CST, 79839W2, Glucocorticoid Receptor (D8H2) Rabbit Monoclonal Antibody (SignalFlex™ mFluor™ UV375 Conjugate)

Monoclonal Antibody for studying Glucocorticoid Receptor. Highly specific and rigorously validated in-house, Glucocorticoid Receptor (D8H2) Rabbit Monoclonal Antibody (SignalFlex^™ mFluor^™ UV375 Conjugate) (CST #79839) is ready to ship. Product Usage Information SignalFlex™ conjugates are produced using highly validated Cell Signaling Technology ® primary antibodies and conjugation methods that have been rigorously tested, ensuring high-quality conjugates and lot-to-lot consistency. These conjugates are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity. However, they are not tested on specific assays. Optimal dilutions/concentrations should be determined by the end user. When performing flow cytometry, we recommend using an isotype control conjugate at the same concentration as the antibody conjugate. Storage Supplied in PBS (pH 7.2), less than 0.1% sodium azide, and 2 mg/mL BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze. Specificity / Sensitivity Glucocorticoid Receptor (D8H2) Rabbit Monoclonal Antibody (SignalFlex™ mFluor™ UV375 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. Species Reactivity: Human, Mouse, Rat, Monkey Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu378 of human glucocorticoid receptor protein. 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 M R Mk SENSITIVITY: Endogenous Source/Isotype: Rabbit IgG