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FKBP52 Monoclonal Antibody(Clone Hi52C)
本产品不向个人销售,仅用作科学研究,不用于任何人体实验及非科研性质的动物实验。
FKBP52 Monoclonal Antibody(Clone Hi52C)图片
包装与价格:
包装价格(元)
25 µg电议
100 µg电议

产品介绍
For immunochemical analysis of FKBP52
分子量52
储存条件-20°C
General tipsFor obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.
Shipping ConditionEvaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
产品描述

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.1One 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.2FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex.3The N-terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPlase) activity that converts prolyl peptide bonds within target proteins fromcis-to trans-proline. The C-terminal domains contain the TRP repeats involved in protein-protein interactions with Hsp40.4Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by the glucocorticoid receptor in opposing manners and have different Hsp90-binding characteristics.3,5Also, 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

1.Cheung-Flynn, J., Roberts, P.J., Riggs, D.L., et al.C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90The Journal of Biological Chemisty278(19)17388-17394(2003) 2.Davies, T.H., Ning, Y.M., and SÁnchez, E.R.A new first step in activation of steroid receptors. Hormone-induced switching of FKBP51 and FKBP52 immunophilinsThe Journal of Biological Chemisty277(7)4597-4600(2002) 3.Wu, B., Li, P., Liu, Y., et al.3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin hetrocomplexThe Journal of Biological Chemisty101(22)8348-8353(2004) 4.Denny, W.B., Prapapanich, V., Smith, D.F., et al.Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activityEndocrinology146(7)3194-3201(2005) 5.Cox, M.B., Riggs, D.L., Hessling, M., et al.FK506-binding protein 52 phosphorylation: A potential mechanism for regulating steroid hormone receptor activityMol. Endocrinol.21(12)2956-2967(2007)