Glucocorticoid Receptor beta Polyclonal Antibody, Invitrogen™

Description

PA3-514 detects glucocorticoid receptor (GR) beta from human cells. PA3-514 has been successfully used in Western blot, immunocytochemistry and immunoprecipitation procedures. By Western blot, this antibody detects a ∽90 kDa protein representing GR beta from HeLa cell lysate. Immunocytochemical staining of GR beta in HeLa cells with PA3-514 results in nuclear staining. PA3-514 immunizing peptide corresponds to amino acid residues 728-742 from human GR beta. This peptide (Cat. # PEP-222) is available for use in neutralization and control experiments.

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 the alpha and beta forms of human GR are 777 and 742 amino acids long, respectively. They are identical up to residue 727, after which they diverge. After ligand binding, the 94 kDa GR alpha isoform has been observed to translocate from the cytoplasm to the nucleus where it regulates gene expression. In contrast, the 90 kDa 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 beta might function as a dominant negative inhibitor of GR alpha activity.