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 elevated temperature (50-60°C). The recommended working concentration is 50-100µg/ml for protein removal and enzyme inactivation, and up to 2mg/ml for tissue treatment. Proteinase K products are free of detectable DNAse and RNAse.
- Broad-spectrum serine protease
- Active under denaturing conditions
- Stable at high temperatures
- Molecular biology grade
- Proteinase K is also available as a stabilized stock solution
- Inactivation of RNAses/DNAses during nucleic acid extraction
- Protein modification
- General protein digestion
- Determination of enzyme localization
Unit Definition: One AU is defined as the amount of enzyme that liberates 1.0µmol (181µg) of tyrosine from casein per minute at pH 7.5 at 37°C.
Storage: Proteinase K can be stored for 12 months at -20°C.