Jax Labs eBook - 31

Quick Facts to Improve Antibody Half-Life Measurements
JANINE LOW-MARCHELLI, PhD, Senior Technical Information Scientist

I

f you're developing a therapeutic molecule, the half-life of your molecule in circulation is an essential factor to consider. A longer
half-life means patients don't need to be dosed as often, therapies are more likely to be efficacious, and therefore, the treatment is
more likely to be approved by regulatory agencies like the FDA.
Figure 1. Examples of monoclonal antibodies used in
cancer therapy. IgGs are versatile molecules that generate
a therapeutic response through a variety of mechanisms:
eliciting immune effector functions (A), blocking ligandreceptor interactions (B, C), or delivering targeted chemical
payload (D). Adapted from Weiner GJ, 2015.

WHICH MOLECULES HAVE A LONG HALF-LIFE IN BLOOD?
Monoclonal antibodies, specifically those of the IgG class, experience significantly
longer half-lives than other molecules. Additionally, IgGs have a high degree of
target specificity. Both of these characteristics make IgGs desirable therapeutic
molecules (Figure 1).
IgG half-life is primarily regulated by binding to the neonatal Fc Receptor (FcRn),
through the IgG's constant region, Fc. This Fc-FcRn binding occurs in the acidic
lysosome of endothelial cells and rescues IgG from cellular degradation pathways.
Intact IgG is then released back into the bloodstream at neutral pH. Fc- and
albumin-conjugates also have long half-lives because they, too, bind FcRn and are
protected similarly (Figure 2).
31 | GENengnews.com

Figure 2. IgGs experience high serum half-life due to the
protective FcRn recycling pathway. Adapted from Roopenian et
al., 2007.


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