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 300 nM, 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 50 mM HEPES, pH 7,0, 10 mM CaCl₂, 0,05% Brij-35. For more information, contact Enzo Life Sciences Technical Support.
- NOTE: This kit now provides 10 µg of each enzyme!
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.
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.
Bestellinformation: Contents:
MMP-3 enzyme, BML-SE109-0010 (human) (recombinant)
FORMULATION: 0,1 µg/µl in 50 mM TRIS, pH 7,5, 5 mM CaCl₂, 300mM sodium chloride, 20 µM ZnCl₂, 30 % Glycerol, 0,5 % Brij-35. Purity >95 % (SDS-PAGE).
STORAGE: -70 °C; avoid freeze/thaw cycles
QUANTITY: 10 µg
SPECIFIC ACTIVITY: xxx U/µg. One U=100 pmol/min at 37ºC using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate.
PRESENTATION: Screw-cap microfuge tube.
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.
MMP-7 enzyme, BML-SE181-0010 (human) (recombinant)
FORMULATION: 0,1 µg/µl in 50 mM TRIS, pH 7,5, 5 mM CaCl₂, 300 mM sodium chloride, 20 µM ZnCl₂, 30 % Glycerol, 0,5% Brij-35. Purity >95 % (SDS-PAGE).
STORAGE: -70 °C; avoid freeze/thaw cycles
QUANTITY: 10 µg
SPECIFIC ACTIVITY: xxx U/µg. One U=100 pmol/min at 37ºC using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100µM; Prod. No. BML-P125) as substrate.
PRESENTATION: Screw-cap microfuge tube.
MMP-10 enzyme, BML-SE329-0010 (human) (recombinant)
FORMULATION: 0,1 µg/µl in 50 mM TRIS, pH 7,5, 5 mM CaCl₂, 300 mM sodium chloride, 20 µM ZnCl₂, 30 % Glycerol, 0,5% Brij-35. Purity >95% (SDS-PAGE).
STORAGE: -70 °C; avoid freeze/thaw cycles
QUANTITY: 10 µg
SPECIFIC ACTIVITY: xxx U/µg. One U=100 pmol/min at 37ºC using "MsoNormal"
