Recombinant Proteinase K, molecular biology grade

Proteinase K is a broad-spectrum serine protease originally isolated from the fungus Engyodontium album. Proteinase K has no pronounced cleavage specificity, the preferential cleavage site is the peptide bond adjacent to hydrophobic amino acids. Recombinant Proteinase K is a mutant form of the native protease with improved activity, higher yield, and a wider activity range in terms of pH and temperature. Large-scale recombinant preparation guarantees high lot-to- lot consistency, superior purity, and cost-efficiency.

Proteinase K is commonly used in molecular biology to remove DNases and RNases from preparations of highly native undamaged nucleic acid and to non-specifically degrade proteins in lysates. Proteinase K is active in 1% Triton X-100 and fully active in 0.5% (w/v) SDS which denatures protein substrates to increase digestion rates. The enzyme works best at 50-200 ug/mL at pH 7.5-11.0, 37-70 °C and is usually denatured by subsequent phenol extraction rounds. Incubation times vary from 30 minutes to 18 hours and Proteinase K can auto digest during long incubation times.