Proteinase K
Our proteinase K (MW: 28.9 kDa) is a non-specific serine protease with a very high proteolytic activity (> 30 U/mg). The enzyme was expressed in Komagataella phaffii (Pichia pastoris) and is free of endogenous nucleases (DNAses, RNAses) and exonucleases. Due to its high efficiency in the digestion of native proteins, the protease is very well suited for the isolation of genomic DNA from cultured cells or tissue (e.g. mouse tails) and for the reliable inactivation of endogenous nucleases (DNAses, RNAses) during DNA/RNA preparation.
Our Proteinase K is available both lyophilized and in solution (20 mg/ml).
Properties
High stability in a wide pH range (4.0 - 12.5; optimal at pH 7.5 - 8.0)
High activity at temperatures up to 56°C and under denaturing conditions (active in the presence of SDS, urea and EDTA)
High effectiveness at low dosage (50-100 µg/ml sufficient for most applications)
Good to know
Proteinase K is secreted by cultures of the mold Tritirachium album and naturally serves the keratin digestion ('K') of the fungus to cover its carbon and nitrogen balance. Proteinase K is structurally stabilized by Ca2+ ions and preferentially cleaves peptide bonds of aliphatic, aromatic or other hydrophobic amino acids (C-terminal). In the absence of Ca2+ ions, proteinase K shows a slightly reduced activity. However, the overall activity remains high, which is why proteinase K digestion can also be carried out in the presence of EDTA. Denaturing agents such as SDS or urea serve as activators for the enzyme. Protease activity is inhibited by Hg2+ ions, DFP, PMSF, phenol, sulfhydryl reagents and trypsin or chymotrypsin inhibitors.
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