Protease V.8 specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. In the presence of ammonium, the specificity is limited to glutamic sites.
Application Notes
The enzyme specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. | 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. It has also been used in a study to investigate immobilized residue-specific endoproteinases for protein sequencing.
Usage Statement
Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
Key Applications
Proteomics
| SKU | 08399001 |
| Alternate Names | SplB serine protease; endoproteinase Glu-C; Glu-C protease; staphylococcal serine proteinase; Staphylococcus V8 serine endopeptidase |
| Application Notes | The enzyme specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. | 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. It has also been used in a study to investigate immobilized residue-specific endoproteinases for protein sequencing. |
| Base Catalog Number | 399001 |
| Formulation Details | Lyophilized |
| Molecular Weight | 27;700 (by sedimentation equilbrium) |
| Pack Size | 5 mg |
| pH | pH Optima: 4.0 and 7.8 (hemoglobin substrate) |
| Preparation Method | The enzyme was isolated, by the method of Drapeau, from the culture filtrate of <i>S. aureus</i> V.8 strain. The preparation is homogenous on ultracentrifugation and disc electrophoresis. |
| Source | S. aureus; strain V8 |
| Specific Activity | ≥ 500 Units/mg |
| Specificity | The enzyme specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. In the presence of ammonium; the specificity is limited to glutamic sites. |
| Unit Definition | One unit is that amount of enzyme required to cause a change of 0.001 A280 nm per minute at 37 °C, pH 7.8, using casein as the substrate |
| Usage Statement | Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department. |
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