Human blood plasma is rich in proteins, including immunoglobulins (IgG), coagulation
factors (Factors II, VIII, IX, and X), alpha-1 antitrypsin, fibrin sealants, and albumin.
These proteins boost the immune system and fight inflammation and infection, making
plasma-derived biotherapeutics useful in treating rare, chronic, and often genetic
diseases. Unfortunately, the current worldwide demand for intravenous IgG (IVIG)
products exceeds current plasma collection supply.

For over 70 years, IgG has been produced using the Cohn process, which fractionates –
plasma proteins based on their differential solubility in ethanol with variances in
temperature, pH, ionic strength, and protein concentration. The modern Cohn process is
widely known to achieve yields of only 50-60% of the starting IgG, and the process
takes between 7-10 days to complete. Not only does working with large volumes of
ethanol create environmental concerns, IgG produced by Cohn fractionation also carries
an inherent risk of protein denaturation, because it is produced with the combination of
alcohol and extreme pH changes.

Avoiding the combined effects of alcohol and low pH could improve protein stability, in vivo half-life, patient tolerability, and reduce the immunogenicity of protein therapeutics. Given the scarcity of IgG products and the inability of plasma collections to satisfy patient demands for IgG, there is a clear need for a new process that addresses the shortcomings of the Cohn fractionation process.