CST, 65097S, Total Glucocorticoid Receptor Matched Antibody Pair

Matched Antibody Pair for studying Glucocorticoid Receptor in the research area. Product Usage Information Matched Antibody Pairs consist of capture and detection antibodies that bind to non-overlapping epitopes. For specific identification of the capture and detection antibodies in this pair, please refer to the data figure caption. Optimal dilutions/concentrations should be determined by the end user. Formulation Supplied in 1X PBS (10 mM Na 2 HPO 4 , 3 mM KCl, 2 mM KH 2 PO 4 , and 140 mM NaCl (pH 7.8)). BSA and Azide Free. Storage Store at -20ºC. This product will freeze at -20ºC so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles . A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance. Background 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 (1). GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which also contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. On hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with specific DNA sequences termed glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes (2). It was demonstrated that GR-mediated transcriptional activation is modulated by phosphorylation (3-5). Although GR can be basally phosphorylated in the absence of hormone, it becomes hyperphosphorylated upon binding receptor agonists. It has been suggested that hormone-dependent phosphorylation of GR may determine target promoter specificity, cofactor interaction, strength and duration of receptor signaling, receptor stability, and receptor subcellular localization (3). Alternate Names GCCR; GCR; GCRST; glucocorticoid nuclear receptor variant 1; Glucocorticoid receptor; GR; GRL; NR3C1; Nuclear receptor subfamily 3 group C member 1; nuclear receptor subfamily 3 group C member 1 variant hGR-B(54); nuclear receptor subfamily 3 group C member 1 variant hGR-B(77); nuclear receptor subfamily 3 group C member 1 variant hGR-B(93); nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) Specification REACTIVITY: H