FKBP12 (FK506-binding protein 12 kDa) is a ubiquitously expressed intracellular protein belonging to the immunophilin family, known for its peptidyl-prolyl isomerase (PPIase) activity. It plays a critical role in modulating cellular processes by interacting with various signaling molecules, including the TGF-β receptor, ryanodine receptors (RyRs), and the mTOR (mechanistic target of rapamycin) pathway. FKBP12 is notably recognized for its high-affinity binding to immunosuppressive drugs like FK506 (tacrolimus) and rapamycin (sirolimus), forming complexes that inhibit calcineurin or mTOR, respectively, influencing immune response and cell growth regulation.
Antibodies targeting FKBP12 are widely used as research tools to study its expression, localization, and interactions in physiological and pathological contexts. These antibodies enable detection of FKBP12 in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry. Given its involvement in calcium signaling, protein folding, and pathways linked to cancer, neurodegeneration, and cardiovascular diseases, FKBP12 antibodies are valuable for investigating disease mechanisms or drug effects.
Most FKBP12 antibodies are raised against conserved epitopes, ensuring cross-reactivity across species (human, mouse, rat). However, specificity validation is essential due to potential cross-reactivity with other immunophilins. Monoclonal and polyclonal variants are commercially available, with applications spanning basic research to preclinical studies. Understanding FKBP12's regulatory roles through antibody-based assays continues to advance insights into cellular homeostasis and therapeutic targeting.