Proteinase K (PK) Solution

Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples. It has been purified to remove RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparation...

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Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples. It has been purified to remove RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparations of DNA and RNA. A typical working concentration for Proteinase K is 50–100μg/ml.

Formulation: Proteinase K (PK) Solution is supplied at a concentration of 20mg/ml in 10mM Tris-HCl (pH 7.5), 1mM calcium chloride and 50% glycerol.

Features - Benefits

• Stable: Active over a pH range of 4.3–12.0 in 0.5% SDS or 1% Triton® X-100 and retains >80% of its activity at temperatures up to 60°C.
• Easy to Use: Provided in solution stable at room temperature and does not require resuspension or thawing prior to use.

References

1. Ebeling, W. et al. (1974) Eur. J. Biochem. 47, 91–7.
2. Schwartz, D.C. and Cantor, C.R. (1984) Cell 37, 67–75.
3. Cleveland, D.W. et al. (1977) J. Biol. Chem. 252, 1102–6.
4. Hames, B.D. (1981) In: Gel Electrophoresis of Proteins: A Practical Approach, B.D. Hames and D. Rickwood, eds., IRL Press, Oxford, 219.
5. Herrmann, B.G. and Frischauf, A.M. (1987) Meth. Enzymol. 152, 180–3.
6. Lee, J.J. and Costlow, N.A. (1987) Meth. Enzymol. 152, 633–48.
7. Sambrook, J. et al. (1989) Molecular Cloning: A Laboratory Manual, Vol. 3, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
8. Sweeney, P.J. and Walker, J.M. (1993) Enzymes of molecular biology. In: Methods in Molecular Biology, Vol. 16, M.M. Burrell, ed., Humana Press, Inc., Totowa, NJ, 305.

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