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A DNA sequence encoding the signal peptide and extracellular domain of human Interleukin 7 receptor alpha chain (IL-7Ra)(aa 1-236) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Interleukin 7 (IL-7) is a cytokine that is essential for lymphopoiesis as well as T cell homeostasis and the maintenance of T cell diversity. Additionally, IL-7 promotes T cell cytolytic responses, and acts as co-stimulator for the activation of mature B cells. The biological effects of IL-7 are mediated through binding to the IL-7 receptor (IL-7R) complex. The high affinity receptor complex for IL-7 is composed of the ligand binding IL-7 receptor-alpha (IL-7 R alpha; IL-7Ra) chain and a common gamma chain shared by cytokine receptors for IL-2, IL–4, IL–9 and IL–15. IL-7Ra is expressed on bone marrow lymphoid precursors, pro-B cells, monocytes/macrophages, natural killer (NK) cells, naïve T cells and memory CD4+ and CD8+ T cells. IL-7Ra is also expressed on non-immune somatic cells such as intestinal colorectal and renal carcinoma cell lines and keratinocytes. IL-7Ra is a 439 amino acid membrane glycoprotein and contains 7 potential N-linked and 2 C-linked glycosylation sites. For a recent review of the role of IL-7 please refer to Fry TJ et al., (2005) J Immunol. 174(11): 6571-6.