Antibody TurboGFP-Trap

for biochemistrycell imagingprotein

Fluorescent fusion proteins are popular tools to study protein localization and cellular dynamics. These constructs usually fuse the entirety–or at least a functional domain–of a target protein to one of the many types of reporter fluorescent proteins. The dimeric green fluorescent protein TurboGFP is derived from the green fluorescent protein CopGFP of the copepod Pontellina plumata (Shagin et al., 2004). It possesses bright green fluorescence with excitation maximum at 482 nm and emission maximum at 502 nm. TurboGFP is a fast maturating protein — its fluorescent signal within a cell is visible sooner than other green fluorescent proteins. TurboGFP shares only about 20 % sequence identity with jellyfish GFP variants. Therefore, most anti-GFP antibodies do not bind to TurboGFP – including our GFP-Nanobody used in GFP-Trap. It’s easy to image cells using a TurboGFP-fusion protein construct, though to get the full picture such imaging data is often combined with additional biochemical information for the protein (or protein domain) of interest. For such biochemical experiments, typically a second fusion protein is designed using a different “tag” domain that allows for purification. These additional in vitro analyses can be used to confirm functionality of the “tagged” fusion construct, as well as to pull out multi-protein complexes that may form in the cellular milieu. The lack of specific, reliable, and efficient reagents has limited the use of GFP, and related fluorescent fusion proteins, for use in both cell biology studies and direct biochemical analysis.