Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachiumalkaline phosphatase) (EC 3.4.21.64) is a non-specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album. Proteinase K is routinely used for the purification of target…

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)…

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, suitable for both protein and nucleic acid isolation, it exhibits proteolytic…

A serine proteinase used to inactivate RNAse and DNAse in RNA and DNA isolation protocols. Useful in the study of membrane and protein structure. Proteinase K is a highly active protease (MW 28,500 Da) isolated from the fungus Tritirachium album . The enzyme exhibits broad specificity on…