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Retinoid X receptor beta (RXRβ), like other members of the RXR subfamily, possesses a characteristic tripartite modular structure consisting of (a) a highly conserved central region containing the C4/C5 zinc-finger domain, which is responsible for DNA binding; (b) a relatively well-conserved C-terminal region, which contains the hormone binding and dimerization domains; and © a variable N-terminal domain, which has been implicated in either transactivation or repression of target genes. Variability within the N-terminal domain is thought to be the result of alternative splicing and/or differential promoter usage. The murine RXRβ was initially identified because of its ability to bind to the regulatory region II in the murine major histocompatability complex (MHC) class I promoter and is therefore also referred to as H-2RIIBP. Genetic ablation of murine Rxrb produced approximately 50% lethality in utero and males that survived had defects of spermatazoa, which resulted in sterility. Further studies revealed that expression of a Rxrb mutant with an impaired AF-2 core led to abnormal lipid metabolism in Sertoli cells, suggesting functional interactions between Rxrb and other nuclear receptors that control lipid metabolism. This antibody can recognize the RXRβprotein, and give a 58kd band.