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A DNA sequence encoding the signal peptide and extracellular domain of human Interleukin 2 receptor beta chain (aa 1-237) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Interleukin-2 (IL-2) is a pleiotropic glycoprotein that mediates the production of regulatory T cells and promotes T cell dependent tolerance. Additionally, IL-2 promotes the proliferation of antigen-activated T lymphocytes, facilitates the cytolytic activity of natural killer (NK) cells and stimulates anti-tumor activity in monocytes by inducing synthesis of GM-CSF, IL-1b and IL-6. IL-2 also promotes the proliferation of large granular lymphocytes and the growth and differentiation of mitogen activated B lymphocytes in vitro. The biological effects of IL-2 are mediated through the IL-2 receptor, which is predominantly expressed on activated T cells, B cells and monocytes. There are three subunits that may associate in different combinations to form the IL-2 receptor. These subunits include IL-2Ra, IL-2 R beta (IL-2Rb), which is shared with IL-15 receptor and IL-2Rg, which is also known as the common cytokine receptor gamma chain (gc) as it is shared with receptors for IL-4, IL-7, IL-9, IL-15 and IL-21. Different associations of these subunits form low affinity, intermediate affinity or high affinity IL-2 receptors. The low affinity receptor comprises the IL-2Ra glycopeptide, the intermediate affinity receptor is formed by the association of IL-2R beta and the gc while the high affinity receptor comprises IL-2 Ra, IL-2 Rb and gc chains. IL-2 R beta is expressed on resting T cells and is up regulated by T cell activation, particularly by treatment with IL2, anti-CD3 and anti CD28. The beta subunit is involved in both binding to IL2 and mediating signal activation. IL-2 R beta is a glycoprotein that contains 4 potential N-linked glycosylation sites.