Recombinant Human IL-8 protein

Interleukin-8 (IL-8), also known as CXCL8. is a small chemokine protein belonging to the CXC subfamily. It plays a central role in mediating inflammatory and immune responses by acting as a potent chemoattractant for neutrophils, T-cells, and other immune cells. Initially identified in the 1980s, IL-8 is secreted by various cell types, including macrophages, endothelial cells, and epithelial cells, in response to pro-inflammatory stimuli like TNF-α, IL-1β, or bacterial lipopolysaccharides (LPS). Its primary function involves recruiting immune cells to infection or injury sites, promoting angiogenesis, and facilitating wound healing. However, dysregulated IL-8 expression is linked to chronic inflammation, autoimmune disorders, and cancer progression, particularly in tumor microenvironment modulation and metastasis.

Recombinant IL-8 protein is produced using genetic engineering techniques, often in *E. coli* or mammalian expression systems, ensuring high purity and biological activity. The non-glycosylated form from prokaryotic systems retains functional efficacy, while eukaryotic systems may yield glycosylated variants closer to native human IL-8. Structurally, IL-8 contains a conserved CXC motif and a flexible N-terminal domain critical for receptor binding, primarily targeting CXCR1 and CXCR2 on neutrophils.

In research, recombinant IL-8 is widely used to study neutrophil migration, inflammatory pathways, and cancer biology. It serves as a tool for drug discovery, particularly in developing inhibitors targeting IL-8 signaling to treat inflammatory diseases or block tumor-associated angiogenesis. Studies also explore its role in COVID-19-related cytokine storms and fibrosis. Despite its pathogenic associations, IL-8 remains vital for understanding immune regulation, making its recombinant form indispensable for both basic and applied biomedical research.