Author: Frenzel, André; Hust, Michael; Schirrmann, Thomas
Title: Expression of Recombinant Antibodies Document date: 2013_7_29
ID: 06o7pa3d_4
Snippet: The smallest antigen binding fragment of immunoglobulins maintaining its complete antigen binding site is the Fv fragment, which consists only of variable (V) regions. A soluble and flexible amino acid peptide linker is used to connect the V regions to a scFv (single chain fragment variable) fragment for stabilization of the molecule (24), or the constant (C) domains are added to the V regions to obtain a Fab fragment (Figure 1) . Today, scFv and.....
Document: The smallest antigen binding fragment of immunoglobulins maintaining its complete antigen binding site is the Fv fragment, which consists only of variable (V) regions. A soluble and flexible amino acid peptide linker is used to connect the V regions to a scFv (single chain fragment variable) fragment for stabilization of the molecule (24), or the constant (C) domains are added to the V regions to obtain a Fab fragment (Figure 1) . Today, scFv and Fab are the most widely used antibody fragments which are produced in prokaryotes. Other antibody formats have been produced in prokaryotic and eukaryotic cells, for example, disulfide-bond stabilized scFv (ds-scFv) (25), single chain Fab fragments (scFab) combining scFv and Fab properties (26) as well as di-and multimeric antibody formats like dia-, tria-, or tetra-bodies (27, 28) or minibodies (miniAbs) comprising different formats consisting of scFvs linked to oligomerization domains like immunoglobulin CH 3 domain (28), leucin zipper, helix turn helix motif streptavidin, or scFv-scFv tandems (29-31). Bispecific antibody formats combine two different antigen binding domains in one molecule (32-34). The smallest antibody fragments are V HH s of cameloide heavy chain antibodies (35) and single domain antibodies (dAb) (36, 37).
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