Description
Pepsin is a digestive protease that is specific for the cleavage at the carboxy terminus side of tyrosine (Y), tryptophan (W), phenylalanine (F), and leucine (L) bonds. Pepsin typically does not cleave at bonds containing valine, alanine, or glycine. Protea's pepsin is highly purified, resulting in a product suitable for proteomics work. Pepsin is an acidic protease, and its inactive zymogen precursor, pepsinogen, is produced in the stomach mucosa. Pepsin digestions are optimally carried out at pH 1 to 3.
