of the target protein, and highly immunoreactive. The FLAG epitope is
a synthetic epitope that consists of eight amino acid residues (DYKDDDDK).5
The c-myc epitope is derived from the human c-myc gene and contains
10 amino acid residues (EQKLISEEDL).6
In addition to the epitope
tag sequences, the pCMV-Tag1 vector contains features for expression of
fusion proteins in eukaryotic cells. The cytomegalovirus (CMV) promoter
allows constitutive expression of the cloned DNA in a wide variety of
mammalian cell lines. The neomycin-resistance gene is under control of
both the prokaryotic b
-lactamase promoter to
provide kanamycin resistance in bacteria and the SV40 early promoter to
provide G418 resistance in mammalian cells. The multiple cloning site
(MCS) of the pCMV-Tag1 vector is arranged to allow a variety of cloning
strategies to be used, resulting in C-terminal, N-terminal or internal
tagging of the protein of interest. A Kozak consensus sequence of GCC(A
provides optimal expression of the fusion protein
when the N-terminal FLAG epitope tag is used. Other cloning options, which
require fusion proteins to include their own translational start sequence,
are also possible.
Cloning Strategies for Epitope Tagging
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