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Polyclonal Anti-GR

Cat no: PA1107


Supplier: Boster Immunoleader
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Rabbit IgG polyclonal antibody for Glucocorticoid receptor (NR3C1) detection. Tested with WB, IHC-P in Human;Mouse;Rat.
Catalogue number: PA1107
Price: $200.00
Reactivities: Human, Mouse, Rat
Applications: Immunohistochemistry, Western Blot
Size: 100ug/vial
Gene: NR3C1
Swiss prot: P04150
Form: Lyophilized
Format: Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
Storage temp: "At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time. Avoid repeated freezing and thawing. "
Scientific background: 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.
References: 1. Encio, I. J.; Detera-Wadleigh, S. D. : The genomic structure of the human glucocorticoid receptor. J. Biol. Chem. 266: 7182-7188, 1991. 2. 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. 3. 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: A synthetic peptide corresponding to a sequence at the C-terminal of human GR, identical to the related rat and mouse sequences.