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Methods of Purifying Antibodies

Technology Number: 

1865
Summary 

THE INNOVATION:

 

A non-chromatographic antibody purification method not relying on Protein A nor any ligand, had been developed. Highly pure (>95%) human, mouse, rabbit or sheep IgG's are obtained in good yields within 20-30 minutes. The technology addresses a projected $440M antibody purification reagents market.

 

MARKET OPPORTUNITY:

 

The past two decades have evidenced a strong focus on monoclonal antibody (mAb) therapeutics. Today, there are already 50 antibody-based drugs on the market; more than 550 are at various stages of development; and the competition among the large biopharmaceutical companies is aggressive. The global market for mAb therapeutics in 2014 reached USD 80.3 billion. The global mAb market is expected to rise at a compound annual growth rate (CAGR) of 8.1% to nearly USD 128 billion by 2020. The development of these new molecular agents, successfully directed to specific cellular targets, is playing a crucial role in the pharmaceutical industry. This trend shows the strong focus of top biopharmaceutical companies on biologics, including mAb therapeutics (Frost & Sullivan 2015).

 

Accordingly, the rapid growth of the mAb market is driving pharmaceutical firms to find avenues that will reduce production costs. Purification of mAb's, is still a major contributor (50-80%) of manufacturing costs, particularly due to the use of Protein A columns. Whereas Protein A is the most efficient, specific and common ligand used by all biopharmaceutical companies, it is also highly expensive. It is estimated that removal of the Protein A step would cut 40% in the total production costs of mAb's and this is exactly what our technology is aiming at. 

 

THECHNOLOGY:

 

The technology relies on unique detergent scaffolds onto which IgG's bind almost quantitatively, whereas the vast majority of non-IgG proteins are rejected. Bound IgG's are recovered from the detergent scaffolds in great purity (>95%) while leaving residual impurities behind. IgG purification was demonstrated in serum-free media containing BSA\HSA. The fact that, purified IgG's preserve their binding specificity, implies that, the presented method may provide a cost-effective viable alternative to: Protein A chromatography