Description
Protocol
Available protocols: ELISA+
Specificity / Sensitivity
The FastScan™ Phospho-Glucocorticoid Receptor (Ser226) ELISA Kit detects endogenous levels of glucocorticoid receptor when phosphorylated at Ser226, as shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity: Human, Mouse
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). Phosphorylation of GR at Ser226 by JNK enhances nuclear export after ligand depletion (6,7). Phosphorylation of various serine residues, including Ser226, also affects GR binding to different target genes, contributing to an additional layer of transcriptional regulation (8). Ser226 phosphorylation has also been linked to depression disorders as well as inflammation (9-11).
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)
