Enzyme, Protein Biology, COVID-19 

Proteinase K, Recombinant, PCR Grade

  • Catalog Number : ER1021
  • Number : ER1021
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Proteinase K is a stable serine protease with broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. Proteinase K was isolated from a fungus able to grow on keratin and the enzyme can digest native keratin (hair), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. Proteinase K is used for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids. PCR grade recombinant Proteinase K is derived from yeast based on the optimized gene of Engyodontium album by site-directed mutation. It is purified by chromatography process, and with calcium and glycerin as protective agents. Free of DNase and RNase.

General Information

Application Cell
Assay principle Reconstitute lyophilized recombinant proteinase K in 50% glycerol solution and store at -20°C.Please avoid repeated freeze-thaw cycles after reconstitution.
Purity >95% (SDS-PAGE)
Storage instruction The lyophilized recombinant proteinase K has been sterilized and filtered through a 0.22 µm filter, which can maintain its activity for a long time at 2-8°C. It is recommended to store at -20°C for long-term storage.


Viral DNA/RNA isolation

DNA/RNA Experiment, for DNA/RNA Isolation



Source: Yeast

Physical Appearance: White or light beige lyophilized powder 

Bioactivity: ≥30U/mg

E.C. No.:

Quality control: DNase and RNase Non-detection

Expiry date: 24 months.



1-5 mM Ca2+ is required for activation. When calcium is removed from the enzyme (addition of EDTA) 25% of the catalytic activity is lost. However, if the EDTA-Ca2+ complex is removed from the enzyme solution by gel filtration, a total of 80% of the enzyme activity is lost and only a small activation will occur upon addition of excess Ca2+ to the Ca2+-free enzyme.


Proteinase K is inhibited by DIFP or PMSF (the latter used at final concentration 5 mM). It is partly inactivated, but not inhibited, by EDTA (see Activators). Proteinase K is not inhibited by iodoacetic acid, the trypsin-specific inhibitor TLCK, the chymotrypsin specific inhibitor TPCK and phloromercuribenzoate.



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