GNG5 polyclonal antibody

Heterotrimeric G proteinsfunction to relay information from cell surface receptors to intracellular effectors. Each of a very broad range of receptors specifically detects an extracellular stimulus (a photon, pheromone, odorant, hormone or neuro transmitter) while the effectors (e.g., adenylcyclase), which act to generate one ormore intracellula rmessengers, are less numerous. In mammals, G protein α, β and γ polypeptides are encoded by at least 16, 4 and 7 genes, respectively. Most interest in G proteins has been focused on their α subunits, since these proteins bind and hydrolyze GTP andmost obvously regulate the activity of the beststudied effectors. Evidence, however, has established an important regulatory role for the βγ subunits. It is becoming increasingly clear that different G protein complexes expressed in diffeent tissues carry structurally distinct members of the γ aswell astheαand β subunits and that preferential associations between members of subunit families increase G protein functional diversity.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of GNG5 polyclonal antibody at 1:500 dilution Lane1:HEK293T whole cell lysate Lane2:RAW264.7 whole cell lysate Lane3:H9C2 whole cell lysate