Group of RXR-alpha

Nuclear receptors form the largest known family of transcription factors and have a crucial role in nearly all aspects of vertebrate development and adult physiology by transducing the effects of hormones into transcriptional responses (1). The family is defined by two domains: (a) the central, highly conserved, DNA-binding domain (DBD) of approx. 66 amino acids, and (b) the C-terminal, structurally conserved, ligand-binding domain (LBD) of approx. 250 amino acids (2, 3). In addition to binding to DNA and activating transcription in response to 9-cis retinoic acid, RXR forms heterodimers with the receptors for thyroid hormone (TR), retinoic acid (RAR), vitamin D (VDR), prostanoids (PPAR), and numerous orphan receptors (4). RXR acts as both activator and repressor of transcription (5). In the absence of hormone, RXR (homo- or heterodimer) interacts with SMRT (silencing mediator for retinoid and thyroid hormone receptors) and N-CoR (nuclear receptor corepressor) and represses transcription through recruitment of histone deacetylases (6, 7). In the presence of hormone, RXR interacts with a number of activators including the SRC-1 family (8), CBP/p300 (9), pCAF (10) and the TRAP complex (11) to target chromatin acetylation activate of transcription (12).
Recombinant His tagged and GST tagged RXR and RXR alpha-LBD are isolated from an E. coli strain that carries the coding sequence of the human protein under the control of a T7 promoter.
RXRα can be applied in reconstituted in vitro transcription assays and protein-protein interactions assays.
Proteins are greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 20 units are sufficient for reconstituted transcription assay and 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, D. J., et al., (1995) Cell 83, 835–839
2. Glass, C. K. (1994) Endocrinol. Rev. 15, 391–407
3. Moras, D., et al., (1998) Curr. Opin. Cell Biol. 10, 384-391
4. Kliewer S.A., et al., (1992) Nature 355, 446–449
5. Glass C.K., et al., (1989) Cell 59, 697-708
6. Nagy L., et al., (1997) Cell 89, 373-380
7. Heinzel, T., et al., (1997) Nature 387, 43-48
8. Onate, S. A., et al., (1995) Science 270, 1354-1357
9. Kamei, Y., et al., (1996) Cell 85, 403-414
10. Blanco, J.C., et al., (1998) Genes Dev. 12, 1638-1651
11. Fondell, J.D., et al., (1996) Proc. Natl. Acad. Sci. USA 93, 8329-8333
12. Wolffe, A., et al., (1997) Genes Cells 2, 291-302