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.Stability: pH 4.0-12.5. pH optimum: 8,0.Also stable even when denaturing agents, e.g. SDS and urea are present.Stabilisers: Ca²⁺-ions (1-5 mM) prevent autolysis.

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.