Proteinase K (from Tritirachium album) is a non-specific protease of the serine protease family. Proteinase K is used for the cleavage of proteins in nucleic acid preparations. It is mainly used in nucleic acid purification or for the removal of nucleases.Proteinase K is active under a wide range of reaction conditions, including elevated temperatures and presence of SDS.

Foreign activity: RNAse and DNAse not detectableOptimum temperature: +65 °C.Activity at +65 °C is ca. 12 x higher than at +25 °C. Over +65 °C, inactivation due to denaturation.Activators: Denaturating agents like SDS (0,5-1 %), urea.Inhibitors: Inhibition with Hg²⁺-ions, DFP, PMSF and phenol. Not inhibited by EDTA, sulfhydryl reagents and trypsin or chymotryps ininhibitors.

Endopeptidase for the degradation of proteins with very high solubility, specific activity and DNA purity. Extra high purified.

Activity:≥ 35 U/mg lyophilizateSpecific activity:≥ 45 U/mg proteinDNA content: ≤ 0.1 pg/mg

Working solution: 50 µg/mlReaction buffer:50 mM Tris-HCl; pH 7.5; 5 mM CaCl₂; 0.5 % SDS