Recombinant Human IL5 protein

Interleukin-5 (IL-5) is a cytokine primarily involved in regulating the growth, differentiation, and activation of eosinophils, a type of white blood cell critical in immune responses against parasites and allergic inflammation. It functions by binding to a heterodimeric receptor complex (IL-5Rα and βc subunits) on target cells, triggering signaling pathways like JAK-STAT, which promote eosinophil survival and recruitment to tissues. Dysregulated IL-5 signaling is implicated in eosinophilic disorders, including asthma, chronic rhinosinusitis, and hypereosinophilic syndromes.

Recombinant IL-5 protein, produced via genetic engineering in systems like mammalian (e.g., CHO cells) or bacterial (e.g., E. coli) expression platforms, enables precise study of IL-5 biology and therapeutic development. Unlike native IL-5. recombinant forms are highly purified, standardized, and free of contaminants, making them essential tools for in vitro assays, animal studies, and drug screening. They retain functional activity, binding to IL-5 receptors to simulate or inhibit downstream effects.

Clinically, IL-5-targeted biologics—such as monoclonal antibodies (e.g., mepolizumab, reslizumab)—leverage insights from recombinant IL-5 research to neutralize IL-5 or its receptor, reducing eosinophil levels in diseases like severe eosinophilic asthma. However, recombinant IL-5 itself has limited therapeutic use due to its pro-inflammatory role. Current studies focus on optimizing IL-5 pathway modulation, balancing efficacy with safety, and exploring combination therapies. Challenges remain in understanding tissue-specific effects and long-term impacts of IL-5 inhibition, driving ongoing research into its molecular mechanisms and translational applications.