Recombinant Human IL-1α protein

Interleukin-1 (IL-1) pseudo-recombinant proteins are engineered molecules designed to modulate IL-1 signaling, a critical pathway in inflammation and immune responses. The IL-1 family comprises key cytokines like IL-1α and IL-1β, which bind to IL-1 receptors (IL-1R1 and IL-1R2) to regulate pro-inflammatory processes. Dysregulation of this pathway is implicated in autoimmune diseases, chronic inflammation, and cytokine storm syndromes. Traditional IL-1 inhibitors, such as recombinant IL-1 receptor antagonists (e.g., anakinra) or neutralizing antibodies, have therapeutic limitations, including short half-life or immunogenicity.

IL-1 pseudo-recombinant proteins are hybrid molecules combining functional domains of IL-1 receptors or binding proteins with stabilizing elements (e.g., Fc regions). For example, constructs may fuse the extracellular domain of IL-1R1 or IL-1R2 (which binds IL-1 cytokines) to immunoglobulin Fc fragments to enhance pharmacokinetics. These proteins act as decoy receptors, competitively inhibiting IL-1α/β from engaging native receptors, thereby suppressing downstream NF-κB and MAPK signaling. Unlike natural inhibitors, pseudo-recombinant variants are optimized for prolonged serum stability and reduced clearance.

Their development leverages recombinant DNA technology, often using mammalian expression systems to ensure proper post-translational modifications. Applications span therapeutic research (e.g., rheumatoid arthritis, sepsis) and mechanistic studies of IL-1-driven pathologies. Challenges include balancing high-affinity binding with minimal off-target effects and ensuring proper dimerization for functional activity. Ongoing research aims to refine specificity and delivery methods, positioning IL-1 pseudo-recombinant proteins as versatile tools for both clinical and experimental immunology.