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Catalog Number | orb420132 |
---|---|
Category | Proteins |
Description | Protease S. aureus |
Concentration | 1 mg/mL |
Form/Appearance | Lyophilized |
Purity | 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. |
Conjugation | Unconjugated |
Target | sspA |
Hazard Information | Non-Toxic |
UniProt ID | P0C1U8 |
Biological Activity | 1,980 units/mg by dry weight |
NCBI | 1280 |
Storage | Store vial at 4° C prior to restoration. For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use. |
Buffer/Preservatives | Preservative: None. Stabilizer: None. None |
Alternative names | Glutamyl endopeptidase, Endoproteinase Glu-C, Stap Read more... |
Note | For research use only |
Application notes | 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. |
Expiration Date | 12 months from date of receipt. |
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