Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

Retinoic Acid and Retinoid X Receptors Antibody Sampler Kit #8589

Kit Includes Quantity Applications Reactivity MW (kDa) Isotype
RXRα (D6H10) Rabbit mAb #3085 40 µl W IP H M R 53 Rabbit IgG
RARα Antibody #2554 40 µl W M R 55 Rabbit
RXRβ Antibody #8715 40 µl W IP H M (R) (Mk) (B) (Dg) (Pg) 70-72 Rabbit
RARγ1 (D3A4) XP® Rabbit mAb #8965 40 µl W IP IHC-P IF-IC H M (R) (Hm) (B) (Dg) 58 Rabbit IgG
RXRγ Antibody #5629 40 µl W IP H M (R) (Mk) (B) (Dg) 55 kDa Rabbit
Anti-rabbit IgG, HRP-linked Antibody #7074 100 µl Goat

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  Mk=Monkey  B=Bovine  Dg=Dog  Pg=Pig
Species enclosed in parentheses are predicted to react based on 100% sequence homology.

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 and C6 cells using RARα Antibody #2554.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using RXRα (D6H10) Rabbit mAb #3085.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, either mock transfected (-) or transfected with Myc/DDK-tagged cDNA expression constructs encoding full-length human RXRα (hRXRα; +), RXRβ (hRXRβ; +), or RXRγ (hRXRγ; +), using RXRα (D6H10) Rabbit mAb #3085 (upper) and DYKDDDDK Tag Antibody (Binds to same epitope as Sigma's Anti-FLAG® M2 Antibody) #2368 (lower).


Western Blotting

Western Blotting

Western blot analysis of extracts from various tissues using RXRγ Antibody #5629.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using RXRβ Antibody #8715.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using RARγ1 (D3A4) XP® Rabbit mAb #8965.


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.

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.

Background

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. Delacroix, L. et al. (2010) Mol Cell Biol 30, 231-44.
  3. Eifert, C. et al. (2006) Mol Reprod Dev 73, 796-824.
  4. Mark, M. et al. (2006) Annu Rev Pharmacol Toxicol 46, 451-80.
  5. Niederreither, K. and Dollé, P. (2008) Nat Rev Genet 9, 541-53.
  6. Mark, M. et al. (2009) Nucl Recept Signal 7, e002.
  7. Dollé, P. (2009) Nucl Recept Signal 7, e006.
  8. Purton, L.E. et al. (2006) J Exp Med 203, 1283-93.
  9. Fisher, G.J. et al. (1994) J Biol Chem 269, 20629-35.
  10. Zelent, A. et al. (1989) Nature 339, 714-7.
  11. Elder, J.T. et al. (1991) J Invest Dermatol 96, 425-33.
  12. Giannì, M. et al. (2002) EMBO J 21, 3760-9.
  13. Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
  14. Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.

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