Specific Activity (Protein): ≥30 units/mg dry weight. A non-specific serine protease, Proteinase K will inactivate nucleases during native mRNA and DNA preparation. The enzyme cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. The smallest peptide to be hydrolyzed by this enzyme is a tetrapeptide. Recommended for high molecular weight nucleic acids from mammalian and microorganism sources. Used in the preparation of genomic DNA from bacteria. Active in the presence of SDS. Properties: 1. Stable over a wide pH range: 4.0-12.5, optimum pH 7.5-8.0 2. Not inactivated by metal chelators, by thiol-reactive reagents or by specific trypsin and chymotrypsin inhibitors 3. Activity of the enzyme is stimulated by 0.2-1% SDS or by 1-4M urea 4. Ca2+ protects Proteinase K against autolysis, increases the thermal stability and has a regulatory function for the substrate binding site of Proteinase K Applications: 1. Purification of target material from cont