The expression of Ig fragments in Escherichia coli permits rapid acces
s to engineered molecules with antigen-binding properties. While the e
xpression in 'a functional state by secretion to the periplasm is the
standard method for the production of Fv and Fab fragments, single cha
in Fv fragments are mainly produced by refolding from insoluble aggreg
ates. Although all of these Ig fragments serve as valuable aids in the
study of antigen binding, their different biochemical properties must
be considered when using them as research tools or for medical applic
ations. In addition to these simple univalent antibody fragments, the
bacterial expression of bivalent and bispecific versions and of hybrid
proteins with novel effector functions is gaining increasing importan
ce.