Recombinant Human IL-32 protein

Interleukin-32 (IL-32) is a pro-inflammatory cytokine first identified in 2005. primarily expressed by immune cells (e.g., T cells, NK cells) and epithelial cells. Unlike classical interleukins, IL-32 lacks a secretory signal peptide, suggesting unconventional release mechanisms, such as exosome-mediated transport or passive release during cell death. It exists as nine splice variants (IL-32α to IL-32θ), with IL-32γ being the most biologically active isoform due to its full-length structure. IL-32 activates multiple signaling pathways, including NF-κB, p38 MAPK, and caspase-1. promoting the production of inflammatory mediators (e.g., TNF-α, IL-6. IL-1β) and driving immune responses against bacterial, viral, and fungal infections.

Recombinant IL-32 proteins, produced via bacterial (e.g., E. coli) or eukaryotic expression systems, are critical tools for studying its role in diseases. Studies link IL-32 to chronic inflammatory conditions (rheumatoid arthritis, inflammatory bowel disease), cancer progression, and autoimmune disorders. Its dual role—pro-inflammatory in infections but pathogenic in chronic inflammation—makes it a therapeutic target. Recombinant IL-32γ is widely used to model inflammation in vitro and in vivo, while isoform-specific proteins help dissect functional differences. However, challenges remain, including undefined receptors and context-dependent signaling. Recent work explores IL-32's interaction with intracellular sensors (NOD2) and its regulation of metabolic pathways. Despite unresolved mechanisms, recombinant IL-32 remains pivotal for unraveling its immunomodulatory functions and developing targeted therapies.