GAL4-DBD-PPARγ-LBD-BSD

Background

Peroxisome proliferator-activated receptor gamma (PPARγ, NR1C3), encoded by the PPARG gene, is a ligand-activated nuclear receptor and one of three PPAR subtypes alongside PPARα and PPARβ/δ. PPARγ is the master regulator of adipocyte differentiation and a key determinant of insulin sensitivity, lipid storage, and inflammatory tone. It is the molecular target of thiazolidinedione drugs such as rosiglitazone, which act as PPARγ agonists. Because PPARγ governs central aspects of glucose and lipid homeostasis, it is a prominent target in drug discovery for metabolic disorders, type 2 diabetes, and obesity.

Product Description & Applications

This GAL4-DBD-PPARγ-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 PPARγ. 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 PPARγ, including agonists such as rosiglitazone and antagonists. The system supports drug-discovery efforts focused on PPARγ-activating therapies 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 PPARg. 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.