Immunoproapoptotin consists of a single-chain antibody against tumor-specific surface marker and an active domain which has the function of translocation and pro-apoptosis. This fused recombinant protein can specifically recognize and kill tumor cells. Immunoproapoptotin comes from immunotoxin which is proved not successful in clinical trials by inducing neutralizing antibody and other side effects due to the heterogenous toxins domains from bacteria or plants. To avoid the immunogenicity of immunotoxin, effectors from human were employed in the 2nd generation of Immunoproapoptotin. However, the translocation domain is still heterogenous and the efficiency of translocation is limited. In the latest progress, a furin cleavage site was used to substitute for the translocation domain and thus enhanced the translocation efficiency and greatly reduced the immunogenicity of Immunoproapoptotin, demonstrating a wide clinical application prospects.