||Recombinant His tagged RXR-LBD is isolated from an E.coli strain that carries the coding sequence of the human RXR-alpha ligand binding domain under the control of a T7 promoter. Retinoid X receptor (RXR) serves as a promiscuous heterodimerization partner for many nuclear receptors through the identity box, a 40-amino acid subregion within the ligand binding domain (LBD). RXR partners include thyroid hormone receptors (TRs), retinoic acid receptors (RARs), peroxisome proliferator-activated receptor, several constitutive active orphan nuclear receptors (e.g. Nuclear Growth Factor I-B), oxysterol receptors, and constitutive androstane receptors. RXRs also form homodimers to mediate the effects of 9-cisretinoic acid (9-cRA). Depending on these protein- protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions. The LBD is functionally complex and mediates ligand binding, receptor homo- and heterodimerization, repression of transcription in the absence of ligand, and ligand-dependent activation of transcription. Hormone binding to the structurally conserved LBD of the RXR triggers a conformational change that principally affects the conserved C-terminal transactivation helix H12 involved in transcriptional activation. Recombinant RXR-LBD is isolated from an E.coli strain that carries the coding sequence of the human RXRLBD under the control of a T7 promoter.
||Liquid. Supplied in 20mM Tris-HCl, pH8.0, 100mM KCl, 0.2mM EDTA, 1mM DTT, 20% glycerol.
||20ng are sufficient for an in vitro transcription assay and 100ng are sufficient for a protein-protein interaction assay.
||RXR-LBD has been applied in in vitro transcription assays, DNA, and protein-protein interactions assays.
||>95% by SDS-PAGE.
||For in vitro use only.
||Quality guaranteed for 12 months, store at -80℃. Avoid freeze / thaw cycles.