Endoproteinase Asp-N, Sequencing Grade

for Biochemistry

<Protein Engineering> <Amino Acid Sequencing Analysis Reagent> <Enzyme for sequence analysis> 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 specifically cleaves the N-terminal end of aspartic acid residue in proteins and peptides.The solution after preparation should be stored -20 degrees centigrade.Specificity: Reaction rate after 1 hour using glucagon as a substrate: min 90%.

Manufacturer:	FUJIFILM Wako Pure Chemical Corporation
CAS RN:	9001-92-7
GHS:	Danger
Appearance:	Lyophilisate
Origin / Source:	Pseudomonas fragi mutant
Specfic Activity:	min. 20,000 units/mg protein
Purity:	min. 90 % (SDS-PAGE)

 
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