Proteinase K is a highly active serine protease (MW 28,500 Da) isolated from the fungus Tritirachium album. The enzyme exhibits broad cleavage specificity on native and denatured proteins and is widely used in the purification of native RNA and DNA from tissues or cell lines. Because the solution is tested for the absence of RNases and DNases, it is especially suitable for isolating PCR and RT-PCR templates. The activity of Proteinase K is increased in the presence of denaturants such as SDS (1%) and at elevated temperature (50-60°C). The recommended working concentration is 50-100 µg/mL for protein removal and enzyme inactivation and up to 2 mg/mL for tissue treatment. Proteinase K products are free of detectable DNase and RNase.
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