FK506 Binding Protein 1A, Recombinant, Human (FKBP1A, FK506 Binding Protein 12kD, FKBP12)
Description
Purity ≥ 95%, as determined by SDS-PAGE and visualized by silver stain. FK506 binding protein, 12 kilodalton molecular weight (FKBP12), also called FKBP1, was originally characterized as a peptidyl-prolyl isomerase that catalyzes the transition between cis- and trans-proline residues critical for proper folding of proteins. The macrolide immunosuppressants FK506 (Tacrolimus) and rapamycin bind to FKBP12 with high affinity, while the structurally related-compound cyclosporine binds with a much lower affinity (1). The binding of these drugs causes FKBP12 to become a potent inhibitor of calcineurin phosphatase activity 2 and TOR kinase activity (3). The inhibition of protein phosphatase activity is highly selective for calcineurin (2), making the FK506/FKBP12 complex a useful tool in the study of this enzyme. Knockout mice lacking FKBP12 are morphologically normal, but develop cardiomyopathies that may be related to dysregulation of ryanodyne receptors (4). Source: E. coli-expressed recom