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

 
ALX-201-100-C010 10 µg 758.00 USD
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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.

Product Specification

Alternative Name:Matrix metalloproteinase 14, MT-1 MMP, Membrane-type 1 matrix metalloproteinase
 
MW:~58kDa.
 
Source:Produced in E. coli. Prodomain, catalytic domain and hemopexin domain of human MMP-14 proenzyme (aa 1-501) are fused to a His-tag (Thr-(His)6).
 
EC:3.4.24.-
 
UniProt ID:P50281
 
Concentration:0.2mg/ml
 
Formulation:Liquid. In 50mM TRIS-HCl, pH 7.5, containing 150mM NaCl and 5mM CaCl2.
 
Purity:≥80% (SDS-PAGE)
 
Application Notes: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.
 
Shipping:Shipped on Dry Ice
 
Short Term Storage:-20°C
 
Long Term Storage:-80°C
 
Use/Stability:Stable for several weeks when stored at -20°C.
 
Handling:Avoid freeze/thaw cycles.
 
Scientific 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.
 

Product Literature References

The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study: G.S. Butler, et al.; J. Biol. Chem. 273, 871 (1998), Abstract; Full Text
Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases: M.P. d’Ortho, et al.; Eur. J. Biochem. 250, 751 (1997), Abstract;

General Literature References

The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study: G.S. Butler, et al.; J. Biol. Chem. 273, 871 (1998), Abstract; Full Text

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