Antibodies - Heat Shock Proteins, Oxydative Stress, Apoptosis, Cell Signaling

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Product Name: FKBP52 Antibody
Catalog #: SMC-139C
Package size: 25ug
Price: $139.00 USD

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Alternate Product Sizes: SMC-139D
Type: Monoclonal
Conjugate: N/A
Datasheet: SMC 139 Heat Shock Protein 90 Co Chaperone, FKBP52
Description: Anti-FKBP52
Research Area: Chaperones, Heat Shock, Trafficking
Alternative Names: FK506 binding protein 4, FKBP4, FKBP59, HBI, Hsp56, p52, p59, PPIase, Rotamase, T cell FK506 binding protein
Clone Number: Hi52C
Host Species: Mouse
Isotype: IgG1
Immunogen: Synthetic peptidecorresponding to the residuesof human FKBP52
Applications: WB, IP, IHC: Paraffin embedded
Species Reactivity: Canine, Hamster, Human, Mouse, Rat
Accession Number: NP_002005.1
Gene ID: 2288
SwissProt: Q02790
Background Info: 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.
Recommended Dilutions: 1:2000 (WB), 5µg with 10-20µL Protein A beads (IP), 1:250 (IHC)
Form: Protein G Purified
Storage Buffer: PBS, 50% glycerol, 0.09% sodium azide
Concentration: 1mg/mL
Certificate of Analysis: 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.
Storage Temp: -20°C
Shipping Temp: Blue Ice or 4°C

Prostate tissue was histologically stained with antibodies specific for FKBP52. The strongest staining for FKBP52 is in ductal epithelial cells.
Courtesy of David F. Smith, Mayo Clinic, USA.

Research Background: 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 co-chaperones 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, 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).
References: 1. Cheung-Flynn J., Roberts P.J., Riggs D.L., and Smith D.F. (2003) J. Biol. Chem. 278(19): 17388-17394.
2. Davies T.H., Ning Y.N., and Sanchez E.R. (2002) J Biol. Chem. 277 (7): 4597-4600.
3. Wu, B. et al. (2004) Proc. Natl. Acad. Sci. USA. 101(22): 8348-8353.
4. Denny W.B., Prapapanich V., Smith D.F., and Scammell J.G. (2005) Endocrinology 146(7):3194-3201.
5. Cox M.B. et al. (2007) Molecular Endocrinology. Epub.

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