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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P13210(IL16 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P13210(IL16 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

Interleukin-16 (IL-16) is a pro-inflammatory cytokine primarily produced by CD8+ T cells, though it is also secreted by other immune cells such as mast cells, eosinophils, and dendritic cells. Initially identified as a chemoattractant for CD4+ immune cells, IL-16 plays a regulatory role in immune responses by binding to the CD4 receptor, influencing T-cell activation, migration, and apoptosis. Its structure includes a PDZ domain and a C-terminal bioactive region, with the precursor protein (pro-IL-16) requiring proteolytic cleavage to release the active cytokine. Dysregulation of IL-16 has been linked to chronic inflammatory diseases, autoimmune disorders (e.g., rheumatoid arthritis, multiple sclerosis), and allergic conditions like asthma.

IL-16 antibodies are critical tools for detecting and quantifying IL-16 in research and diagnostics. They enable the study of IL-16 expression patterns, signaling pathways, and its role in disease mechanisms. Monoclonal antibodies offer high specificity, while polyclonal antibodies provide broader epitope recognition. Applications include ELISA, Western blot, immunohistochemistry, and flow cytometry. In therapeutic contexts, IL-16-neutralizing antibodies are explored for mitigating inflammation or autoimmune activity. However, challenges remain in understanding IL-16's dual roles in immune regulation and pathology, necessitating further research to clarify its therapeutic potential.