PPIA抗体—艾普蒂

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     Black line: Control Antigen (100 ng);Purple line: Antigen (10ng); Blue line: Antigen (50 ng); Red line:Antigen (100 ng)    

  
  

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     Flow cytometric analysis of Ramos cells using CD16 mouse mAb (green) and negative control (red).    

  
  

Cyclophilin A (PPIA), also known as peptidylprolyl isomerase A, is a ubiquitously expressed protein belonging to the cyclophilin family. It functions as a chaperone, facilitating protein folding through its enzymatic peptidylprolyl cis-trans isomerase (PPIase) activity. PPIA plays critical roles in diverse cellular processes, including immune regulation, apoptosis, and inflammation. Notably, it interacts with the HIV-1 capsid protein, aiding viral replication, and serves as a key target for immunosuppressive drugs like cyclosporine A (CsA), which inhibits its PPIase activity.

PPIA antibodies are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. They are widely used in techniques such as Western blotting, immunohistochemistry, and immunofluorescence to investigate PPIA's involvement in diseases like cancer, neurodegenerative disorders, and viral infections. These antibodies also help elucidate PPIA's dual roles: intracellularly as a chaperone and extracellularly as a chemotactic factor in inflammatory responses. Due to PPIA's high conservation across species, many antibodies exhibit cross-reactivity, enabling comparative studies in model organisms. Additionally, PPIA antibodies have potential diagnostic and therapeutic applications, particularly in targeting pathways associated with autoimmune diseases or viral pathogenesis. Understanding PPIA's multifaceted biology through these antibodies continues to advance research in immunology, virology, and molecular medicine.