Recombinant DNA technology allows the addition of short pieces of well-defined tags, "peptides" or proteins at the amino or c-terminus of target genes, which can provide 'affinity handles' designed to bind specific matrices.
Therefore, tags enable a selective identification and purification of the protein of interest.
Eukaryotic genes are often cloned into E.
coli B-galactosidase (lacZ) gene, resulting in the expression of a desired protein as a fusion hybrid with B-galactosidase (1-3).
Anti-B-galactosidase antibodies allow a simple isolation of fusion proteins directly from the crude bacterial lysates, using immunoaffinity chromatography (1-5) or used in immunoprecipitation.
Anti-Beta galactosidase can also be used for the immunocytochemical detection of B-galactosidase in cells and tissues that express transfected bacterial lacZ gene (6).
Ant-beta galactosidase may be used in various immunoassays to identify the expression of beta-galactosidase fusion protein.