| Antibody is an important tool in cancer targeting therapy. The specific delivery of drugs to the targeting site can significantly enhance the efficacy and decrease the side effects of the drug. As an appealing approach, the use of antibody has entered clinical stages. However, there still have many limitations in the field of antibody-based therapy. Because of macromolecular size, the intact antibody molecule poorly penetrates into the solid tumor. In addition, the monoclonal antibody of mouse origin can induce human anti-mouse antibody response. Therefore, one of the trends in development of monoclonal antibody therapeutics is the molecule-downsizing of the drug. The antibody miniature studies highlight on the fragments of F(ab')2, Fab, scFv and single antibody domain (dAbs). The single antibody domain only has the 1/12 molecular size of entire antibody and shows low immunogenicity. Like other minimizations, dAbs offer the advantages of increasing rates of tumor penetration. Using the antibody single domain as the guided vehicle to combine with extremely potent drug as the "warhead" agent may lead to constructing highly potent antibody-based therapeutics with down-sized molecule.In this study, we constructed an energized fusion proteins consisting of LDM and single domain antibodies derived from rat mAb 3A5 directed against hepatocarcinoma and further studied its biological activity. 1. Immunoaffinity determination of the rat mAb 3A5mAb 3A5, an anti-hepatocarcinoma mAb, was secreted by hybridoma cells that were obtained by immunize LOU/C rats with Bel 7402 cells (human liver caner cells), followed by fusion of spleen cells and rat IR983F myeloma cells. The immunofluorescence assay results showed that rat mAb 3A5 stained mainly on the... |
PDF Full Text Request