SG-Aspartic-N™
SG-Aspartic-N™ is a metallo-endoproteinase, isolated from a mutant strain of Pseudomonas fragi that specifically hydrolyzes peptide bonds on the N-terminal side of aspartic acid and cysteine residues. It has an optimal activity at pH6.5-8.0.
SG-Aspartic-N™ is subjected to extensive purification to remove contaminating proteases, which could affect the specificity of the digestion process. The highly purified SG-Aspartic-N™ is subsequently modified chemically, resulting in increased resistance to autolysis and improved stability.
For protein fragmentation the enzyme is added to the protein to be digested at a ratio of 1:100 to 1:50, by weight in a standard digestion buffer (50mM Tris.HCl, pH 8.0, 50mM sodium phosphate pH 8.0, or 50mM (NH4)HCO3). Ideally incubate at 25-30°C for 2 to 6 hours; but can be extended to 24 hours if required. For overnight incubation a ratio of 1:100, enzyme to protein is adequate for most proteins.
FEATURES
- Modified Aspartic-N for sequence analysis.
- Resistant to autolysis and degradation.
- High Specificity, free from other known endopeptidases.
- Consistency of activity levels from lot to lot for reproducible digestions.
- Recommended SG-Aspartic-N™ to protein ratio, 1:100 to 1:50.
APPLICATIONS
- Digestion of proteins for sequence analysis.
- Suitable for sequencing applications.