High activity – broad-spectrum serine protease
Active under denaturing conditions – useful for a variety of applications
Stable – at high temperatures
Molecular biology grade – useful for general digestion of proteins
Proteinase K is also available as a stabilized stock solution
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 ideal for isolating PCR and RT-PCR templates.
The activity of Proteinase K is increased in the presence of denaturants such as SDS (1%) and 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.
Inactivation of RNases/DNases during nucleic acid extraction
General protein digestion
Determination of enzyme localization
Remove nucleases for in situ hybridization
Improving cloning efficiency of PCR products