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. This promotes nuclear localization and binding of AR to androgenresponse elements in androgen target genes. AR plays a crucial role in several stages of male development and the progression of prostate cancer. Estrogen receptor alpha (ERalpha), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains. Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERalpha regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery. 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. Peroxisome proliferator-activated receptor gamma (PPARgamma) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator. PPARgamma is preferentially expressed in adipocytes, as well as in vascular smooth muscle cells and macrophages. Besides its role in mediating adipogenesis and lipid metabolism, PPARgamma also modulates insulin sensitivity, cell proliferation, and inflammation. 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 164aa residues of PR B. Both PR A and PR B are ligand activated, but differ in their relative ability to activate target gene transcription. Nuclear retinoic acid receptors (RARs) consist of three subtypes encoded by separate genes: alpha (NR1B1), beta (NR1B2), and gamma (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. 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. The human retinoid X receptors are encoded by three distinct genes (RXRalpha, RXRbeta, and RXRgamma) 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.
Specificity:Human
Intended Use:The Nuclear Receptor Antibody Sampler BioAssay™ 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.
Applications:Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution:Western Blot: 1:500-1:2000Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
