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Matrix metalloproteinase (MMP) multipack-2

 
BML-AK014-0001 1 Kit 661.00 USD
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The MMP multipack-2 contains 10µg each of five highly active recombinant MMP catalytic domains: MMP-3, MMP-7, MMP-10, MMP-11, and MMP-12.

Product Specification

Applications:FUNC, HTS
 
Application Notes:Enzyme regulation and kinetics, comparative studies of substrate or inhibitor specificities, cleavage of target proteins. Assay or digest conditions can vary widely, but concentrations for the MMP enzymes can range between 10 and 300nM, or higher. Reaction temperatures can be between 25 and 37°C, and reaction times can range from 10 min to overnight, again depending on application and substrate. A typical assay buffer is 50mM HEPES, pH 7.0, 10mM CaCl2, 0.05% Brij-35. For more information, contact Enzo Life Sciences Technical Support.
 
Kit/Set Contains:

Contains 10µg of each enzyme, provided in a screw-cap microfuge tube.

MMP-3 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE109),

MMP-7 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE181),

MMP-10 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE329),

MMP-11  (catalytic domain) (human), (recombinant) (Prod. No. BML-SE282),

MMP-12 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE138).

 
Formulation:Liquid. Each enzyme is supplied in 50mM TRIS, pH 7.5, containing 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 30% glycerol, 0.5% Brij-35.
 
Concentration:Each enzyme is supplied at a concentration of 0.1µg/µl.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:The matrix metalloproteinases, or MMPs, are extracellular proteases that function at a neutral pH to cleave a wide variety of substrates. These include basement membrane and extracellular matrix components, growth and death factors, cytokines, and cell and matrix adhesion molecules. The broad range of substrate specificities and expression patterns of MMPs results in their involvement in many different processes, both normal and pathological. Aberrant expression has been noted in cancer, angiogenesis, arthritis, inflammation, periodontal disease, emphysema, multiple sclerosis, pre-eclampsia, and chronic wounds, among others. The general structure of an MMP protein consists of a pre domain to direct secretion from the cell, a pro domain, a catalytic domain, and a C-terminal hemopexin domain. The catalytic site involves a coordinately-bound zinc ion. The inactive, or zymogen, form of the enzyme is activated by disruption of one of the coordinate bonds, usually via proteolytic removal of the pro domain.
 
Technical Info/Product Notes:Note: MMP-3 is unique in that its pH optimum is 6.0. Activity of this enzyme in pH 7.0 buffers is significantly reduced.
Note: Human (but not mouse) MMP-11 has very unique substrate preferences, and only poorly cleaves typical MMP substrates. Use much higher substrate concentrations and longer incubation times.
 

General Literature References

Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1.: V. Noë et al.; J. Cell Sci. 114, 111 (2001),
Extrinsic regulators of epithelial tumor progression: metalloproteinases.: G. Bergers & L.M. Coussens; Curr. Opin. Genet. Dev. 10, 120 (2000),
Matrix metalloproteinases: biologic activity and clinical implications.: A.R. Nelson et al.; J. Clin. Oncol. 18, 1135 (2000),
Metalloproteinases and TIMPs.: J.F. Woessner & H. Nagase; Oxford University Press (2000),
Truncated active matrix metalloproteinase-8 gene expression in HepG2 cells is active against native type I collagen.: F. Siller-López et al.; J. Hepatol. 33, 758 (2000),
Structural properties of matrix metalloproteinases.: W. Bode et al.; Cell. Mol. Life Sci. 55, 639 (1999),
Matrix metalloproteinase degradation of extracellular matrix: biological consequences.: S.D. Shapiro; Curr. Opin. Cell Biol. 10, 602 (1998),
Relating matrix metalloproteinase structure to function: why the "hemopexin" domain?: G. Murphy & V. Knäuper; Matrix Biol. 15, 511 (1997),
The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction.: V. Knäuper et al.; J. Biol. Chem. 272, 7608 (1997),

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