Proteinase K, lyophil., min 30 U/mg, 25 mg, glass

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.

Proteinase K is often used for cell and tissue disruption and for isolation and purification of nucleic acids.

The recommended working concentration: 50-100 µg/ml for protein and up to 2 mg/ml for tissue treatment.

One unit is defined as the amount of enzyme that hydrolyzes a defined casein substrate to 1 μM L-tyrosine per minute at 55 °C and pH 8.0.