RXRγ Antibody

5629:

Immunoprecipitation , Western Blotting

RXRγ Antibody recognizes endogenous levels of total RXRγ protein. This antibody does not cross-react with either RXRα or RXRβ.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RXRγ protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from 293T cells, either mock transfected or transfected with human RXRα, RXRβ, or RXRγ DYKDDDK-tagged constructs, using RXRγ Antibody (upper) and DYKDDDK Tag Antibody (Binds to same epitope as Sigma's Anti-FLAG^® M2 Antibody) #2368 (lower).

Western Blotting

Western blot analysis of extracts from various tissues using RXRγ Antibody.

The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXR α, RXR β, and RXR γ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis- retinoic acid. RXRs are type-II nuclear hormone receptors that are largely localized to the nuclear compartment independent of ligand binding. Nuclear RXRs form heterodimers with nuclear hormone receptor subfamily 1 proteins, including thyroid hormone receptor, retinoic acid receptors, vitamin D receptor, peroxisome proliferator-activated receptors, liver X receptors, and farnesoid X receptor (1). Since RXRs heterodimerize with multiple nuclear hormone receptors, they play a central role in transcriptional control of numerous hormonal signaling pathways by binding to cis -acting response elements in the promoter/enhancer region of target genes (2).

RXRγ expression, unlike that of RXRα and RXRβ, is restricted largely to cardiac muscle, skeletal muscle, thyroid gland, and thyrotrope cells of the anterior pititary gland (3-6). It is posited that RXRγ plays a pivitol role in the transcriptional control of skeletal muscle differentiation as RXRγ has been found to be directly associated with the promoter regions of MyoD and myogenin (7-10). RXRγ is also involved in the transcriptional control of the hypothalamic-pituitary-thyroid axis through repression of the TSH β promoter (11-13).

1. Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
2. Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.
3. Krezel, W. et al. (1996) Proc Natl Acad Sci USA 93, 9010-4.
4. Dollé, P. et al. (1994) Mech Dev 45, 91-104.
5. Sugawara, A. et al. (1995) Endocrinology 136, 1766-74.
6. Liu, Q. and Linney, E. (1993) Mol Endocrinol 7, 651-8.
7. Georgiades, P. and Brickell, P.M. (1997) Dev Dyn 210, 227-35.
8. Downes, M. et al. (1994) Endocrinology 134, 2658-61.
9. Muscat, G.E. et al. (1994) Nucleic Acids Res 22, 583-91.
10. Downes, M. et al. (1993) Cell Growth Differ 4, 901-9.
11. Haugen, B.R. et al. (1997) Mol Endocrinol 11, 481-9.
12. Brown, N.S. et al. (2000) J Clin Invest 106, 73-9.
13. Sharma, V. et al. (2006) Endocrinology 147, 1438-51.

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• 7071 Phototope^® -HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
• 7074 Anti-rabbit IgG, HRP-linked Antibody
• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide
• 5388 RXRα Antibody
• 2554 RARα Antibody

For Research Use Only. Not For Use In Diagnostic Procedures.