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Proteinase K
Cat No.
NATZ-112
Description
Proteinase K is a serine protease, sourced from Parengyodontium album (formerly known as Tritirachium album). It exhibits robust activity across a broad range of conditions, including high temperatures and environments containing Sodium Dodecyl Sulfate (SDS).
As a versatile endopeptidase with exceptional specific activity, Proteinase K efficiently degrades proteins, including DNases and RNases, during nucleic acid extraction processes. This ensures the integrity of isolated DNA or RNA remains intact.
Produced through expression in Pichia pastoris, Proteinase K is rigorously purified to eliminate any traces of exonucleases, endonucleases, and ribonucleases, making it highly suitable for sensitive molecular biology applications.
As a versatile endopeptidase with exceptional specific activity, Proteinase K efficiently degrades proteins, including DNases and RNases, during nucleic acid extraction processes. This ensures the integrity of isolated DNA or RNA remains intact.
Produced through expression in Pichia pastoris, Proteinase K is rigorously purified to eliminate any traces of exonucleases, endonucleases, and ribonucleases, making it highly suitable for sensitive molecular biology applications.
Source
Parengyodontium album
Form
Powder or Solution
Activity
≥30 U/mg lyophilizate
≥40 U/mg protein
≥800 U/mL liquid
≥40 U/mg protein
≥800 U/mL liquid
Unit Definition
One unit of Proteinase K hydrolyzes urea-denatured hemoglobin producing the color equivalent of 1 μmol tyrosine per 1 minute at 37°C and pH 7.5 (Folin & Ciocalteu’s method), 1 U = 1 mAnsonU.
Storage
–20°C
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