Adding highly antigenic peptides, called epitope tags, to the amino or carboxy terminus of a protein enhances the ability of com
mercially available antibodies to be used for Western blotting and immunoprecipitation. Which of the following best describes how epitope-tagged proteins are produced? A. A unique peptide sequence, like the FLAG epitope, is chemically crosslinked to the mature protein of interest.
B. The gene encoding the protein of interest is modified to include a short sequence of amino acids that is not commonly found in proteins.
C. An epitope tag consisting of a long stretch of nonpolar amino acids is incorporated into the protein of interest.
D. A sequence of amino acids common to most proteins in the cell is added to the gene for the protein of interest.
Epitope tagging is a method wherein a realized epitope is intertwined to a recombinant protein by methods for hereditary designing. By picking an epitope for which an immune response is accessible, the procedure makes it conceivable to recognize proteins for which no counter acting agent is accessible.
This is particularly helpful for the portrayal of newfound proteins and proteins of low immunogenicity. By determination of the fitting epitope and antibody pair, it is conceivable to discover a blend with properties that are appropriate for the ideal test application, for example, Western blot analysis, affinity purification, immunoprecipitation, immunochemistry.
