PPIC (peptidyl-prolyl cis-trans isomerase C), also known as cyclophilin C, belongs to the cyclophilin family of proteins that catalyze the cis-trans isomerization of proline residues in polypeptides, facilitating proper protein folding. Encoded by the PPIC gene, this ubiquitously expressed enzyme shares structural and functional homology with other cyclophilins but exhibits distinct tissue-specific expression patterns. PPIC interacts with immunosuppressive drugs like cyclosporine A and plays roles in immune regulation, intracellular signaling, and chaperone-mediated protein trafficking. Its involvement in modulating apoptosis, inflammation, and cellular stress responses has linked PPIC to pathological conditions including neurodegenerative diseases, cancer progression, and autoimmune disorders.
PPIC antibodies are essential tools for detecting and quantifying this protein in research applications such as Western blotting, immunohistochemistry, and flow cytometry. They help elucidate PPIC's subcellular localization, interaction networks, and disease-associated expression changes. Specific monoclonal or polyclonal antibodies enable differentiation between PPIC and other cyclophilin family members (e.g., cyclophilin A/PPIA), ensuring experimental accuracy. Recent studies utilizing PPIC antibodies have explored its potential as a biomarker in tumor microenvironments and its functional crosstalk with viral pathogens. Validation of antibody specificity through knockout controls or siRNA knockdown remains critical due to high sequence conservation among cyclophilins.