The Regulator of G-protein Signaling 6 (RGS6) is a member of the RGS protein family, which negatively regulates G-protein-coupled receptor (GPCR) signaling by accelerating GTP hydrolysis on Gα subunits. RGS6 exists as multiple splice variants and contains a conserved RGS domain for Gα interaction and a GGL (G-protein γ-like) domain that enables dimerization with Gβ5. forming a complex critical for stability and function. It is broadly expressed in tissues, including the brain, heart, and cancer cells, and plays roles in neuronal development, oxidative stress response, and tumor suppression. Studies link RGS6 to diseases such as cancer, neurodegenerative disorders, and cardiovascular conditions. For instance, RGS6 acts as a tumor suppressor by promoting apoptosis and DNA repair in breast cancer, neuroblastoma, and other malignancies, while its dysfunction is implicated in Parkinson’s disease and heart failure.
RGS6 antibodies are essential tools for studying its expression, localization, and molecular interactions. These antibodies, often raised in rabbits or mice, target specific epitopes within RGS6 isoforms and are validated for applications like Western blotting, immunohistochemistry, and co-immunoprecipitation. High-quality RGS6 antibodies exhibit specificity confirmed by knockout controls or siRNA-mediated silencing. Researchers use them to explore RGS6’s tissue distribution, dynamic regulation under stress, and mechanisms in disease pathways. Challenges include distinguishing between splice variants and minimizing cross-reactivity with homologous RGS proteins. Overall, RGS6 antibodies advance understanding of its dual roles in cell survival and death, offering insights for therapeutic targeting in cancer and neurological disorders.