α-Chymotrypsin Protease, MS Grade

• sizes: 50 μg
• Description: Chymotrypsin is a serine endoprotease that specifically cleaves C-terminal peptide bonds of Tyr, Phe, Trp, and Leu. It also exhibits secondary cleavage activity at the C-terminal peptide bonds of Met, Ala, Asp, and Glu. Residual trypsin activity is inhibited by TLCK during purification. The protease is activated and stabilized by Ca2+ ions.
• Physical Appearance: Lyophilized powder
• Molecular Weight: 25 kDa
• Resuspension Buffer: Reconstitute lyophilized powder in 100 μL 1 mM hydrochloric acid containing 2 μM CaCl2 (recommended).
• Storage: Store freeze-dried powder at -20 °C; store dissolved enzyme at -20 °C (valid for 1 week).
• Shelf life: 24 months at -80 ℃
• Stability: Maximally active at pH 7.8
• Usage Notes: Use α-chymotrypsin at a protease-to-protein ratio of 1:50 (w/w), and perform digestion in 100 mM Tris-HCl (pH 7.8) containing 10 mM CaCl2 at 30 °C for 2 - 12 hours.
• Activity: 70 U/mg