Description:
Proteinase K, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits a very broad cleavage specificity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples . It has been purified to be free of RNase and DNase activities. The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications.
Application:
Mitochondria isolation
Protein digestion for nucleic acid (DNA and RNA) purification
Removal of endotoxins bound to cationic proteins, such as lysozyme and ribonuclease A
Determination of enzyme localization on membranes
Exposure of antigen binding sites on paraffin embedded tissue sections for antibody labeling
Removal nucleases for in situ hybridization
Digestion of proteins from brain tissue samples
Protease footprinting to reveal protein-protein surface interactions
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Catalog No.
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EBY0027I
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Product Name
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Proteinase K
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Source
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Tritirachium album limber
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Appearance
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White lyophilized powder
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Activity
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≥30U/mg protein
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Molecular Weight
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29kDa(SDS-PAGE)
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CAS No.
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39450-01-6
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EC No.
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3.4.21.64
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Unit Definitions
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One unit is defined as the amount of enzyme that
will liberate 1 μmol of tyrosine per minute at 37º C, pH7.5.
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DNase residue
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Not detectable with λ DNA after 6 hours incubation at 37ºC.
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RNase residue
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Not detectable in up to 40 μg after 16 hours incubation at +25°C.。
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Inhibitors
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Proteinase K is inhibited by diisopropyl fluorophosphate and
phenylmethylsulfonyl fluoride (PMSF) and is also totally
inactivated by mercuric ions.
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Package
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100g/bottle；500g/bottle；1Kg/bottle
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