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Specifications Synonym: Pepsin A, Pepsin from hog stomachCAS Number: 9001-75-6EC Number: 232-629-3Analysis Note Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.Protein determined by E1%/280Used 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. Product P6887 is provided as a lyophilized powder and has been used to digest protein during dietary fiber analysis1.Unit Definition One unit will produce a ?A280 of 0.001 per min at pH 2.0 at 37°C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 ml. Light path = 1 cm.)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 ß chain of insulin. Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.2Preferential 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 ß chain of insulin.Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.2Quality Level: PREMIUMForm: Lyophilized powderMol. Wt.: Mol. Wt 35 kDaImpurities: Salt, essentially freeStorage Temp.: -20°CGene information: pig ... LOC396892(396892)
