Description
Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP.
Abbr
Proteinase K, Native (Tritirachium album limber)
Source
Tritirachium album limber
Applications
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 mit ochondria Determination of enzyme l ocalization 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.
Form
Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol.
Enzyme Commission Number
EC 3.4.21.64
Activity
Type I, > 20 units per mg dry weight; Type II, > 400 u/ml
Purity
Purified to remove DNase and RNase.
Unit Definition
One Unit releases one micromole of Folin positive amino acids, measured as tyrosine, at 37°C, pH 7.5, using urea denatured hemoglobin as the substrate.
Storage
Powder: 2-8°C; Liquid: −20°C
Synonyms
Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K
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