Proteinase K (Tritirachium album limber)

• Catalog Number: orb420129
• Category: Proteins
• Description: Proteinase K (Tritirachium album limber)
• Conjugation: Unconjugated
• Form/Appearance: Lyophilized
• Buffer/Preservatives: None
• Purity: A lyophilized powder. Chromatographically purified to remove DNase and RNase activity. Stable over a wide pH range : 4.0-12.5, optimal pH 7.5-8.0, using denatured hemoglobin as substrate. Although calcium ions do not affect the enzyme activity, they do protect Proteinase K against autolysis and increase thermal stability when present at a concentration of 1-5µmoles. It retains its activity in the presence of SDS or urea (0.5-1% SDS and 1-4M urea). Raising the temperature of the reaction from 37°C to 50-60°C can increase the activity several fold. Proteinase K is inactivated by diisopropyl fluorophosphate or phenyl methane sulphonyl fluoride. Chelating agents such as citrate and EDTA have no effect on the enzyme activity. Proteinase K can also be inactivated by heating above 65°C for 15-20 min or by extraction with phenyl/chloroform.
• Application notes: Proteinase K is specifically formulated for molecular cloning, nucleic acid research and protein/peptide structural analysis. One unit liberates one µmole of Folin positive amino acids, measured as tyrosine, at 37° C at pH 7.5 using urea denatured hemoglobin as the substrate. Recommended working concentration 0.05-0.1mg/mL.
• Biological Activity: 31.4 units/mg by dry weight
• Storage: Store vial at 2-8°C prior to restoration. Solutions in 50mM Tris-HCl, pH 8.0, 1mM CaCl2 stored at 2-8°C are stable for months.
• Alternative names: Protease K, Endopeptidase K
• Hazard Information: Non-Toxic
• Note: For research use only