrix, including fibrillar collagens. Proenzyme is activated by trace amounts of MMP-14 catalytic domain.

Background :

MMP-14 is expressed in adult lung, placenta, kidney, ovaries, intestine, prostate and spleen. Increased amounts of the enzyme are found in tumor tissues as lung carcinoma, gastric carcinoma, colon, breast, head and neck carcinoma. It activates pro-MMP-2 and pro-MMP-13 by proteolytic cleavage of their prodomains. The ability to activate other MMPs provides potential for enhanced pericellular proteolysis in physiological and pathological processes. In particular, activation of pro-MMP-2 by MMP-14 is considered to contribute to local degradation of extracellular matrix during cell migration and proliferation. MMP-14 hydrolyzes also fibrillar collagens I, II and III into characteristic 3/4 and 1/4 fragments and it cleaves a number of other proteins of the extracellular matrix, among them fibronectin, vitronectin, laminin-1 and dermatan sulfate proteoglycan. The activity of MMP-14 is poorly inhibited by tissue inhibitor of matrix metalloproteinases-1 (TIMP-1), but efficiently inhibited by TIMP-2 and TIMP-3. MMP-14 proenzyme is activated by removal of its prodomain. The reaction is catalyzed by furin, a subtilisin-type serine protease, which recognizes a motif of four basic aa located between prodomain and catalytic domain.

ALTnames :

Matrix metalloproteinase 14, MT-1 MMP, Membrane-type 1 matrix metalloproteinase

Purity :

≥80% (SDS-PAGE)

Buffer :

Liquid. In 50mM TRIS-HCl, pH 7.5, containing 150mM NaCl and 5mM CaCl2.

Uses :

Used as antigen for antibody generation and as antigen standard in immunoassays. The proenzyme can be activated with trace amounts of MMP-14 catalytic domain. Active MMP-14 is used to study the activation of progelatinase A (matrixmetalloproteinase 2) and the degradation of proteins of the extracellular matrix. The enzyme allows screening of matrixmetalloproteinase inhibitors and characterization of inhibitor action.

Storage :

-80°C