GAL4-DBD-PPARα-LBD-BSD

Background

Peroxisome proliferator-activated receptor alpha (PPARα, NR1C1), encoded by the PPARA gene, is a ligand-activated nuclear receptor and one of three PPAR subtypes alongside PPARγ and PPARβ/δ. PPARα is highly expressed in liver, heart, and other oxidative tissues, where it governs fatty acid uptake and oxidation, ketogenesis, and overall energy homeostasis; its activation lowers circulating triglycerides. PPARs collectively act as central regulators of lipid and glucose metabolism. PPARα is widely studied for its roles in dyslipidemia, fatty liver disease, and cardiovascular health, and is a recognized target in metabolic drug discovery.

Product Description & Applications

This GAL4-DBD-PPARα-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 PPARα. 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 for investigating ligand interactions with PPARα. The system is used to characterize PPARα 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 PPARa. 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.