Proteinase K (Recombinant), Molecular/PCR Grade
- MW:29.3 kDa
- Appearance:White to off-white lyophilized solid
Proteinase K is a highly reactive serine protease that displays the ability to digest native proteins, thereby inactivating enzymes such as DNase and RNase without recourse to a denaturation process. It is the most powerful proteinase among all proteinases characterized so far. It cleaves at the peptide bond adjacent to the carboxylic acid group of aliphatic, aromatic or hydrophobic amino acids.
Recombinant Proteinase K is used in the isolation or preparation of high molecular weight nucleic acids. It is highly pure and has a higher specific activity and is more stable at room temperature as compared to native Proteinase K.
• Recombinant Proteinase K is extremely effective on native proteins and can, therefore, be used to rapidly inactivate endogenous nucleases such as RNases and DNases. This property makes Proteinase K particularly suitable for the isolation of native RNA and DNA from tissues or cell lines.
• Promotes cell lysis by activating a bacterial autolytic factor.
• Used for the analysis of membrane structures by modifying proteins and glycoproteins on cell surfaces.
• Particularly well suited for isolating nucleic acids for amplification reactions.
• Used to remove cellular debris during the preparation of colony lifts, and to treat tissue sections to ensure efficient probe infiltration during in situ hybridization.
• Stable and active over a wide pH range of 4-12.
• Active with SDS, urea and EDTA. The most active temperature is 65°C.
• Inactivated by diisopropyl fluorophosphates (DFP) and phenyl methane sulfonyl fluoride (PMSF).
• EC #: 18.104.22.168
Not for human therapeutic use or for medicinal purposes. For research applications only.
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