Pepsin, an acid protease, contains a proteolytic enzyme. Pepsin contains the "cathepsin" component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.
Pepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice.
Pepsin hydrolyzes peptide bonds, not amide or ester linkages. Pepsin cleaves peptides with an aromatic acid on either side of the peptide bond. Sulfur-containing amino acids increase susceptibility to hydrolysis when they are close to the peptide bond. Pepsin preferentially cleaves at the carboxyl side of phenylalanine and leucine and at the carboxyl side of glutamic acid residues. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin. Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.
Specific Activity: ≥1:10,000
Key Applications: Pepsin is used as a proteolytic enzyme, used to break down the proteins into their components, i.e., peptides and aminoacids
Application Areas: Molecular biology, Proteomics
Research Areas: Cell biology
Product Type: Proteins, Enzymes & Peptides
Protein or Enzyme Type: Proteins, Enzymes & Peptides
Extinction Coefficient (E1%): E1%280 = 14.7
Presentation: Off-white Lyophilized Powder
Format: Powder
Isoelectric point (pI): pH 1.0
pH: 2.5-4.5 (2% aq soln)
Foreign activity: E. coli Negative. Salmonella Negative
Moisture content: ≤10%
Solubility: Freely soluble in water; dissolves readily in 0.01 M HCl (0.5 mg/mL - clear, colorless solution); practically insoluble in alcohol, chloroform or ether.
Storage & Handling: Room Temperature