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Metalloproteinase from Staphylococcus aureus

Cat No.
NATE-1617
Description
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example of this would be meltrin which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands co-ordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline.
Abbr
Metalloproteinase (S. aureus)
Source
Staphylococcus aureus
Applications
Enzyme used for structural and enzymological studies. Specificity similar to that of thermolysin with preference to hydrophobic P1' residues.
Form
Lyophilized from 20 mM Tris/HCl pH 7.8, containing 5-10 mM CaCl2 .
Enzyme Commission Number
EC 3.4.24.29
CAS No.
39335-13-2
Molecular Weight
28000
Purity
> 95 % (SDS-PAGE)
Storage
at -15 °C to -25 °C
Synonyms
Aureolysin
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CatalogEXWM-4310
ProductNameaureolysin
EC No.EC 3.4.24.29
CAS No.39335-13-2
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