Proteinase K from Tritirachium album, expressed in Pichia pastoris, is a subtilisin-related serine protease. It is a highly purifed and stable endopeptidase, widely used to remove DNases and Rnases during DNA/RNA isolation. It remains stable and active in the presence of chemicals that usually denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. The optimum pH is between 7.5-9.0 and the isoelectric point is 8.9. Ca2+ (1-5 mM) is required for activation.
MW: 28.9 kDa
CAS Number: 39450-01-6
EC: 3.4.21.14
Origin: Recombinant Proteinase K from Tritirachium album
Storage buffer: 10 mM Tris-HCl, pH 7.8, 1 mM (CH3COO)2Ca, and 50% glycerol
Storage: 4 °C for short term use and −20°C for long term storage
Stability: At least 2 years from the release date
- Concentration: 20 mg/mL
- Purity: DNAses and RNAses not detected
- Specific activity: ≥ 800 U/mL
- DNA content: <0.25 pg/U by qPCR
- Bioburden: <1 CFU/mL