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-cis-retinoic acid (9-cRA). Depending on these protein-protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions (1, 2). 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 (3). 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 (4). Coactivators directly recruited by liganded receptors include members of the steroid receptor coactivator/p160 family such as SRC-1, transcriptional intermediary factor 2/glucocorticoid receptor interacting protein 1, and RAC3/activator of thyroid and retinoic acid receptors/amplified in breast cancer 1 (5).

Recombinant GST-RXR-LBD is isolated from an E. coli strain that carries the coding sequence of the human RXR-LBD under the control of a T7 promoter.
GST-RXR-LBD has been applied in DNA and protein-protein interactions assays.

The purified fusion protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 100 units are sufficient for a protein-protein interaction assay.
variable in different lots

1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA

References:
1. Mangelsdorf et al., (1995) Cell 83, 841-850
2. Mangelsdorf et al., (1995) Cell 83, 835-839
3. Nakashima et al., (1999) Science 284, 479-482
4. Egea et al., (2001) J. Mol. Biol. 307, 557-576
5. Leo et al., (2000) Gene 245, 1-11

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