| Product Includes | Product # | Quantity | Mol. Wt | Isotype/Source |
|---|---|---|---|---|
| RARα (E6Z6K) Rabbit mAb | 62294 | 20 µl | 60 kDa | Rabbit IgG |
| RARγ1 (D3A4) XP® Rabbit mAb | 8965 | 20 µl | 58 kDa | Rabbit IgG |
| RXRα (D6H10) Rabbit mAb | 3085 | 20 µl | 53 kDa | Rabbit IgG |
| Glucocorticoid Receptor (D8H2) XP® Rabbit mAb | 3660 | 20 µl | 80, 91, 94 kDa | Rabbit IgG |
| Progesterone Receptor A/B (D8Q2J) XP® Rabbit mAb | 8757 | 20 µl | 90 (PR-A), 118 (PR-B) kDa | Rabbit IgG |
| Androgen Receptor (D6F11) XP® Rabbit mAb | 5153 | 20 µl | 110 kDa | Rabbit IgG |
| Estrogen Receptor α (D8H8) Rabbit mAb | 8644 | 20 µl | 66 kDa | Rabbit IgG |
| PPARγ (C26H12) Rabbit mAb | 2435 | 20 µl | 53, 57 kDa | Rabbit IgG |
| Anti-rabbit IgG, HRP-linked Antibody | 7074 | 100 µl | Goat |
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Description
The Nuclear Receptor Antibody Sampler Kit provides an economical means to evaluate the presence and status of nuclear receptors. This kit contains enough primary antibody to perform two western blots per primary.
Storage
Background
Nuclear Receptors are transcription factors responsible for sensing bioactive molecules, including steroid and thyroid hormones. They are regulated by multiple posttranslational modifications, which in turn impacts their ability to regulate the expression of specific genes involved in the control of reproduction, development, and metabolism.
Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).
Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (4). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (5).
Glucocorticoid hormones control cellular proliferation, inflammation, and metabolism through their association with the glucocorticoid receptor (GR)/NR3C1, a member of the nuclear hormone receptor superfamily of transcription factors (6).
Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (7). PPARγ is preferentially expressed in adipocytes, as well as in vascular smooth muscle cells and macrophages (8). Besides its role in mediating adipogenesis and lipid metabolism (8), PPARγ also modulates insulin sensitivity, cell proliferation, and inflammation (9).
Human progesterone receptor (PR) is expressed as two forms: the full length PR B and the short form PR A. PR A lacks the first 164 amino acid residues of PR B (10,11). Both PR A and PR B are ligand activated, but differ in their relative ability to activate target gene transcription (12,13).
Nuclear retinoic acid 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 (14). 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 (15,16).
The human retinoid X receptors 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 (17).
- Li, J. and Al-Azzawi, F. (2009) Maturitas 63, 142-8.
- Avila, D.M. et al. (2010) J Steroid Biochem Mol Biol 76, 135-42.
- Montgomery, J.S. et al. (2001) J Pathol 195, 138-46.
- Mangelsdorf, D.J. et al. (1995) Cell 83, 835-9.
- Glass, C.K. and Rosenfeld, M.G. (2000) Genes Dev 14, 121-41.
- Yamamoto, K.R. (1985) Annu Rev Genet 19, 209-52.
- Tontonoz, P. et al. (1995) Curr Opin Genet Dev 5, 571-6.
- Rosen, E.D. et al. (1999) Mol Cell 4, 611-7.
- Murphy, G.J. and Holder, J.C. (2000) Trends Pharmacol Sci 21, 469-74.
- Evans, R.M. (1988) Science 240, 889-95.
- Kastner, P. et al. (1990) EMBO J 9, 1603-14.
- Giangrande, P.H. et al. (2000) Mol Cell Biol 20, 3102-15.
- Wen, D.X. et al. (1994) Mol Cell Biol 14, 8356-64.
- Rochette-Egly, C. and Germain, P. (2009) Nucl Recept Signal 7, e005.
- Delacroix, L. et al. (2010) Mol Cell Biol 30, 231-44.
- Eifert, C. et al. (2006) Mol Reprod Dev 73, 796-824.
- Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
Background References
Trademarks and Patents
Limited Uses
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