Wako, 050-05941, Endoproteinase Glu C, Sequencing grade

Cleavage of polypeptide chains by protease is performed under a mild condition and, therefore, modification (oxidation, halogenation, deamidation, etc.) of side-chain amino acid residues does not occur and peptides containing the groups (binding sites in carbohydrate chains, lipids, phosphate, sulfuric acid, etc.) for modification are usually recovered in a complete form at a good yield. Segments with good reproducibility can be obtained under identical conditions of digestion. Highly substrate-specific enzymes are used for the primary structure analysis of proteins, because it is possible to roughly predict the number of fragments and their average sizes from amino-acid composition, and more importantly, because it is possible to avoid complex isolation due to partial (nonspecific) cleavages.This enzyme cleaves the C-terminal end of glutamic acid in the reaction in ammonium dicarbonate buffer (pH 7.8) or ammonium acetate buffer (pH 4.0). In the reaction in phosphate buffer (pH 7.8), the product specifically cleaves the C-terminal end of glutamic acid and aspartic acid.Degradation specificity: Reaction rate after 1 hour using insulin B chain (insulin Box) as a substrate: min 85 %