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- W93891636 abstract "Epitope tagging is an experimental strategy in which a specific amino acid sequence that is recognized as an epitope by a particular antibody is incorporated into a recombinantly expressed protein. Advances in molecular biology have made it easier to prepare recombinant protein to be used as an antigen as long as the cDNA for the protein has been cloned. In many cases, proteins can be expressed as a fusion protein with glutathione S-transferase (GST) in Escherichia coli. The protein can be purified easily using glutathione agarose and can be injected into animals to raise antibody. The advantages of epitope tagging in protein-protein association experiments are as follows: (1) if a specific antibody that recognizes X protein (X is a protein of your interest) is not available, epitope-tagged recombinant X protein can be expressed and recognized by a specific antibody raised against the epitope. Using this system, the proteins that are associated with X protein can be analyzed in vitro or in vivo. Two different epitopes can be used in the same set of experiments when the two proteins have different epitope tags. The association between these proteins could be demonstrated by using antibodies directed against each epitope. (2) Even if the specific antibody against X protein is available, the epitope tagging system has remarkable advantages. When the protein-protein interactions are analyzed in cell culture by cDNA transfection, the X protein expressed from the transfected plasmid can be distinguished from the endogenous X protein. This technique is especially useful when the behavior of the mutant X proteins is analyzed." @default.
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- W93891636 date "1995-01-01" @default.
- W93891636 modified "2023-10-14" @default.
- W93891636 title "[33] Epitope tagging" @default.
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- W93891636 doi "https://doi.org/10.1016/0076-6879(95)54035-0" @default.
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