FK506 Binding Protein 5 (FKBP5) antibody

Details for Product No. ABIN361795
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Synonyms FKBP5, FKBP-5, AIG6, FKBP51, FKBP54, P54, PPIase, Ptg-10, D17Ertd592e, Dit1, si:zc263a23.8, wu:fc31g11, wu:fl87b03, zgc:64082
Dog (Canine), Hamster, Human, Rat (Rattus), Rabbit
(73), (26), (22), (6), (5), (4), (2), (2), (1), (1), (1), (1), (1)
(40), (36), (2)
Clonality (Clone)
Monoclonal ()
(4), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB)
(63), (28), (20), (13), (13), (10), (7), (3), (3), (3), (1)
Pubmed 5 references available
Quantity 100 μg
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Catalog No. ABIN361795
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Immunogen Synthetic peptide corresponding to the AA of human FKBP51
Clone Hi51B
Isotype IgG
Specificity Detects an approx. 51 kDa protein representing FKBP51 in cell lysate. Also detects FKBP51 in whole tissue extracts from rat kidney and rat and mouse testes.
Sensitivity A 1:2000 dilution was sufficient for detection of FKBP51 in ~50 µg total protein using WB anaylsis.
Purification Protein G Purified
Alternative Name FKBP51
Background Synonyms:
AIG6, FK506 binding protein 5, FKBP5, FKBP54, Hsp90 binding immunophilin, p54, Pplase, Ptg10, Rotamase, T cekk FK506 binding protein antibody
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 cochaperones 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 arelarge 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 approx. 75 % sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different Hsp90-binding characteristics.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.
Gene ID 2289
NCBI Accession NP_001139247
UniProt Q13451
Research Area Signaling, Heat Shock Proteins
Application Notes Recommended Dilution: 1:2000 (WB)
Restrictions For Research Use only
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
anti-FK506 Binding Protein 5 (FKBP5) antibody FKBP51 HS Hela 10ug 1 in 1000 Western Blotting copy.
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).

Hubler, Denny, Valentine et al.: "The FK506-binding immunophilin FKBP51 is transcriptionally regulated by progestin and attenuates progestin responsiveness." in: Endocrinology, Vol. 144, Issue 6, pp. 2380-7, 2003 (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).

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