Pepsin (Porcine)

Pepsin endopeptidase (Porcine) is a serine Endoproteinase with its optimum activity in the acid range (pH 2.0 – pH 4.0). It predominantly cleaves peptide bonds on the carboxy side of aromatic and hydrophilic residues.

Characteristics:

Porcine Pepsin is a serine Endoproteinase with molecular weight of 35 kD. Its optimum activity is in the acid range (pH 2.0 – pH 4.0) and it predominantly cleaves peptide bonds on the carboxy side of aromatic and hydrophilic residues. However, it exhibits no hydrolytic activity if the adjacent amino acids are Valine, Alanine or Glycine. The fact that Pepsin has Proteolytic activity in the acid pH range, makes this enzyme a useful reagent for the fragmentation of proteins that are soluble exclusively in acid medium.

Application:

Pepsin, Sequencing Grade, modified is supplied lyophilized in 20 µg vials. The enzyme is typically reconstituted with 40 µL of deionized water to obtain a final concentration of 0.5 µg/µL in 50 mM Ammonium Acetate, pH 4.5. The modified enzyme retains in excess of 80% of its activity after four hours at 30°C in reaction mixture and in excess of 70% of its activity under the same conditions after 24 hours. To use, the enzyme is added to the protein sample at a ration of 1/50 (enzyme to protein, by weight) in 10 mM HCl. The incubation is allowed to proceed at 30°C for 4 hours or overnight. The Princeton Separations enzyme is stable for at least 24 hours at 30°C and the autolysis products are minimal.

Quality Control:

The modified Pepsin activity is monitored by a protease assay using bovine hemoglobin as a substrate. In addition, the process of fragmentation of a standard protein (lysozyme) is also monitored.

Price and ordering information:

Product must be shipped 2 day air

 

Price: $0.00
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Procedure Guide for Pepsin (Procine)46.86 KB

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