FKBP52 Monoclonal Antibody (Clone Hi52C)

Antigen: synthetic peptide corresponding to the residues of human FKBP52 . Host: mouse, clone Hi52C . Isotype: IgG1 . Cross Reactivity: (+) canine, hamster, human, mouse, and rat FKBP52 . Applications: IHC (paraffin embeded sections), IP, and WB . FKBP52 is part of the mature glucocorticoid receptor heterocomplex. The N-terminal domain binds FK506 and has peptidyl-prolyl isomerase activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TRP repeats involved in protein-protein interactions with Hsp40.

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SPECIFICATIONS

Catalog Number

10011442

Applications

IHC, IP, WB

Hosts

Mouse

Form

100 microg

P Type

Antibodies|Intracellular Signaling

Weight

52

Antigen

synthetic peptide corresponding to the residues of human FKBP52

Isotype

IgG1

Storage Temp

-20

Shipping Temp

-20

Additional Info

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 co-chaperones. One class of Hsp90-binding co-chaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an Hsp90 binding site. Among the TRP co-chaperones of Hsp90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins. FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex. The N-terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPlase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TRP repeats involved in protein-protein interactions with Hsp40. Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by the glucocorticoid receptor in opposing manners and have different Hsp90-binding characteristics. 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.