FKBP52/FKBP4 Antibody

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 Abinding 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 approx. 75% sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different Hsp90- binding characteristics (3, 5). Also, whereas FKBP51 typically has a role with the progesterone receptor, FKBP52 has been found to be linked to the progesterone, androgen and glucocorticoid receptors (5).

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Publication using NBP1-84675	Applications	Species
Tyleckova J, Hrabakova R, Mairychova K et al. Cancer Cell Response to Anthracyclines Effects: Mysteries of the Hidden Proteins Associated with These Drugs. Int J Mol Sci 2012-11-22 [PMID: 23443080]

Array NBP1-84675

• FKBP52/FKBP4 Antibodies
• FKBP52/FKBP4 ELISA Kits
• FKBP52/FKBP4 Lysate
• FKBP52/FKBP4 Proteins