Protease S. aureus
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- Purification
- 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 27,000 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.
- Biological Activity Comment
- 880 units/mg
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- Application Notes
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Application Note: Protease S. aureus has shown that one unit causes a change of 0.001 A280 nm per minute at 37° C at pH 7.8 using casein as a substrate. Specific conditions for reactivity should be optimized by end user.
- Comment
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Synonyms: Glutamyl endopeptidase,Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase
Background: 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 27,000 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. Protease S. aureus is ideal for investigators involved in enzyme and infectious diease research.
Gene Name: sspA
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
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Reconstitution Volume: 1.0 mL
Reconstitution Buffer: Restore with deionized water (or equivalent)
- Concentration
- 1 mg/mL
- Buffer
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Buffer: None
Stabilizer: None
- Preservative
- Without preservative
- Storage
- 4 °C,-20 °C
- Expiry Date
- 12 months
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- Gene ID
- 1280
- UniProt
- P0C1U8
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