Size: 100mg Contents: Hy-Proteinase K 100mg Specific Activity: 40 U/mg protein Form: Contains 100 mg Hy-Proteinase K, Lyophilized Powder Description 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. Features Active in a wide range of reaction products Applications
Storage For long time storage, store the Proteinase K powder at 4ºC and Delution Buffer at -20℃ separately. For use, dissolved solution should be stored at -20ºC. Quality Control DNase Activity: None detectable enzyme activity with λDNA after 6 hrs incubation at 37ºC. RNase Activity: None detectable ribonuclease activity after 16 hrs incubation at 25ºC. Definition of Activity Unit One unit of the enzyme liberates Folin-positive amino acids and peptides corresponding to 1 μmol tyrosine in 1min at 37°C, 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. Source 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 95°C for 10 minutes. |
