Background:  The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Several related immunophilins, FKBP12, FKBP51 and FKBP52, are characterized as cytosolic FK506-binding proteins, and following ligand binding, they functionally inhibit the phosphatase activity of calcineurin. The ubiquitously expressed FKBP12 also associates with the cytoplasmic domain of the TGF?type I receptor, where it stabilizes the inactive conformation of the receptor and blocks the activation of the TGF?pathway. FKBP51 and FKBP52 are two highly related proteins. FKBP51 is predominantly expressed in T cells and is induced by glucocorticoids. FKBP51 mediates the effects of FK506 and rapamycin by inhibiting intracellular calcineurin activity, and by blocking T-cell activation and proliferation. FKBP52, known also as FKBP-59 or heat shock protein 56, is expressed in a variety of tissues and can also associate with the heat shock protein (hsp90) in mature steroid receptor complexes.

Description: Rabbit polyclonal to FKBP51

Immunogen: KLH conjugated synthetic peptide derived from FKBP51

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 51 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry: 1/100;

·Immunofluorescence: 1/50-200;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.