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|Storage Temperature:||Below -10oC|
|Formulation:||In powder form|
|Stability:||> 2 years below -10oC|
|Source:||Parengyodontium album (Tritirachium album)|
|Expression:||Recombinant from Parengyodontium album (Tritirachium album)|
|Specificity:||Proteinase K from Parengyodontium album (Tritirachium album) is a subtilisin-related serine protease with broad substrate specificity for hydrolysis of peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. It is able to hydrolyse peptide bonds in the presence of Triton, SDS, urea and EDTA.|
|Specific Activity:||> 40 U/mg protein (37oC, pH 7.5 on urea-denatured haemoglobin)|
|Unit Definition:||One Unit of Proteinase K will hydrolyse urea-denatured hemoglobin to produce a colour (by Folin-Ciocalteu reagent) equivalent to 1 µmole of L-tyrosine per min at pH 7.5 and 37oC. 1 U = 1 mAnsonU.|
|Application examples:||Proteinase K can be used for removal or inactivation of proteins in various analytical or research applications. It is used to inactivate nucleases during isolation of DNA and RNA. Activity in the presence of EDTA permits the use of EDTA in the purification of DNA or RNA to inhibit calcium dependent nucleases.|
High purity Proteinase K (Molecular Biology Grade) from Parengyodontium album (Tritirachium album) for use in research and analytical applications.
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