Rar - Hem#265

The chimera is constructed by fusing the ligand-binding domain of the retinoic acid receptor (RAR) to a reporter sequence that allows tracking (e.g., green fluorescent protein).

Development and Application of a Glucocorticoid/Retinoic Acid Receptor (GR-RAR) Chimera for In Vivo Translocation Assays Hem#265 rar

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 The chimera is constructed by fusing the ligand-binding

Do you need me to expand on the (such as specific cell lines used)? This chimeric receptor provides a robust, in vivo,

Marine-Derived Bioactive Ingredients in Functional Foods for Aging

This paper highlights a novel method that combines the ligand-binding domain (LBD) of RAR with the trafficking machinery of the GR, creating a chimeric receptor that moves from the cytoplasm to the nucleus upon ligand binding. 2. Methodology: Design of the GR-RAR Chimera