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.