chimeric antibody

Initial therapeutic antibodies were usually murine molecules. These murine-derived antibodies have a short half-life in vivo, a limited penetration into tumour sites and inadequately recruit host effector functions. Therefore, chimeric antibodies have gradually replaced them in therapeutic applications, being a new generation of therapeutic candidates. The chimeric antibodies can be created by fusing murine variable domains, responsible for the binding activity, with human constant domains. These antibodies are 70% human and possess a fully human Fc portion, which makes them considerably less immunogenic in humans as well as allows them to interact with human effector cells and the complement cascade.