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. Directions for use Foreign activity: RNAse and DNAse not detectable Optimum 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 Hg 2+ -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: Ca 2+ -ions (1-5 mM) prevent autolysis. Proteinase K - Solution 20 mg/ml, ready-to-use, for biochemistry and molecular biology 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. Sterile ready-to-use solution Activity ≥ 800 mAnsonU/ ml Stable over a wide pH range: 4.0–12.5 Active at high temperatures and denaturing conditions