Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Tags: His tag C-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant human MMP24 protein
Biological activity>120mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 per min. at 37°C, pH 7.5.
Purity> 90 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthProtein fragment
Predicted molecular weight23 kDa including tags
TagsHis tag C-Terminus
Our Abpromise guarantee covers the use of ab157081 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Measurement of catalytic activity
- Preparation and stability of solutions:
- Peptide hydrolysis buffer: 50mM TRIS-HCl, pH 7.5, 150mM NaCl, 5mM CaCl2, 0.025% Brij 35. Solution is stable for several weeks at 4°C.
- Stock solution of peptide substrate: 100µM solution of Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg in 20% DMSO. Store at -20°C.:
- Stock solution of unquenched peptide: 10µM solution of (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-NH2 (Mca-Pro-Leu) in 20% DMSO. Store at -20°C.:
- The activity of MMP-24 is measured fluorimetrically with a synthetic internally quenched fluorescent substrate according to Knight et al. An excitation wavelength of 328nm and an emission wavelength of 393nm are set in an appropriate fluorimeter. The instrument is calibrated with the unquenched peptide Mca-Pro-Leu at a concentration corresponding to between 2 and 10% hydrolysis of the protease substrate. Kinetic reactions are conveniently carried out in a constant volume of 2.5ml. The substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg is diluted in peptide hydrolysis buffer to a concentration of 0.8µM and equilibrated at a temperature of 37°C. Aliquots of 2 to 4µl of the activation mixture are than added and the increase in fluorescence is recorded over a time interval between 2 and 12 minutes. Activity units per ml enzyme solution are calculated according to the following equation: Activity (U/ml) = (CMca-Pro-Leu/FMca-Pro-Leu) x (dFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg/Venzyme) x Vtotal CMca-Pro-Leu: Concentration of Mca-Pro-Leu used for calibration of the fluorimeter (µmoles/ml). FMca-Pro-Leu: Fluorescence of Mca-Pro-Leu at the concentration CMca-Pro-Leu used for fluorimeter calibration. dFMca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg: Change in fluorescence during peptide hydrolysis per min. Vtotal: Volume of peptide hydrolysis reaction (2.5ml). Venzyme: Volume of added enzyme (0.002 to 0.004ml).
- The catalytic domain of MMP-24 is inhibited by tissue inhibitors of MMP-2 (TIMP-2) and by chelators of divalent cations like EDTA or o-phenanthroline.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Please see notes section.
Constituents: 0.06% Calcium chloride, 0.79% Tris HCl, 0.88% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Matrix metallopeptidase 24
- Matrix metallopeptidase 24 (membrane inserted)
- Membrane type 5 matrix metalloproteinase
FunctionActivates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin.
Tissue specificityPredominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.
Sequence similaritiesBelongs to the peptidase M10A family.
Contains 4 hemopexin-like domains.
DomainThe conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
modificationsThe precursor is cleaved by a furin endopeptidase.
Cellular localizationCell membrane and Secreted > extracellular space > extracellular matrix. Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab157081 has not yet been referenced specifically in any publications.