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Analyze GST fusion proteins – in a tube

Fusion of proteins to Glutathione S-Transferase (GST) of Schistosoma japonicum is a common technique to increase solubility and expression level of a protein. This tag also serves the additional function of an affinity tag for GST-fusion proteins. Binding of GST was historically accomplished by its natural substrate Glutathione SH, but now usually performed with conventional antibodies. GST-fusions are often used in protein-protein interaction studies and biochemical analysis. Both approaches require highly specific tools to isolate and detect GST-fusion proteins. The conventional approach usually yields heavy and/or light chain contaminants. Now, with the GST-Trap, it is possible to yields a much cleaner result free from these contaminants in under 30 minutes. Save time, save effort and get cleaner results.

The secret to GST-Traps success are the use of super-high affinity Camelidae antibody fragments called Nanobodies. GST-Traps may be used for immuno-precipitation, immuno-purification and immuno-pull down experiments with up to 10-fold better purity and yield than that of classic mouse monoclonal antibodies. Compatible with a variety of source materials, Nano-Traps may be used with mammalian cells, tissues & organs, bacteria, yeast and even plants. These reagents allow your GST-fusions to be perfect candidates for immunoprecipitations, Co-IP, mass spectroscopy, and enzyme activity measurements.

GST-Trap for immunoprecipitatations

Immunoprecipitations (IP) of GST from protein extracts of GST-expressing E.coli cells. 
Input (I), non-bound (FT) and bound (B) fractions were separated by SDS-PAGE followed by Coomassie staining and Western Blotting. Unlike conventional antibodies, the GST-Trap is free from heavy and/or light chain contaminants and therefore yields cleaner results.

Camelidae single-domain antibodies are like IgGs on steroids

The family of animals known as Camelidae (camels, dromedaries, llamas and alpacas) produce functional antibodies devoid of light chains, so called "heavy chain" antibodies. These heavy chain antibodies recognize and bind their antigens via a single variable domain. When cleaved from their carboxy tail, these barrel-shaped structures (2x3 nm) are extraordinarily small, naturally-occurring, and intact antigen binding fragments (MW  of 13 kDa). These fragments, called Nanobodies, are characterized by high specificity and affinities in the low nanomolar range, and dissociation constants in the sub-nanomolar range (typically 10- to 100-fold better than mouse IgGs). The compact size of Nanobodies makes them extremely stable at temperatures up to 70°C, and functional even in 2M NaCl or 0.5% SDS. These small and powerful antibody fragments can be used in a variety of unique applications. They will open up your research possibilities.