recombinant from Tritirachium album, Endopeptidase K
Proteinase K is a serine protease that exhibits a very broad cleavage specificity. The Protein with a molecular weight of 28.9 kDa cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. Proteinse K is not inactivated by metal chelating reagents such as EDTA or detergents such as SDS and is active over a wide range of pH (4-12.5). Proteinase K is a highly active and stable protease with low cutting specificity. The enzyme belongs to the group of subtilisine-related serine proteases and is strongly inhibited by PMSF. In presence of 0.5-1% SDS Proteinase K inactivates DNases and RNases in eucaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of intact highly-molecular nucleic acids.
Concentration:
20 mg/ml
Molecular Weight:
Theoretical MW: 28.9 kDa
Purity:
free of RNases, DNases and Exonucleases
Form:
Proteinase K solution in 10 mM Tris-HCl, 1 mM Ca(H 3C2O2)2, 10 % (v/v) Glycerol, pH 7.8 (22C)
CAS Number:
[39450-01-6]
Application Notes:
Biological Activity: > 600 mAnsonU/ml. Application Notes: Digestion of proteins during DNA and RNA preparation
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