Researchers at NIDDK have developed polyclonal antibodies against the Regulator of G Protein Signalling (RGS) protein, RGS7. RGS7 binds tightly to Gbeta5, a unique and highly specialized G protein that exhibits much less homology than other Gbeta isoforms (~50%). RGS7 is preferentially expressed in brain and neuroendocrine tissue. Like Gbeta5, RGS7 is expressed prominently in the cell membrane, as well as in the cytosol. Although this distribution pattern suggests that complexes containing Gbeta5 and RGS7 may shuttle information between classical G protein-signaling elements at the plasma membrane and the cell interior, the function of the complex in the brain is largely unknown.
The antibodies were generated in rabbits to a glutathione S-transferase (GST) fusion protein with residues 312-469 of bovine RGS7 (antibody 7RC-1) and react with human and rodent RGS7. The antibodies (7RC-1) can be used for immunoblotting and immunoprecipitation. They can be used to facilitate our understanding of the function of Gbeta5/ RGS7 complexes in brain and neurons.
These antibodies can be used for research purposes (immunoblotting, immunoprecipitation) by those studying the biology and function of RGS7.
High-titer, multi-epitope antibodies to study RGS7 and RGS7/Gbeta5 complexes and G protein signaling.