Recombinant Human FKBP3 protein

FKBP3 (FK506-binding protein 3), a member of the FKBP immunophilin family, is a peptidyl-prolyl cis-trans isomerase (PPIase) involved in protein folding and conformational regulation. It binds to the immunosuppressive drug FK506 (tacrolimus) and rapamycin, mediating their biological effects through interactions with target proteins like mTOR (mechanistic target of rapamycin). Structurally, FKBP3 contains a conserved FK506-binding domain that facilitates its enzymatic activity and molecular chaperone functions.

As an intracellular protein predominantly localized in the nucleus, FKBP3 plays roles in diverse cellular processes, including transcriptional regulation, apoptosis, autophagy, and stress response. It interacts with steroid hormone receptors (e.g., glucocorticoid receptor) and chromatin-modifying complexes, influencing gene expression. Studies link FKBP3 dysregulation to cancer progression, neurodegenerative diseases, and immune disorders, highlighting its therapeutic relevance.

Recombinant FKBP3 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional protein for research and drug development. Its applications include studying PPIs (protein-protein interactions), screening small-molecule inhibitors, and exploring FKBP3’s role in cellular pathways. Recombinant variants may incorporate tags (e.g., His, GST) for affinity purification or tracking. Current research focuses on targeting FKBP3 in cancer therapy and modulating its PPIase activity to correct protein misfolding in neurodegenerative conditions.

Overall, recombinant FKBP3 serves as a critical tool for dissecting immunophilin biology and advancing translational studies in disease mechanisms and drug discovery.