Proteinase K, >30 mAnson U/mg

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Application Notes Proteinase K is suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Addition of either 0.5-1% of sodium dodecyl sulfate or 1-4 mmol/l of urea increases the activity, because the substrates are more easily attacked when denatured. In experiment to recover the undigested DNA, proteins were digested with 0.1 mg/ml of proteinase K. Usage Statement Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department. Key Applications Protein and nucleic acid isolation