Go Back IL-1 RI - Fc Chimera

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A DNA sequence encoding the signal peptide and extracellular domain of human IL-1 Receptor I (IL-1RI) (aa 1-333) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells

IL-1RI is an 80kDa type I transmembrane glycoprotein expressed on T cells and fibroblasts. Structurally the extracellular domain (ECD) of IL-1R1 contains 3 Immunoglobulin like domains. Glycosylation of IL-1R1has been shown to be necessary for optimal binding of IL-1, as blocking of glycosylation sites reduces binding to IL-1. IL-1 is a proinflammatory cytokine involved in immune responses including both innate and acquired immunity and specifically stimulates T-helper cells to express cytokines associated with inflammatory responses. IL-1 also induces the expression of adhesion molecules such as intracellular adhesion molecule-1 (ICAM-1) on mesenchymal cells and vascular-cell adhesion molecule-1 (VCAM-1) on endothelial cells, which promotes infiltration of inflammatory cells. Deregulation of IL-1 expression has been implicated in autoimmune disease and inhibition of IL-1 signaling alleviates joint destruction in rheumatoid arthritis. Additionally, IL-1 also increases the expression of vascular endothelial growth factor (VEGF), so may play a role in blood vessel supply in tumor progression. The functional effects of IL-1 are mediated through binding to the IL-1 receptors. There are three major receptors for IL-1 namely, IL-1RI, IL-1RII and IL-1R3, all three receptors bind to IL-1a and IL-1b while IL-1RI and IL-RII also bind to IL-1ra. For a recent review on a novel regulator of IL-1R refer to Immunol Lett. 2005 96:27-31.