Proteinase K is a highly active serine protease with broad cleavage specificity on native and denatured proteins.
Proteinase K is widely used in the purification of native RNA and DNA from tissues or cell lines, as well as for many other applications.
- 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
- Protein modification
- General protein digestion
- Determination of enzyme localization
- Remove nucleases for in situ hybridization
- Improving cloning efficiency of PCR products