Bacterial alkaline phosphatase (E. coli) nonspecifically catalyzes the removal of most phosphomonoester bonds from the 5" and 3" terminiofDNA and RNA withoutdegrading diphosphate or triphosphate linkages. The enzyme is purified from an E. coli strain that does notharbor 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.