Technical Data
Glucocorticoid Receptor (GR)
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 Glucocorticoid Receptor (GR) and that complex's subsequent association with DNA. All normal mammalian tissues examined to date have been shown to contain GR. The human GR exists in two forms, alpha and beta, which are thought to be the result of alternative splicing of a single gene. Sequence analysis indicates that alpha and beta forms of human GR are 777 and 742aa long, respectively. They are identical up to residue 727, after which they diverge. After ligand binding, the 94kD GR alpha isoform translocates from the cytoplasm to the nucleus where it regulates gene expression. In contrast, the 90kD GR beta isoform does not appear to bind either glucocorticoid agonists or antagonists, and has been localized predominantly in the nucleus independent of hormone treatment in some human cell lines. Studies suggest that human GR alpha has a greater affinity for GR response elements (GREs) than GR beta only when in the ligand bound state.

Suitable for use in Flow Cytometry, Gel Shift assay, Western Blot, Immunoprecipitation, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 5ug/ml. Detects a band of ~97kD
Immunohistochemistry (Paraffin): 5ug/ml.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
100ug-20CBlue IceRatMouse
Partially purified rat GR (glucocorticoid receptor).
Supplied as a lyophilized powder from PBS, pH 7.2, 0.05% sodium azide. Reconstitute with 100ul sterile ddH2O.
Recognizes rat GR. Recognizes full-lengh GR, the 17kD DNA binding trypsin fragment and the 45kD steroid- and DNA-binding chymotrypsin fragment. Species Crossreactivity: human, mouse, sheep, guinea pig, rabbit and yeast. Does not cross-react with primate, avian or amphibian GR.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
11. Analysis of the disruptive action of an epididymal protease and the stabilizing influence of molybdate on nondenatured and denatured glucocorticoid receptor: W.J. Hendry, 3rd, et al.; Endocrinology 120, 629 (1987) 2. Phosphorylated sites within the functional domains of the approximately 100-kDa steroid-binding subunit of glucocorticoid receptors: L.I. Smith, et al.; Biochemistry 28, 4490 (1989) 3. Disruption of the glucocorticoid receptor assembly with heat shock protein 90 by a peptidic antiglucocorticoid: H.P. Dao-Phan, et al.; Mol. Endocrinol. 11, 962 (1997) 4. Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes: R.L. Barent, et al.; Mol. Endocrinol. 12, 342 (1998) 5. Glucocorticoid receptor/signal transducer and activator of transcription 5 (STAT5) interactions enhance STAT5 activation by prolonging STAT5 DNA binding and tyrosine phosphorylation: S.L. Wyszomierski, et al.; Mol. Endocrinol. 13, 330 (1999)