Product Pathways - Nuclear Receptor Signaling
Glucocorticoid Receptor (D8H2) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) #12007
|12007S||100 µl (50 tests)||---||In Stock||---|
|12007||carrier free and custom formulation / quantity||email request|
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|IF-IC||1:50||Human, Mouse, Rat, Monkey||Endogenous||Rabbit IgG|
Species cross-reactivity is determined by western blot using the unconjugated antibody.
Applications Key: IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
Glucocorticoid Receptor (D8H2) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) recognizes endogenous levels of total glucocorticoid receptor protein. Based upon sequence alignment, this antibody is predicted to cross-react with all known alternative translation start site generated isoforms of glucocorticoid receptor-α and glucocorticoid receptor-β. This antibody does not cross-react with mineralocorticoid receptor.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu378 of human glucocorticoid receptor protein.
Confocal immunofluorescent analysis of HeLa cells, grown in phenol red-free media containing 5% charcoal-stripped FBS for 2 d, and either untreated (left) or dexamethasone-treated (100 nM, 2 hr; right), using Glucocorticoid Receptor (D8H2) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) (green). Actin filaments were labeled with DY-554 phalloidin (red).
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Glucocorticoid Receptor (D8H2) XP® Rabbit mAb #3660.
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 GR in vivo. 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 intiation start sites, thus increasing the repertoire of functional signaling homo- and heterodimers (6,7).
- Yamamoto, K.R. (1985) Annu. Rev. Genet 19, 209-252.
- Necela, B.M. and Cidlowski, J.A. (2003) Trends Pharmacol. Sci. 24, 58-61.
- Wang, Z. et al. (2002) J. Biol. Chem. 277, 26573-26580.
- Rogatsky, I. et al. (1998) J. Biol. Chem. 273, 14315-14321.
- Krstic, M. D. et al. (1997) Mol. Cell. Biol. 17, 3947-3954.
- Yudt, M.R. and Cidlowski, J.A. (2001) Mol Endocrinol 15, 1093-103.
- Lu, N.Z. and Cidlowski, J.A. (2005) Mol Cell 18, 331-42.
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For Research Use Only. Not For Use In Diagnostic Procedures.
XP® is a trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
The Alexa Fluor® dye antibody conjugates in this product are sold under license from Molecular Probes, Inc., for research use only, except for use in combination with DNA microarrays. The Alexa Fluor® dyes (except for Alexa Fluor® 430 dye) are covered by pending and issued patents. Alexa Fluor® is a registered trademark of Molecular Probes, Inc.