FKBP5 (D5G2) Rabbit mAb

FK506 binding protein 51 (FKBP51, also called FKBP5) belongs to the FKBP family of immunophilins (1). FKBP family proteins contain FK domains and TPR (tetratricopeptide repeat) domains. The FK domains are responsible for PPIase (peptidylprolyl isomerase) activity and allow binding to FK506 and rapamycin (2,3). The C terminal TPR domains are involved in protein-protein interactions. The TPR domain of FKBP5 mediates binding to HSP90 complexes (4), as well as glucocorticoid, androgen, and progesterone receptors, which account for its regulatory role in steroid hormone receptor function (5). FKBP5 also binds to IKKα and is involved in NF-κB signaling (6,7). In addition, FKBP5 was identified as a negative regulator of Akt through promotion of Akt - PHLPP interaction and enhanced dephosphorylation of Akt (8). 1.Avilés, A. et al. (1995) Clin Oncol (R Coll Radiol) 7, 97-101. 2.Fruman, D.A. et al. (1994) FASEB J 8, 391-400. 3.Fix, M.L. et al. (2008) Blood Press Monit 13, 199-203. 4.Scheufler, C. et al. (2000) Cell 101, 199-210. 5.Schülke, J.P. et al. (2010) PLoS One 5, e11717. 6.Bouwmeester, T. et al. (2004) Nat Cell Biol 6, 97-105. 7.Avellino, R. et al. (2005) Blood 106, 1400-6. 8.Pei, H. et al. (2009) Cancer Cell 16, 259-66.