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FK506 Binding Protein 4, 59kDa (FKBP4) antibody

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Dog (Canine), Hamster, Human, Mouse (Murine), Rat (Rattus)
(150), (52), (47), (25), (24), (4), (2), (1), (1)
(79), (58), (20)
Clonality (Clone)
Monoclonal ()
(5), (5), (4), (4), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
(137), (70), (64), (42), (38), (36), (26), (11), (5), (2), (2), (1), (1), (1)
Pubmed 4 references available
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Quantity 25 μg
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Synthetic peptide corresponding to the residues of human FKBP52
Clone Hi52C
Specificity Detects ~52 kDa. Heavy chain migrates close to FKBP52 on SDS PAGE.
Sensitivity 0.5 µg/ml was sufficient for detection of FKBP52 in 20 µg total protein using WB by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
Purification Protein G Purified
Alternative Name FKBP52 (FKBP4 Antibody Abstract)
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 cochaperones 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). FK506 binding protein 51 kDa (FKBP51 or otherwise referred to as FKBP54) has been identified as a progestininducible gene. This protein is predominantly expressed in murine T cells but in humans, it is abundantly expressed in numerous tissues at levels many times higher than FKBP12. The FKBP51 gene is known to be induced by glucocorticoids (5).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 2288
NCBI Accession NP_002005
UniProt Q02790
Research Area Chromatin and Nuclear Signaling, Cytoskeleton, Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2000), IHC (1:250), ICC/IF (1:1000), IP (5 μg), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-FK506 Binding Protein 4, 59kDa (FKBP4) antibody (ABIN361686) FKBP52 (Hi52C) Prostate tissue (strong staining in ductal epithelial cells Courtesy o...
Background publications 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).

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).

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).

Davies, Ning, Sánchez: "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).

Catalog No. ABIN361686
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