The FKBP1A antibody targets the FK506-binding protein 1A (FKBP1A), a 12 kDa member of the immunophilin family. FKBP1A, also known as FKBP12. functions as a peptidyl-prolyl cis-trans isomerase (PPIase), facilitating protein folding by catalyzing the conformational switching of proline residues. It plays a critical role in modulating intracellular signaling pathways, particularly through interactions with immunosuppressive drugs like FK506 (tacrolimus) and rapamycin (sirolimus). These drugs form complexes with FKBP1A to inhibit calcineurin or mTOR pathways, respectively, impacting T-cell activation and cellular growth regulation.
FKBP1A is ubiquitously expressed and localizes to the cytoplasm and nucleus. It has been implicated in diverse physiological and pathological processes, including neuroprotection, calcium signaling, and stress response. Dysregulation of FKBP1A is associated with neurodegenerative diseases (e.g., Alzheimer’s), cancer, and cardiovascular disorders. For instance, it interacts with tau protein in Alzheimer’s models and modulates drug resistance in certain cancers.
Antibodies against FKBP1A are widely used in research to study its expression, localization, and interactions via techniques like Western blotting, immunoprecipitation, and immunohistochemistry. They are essential for validating FKBP1A’s role in disease mechanisms, drug response studies, and biomarker discovery. Commercial antibodies are often validated using knockout cell lines to ensure specificity, aiding in the exploration of FKBP1A’s therapeutic potential and molecular functions.