This antibody-cytokine fusion protein was achieved by conjugating/fusing the Anti-EpCAM dI-IgG (FN>AQ)-ala to IL2 (D20T). It was expressed in CHO and purified with affinity chromatography. The immunocytokine retains the ability to bind the EpCAM as well as the biological activity of IL2. The Ig-moiety for this IL-2 (D20T) fusion protein was derived from the constant region of an IgG γ4 subclass, which in addition retained features of the IgG γ1 hinge. Furthermore, mutations that remove potential T-cell epitopes were introduced. Additionally, this fusion protein contains the substitution from asparagine to glutamine, which eliminates the N-glycosylation site in Fc. The concomitant substitution of a phenylalanine to alanine removes the potential T-cell epitope. This immunocytokine was designed for treating solid tumor.
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