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Proteinase K, Recombinant, PCR Grade: the Ideal Tool for Template Preparations

The endopeptidase originally isolated from the filtrate of the lower fungus Tritirachium album limber is recombinantly expressed in Pichia pastoris. Proteinase K is extremely effective on native proteins from different sources, and remains active in the presence of denaturing reagents. This makes it a useful tool in the isolation of DNA/RNA species. The proteinase is an enzyme with a molecular weight of 28.9 kDa, as shown by MALDI mass spectroscopy, and consists of a single peptide chain of 279 amino acids. Like other serine proteases, the enzyme is inactivated by sulfonyl fluoride analogs such as Pefabloc SC*. The pH activity of Proteinase K for hydrolysis of the synthetic substrate Chromozym TRY* is optimal in the range pH 6.59.5.

For the isolation of undamaged high molecular-weight nucleic acids from different sources an increased purity of the product is attained. The most stringent specification parameters and the minimized contamination result in the best quality available on the market. That means absence of endonucleases, nicking activity, and ribonucleases, a DNA content of less than 10 pg/mg, and a low bioburden content of less than 5 cfu/ml in solution, and less than 125 cfu/g in the lyophilized form.

Advantages of the new recombinant Proteinase K

  • Improved overall performance due to lot-to-lot consistency
  • Superior quality due to a minimized contaminant level
  • Reliable and sensitive tests are conducted to assay for trace contaminants, resulting in superior product purity

The performance of the new recombinant enzyme has been extensively tested and compared to the performance of the native enzyme (Figure 1). There are no differences in the performance or physical and chemical parameters compared to the native enzyme, thus no protocol changes are necessary.


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