Recombinant Human IL6 protein

Interleukin-6 (IL-6) is a multifunctional cytokine central to immune regulation, inflammation, hematopoiesis, and tissue homeostasis. Discovered in 1986. it is produced by various cell types, including macrophages, T cells, and endothelial cells, in response to infections or tissue injuries. Structurally, IL-6 is a 21-28 kDa glycoprotein featuring a four-helix bundle fold, binding to its receptor complex (IL-6Rα and gp130) to activate downstream signaling pathways like JAK/STAT, MAPK, and PI3K. Its dual role in pro-inflammatory and anti-inflammatory responses makes it pivotal in both host defense and pathological conditions such as chronic inflammation, autoimmune diseases, and cancer.

Recombinant IL6 protein, produced via genetic engineering in systems like *E. coli*, mammalian cells, or yeast, allows controlled study of IL-6 biology. The production involves cloning the IL6 gene into expression vectors, followed by purification using affinity chromatography (e.g., His-tag) and quality validation (SDS-PAGE, bioactivity assays). Unlike native IL-6. recombinant forms offer batch consistency and scalability, critical for research and therapeutic development.

In research, recombinant IL6 is used to model inflammatory diseases, cancer progression (e.g., promoting tumor growth via STAT3), and regenerative processes (e.g., liver regeneration). It also aids in drug discovery, such as screening IL6 pathway inhibitors (tocilizumab, sirukumab). Clinically, dysregulated IL6 signaling is linked to rheumatoid arthritis, cytokine storms (e.g., COVID-19), and multiple myeloma, positioning recombinant IL6 tools as vital for mechanistic studies and therapeutic targeting. However, its pleiotropic effects necessitate careful experimental design to dissect context-specific roles.