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Proteinase K

(from Tritirachium album) chromatographically purified lyophilized 30 mAnson-U/mg for biochemistry and molecular biology EC

Endopeptidase K, Tritirachium alkaline proteinase, Proteinase K from Tritirachium album
CAS Number:
Enzyme Commission number:
MDL number:
EC Index Number:

Quality Level

mol wt

28.93 kDa


6.2-6.8 (20 °C, 10 g/L in H2O)


1.1 g/cm3

bulk density

35 kg/m3

storage temp.


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Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removes endotoxins that bind 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.

Biochem/physiol Actions

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.

Analysis Note

Appearance (color): white
Appearance (description): lyophilisate
Activity (hemoglobin; pH 7.5; 37 °C): ≥ 30.0 mAnsonU/mg
Spec. activity (calc. on protein): ≥ 40 mAnsonU/mg
DNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectable
RNases (RNA; 2 h; 37°C): not detectable


Health hazard

Signal Word


Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK Germany


Certificate of Analysis

Certificate of Origin

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