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GR (Nuclear receptor subfamily 3 group C member 1)

Cat no: 144592

GR (Nuclear receptor subfamily 3 group C member 1)

Glucocorticoid receptor (GR) maps to the distal long arm of chromosome 5. The human glucocorticoid receptor (hGR) gene contains a total of 10 exons and has a minimum size of 80 kilobases. The identification of complementary DNAs encoding the human glucocorticoid receptor (hGR) predicts two protein forms (alpha and beta; 777 and 742 amino acids long, respectively) which differ at their carboxy termini and both forms of the receptor are related, with respect to their domain structure, to the v-erb-A oncogene product of avian erythroblastosis virus (AEV), which suggests that steroid receptor genes and the c-erb-A proto-oncogene are derived from a common primordial regulatory gene. Transcriptional regulation by the glucocorticoid receptor (GR) is mediated by hormone binding, receptor dimerization, and coactivator recruitment.\n\nUniProt Number:\nP04150\n\nGene ID:\nNR3C1\n\nApplications:\nSuitable for use in Western Blot and Immunohistochemistry (Paraffin).\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Handling:\nStore at -20?C for one year. After reconstitution, store at 4?C for one month. Can also be aliquoted and stored frozen at -20?C for long term.\nAvoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

144592

Size

100ug

Applications

IHC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Encio, I. J.; Detera-Wadleigh, S. D. : The genomic structure of the human glucocorticoid receptor. J. Biol. Chem. 266: 7182-7188, 1991. \n2. Weinberger, C.; Hollenberg, S. M.; Rosenfeld, M. G.; Evans, R. M. : Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product. Nature 318: 670-672, 1985. \n3. Bledsoe, R. K.; Montana, V. G.; Stanley, T. B.; Delves, C. J.; Apolito, C. J.; McKee, D. D.; Consler, T. G.; Parks, D. J.; Stewart, E. L.; Willson, T. M.; Lambert, M. H.; Moore, J. T.; Pearce, K. H.; Xu, H. E. : Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 110: 93-105, 2002.

Additional Info

Recognizes human, mouse and rat GR. No crossreactivity with other proteins.

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