FKBP10 (E8M4E) Rabbit mAb #57551

FK506-binding proteins (FKBPs) are a large family of conserved proteins characterized by the presence of one or more peptidyl-prolyl cis-trans isomerase (PPIase) domains. The founding member FKBP12 was originally identified as a non-covalent binding protein of FK506 and rapamycin, two widely used immunosuppressive drugs, and mediated their immunosuppressive activity. The FKBP12-FK506 complex specifically targets the Ca²⁺-dependent serine-threonine phosphatase calcineurin, and the FBKP12-rapamycin complex acts on mTOR (mammalian target of rapamycin). While both FK506 and rapamycin bind to the PPIase domain and inhibit PPIase activity of FKBP12, the inhibition of PPIase activity per se does not contribute to their immunosuppressive activity. Some members of the FKBP family also contain other functional domains or motifs. FKBPs have been reported to play roles in diverse processes, such as protein folding, cellular signaling, and transcription, and have been implicated in several diseases (1-3).

FKBP10, also known as FKBP65 (65 kDa FK506-binding protein), has four tandem PPIase domains and is an endoplasmic reticulum (ER) resident protein, where it modulates the folding and trafficking of secretory proteins. FKBP10 plays an important role in collagen folding and secretion and its mutation is associated with osteogenesis imperfecta (4-6), and it is considered as a therapeutic target for idiopathic pulmonary fibrosis (IPF) (7,8). Recent reports suggest that FKBP10 may be a biomarker or therapeutic target for several different cancers (9-11).