Description
Product Characteristics: HSP90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more cochaperones (1). One class of HSP90-binding cochaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an HSP90 binding site. Among the TPR cochaperones of HSP90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins (2). FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex (3). The N terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPIase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TPR repeats involved in protein-protein interactions with the HSP90 (4). Although FKBP52 and FKBP51 share ~75 % sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different HSP90-binding characteristics (3). FK506 binding protein 51 kDa (FKBP51 or otherwise referred to as FKBP54) has been identified as a progestininducible gene. This protein is predominantly expressed in murine T cells but in humans, it is abundantly expressed in numerous tissues at levels many times higher than FKBP12. The FKBP51 gene is known to be induced by glucocorticoids (5).
Target Information: The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It is thought to mediate calcineurin inhibition. It also interacts functionally with mature hetero-oligomeric progesterone receptor complexes along with the 90 kDa heat shock protein and P23 protein. This gene has been found to have multiple polyadenylation sites. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Mar 2009]