| CatalogCode: | NB300-731 |
| ProductName: | Glucocorticoid Receptor Antibody |
| Product Description: | Mouse Monoclonal anti-Glucocorticoid Receptor (BuGR2) |
| Clone: | BuGR2 |
| Clonality: | Monoclonal |
| Immunogen: | Partially purified rat GR |
| Specificity: | Using using enzymatic digestion analysis, has been shown to react with the undigested 97 kDa GR, a 17 kDa DNA-binding trypsin fragment, and a 45 kDa steroid- and DNA-binding chymotrypsin fragment. ICC staining of GR in L929 cells with this antibody results in staining of both the cytoplasm and nucleus, even in the presence of hormone. |
| CrossReactivity: | Cross-reacts with Guinea pig, Mouse, Rabbit, Rat and Sheep. Does not cross-react with Amphibians, Birds or Primate. Not yet tested in other species. |
| Packaging: | 0.1 mg IgG purified Mouse ascites. |
| Uses: | Immunohistochemistry: use at a concentration of 5 ug/ml. Western Blot: use at a concentration of 5 ug/ml. Gel Shift: Use at an assay dependent dilution. Immunofluorescence: Use at an assay dependent dilution. Immunoprecipitation: Use at an assay dependent dilution. Not tested in other applications. Optimal dilutions / concentrations should be determined by the end user. By Western blot, this antibody detects a 97 kDa protein representing GR in L929 cell extract. Immunocytochemical staining of GR in L929 cells with this antibody results in staining of both the cytoplasm and nucleus, even in the presence of hormone.This antibody, using enzymatic digestion analysis, has been shown to react with the undigested 97 kDa GR, a 17 kDa DNA-binding trypsin fragment, and a 45 kDa steroid- and DNA-binding chymotrypsin fragment. |
| Localization: | Cytoplasmic in the absence of ligand; nuclear after ligand-binding. |
| Control: | L929 cells and mouse liver extract |
| Background: | Steroid receptors are ligand-dependent, intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate hormone. Glucocorticoids are a family of steroids necessary for the regulation of energy metabolism and the immune and inflammatory responses. These compounds exert their effect through their interaction with the glucocoticoid receptor (GR) and that complex's subsequent association with DNA. All normal mammalian tissues examined to date have been shown to contain glucocorticoid receptor. The corresponding gene for the glucocorticoid receptor is NR3C1. |
| Storage: | Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
| Purity: | IgG purified |
| Isotype: | IgG2 |
| Host_Name: | Mouse |
| Buffer: | PBS pH 7.2 |
| ListPrice: | 295 |
| AppSummary: | IHC-P, IF, IP, WB, GS |
| SpeciesSummary: | Mu, Rt, Rb, Gp, Sh, Am(-), Av(-), Mk(-) |
| ALTnames: | anti-GCCR antibody, anti-GCR antibody, anti-Glucocorticoid receptor lymphocyte antibody, anti-GR antibody, anti-GRL antibody, anti-Grl1 NR3C1 antibody, anti-Nuclear receptor subfamily 3 group C member 1 antibody |
| ProteinTarget: | Glucocorticoid Receptor |
| PackageSize: | 0.1 mg |
| GeneralRef: | This product has been used in:Wyszomierski SL et al. Glucocorticoid receptor/signal transducer and activator of transcription 5 (STAT5) interactions enhance STAT5 activation by prolonging STAT5 DNA binding and tyrosine phosphorylation. Mol Endocrinol 13:330-43 (1999). Barent RL et al. Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes. Mol Endocrinol 12:342-54 (1998). Dao-Phan HP et al. Disruption of the glucocorticoid receptor assembly with heat shock protein 90 by a peptidic antiglucocorticoid. Mol Endocrinol 11:962-72 (1997). Dittmar KD & Pratt WB Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation. J Biol Chem 272:13047-54 (1997). Chang HC et al. In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol Cell Biol 17:318-25 (1997). Sackey FN et al. Determinants of subcellular distribution of the glucocorticoid receptor. Mol Endocrinol 10:1191-205 (1996). Renoir JM et al. Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: a possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression. Proc Natl Acad Sci U S A 92:4977-81 (1995). Nordeen SK et al. Modulation of glucocorticoid-regulated transcription by purines: novel characteristics and implications for tissue specificity of steroid responses. Endocrinology 136:1120-7 (1995). Berghorn KA et al. Induction of glucocorticoid receptor expression in hypothalamic magnocellular vasopressin neurons during chronic hypoosmolality. Endocrinology 136:804-7 (1995). Opoku J & Simons SS Absence of intramolecular disulfides in the structure and function of native rat glucocorticoid receptors. J Biol Chem 269:503-10 (1994). Hutchison KA et al. All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a foldosome. J Biol Chem 269:27894-9 (1994). Stancato LF et al. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J Biol Chem 268:21711-6 (1993). Chang TJ et al. Inhibition of mouse GATA-1 function by the glucocorticoid receptor: possible mechanism of steroid inhibition of erythroleukemia cell differentiation. Mol Endocrinol 7:528-42 (1993). Schlatter LK et al. Comparison of the 90-kilodalton heat shock protein interaction with in vitro translated glucocorticoid and estrogen receptors. Mol Endocrinol 6:132-40 (1992). Hutchison KA et al. Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system. J Biol Chem 267:2902-8 (1992). Distelhorst CW & Howard KJ Evidence from pulse-chase labeling studies that the antiglucocorticoid hormone RU486 stabilizes the nonactivated form of the glucocorticoid receptor in mouse lymphoma cells. J Steroid Biochem 36:25-31 (1990). Raaka BM et al. The glucocorticoid antagonist 17 alpha-methyltestosterone binds to the 10 S glucocorticoid receptor and blocks agonist-mediated dissociation of the 10 S oligomer to the 4 S deoxyribonucleic acid-binding subunit. Mol Endocrinol 3:332-41 (1989). Orti E et al. Phosphorylation of glucocorticoid receptor-associated and free forms of the approximately 90-kDa heat shock protein before and after receptor activation. J Biol Chem 264:231-7 (1989). Distelhorst CW & Howard KJ Kinetic pulse-chase labeling study of the glucocorticoid receptor in mouse lymphoma cells. Effect of glucocorticoid and antiglucocorticoid hormones on intracellular receptor half-life. J Biol Chem 264:13080-5 (1989). Smith LI et al. Phosphorylated sites within the functional domains of the approximately 100-kDa steroid-binding subunit of glucocorticoid receptors. Biochemistry 28:4490-8 (1989). Unger AL et al. Isolation of ribonucleic acid from the unactivated rat liver glucocorticoid receptor. Mol Endocrinol 2:952-8 (1988). Bresnick EH et al. Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptor. J Steroid Biochem 30:267-9 (1988). Hendry WJ et al. Analysis of the disruptive action of an epididymal protease and the stabilizing influence of molybdate on nondenatured and denatured glucocorticoid receptor. Endocrinology 120:629-39 (1987). Gametchu B & Harrison RW Characterization of a monoclonal antibody to the rat liver glucocorticoid receptor. Endocrinology 114:274-9 (1984). General / background references:Yoshinaga SK et al. Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors. Science 258:1598-604 (1992). Chadwick CC et al. Structural and functional characterization of an inositol polyphosphate receptor from cerebellum. J Biol Chem 267:3473-81 (1992). Bresnick EH et al. Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 29:520-7 (1990). LaFond RE et al. Immunocytochemical localization of glucocorticoid receptors in cells, cytoplasts, and nucleoplasts. Exp Cell Res 175:52-62 (1988). Rehmus EH et al. Immunochemical comparison of mutant glucocorticoid receptors and wild type receptor fragments produced by neutrophil elastase and chymotrypsin. J Steroid Biochem 28:167-77 (1987). |
|