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| Product Name | Protease, S. aureus V8 (Endoproteinase Glu-C) |
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| Description | Chromatographically purified. Endoproteinase-Glu-C Protease from S. aureus V8 specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acid. In the presence of ammonium buffers, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27,000 daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. It is 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 (Methods Enzymol., 45, 469, 1976). Activity: ≥500 units per mg dry weight Absorbance (A280) at 1 mg/ml: As reported Unit Definition: One Unit causes a change of 0.001 absorbance unit (at 280nm) per minute at 37°C, pH 7.8 using casein as the substrate. Extinction Coefficient: 4.26 Optimum pH: 4.0 and 7.8 with hemoglobin substrate Inhibitors: Diisopropyl fluorophosphate (DFP) and monovalent anions such as F-, Cl-, Br-, CH3COO-, and NO3 |
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| Size | 1mg, 5mg |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | EC=3.4.21.19 |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | P9075 |
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| Order / More Info | Protease, S. aureus V8 (Endoproteinase Glu-C) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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