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A DNA sequence encoding the signal peptide and extracellular domain of human Ox40 (aa 1-207) was fused to the Fc region of human IgG1 (93-330). The chimeric protein was expressed in modified human 293 cells.

Ox40 is a member of the tumor necrosis factor receptor (TNFR) family. It is a type I transmembrane protein expressed primarily on the surface of activated CD4+ T-cells. It is also expressed at low levels on the surface of activated CD8+ T cells, B cells, dendritic cells and eosinophils. Ox40 is a co-stimulatory molecule involved in T-cell activation and proliferation, the induction of cytokine production by effector T-cells, generation of memory T-cells, and arresting peripheral T-cell tolerance in vivo. Expression of Ox40 is induced following the initiation of a CD28 signal. It has been reported that the interaction of Ox40 with its ligand plays a role in the expansion of T-cell numbers at the height of the immune response as well as the generation of memory T-cells. Human Ox40 comprises a 186 amino acid extracellular domain containing four TNFR-Cys repeats, followed by a 21 amino acid transmembrane domain and a 42 amino acid cytoplasmic domain. Ox40 activity is mediated by NF-kappaB signaling via interaction of the intracellular domain of Ox40 with TRAF proteins. Deregulated levels of Ox40 or an imbalance between Ox40 and Ox40L may result in T-cell mediated diseases especially allergic, inflammatory and autoimmune diseases. Additionally, Ox40 may also be important in the enhancement of anti-tumor responses. For a review of the potential of Ox40 as a clinical target please refer to Weinberg AD (2002) Trends Immunol. 23(2): 102-9.