Proteinase K from Tritirachium album 

Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp³⁹-His⁶⁹-Ser²²⁴). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

In nucleic acid isolation procedures^1,2; DNA detection in liver by flow cytometry after proteinase K digestion³

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol N-acetyl-L-tyrosine-ethylester (ATEE) per minute at pH 9.0 and 30 °C

Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removal endotoxins bound to cationic proteins such as lysozyme and ribonuclease A.
Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria
Determination of enzyme localization on membranes
Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.
Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.


.

for molecular biology

BioChemika

solution in 10 mM TRIS HCl, pH 7.5, 40% (v/v) glycerol, 1 mM Ca-acetate

≥1000 units/mg protein

M_r 27000-29000

mol wt 28.93 kDa

~20000 U/mL

DNases, none detected

RNases, none detected

phosphatases, none detected

2-8°C

1. J. Sambrook et al. Molecular Cloning: A Laboratory Manual, (1989)

2. C.G.P. Mathew Methods Mol. Biol. 2, 31, (1984)

3. J. Albro et al. Cytometry 14, 673, (1993) abstract

, Sambrook, J., et al. Molecular Cloning: A Laboratory Manual Cold Spring Harbor, NY , (1982)

Sweeney, P.J. and Walker, J.M., Burrell, M.M., Enzymes of molecular biology. Methods Mol. Biol. Towanam NJ , (1993) 16, 306

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