The E. colilacZ gene, encoding β-D-galactosidase, is extensively used as a reporter gene for detecting the expression of recombinant fusion genes and for monitoring transfection efficiency in mammalian, yeast, and bacterial cells. Although mammalian cells do contain β-galactosidases, they are generally lysosomal enzymes with low pH optima and therefore exhibit low activity at neutral pH. Combining this with the fact that E. coli β-D-galactosidase has a high turnover rate, the enzyme can be detected at very low levels, making it a sensitive reporter of gene expression.
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