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Specifications
- Source:Staphylococcus aureus, Strain V8
- Size:5 mg
- Storage Conditions:Store at 2...8 °C, –20 °C for Extended Storage
- Enzyme Name:Protease
- pH:pH Optimal: 4.0 and 7.8 (Hemoglobin Substrate)
- Cat. No.:IC399001
- Supplier no.:399001
Specifications
About this item
Protease V.8 specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids.
- Lyophilized powder that has been chromatographically purified
- Specific activity: 915 units/mg (dry weight)
- pH Optimal: 4.0 and 7.8 (hemoglobin substrate)
- Robust activity, greater than 915 units/mg protein
- Specific cleavage for glutamic acid in ammonium buffer
- Selective digestion at both glutamic and aspartic acid residues in phosphate buffer at pH 7.8
- Cleavage activity remains in the presence of many denaturing agent, such as SDS, urea and guanidine-HCl
- Lyophilized format for longer stability and easier storage
In the presence of ammonium, the specificity is limited to glutamic sites. The enzyme specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. It is used in a study to investigate immobilized residue-specific endoproteinases for protein sequencing. Protease V8 is used in a study to assess enzymatic cleaning of inorganic ultrafiltration membranes used for whey protein fractionation.
The enzyme was isolated, by the method of Drapeau, from the culture filtrate of Staphylococcus aureus V.8 strain. The preparation is homogenous on ultracentrifugation and disc electrophoresis.