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Rabbit polyclonal NR3C1 antibody (A2164)
Supplier: ABclonal Inc.
Recommended applications: WB,IHC,IF
WB 1:500 – 1:2000 IHC 1:50 – 1:200 IF 1:20 – 1:100
Recommended protocols: check protocols
Click or hover above images to see image description for Rabbit polyclonal NR3C1 antibody.
Check alternative names for the antibodyExpand
GCCR antibody, GCR antibody, GR antibody, GRL antibody
GCCR antibody|GCR antibody|GCR_HUMAN antibody|GCRST antibody|glucocorticoid nuclear receptor variant 1 antibody|Glucocorticoid receptor antibody|GR antibody|GRL antibody|Grl1 antibody|nr3c1 antibody|Nuclear receptor subfamily 3 group C member 1 antibody|nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) antibody|Anti-Glucocorticoid Receptor antibody [BuGR2] – ChIP Grade (ab2768)
SCBT cat No: sc-376425|sc-1003|sc-376426|
Rabbit polyclonal NR3C1 antibody
|Catalogue No.|| |
Human, Mouse, Rat
Recombinant protein of human NR3C1
WB, IHC, IF
|Recommended dilution|| |
WB 1:500 – 1:2000
|Molecular weight|| |
Predicted: 86kDa/Observed: Refer to Figures
NR3C1 antibody was tube-contained.
NR3C1 antibody was purified using affinity purification.
Store at -20 Celsius degree. Avoid freeze / thaw cycles.
|Alternative antibody names|| |
GCCR antibody, GCR antibody, GR antibody, GRL antibody
|Database links|| |
|Protein names|| |
GCCR, GCR, GR, GRL
|Protein function|| |
Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling . Plays a role in rapid mRNA degradation by binding to the 5′ UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay . Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity).; Isoform Alpha: Has transcriptional activation and repression activity . Mediates glucocorticoid-induced apoptosis . Promotes accurate chromosome segregation during mitosis . May act as a tumor suppressor . May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression (By similarity).; Isoform Beta: Acts as a dominant negative inhibitor of isoform Alpha . Has intrinsic transcriptional activity independent of isoform Alpha when both isoforms are coexpressed . Loses this transcription modulator function on its own . Has no hormone-binding activity . May play a role in controlling glucose metabolism by maintaining insulin sensitivity (By similarity). Reduces hepatic gluconeogenesis through down-regulation of PEPCK in an isoform Alpha-dependent manner . Directly regulates STAT1 expression in isoform Alpha-independent manner .; Isoform Alpha-2: Has lower transcriptional activation activity than isoform Alpha. Exerts a dominant negative effect on isoform Alpha trans-repression mechanism .; Isoform GR-P: Increases activity of isoform Alpha.; Isoform Alpha-B: More effective than isoform Alpha in transcriptional activation, but not repression activity.; Isoform 10: Has transcriptional activation activity.; Isoform Alpha-C1: Has transcriptional activation activity.; Isoform Alpha-C2: Has transcriptional activation activity.; Isoform Alpha-C3: Has highest transcriptional activation activity of all isoforms created by alternative initiation . Has transcriptional repression activity . Mediates glucocorticoid-induced apoptosis .; Isoform Alpha-D1: Has transcriptional activation activity.; Isoform Alpha-D2: Has transcriptional activation activity.; Isoform Alpha-D3: Has lowest transcriptional activation activity of all isoforms created by alternative initiation . Has transcriptional repression activity .
|Protein tissue specificity|| |
Widely expressed including bone, stomach, lung, liver, colon, breast, ovary, pancreas and kidney . In the heart, detected in left and right atria, left and right ventricles, aorta, apex, intraventricular septum, and atrioventricular node as well as whole adult and fetal heart . Isoform Beta: Widely expressed including brain, bone marrow, thymus, spleen, liver, kidney, pancreas, lung, fat, skeletal muscle, heart, placenta and blood leukocytes . Isoform Alpha-2: Expressed at low level.
|Protein sequence and domain|| |
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain . The ligand-binding domain is required for correct chromosome segregation during mitosis although ligand binding is not required .Belongs to the nuclear hormone receptor family. NR3 subfamily.; Contains 1 nuclear receptor DNA-binding domain.
|Protein post-translational modifications|| |
Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity.; Increased proteasome-mediated degradation in response to glucocorticoids . Isoform Alpha-B appears to be more susceptible to proteolytic degradation than isoform Alpha .; Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203, Ser-226 and Ser-404-phosphorylated forms are mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear . Phosphorylation at Ser-211 increases transcriptional activity . Phosphorylation at Ser-203, Ser-226 and Ser-404 decreases signaling capacity . Phosphorylation at Ser-404 may protect from glucocorticoid-induced apoptosis . Phosphorylation at Ser-203 and Ser-211 is not required in regulation of chromosome segregation . May be dephosphorylated by PPP5C, attenuates NR3C1 action (By similarity).; Sumoylation at Lys-277 and Lys-293 negatively regulates its transcriptional activity . Sumoylation at Lys-703 positively regulates its transcriptional activity in the presence of RWDD3 (By similarity). Sumoylation at Lys-277 and Lys-293 is dispensable whereas sumoylation at Lys-703 is critical for the stimulatory effect of RWDD3 on its transcriptional activity (By similarity). Heat shock increases sumoylation in a RWDD3-dependent manner (By similarity).; Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling.
|Protein cellular localization|| |
Isoform Alpha: Cytoplasm . Nucleus . Mitochondrion . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Note: After ligand activation, translocates from the cytoplasm to the nucleus.; Isoform Beta: Nucleus . Cytoplasm . Note: Expressed predominantly in the nucleus with some expression also detected in the cytoplasm.; Isoform Alpha-B: Nucleus . Cytoplasm . Note: After ligand activation, translocates from the cytoplasm to the nucleus.
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).
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