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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
RXRα (D6H10) Rabbit mAb 3085 40 µl
Western Blotting Immunoprecipitation
H M R 53 Rabbit IgG
RARα Antibody 2554 40 µl
Western Blotting
M R 55 Rabbit 
RXRβ Antibody 8715 40 µl
Western Blotting Immunoprecipitation
H M 70-72 Rabbit 
RARγ1 (D3A4) XP® Rabbit mAb 8965 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence
H M 58 Rabbit IgG
RXRγ Antibody 5629 40 µl
Western Blotting Immunoprecipitation
H M 55 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Retinoic Acid and Retinoid X Receptors Antibody Sampler Kit provides an economical means to investigate the expression of various subtypes of retinoic acid and retinoid X receptors. The kit contains enough primary antibody to perform four western blot experiments per primary.


Specificity / Sensitivity

Each antibody in the Retinoic Acid and Retinoid X Receptors Antibody Sampler Kit recognizes endogenous levels of total respective protein. The antibodies do not cross react with other subtypes of retinoic acid or retinoic X receptors.


Source / Purification

Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RARγ1 protein or human RXRα protein. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human RARα protein, residues near the amino terminus of human RXRβ protein, or residues near the amino terminus of human RXRγ protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

Nuclear retinoic acid (RA) receptors (RARs) consist of three subtypes encoded by separate genes: α (NR1B1), β (NR1B2), and γ (NR1B3). For each subtype, there are at least two isoforms, which are generated by differential promoter usage and alternative splicing and differ only in their N-terminal regions. Retinoids, which are metabolites of vitamin A, serve as ligands for RARs (1). RARs function as ligand-dependent transcriptional regulators and are found to be heterodimerized with retinoid X receptors (RXRs). These transcriptionally active dimers regulate the expression of genes involved in cellular differentiation, proliferation, and apoptosis (2,3). Consequently, RARs play critical roles in a variety of biological processes, including development, reproduction, immunity, and organogenesis (4-6). RAR mutations, fusion proteins, altered expression levels, or aberrant post-translational modifications result in multiple diseases due to altered RAR function and disruption of homeostasis.

In contrast to the ubiquitously expressed RARα subtype, RARγ displays a complex tissue-specific expression pattern (7). The hematopoietic system expresses significant levels of RARγ, and a recent study identified a role for RARγ in hematopoietic stem cell maintenance (8). RARγ is the predominant subtype in human and mouse epidermis, representing 90% of the RARs in this tissue (9-11). Given the high level of RARγ expression in the skin, it has been suggested that this nuclear receptor participates in a transcriptional program that governs maintenance and differentiation of normal epidermis and skin appendages. The transcriptional activity of RARγ is under stringent control, in part, through retinoic acid-induced phosphorylation and proteasomal degradation (12).

The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXRα, RXRβ, and RXRγ) 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 (13). 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 (14).


1.  Rochette-Egly, C. and Germain, P. (2009) Nucl Recept Signal 7, e005.

2.  Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.

3.  Delacroix, L. et al. (2010) Mol Cell Biol 30, 231-44.

4.  Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.

5.  Eifert, C. et al. (2006) Mol Reprod Dev 73, 796-824.

6.  Mark, M. et al. (2006) Annu Rev Pharmacol Toxicol 46, 451-80.

7.  Niederreither, K. and Dollé, P. (2008) Nat Rev Genet 9, 541-53.

8.  Mark, M. et al. (2009) Nucl Recept Signal 7, e002.

9.  Dollé, P. (2009) Nucl Recept Signal 7, e006.

10.  Giannì, M. et al. (2002) EMBO J 21, 3760-9.

11.  Purton, L.E. et al. (2006) J Exp Med 203, 1283-93.

12.  Fisher, G.J. et al. (1994) J Biol Chem 269, 20629-35.

13.  Zelent, A. et al. (1989) Nature 339, 714-7.

14.  Elder, J.T. et al. (1991) J Invest Dermatol 96, 425-33.


Entrez-Gene Id 5914, 5916, 6257, 6258, 6256
Swiss-Prot Acc. P10276, P13631, P28702, P48443, P19793


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
XP® is a trademark of Cell Signaling Technology, Inc.
Anti-FLAG® is a registered trademark of Sigma-Aldrich Biotechnology.