Hy-Proteinase K
Cat No. N9016

Size: 100mg
Contents: Hy-Proteinase K 100mg
Specific Activity: 40 U/mg protein
Form: Contains 100 mg Hy-Proteinase K, Lyophilized Powder

Hy-Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. The Hy-Proteinase K is classified as a serine protease. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.

Active in a wide range of reaction products

  • Isolation of genomic DNA from cultured cells and tissues
  • Removal of DNases and RNases when isolating DNA and RNA from tissues or cell lines
  • Determination of enzyme localization
  • Improving cloning efficiency of PCR products

For long time storage, store the Proteinase K powder at 4C and Delution Buffer at -20℃ separately. For use, dissolved solution should be stored at -20C.

Quality Control
DNase Activity: None detectable enzyme activity with λDNA after 6 hrs incubation at 37C.
RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25C.

Definition of Activity Unit
One unit of the enzyme liberates Folin-positive amino acids and peptides corresponding to 1 μmol tyrosine in 1min at 37C, pH 7.5 using denatured hemoglobin as substrate. Enzyme activity is assayed in the following mixture: 0.08 M potassium phosphate (pH 7.5), 5 M urea, 4 mM NaCl, 3 mM CaCl2 and 16.7 mg/ml hemoglobin.

The absence of ribonucleases is confirmed by appropriate quality test, functionally tested for digestion of template DNA after in vitro transcription.

Molecular Weight 
28.9 kDa monomer.

Dilution Buffer 
50mM Tris-HCl (pH 7.5), containing 5mM calcium chloride and 50% (v/v) glycerol.

Inhibition and Inactivation 
Inhibitors: Proteinase K is not inactivated by metal chelators, by thiol-reactive reagents or by specific trypsin and chymotrypsin inhibitors. Phenylmethylsulfonyl fluoride and diisopropyl phosphorofluoridate completely inhibit the enzyme. Inactivated by heating at 95C for 10 minutes.