GAL4-DBD-NR1D1-LBD-VP16-BSD

Background

NR1D1 encodes REV-ERBα, a nuclear receptor that acts as a transcriptional repressor and a core component of the circadian clock. REV-ERBα itself is expressed in a circadian pattern, particularly in metabolic tissues such as liver, skeletal muscle, adipose tissue, and brain, and it represses positive clock genes to maintain rhythmic timing. Through its target genes, REV-ERBα links the molecular clock to lipid metabolism, glucose homeostasis, and inflammatory responses, helping coordinate physiology with environmental cues. Because of these roles, REV-ERBα and its ligand-binding domain are important targets in circadian biology, metabolic disease research, and drug discovery.

Product Description & Applications

This GAL4-nuclear-receptor reporter lentivirus expresses a chimeric protein in which the GAL4 DNA-binding domain is fused to the ligand-binding domain (LBD) of NR1D1 (REV-ERBα) together with a VP16 activation domain, with blasticidin selection available. Ligand binding to the LBD drives the chimera to upstream GAL4 (UAS) response elements, activating a fluorescent or luminescent reporter such as GFP, RFP, or firefly luciferase with high signal-to-noise relative to endogenous nuclear receptor background.

By isolating LBD-mediated transactivation from endogenous receptor targets, the system enables specific pharmacological characterization of REV-ERBα ligands, including agonists and antagonists. Supplied as high-titer lentiviral particles, it supports establishment of stable cell lines for reproducible results, is amenable to high-throughput screening by luminometry, and avoids repeated transfections in circadian and metabolic drug discovery.

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 NR1D1. 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.