Asp-N Protease

Asp-N protease, also called endoproteinase Asp-N and flavastacin, is a zinc metalloendopeptidase. It is highly specific and cleaves peptide bonds on the N-terminal side of aspartic acid residues, and to a lesser extent, glutamic acid (E) residues. It is derived from a mutant strain of Pseudomonas fragi, and has a molecular mass of 27 kDa. In the presence of zinc, it shows optimal activity in a pH range of 4–9 and can remain active under denaturing conditions. Asp-N Protease can be used in combination with other proteases, such as trypsin, for improved protein digestion. Mass spectrometry grade Asp-N protease can be used for peptide matching, protein identification, in-solution and in-gel digestion of proteins, and peptide mass fingerprinting. Visit the enzyme page for more product information.