Endoproteinase Asp-N is a metallo endoprotease, isolated from a mutant strain of Pseudomonas fragi, which hydrolyzes peptide bonds on the N-terminal side of aspartic and cysteic acid residues. Endoproteinase Asp-N is HPLC purified, resulting in a product that is suitable for seuqencing analysis. In 100mM NH4HCO3, pH 8.5, or 100 mMTris HCl, pH 8.5, Asp-N specifically cleaves peptide bonds on the N-terminal side of aspartic and cysteic acid residues.. Self digestion may occur if temperatures above 37 C are used. A known peptide such as glucagon should be run as a control for all experiments. Specific Activity: 20KU/mg Optimal pH: 6.0-8..5 Applications: Suitable for use in Sequencing. Storage and Stability: Lyophilized powder may be stored at 4C. Reconstituted product is stable for several weeks at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Molekulargewicht:
27
Reinheit:
Homogenous on SDS-PAGE. MW: 27kD
Formulierung:
Supplied as a lyophilized powder in 10mM Tris HCl, pH 7.5. Reconstitute with 50ul sterile ddH2O.
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