GAL4-DBD-RXRα-LBD-BSD

Background

Retinoid X Receptor alpha (RXRα, NR2B1), encoded by the RXRA gene, is a nuclear receptor activated by ligands such as 9-cis-retinoic acid. RXRα is a central heterodimerization partner for many nuclear receptors, including retinoic acid receptors, PPARs, thyroid hormone receptors, and the vitamin D receptor, and it can also form homodimers. Through these partnerships it regulates gene programs governing cellular differentiation, lipid and glucose metabolism, and immune function. Because RXRα integrates signaling from multiple receptor classes, it is an important node in metabolic and endocrine biology and a frequent target in drug discovery focused on metabolic homeostasis.

Product Description & Applications

This GAL4-DBD-RXRα-LBD-BSD lentivirus expresses a chimeric protein in which the yeast GAL4 DNA-binding domain is fused to the ligand-binding domain (LBD) of human RXRα. Upon ligand binding, the LBD changes conformation and recruits co-activators, and the chimera binds upstream GAL4 UAS elements to drive a fluorescent or luminescent reporter (GFP, RFP, or firefly luciferase). The GAL4-LBD design isolates LBD-mediated transactivation from endogenous nuclear receptor activity, giving high signal-to-noise and specificity. The system is used to characterize RXRα agonists, antagonists, and selective modulators in pharmacology and drug discovery, and is amenable to high-throughput screening by luminometry. Supplied as high-titer lentiviral particles that allow researchers to establish their own stable reporter cell lines, reducing repeated transfections.

About This Product

This lentiviral system expresses a chimeric protein consisting of the GAL4 DNA-binding domain fused to the ligand-binding domain (LBD) of RXRa. Upon specific ligand binding, the LBD undergoes conformational change and recruits co-activators; the activated chimera binds upstream GAL4 response elements (UAS×5) to drive expression of a fluorescent or luminescent reporter (GFP, RFP, or Firefly Luciferase) with high signal-to-noise relative to endogenous nuclear receptor background.

The GAL4-LBD design isolates LBD-mediated transactivation from A/B domain-driven constitutive activity and prevents cross-reactivity with endogenous nuclear receptor targets, enabling highly specific pharmacological characterization of LBD agonists, antagonists, and selective receptor modulators (SARMs/SERMs/SPPARMs). This system is established for drug discovery in academic and industrial settings, and is amenable to high-throughput screening (HTS) formats using luminometry.