RXRα Recombinant Rabbit mAb

RXRα (retinoid X receptor alpha, also known as NR2B1) is a key member of the nuclear receptor superfamily. It consists of approximately 462 amino acids and contains an N-terminal A/B domain, a conserved DNA-binding domain (DBD), a hinge region, and a C-terminal ligand-binding domain (LBD). The DBD mediates recognition of target DNA cis-elements, while the LBD is responsible for ligand binding, dimerization, and AF-2-mediated transcriptional activation. RXRα can form homodimers and homotetramers, and serves as a universal heterodimeric partner for multiple nuclear receptors, including RAR, PPAR, LXR, VDR, TR, and FXR, thereby regulating a broad range of physiological processes such as cell proliferation, differentiation, apoptosis, lipid metabolism, immune inflammation, and embryonic development. Its endogenous ligand is 9-cis retinoic acid, and it can also be modulated by dietary fatty acids such as DHA. Beyond classical nuclear transcriptional regulation, RXRα has important non-genomic functions: it can regulate mitochondrial apoptosis, PI3K/AKT survival signaling, and inflammatory responses in the cytoplasm; in tumor cells, it can be proteolytically cleaved to generate a truncated form, tRXRα, which promotes inflammation and tumor progression; during mitosis, it can be phosphorylated by CDK1 and translocate to the centrosome, where it participates in centrosome assembly through phase separation. Abnormal expression or modification of RXRα is associated with cutaneous T-cell lymphoma, colorectal cancer, metabolic syndrome, and neurodegenerative diseases, and the FDA-approved drug bexarotene (Targretin) is an RXR-based anticancer agent.