Proteinase K

Proteinase K is a serine protease that exhibits a very broad cleavage specificity. The Protein with a molecular weight 28.900 kD cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. Proteinase K is not inactivated by chelating reagents such as EDTA or detergents such as SDS and is active over a wide range of pH (4 - 12.5). The enzyme belongs to the group of subtilisine-related serine proteases and is strongly inhibited by PMSF.

Proteinase K is offered as powder or in soluble form.

Customized amounts of Proteinase K Powder and Storage Buffer is available on request.

Sample request - please see below.

Proteinase K

Features of Proteinase K:

Activity: > 30 units/mg protein (hemoglobin, pH 7.5, 37°C)
Unit definition: Unit definition One unit is the amount of enzyme which releases at 37°C in 1 min as many folin-positive amino acids and peptides from hemoglobin as 1 μmol of tyrosine.
Quality: purified by chromatography and lyophilised, RNases, DNases and Exonucleases are not detectable.
Shipment: at ambient temperature
Storage: 4 °C or -20 °C for at least 24 months
Storage Buffer: 50 mM TrisHCl (pH 8,0), 1 mM CaCl2, 50 % Glyzerin (other buffers/concentrations available on request)