With the introduction of the B-cell hybridoma technology, where antibo
dy producing B-lymphocytes are immortalized by fusion with myeloma cel
ls it became possible to produce monoclonal antibodies of almost any d
esired antigen specificity. Although this technique has been described
already 19 years ago and the therapeutic potential of many monoclonal
s has been established since, so far only a single monoclonal antibody
is widely used in the clinic. The application of murine monoclonal an
tibodies for human therapy is hampered by a short half-life in the cir
culation, inefficient activation of human antibody effector functions
and the development of undesired immune responses against the xenogeni
c antibody protein epitopes. As techniques for genetic manipulations o
f murine antibodies and for production of human antibodies are current
ly developing rapidly, it can be expected that these problems will not
impede the successful application of therapeutic monoclonal antibodie
s in the future.