Human RGS8 Antibody

RGS8 (Regulator of G-protein signaling 8) is a 22-23 kDa (predicted) member of the B/R4 subfamily, RGS family of proteins. It is expressed in NK cells and neurons, particularly cerebellar Purkinje cells, and is known to regulate GPCR signaling. When GPCRs are activated, a GPCR cytoplasmic domain associated G alpha beta gamma heterotrimer dissociates in response to GTP binding. This generates G alpha:GTP and G beta gamma dimers that initiate downstream signaling. G alpha has GTPase activity, and when GTP is hydrolyzed, the G alpha beta gamma trimer reforms and stops signaling. RGS8 potentiates G alpha GTP hydrolase activity, particularly when associated with M1 muscarinic acetylcholine receptors. Human RGS8 is 180 amino acids (aa) in length, and is characterized by the presence of one RGS domain (aa 56-171), and an N-terminal GPCR binding motif (aa 6-9). There is one splice variant that shows a 27 aa substitution for aa 1-9. Expression of this variant may negatively impact its regulation of G alpha-coupled responses. Over aa 10-76, human RGS8 shares 98% aa identity with mouse RGS8.