Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

protein

MMP-14 (catalytic domain) (human), (recombinant)

ALX-201-098-C010

10 µg

ALX-201-098-C010

MMP-14 (catalytic domain) (human), (recombinant)

Protein

10 µg

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 caqrcinoma, colon, breast, head and neck carcinoma. MMP-14 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 amino acid residues located between prodomain and catalytic domain. MMP-14 activates pro-MMP-2 and pro-MMP-13 by proteolytic cleavage of their prodomains. The ability of MMP-14 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.

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

≥95% (SDS-PAGE)

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

Used to study the activation of progelatinase A (matrix metalloproteinase 2) and the degradation of proteins of the extracellular matrix. The enzyme allows screening of matrix metalloproteinase inhibitors and characterization of inhibitor action.

-80°C