MP Biomedicals - 0219350490 - Proteinase K from Tritirachium album, 500mg

ITEM #: 13274896
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 e x hibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, e x cluding arginine.
Proteinase K is suitable for both protein and nucleic acid isolation. E x hibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, e x cluding 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 e x periment to recover the undigested DNA, proteins were digested with 0.1 mg/ml of proteinase K.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.
Pkg. Type : Amber Glass Bottle
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