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  3. PhosphoPlus® Glucocorticoid Receptor (Ser226) Antibody Duet

PhosphoPlus® Glucocorticoid Receptor (Ser226) Antibody Duet #36548

    Product Information

    Kit Usage Information

    Protocols

    Product Description

    PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based on superior performance in specified applications.

    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 serine 226 by JNK enhances nuclear export after ligand depletion (6,7). Phosphorylation of various serine residues, including serine 226, also affects GR binding to different target genes, contributing to an additional layer of transcriptional regulation (8). Serine 226 phosphorylation has also been linked to depression disorders as well as inflammation (9-11).

    Database Links

    UniProt ID: P04150


    Entrez-Gene Id: 2908


    Limited Uses

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    For Research Use Only. Not for Use in Diagnostic Procedures.
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