Recombinant Antibodies for Ectopic Expression

  • Andrew Bradbury
Part of the Biotechnology Intelligence Unit book series (BIOIU)


Antibodies or immunoglobulins are divided into 5 classes: IgA, IgD, IgE, IgG and IgM of which IgG is the most abundant in both mouse and human serum. The antibody molecule consists of four polypeptide chains, two identical heavy (H) chains and two identical light (L) chains held together by a combination of disulfide bonds and noncovalent interactions, as shown in Figure 3.1. Digestion of IgG with the proteolytic enzyme papain divides the antibody molecule into two identical antigen binding fragments, called Fabs, and a fragment called Fc. The polypeptide chains of immunoglobulins are composed of domains of similar structure, each consisting of two stacked layers of β sheets surrounding an internal space filled with hydrophobic amino acid side chains, with terminal exposed loops. They are termed either constant (C) or variable (V) on the basis of the degree of sequence variation amongst different antibody molecules, which is focused on the three, hypervariable, exposed loops at the top of the variable domains. The intervening strands of more rigid anti-parallel β sheet are termed framework regions and are highly conserved.1 The hypervariable loops of a pair of VH and VL domains (H1, H2, H3 and L1, L2, L3) together form the antigen binding site. These loops, which vary in length and in sequence, are also known as complementarity determining regions (CDRs) due to their dominant role in determining the shape of the binding site and its specificity.


Phage Display Versus Region Recombinant Antibody Phage Display Library Phage Antibody 
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  • Andrew Bradbury

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