Nuclear receptors, such as the Retinoic Acid Receptor (RAR), are critical in gene regulation but often difficult to monitor in real-time within living cells. This paper explores the development of a GR-RAR chimeric protein, which fuses the nuclear/cytoplasmic translocation properties of the Glucocorticoid Receptor (GR) with the ligand responsiveness of RAR. This chimeric receptor provides a robust, in vivo, real-time translocation assay to detect physiological concentrations of RAR ligands, providing a powerful tool for ligand identification and subcellular trafficking analysis. 1. Introduction
Upon the introduction of the normal RAR ligand, all-trans-retinoic acid, the chimeric receptor undergoes nuclear translocation. 3. Results: Translocation Tracking Hem#265 rar
The system can detect physiological concentrations of RAR ligands. 4. Discussion and Implications Nuclear receptors, such as the Retinoic Acid Receptor