Proteinase K (PK) from fungi, Tritirachium album encodes a 40 kDa protein. The N-terminal propeptide region shows homology with bacterial subtilisin. PK crystallizes even under microgravity conditions on the space shuttle mission. PK is an effective protein system for studying protein engineering…

Proteinase K is an extracellular endopeptidase. It is synthesized by the mold Tritirachium album Limber. Proteinase K belongs to a new subfamily of the subtilisins. It is a 277 amino acid protein with a molecular weight of 28,930 Da. Active proteinase K is characterized with an unhydrolysed…

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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…

Synonyms: Endopeptidase K≥ 30 units/mg (Anhydrous) Purity Limit: ≥ 30 units/mg (anhydrous), Specific activity: ≥ 40 units/mg (protein) CAS No.: 39450-01-6 MDL No.: MFCD00132129 Appearance: Lyophilized white powder Storage Temperature: Store at ≤ -15 °C

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…