FK506 Binding Protein 4, 59kDa (FKBP4) antibody

Antigen: FK506 Binding Protein 4, 59kDa (FKBP4)

Synonyms: HBI, p52, Hsp56, FKBP52, FKBP59, PPIase, FKBP4, MGC127596, P59, hsp56, fkbp52, fkbp59, MGC81078, wu:fb34f09

Clonality: Monoclonal (Hi52C)

Host: Mouse

Reactivity: Dog (Canine), Hamster, Human, Mouse (Murine), Rat (Rattus)

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)

Catalog no.: ABIN361686

Additional Information

Alternative name: FKBP52

Gene ID: 2288

UniProt: Q02790

Immunogen: Synthetic peptide corresponding to the residues of human FKBP52

Isotype: IgG

Clone: Hi52C

Description: 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. 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 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 (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. 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, 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.

Synonyms: FK506 binding protein 4, FKBP4, FKBP59, HBI, Hsp56, p52, p59, PPIase, Rotamase, T cell FK506 binding protein

Characteristics: Accession Number: NP_002005.1

Specificity: Detects an ~52kDa protein representing FKBP52 in cell lysate. Also detects FKBP52 in whole tissue extracts from rat kidney and rat and mouse testes. Heavy chain migrates close to FKBP52 on SDS PAGE.

Sensitivity: 0.5µg/ml was sufficient for detection of FKBP52 in 20µg total protein using WB by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Application Details

Application Notes: 1:2000 (WB), 5µg with 10-20µL Protein A beads (IP), 1:250 (IHC)

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins, Chromatin and Nuclear Signaling, Cytoskeleton

Restrictions: For Research Use only

Images

FKBP52 (Hi52C) Prostate tissue (strong staining in ductal epithelial cells Courtesy of the Mayo Clinic.

Publications

Davies, Ning, Suanchez: "A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins." in: The Journal of biological chemistry, Vol. 277, Issue 7, pp. 4597-600, 2002 (PubMed).

Cheung-Flynn, Roberts, Riggs et al.: "C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90." in: The Journal of biological chemistry, Vol. 278, Issue 19, pp. 17388-94, 2003 (PubMed).

Wu, Li, Liu et al.: "3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 22, pp. 8348-53, 2004 (PubMed).

Denny, Prapapanich, Smith et al.: "Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activity." in: Endocrinology, Vol. 146, Issue 7, pp. 3194-201, 2005 (PubMed).