Bacterial alkaline phosphatase (E. coli)
Bacterial alkaline phosphatase (E. coli) nonspecifically catalyzes the removal of most phosphomonoester bonds from the 5' and 3' termini of DNA and RNA without degrading diphosphate or triphosphate linkages. The enzyme is purified from an E. coli strain that does not harbor RNase activity. Bacterial alkaline phosphatase (E. coli) is supplied in a buffer of 50 mM Tris-HCl (pH 8.0), 100 mM KCl, 1 mM MgCl2, and 50% glycerol.
- Phosphate group removal to reduce self-ligation and vector background
- Dephosphorylation of DNA 5' termini prior to kinase labeling reactions
E. coli strain C75
Bacterial alkaline phosphatase (E. coli) is extremely stable and is not completely heat-inactivated; therefore, to inactivate the enzyme, reaction products need to be purified twice via phenol-chloroform extraction followed by ethanol precipitation.
Supplied with 10X Reaction Buffer [500 mM Tris-HCl (pH 9.0), 10 mM MgCl2]
One unit is defined as the amount of enzyme required to generate 1 µmol/min of p-nitrophenol from p-nitrophenylphosphate at 25°C and pH 8.0.
Reid, T. W. & Wilson, I. B. E. coli Alkaline Phosphatase. Enzym. 4, 373–415 (1971).
Takanami, M. Analysis of the 5'-terminal nucleotide sequences of ribonucleic acids: I. The 5'-termini of Escherichia coli ribosomal RNA. J. Mol. Biol. 23, 135–48 (1967).
Additional product information
Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.
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