性能描述

form       powder 
mol wt    mol wt 35 kDa 

Pepsin is commonly used in the preparation of Fab fragments from antibodies. The optimal pH for the pepsin reaction is 1.5-2.5, which will not be detrimental to the antibody if it is not exposed for longdurations to the low pH. Solutions should be adjusted to neutral
pH for storage. The control of pepsin digestion of antibodies has been reported.For general digestion of proteins, suggested conditions are a 0.4% solution of pepsin in 10 mM HCl, and  digestion for 30 -90 minutes at 37  ° C.Pepsin has an optimal activity with native proteins at
approximately pH 1.0, but with some denatured proteins the optimal activity is at approximately pH 1.5-3.5.Pepsin is inhibited by several phenylalanine -conta ining peptides.

Preparation Instructions
Pepsin is soluble in deionized water at 1% (10 mg/ml) and at 0.4% (4 mg/ml) in cold 10 mM hydrochloric acid.
Storage/Stability
Solutions at pH 4.4 are stable at -20 ° C for about 2-3 months.Pepsin is not active when not at an acidic pH and a solution is stable at pH 6 - 7. Bringing the pH up to 8; however, will irreversibly inactivate pepsin. Pepsin is irreversibly denatured at pH 8.5-11 at room temperature.

Application
Used to produce F(ab′)2 fragments of antibodies.
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.

Biochem/physiol Actions
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.2

Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. 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.