Epitope tagging is a powerful and versatile strategy for detecting and purifying proteins expressed by cloned genes. To utilize this feature, protein expression vectors are typically engineered with a nucleotide sequence that encodes the epitope tag. The gene of interest is cloned in-frame relative to the tag and, upon expression, the protein of interest is synthesized as a fusion protein with the epitope tag. Fusion protein detection and/or purification is mediated by highly specific antibodies to the engineered protein, thus eliminating the need for antibodies to proteins from each newly cloned gene. Commonly used epitope tags include glutathione-S-transferase (GST), c-myc, 6-histidine (6X-His), FLAG, green fluorescent protein (GFP), maltose binding protein (MBP), influenza A virus haemagglutinin (HA), b-galactosidase, and GAL4.
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Regulatory Status |
RUO – Research Use Only |
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