Recombinant Human IL-5 protein

Interleukin-5 (IL-5) is a cytokine primarily involved in the regulation of eosinophil production, activation, and survival. It belongs to the common beta-chain (βc) receptor cytokine family and plays a critical role in innate and adaptive immunity, particularly in responses to parasitic infections and allergic inflammation. Structurally, IL-5 is a homodimeric glycoprotein with two identical subunits linked by disulfide bonds, each containing a four-helix bundle motif. Its gene is located on human chromosome 5.

Recombinant IL-5 is produced using genetic engineering techniques, typically expressed in mammalian cell systems (e.g., CHO cells) or microbial platforms (e.g., E. coli) to ensure proper folding and post-translational modifications. The recombinant protein retains the biological activity of native IL-5. enabling researchers to study its functions in vitro and in vivo. It binds to the IL-5 receptor complex (IL-5Rα/βc) on target cells, activating JAK-STAT, MAPK, and PI3K signaling pathways to promote eosinophil differentiation, proliferation, and effector functions.

IL-5 dysregulation is implicated in eosinophil-related disorders, including asthma, atopic diseases, and hypereosinophilic syndromes. Recombinant IL-5 has become a vital tool for investigating these pathologies and validating therapeutic strategies. Notably, anti-IL-5 biologics like mepolizumab and reslizumab, developed using recombinant protein technology, have shown clinical efficacy in reducing eosinophilic inflammation. Beyond therapeutic applications, recombinant IL-5 is used in cell culture systems to maintain eosinophil populations and study immune cell interactions. Its role in B-cell activation and IgA production also makes it relevant to mucosal immunity research. As eosinophils gain attention in cancer and autoimmune diseases, recombinant IL-5 remains crucial for unraveling its multifaceted roles in health and disease.