Proteinase K (Tritirachium album limber)

SKU: orb420129

Description

Proteinase K (Tritirachium album limber)

Images & Validation

• 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.

Key Properties

• Biological Activity: 31.4 units/mg by dry weight
• 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.
• Conjugation: Unconjugated

Storage & Handling

• 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.
• Form/Appearance: Lyophilized
• Buffer/Preservatives: None
• Hazard Information: Non-Toxic
• Disclaimer: For research use only

Alternative Names

Protease K, Endopeptidase K