Proteinase K is a serine protease that is used in cell
culture to digest proteins in cell lysates and release
nucleic acids. It degrades proteins even in the presence
of detergents. Proteinase K cleaves peptide bonds at
the carboxylic sides of aliphatic, aromatic, or
hydrophobic amino acids. The smallest peptide to be
hydrolyzed by this enzyme is a tetrapeptide.
Proteinase K is a serine protease that is used in cell culture to digest proteins in cell lysates and release nucleic acids. It degrades proteins even in the presence of detergents. Proteinase K cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic, or hydrophobic amino acids. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide.
Molecular Weight
28.9 kDa.
CAS No.
39450-01-6
Quality Control
Appearance
White to off-white lyophilized powder.
Solubility
33.3 mg soluble in 1 mL of water.
Activity
>= 30 U/mg protein
Unit Definition
1 U releases 1.0 micromole of Folin positive amino acids measured as tyrosine using urea denatured hemoglobin as the substrate at pH 7.5 and 37°C.