Proteinase K, Recombinant

Proteinase K is a subtilisin-related serine protease that will hydrolyze a variety of peptide bonds. Proteinase K is active in a wide range of temperatures and buffers with optimal activity between 20 and 60°C and a pH between 7.5 and 12.0. Activity is stimulated when up to 2% SDS or up to 4 M urea are included in the reaction. Calcium is important for thermostability of Proteinase K but it is not required for catalysis, therefore Proteinase K is also active in buffers containing chelating agents such as EDTA.

Overview
• Form : White to Light Yellow Powder, Lyophilized from purified liquid enzyme
• Source : Mutated gene from Tritirachium album limber, Recombinant
• Specific Activity : ≥30U/mg dry weights
• Molecular Weight : 29.3 kDa

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