Description
Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau.
Abbr
V8 Protease, Recombinant (Staphylococcus aureus)
Species
Staphylococcus aureus
Applications
• Digestion of proteins for proteomic analysis by Mass Spectrometry • Protein and peptide identification
Product Overview
Endoproteinase GluC (Staphylococcus aureus Protease V8) is a serine proteinase which selectively cleaves peptide bonds C-terminal to glutamic acid residues. Endoproteinase GluC also cleaves at aspartic acid residues at a rate 100-300 times slower than at glutamic acid residues.
Form
Supplied freeze-dried from a Tris-HCl and sodium chloride buffer.
Activity
38.3 μmol/min/mg
Molecular Weight
29849 daltons
Synonyms
EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase
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