CST, 4161S, Phospho-Glucocorticoid Receptor (Ser211) Antibody

Polyclonal Antibody for studying Glucocorticoid Receptor (Ser211) phosphate. Validated for Western Blotting,Immunoprecipitation,Immunofluorescence (Immunocytochemistry). Highly specific and rigorously validated in-house, Phospho-Glucocorticoid Receptor (Ser211) Antibody (CST #4161) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunoprecipitation: 1:50 Immunofluorescence (Immunocytochemistry): 1:200 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunoprecipitation, Immunofluorescence (Immunocytochemistry) Specificity / Sensitivity Phospho-Glucocorticoid Receptor (Ser211) Antibody detects endogenous levels of glucocorticoid receptor only when phosphorylated at serine 211. This antibody does not cross-react with other unrelated phosphorylated proteins. Species Reactivity: Human, Mouse, Rat Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding serine 211 of human glucocorticoid receptor. Antibodies are purified by protein A and peptide affinity chromatography. 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). Indeed, Ser211 of human GR is phosphorylated to a greater extent in the presence of hormone, and biochemical fractionation studies following hormone treatment indicate that Ser211-phosphorylated GR is found in the nucleus (3). Thus, Ser211 phosphorylation is a biomarker for activated GRÂ . An added layer of complexity to GR signaling lies in the ability of multiple isoforms to be generated through both alternative splicing and the use of alternative translation initiation start sites, thus increasing the repertoire of functional signaling homo- and heterodimers (6,7). 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 M R SENSITIVITY: Endogenous MW (kDa): 95 SOURCE: Rabbit