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Proteinase K

The Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. The Proteinase K is classified as a serine protease. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.


Name Quantity Reference EUR
Proteinase K 100 mg ME-0420-10 116.70


Delivery times

   2 working days

Shipping conditions

   -20°C

Storage conditions

   -20°C

Source
Tritirachium album

Application
Proteinase K is a highly thermostable protease, which shows very little cleavage specificity. It rapidly deactivates RNases and DNases, which makes it suitable for isolation of native RNA or DNA from tissues or cell lines. This enzyme also promotes cell lysis by activation of a bacterial autolytic factor. In RNA or DNA purification procedures, it has to be used at 500 µg/ml in the presence of 1 % SDS.

Quality Control
Tested for the absence of RNases and DNases.

Unit definition
The amount of enzyme required to increase the absorbance of a haemoglobin solution to a value corresponding to 1 µmol of tyrosine in 1 minute at 25 °C.

Notes
Proteinase K is stable over a wide pH range (4–12.5). It is activated by urea and SDS and it is not deactivated by metal ions, chelating agents or (chymo-)trypsin inhibitors. The ready-to-use stability-tested Proteinase K solution contains 20 mg/ml protein in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2 and 50 %  glycerol. Store at -20 °C.

Concentration
20 U/mg

TDS

 

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