Antibody for the detection of FLAG™ conjugated proteins

Epitope tags are short peptide sequences that are easily recognized by tag-specific antibodies. Due to their small size, epitope tags do not affect the biochemical properties of the tagged protein. Most often, sequences encoding the epitope tag are included with the target DNA at the time of cloning to produce fusion proteins containing the epitope tag sequence. This allows Anti epitope tag antibodies to serve as universal detection reagents for any tag-containing protein produced by recombinant means. This means that anti-epitope tag antibodies are a useful alternative to generating specific antibodies to identify, immunoprecipitate or immunoaffinity purify a recombinant protein. The anti-epitope tag antibody is usually functional in a variety of antibody-dependent experimental procedures. This antibody is optimally suited for monitoring the expression of FLAG™ tagged fusion proteins. As such, this antibody can be used to identify fusion proteins containing the FLAG™ epitope. The antibody recognizes the epitope tag fused to either the amino- or carboxy- termini of targeted proteins. This antibody has been tested by ELISA and western blotting against both the immunizing peptide and FLAGä containing recombinant proteins. Although not tested, this antibody is likely functional for immunoprecipitation, immunocytochemistry, and other immunodetection techniques. The epitope tag peptide sequence was first derived from the 11-amino-acid leader peptide of the gene-10 product from bacteriophage T7. Now the most commonly used hydrophilic octapeptide is DYKDDDDK. Rockland Immunochemical's polyclonal antibody to detect FLAG™ conjugated proteins binds FLAG™ containing fusion proteins with greater affinity than the widely used monoclonal M1, M2 and M5 clones, and shows greater sensitivity in most assays. Affinity purification of the polyclonal antibody results in very low background levels in assays and low cross-reactivity with other cellular proteins.