Pepsin

Description

• General description: Pepsin is an aspartic endoproteinase isolated from pig gastric mucosa. It is mainly used for the unspecific hydrolysis of proteins and peptides in acidic media. It also provides a limited hydrolysis of native immunoglobulins to yield biologically active fragments.
• Specificity: Aspartic endopeptidase with relatively broad specificity. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions.
• Application: Pepsin has been used for the digestion of liver tissue obtained from rat.[1]
• Preparation Note: Working concentration: 0.05 to 0.5 mg/mlStorage conditions (working solution): A pepsin solution is stable at 2 to 8 °C, at least for one week, at neutral pH and under germfree conditions. Frozen aliquots of the enzyme solution are expected to be more stable.A stock solution in 10 mM HCl (5-10 mg/ml) should be stable for at least one week at 2 to 8 °C, too. Storage light protected, tightly closed.A short (2 minutes) incubation at 40 °C has negligible effect on the activity of lyophilized pepsin or pepsin in solution.
• Analysis Note: At 37 °C with hemoglobin as the substrate. One unit is the enzyme activity which liberates the amount of Tyr producing an increase in the absorbance of 0.001/minute at 280 nm.
• Other Notes: For life science research only. Not for use in diagnostic procedures.