Endoproteinase Asp-N, Excision Grade, Pseudomonas fragi

Native endoproteinase Asp-N from Pseudomonas fragi. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Metalloprotease that specifically hydrolyzes proteins and the N-terminal side of aspartic acid and cysteic acid residues. Inhibited by aprotinin, DFP, leupeptin, and TLCK.

Native endoproteinase Asp-N from Pseudomonas fragi. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Metalloprotease that specifically hydrolyzes proteins at the N-terminal side of aspartic acid and cysteic acid residues. Inhibited by aprotinin, DFP, leupeptin, and TLCK. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.

Toxicity: Harmful (C)

One unit is defined as the amount of enzyme that will release a sufficient amount of azo dye from AZOCOLL Substrate (Cat. No. 194932) to produce an increase in absorbance at 520 nm of 0.001 per min at 37°C, pH 7.5.

Lyophilized from 10 mM Tris-HCl, pH 7.5.

Following reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 2 days at 4°C or for up to 1 month at -20°C.

Drapeau, G.R. 1980. J. Biol. Chem.255, 839.

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