Proteinase K is a broad-spectrum serine protease originally isolated from the fungus Engyodontium album (formerly Tritirachium album).
Product Name: Proteinase K, powder formulation
- Catalog No.: P2020-124
- Synonyms: Peptidase K; Endoproteinase K; Endopeptidase K
- Species: Tritirachium album
- Sequence: DNase is not detected in quality control procedure of incubation 40 µg Proteinase K with 1 µg λ DNA for 6 hours at 37°C. RNase is not detected in quality control procedure of incubation 40 µg Proteinase K with 2 µg RNA for 2 hours at 37°C. This preparation is considered as RNase and DNase free.
- Expression Host: Pichia pastoris
- Formulation: Supplied as a lyophilized powder
- Format: Below 4 °C storage temperature recommended. Short term shipping and storage at ambient temperatures do not cause activity loss.
- Purity: > 95% as determined by SDS-PAGE
The recombinant enzyme is a mutant to the native protease, which gains higher specific activity and yield as well as tolerance to a wider pH and temperature range. The large scale recombinant preparation has advantage in lot-to-lot consistency, superior purity and cost-efficiency. DNA-free nature of recombinant Proteinase K made it well-suited in isolating PCR and RT-PCR templates.
Crystal structure data indicate that the enzyme belongs to the subtilisin family, which is characterized by a catalytic triad (Asp39-His69-Ser224) in the active site.
Proteinase K does not exhibit pronounced cleavage specificity, and the preferred cleavage site is the peptide bond at hydrophobic amino acids.