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Pepsin from pig stomach. Its inactive precursor is the pepsinogen secreted by the main cells of the gastric mucosa. Pepsinogen is cleaved at acidic pH below 3 into the proteolytically active pepsin.
Pepsin is one of the important proteolytic enzymes in the digestive system. It is a phosphoprotein, or an endopeptidase which preferentially cleaves peptide bonds behind aromatic amino acids. The enzyme consists of 327 amino acids and has a molecular weight of about 35,000 daltons and a catalytic pH optimum of about 1.8. In non-acidic Mileu pepsin shows virtually no activity.
Activity: min. 0.7 FIP U/mg
pH (1%, H2O): 4.0-5.0
Water (K.F.): max. 6%
MW = ca. 36,000 g/mol
Aspartic endopeptidase with relatively broad specificity. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions.
Sicherheits Hinweise / SafetyH-Sätze: H315, H319, H334, H335
GHS-Symbole: GHS07, GHS08
Klassifizierungen / ClassificationEC-Nr: 232-629-3
Dokumente - Protokolle - Downloads
Here you will find information and further literature on Pepsin (EC 18.104.22.168). For further documents (certificates with additional lot numbers, safety data sheets in other languages, further product information) please contact Genaxxon biosience at: email@example.com or phone: +49 731 3608 123.