Tritirachium album Proteinase K, MP Biomedicals

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0219398105 0219398110 0219398125 0219398180 0219398190 0219398191
IC0219398105EA 56.95 USD
IC0219398105 IC0219398110 IC0219398125 IC0219398180 IC0219398190 IC0219398191
Tritirachium album Proteinase K, MP Biomedicals
Enzymes

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.


  • White powder
  • Soluble in water
  • Extinction Coefficient E1%: 14.2 (280 nm,10 mM NaCl and 5 mM CaCl2, pH 8.0) (Lit.)
  • Isoelectric point: pI 8.9 (Lit.)
  • EINECS: 254-457-8
  • pH: 7.5 to 12.00 (denatured hemoglobin as substrate) (Lit.)
  • Foreign Activity: RNase <5 x 10-4 U/mg, DNase <5 x 10-4 U/mg
  • Storage temperature: +4 °C, dessicate


Proteinase K is a stable and highly reactive serine protease


Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA. It is also useful in removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A. It is reported to be useful for the isolation of hepatic, yeast, and mung bean mitochondria. It is useful in determination of enzyme localization on membranes. It is also used in treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. Proteinase K is used in digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.


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 to 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.

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