Binding specificity and internalization properties of an antibody-avidin fusion protein targeting the human transferrin receptor.

摘要: The human transferrin receptor (hTfR1) is a membrane-bound protein involved in (Tf)-mediated iron uptake and highly expressed on malignant cells. A second version of the (hTfR2) also mediates Tf-dependent import. We previously developed composed avidin fused to mouse/human chimeric IgG3 specific for hTfR (anti-hTfR IgG3-Av) that was originally designed deliver biotinylated drugs into cancer have now found anti-hTfR IgG3-Av does not cross-react with hTfR2 binds hTfR1 surface cells, attached solid surface, solution. hemochromatosis (HFE), another ligand TfR, inhibit binding receptor. In addition, using live cell laser scanning confocal microscopy (LCLSCM) we demonstrated are internalized cells expressing at similar rate. Furthermore, our proliferation morphological studies effective cytotoxicity toxin delivered by only hTfR1. Our results better define properties pave way rational design future vitro vivo treatment malignancies.