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Products FKBP52 Monoclonal Antibody (Clone Hi52C)
| Catalogue number: | 10011442 |
| Hosts: | Mouse |
| Applications: | Immunohistochemistry, Immunoprecipitation, Western Blot |
| Weight: | 52 |
| Form: | 100 microg |
| Antigen: | synthetic peptide corresponding to the residues of human FKBP52 |
| P type: | Antibodies|Intracellular Signaling |
| Isotype: | IgG1 |
| Shipping temp: | -20 |
| Storage 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. |
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