FabAct™ Proteinase K (recombinant), Molecular Grade (Solid)
Protease K, Endopeptidase K, Tritirachium alkaline proteinase
|Calculated MW||29.3 kDa|
|Other Names||Protease K, Endopeptidase K, Tritirachium alkaline proteinase|
|Source||Tritirachium album limber gene, recombinant|
|Assay&Purity||Native PAGE and SDS PAGE;≥99%|
|Assay2&Purity2||N/A;Molecular Biology Grade|
|Application Notes||In 50 mM Tris-HCl (pH7.5), 3 mM CaCl2, 50% Glycerol|
|Storage||4°C;Lyophilized with no additives|
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Provided below are standard protocols that you may find useful for product applications.
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. The application of the molecular grade FabAct™ Proteinase K is similar to the Native Proteinase K and is used in the isolation or preparation of high molecular weight nucleic acids. However, FabAct™ Proteinase K is highly pure and has a higher specific activity and is more stable at room temperature as compared to native Proteinase K. It is stable and active over a wide pH range of 4-12. It can be used on any situation to digest native and denatured proteins. FabAct™ Proteinase K is also active with SDS, urea and EDTA and the most active temperature is 65°C. It is inactivated by diisopropyl fluorophosphates (DFP) and phenyl methane sulfonyl fluoride (PMSF).
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