Study shows effective and efficient methods for producing recombinant proteins

A shift in the life science market has begun to steer cell culture scientists to re-evaluate their use of native transferrin and iron chelators to pursue recombinant alternatives.  Transferrin regulates the uptake, transport and utilization of iron for cellular function, increasing cell growth and productivity.  Native transferrin found in bovine or human serum has been widely used in cell culture for these added benefits.  However, regulatory issues continue to arise with the use of native transferrin due to blood-borne pathogens. 

A recent study published May 2010 in the Protein Expression and Purification Journal demonstrated that transferrin is efficiently produced using recombinant technology. The study, 'Expression, Purification and Characterization of Recombinant Human Transferrin from Rice' concluded that recombinant human transferrin can be expressed at very high levels of 10 grams per kilogram of biomass. These results were accomplished by utilizing the unique and proprietary expression system known as ExpressTec.

"Using the ExpressTec system for animal component free production of recombinant proteins has proven to not only provide safety and regulatory advantages, but also allows cost-effective sources of recombinant proteins like transferrin," said Ning Huang, Vice President of Research and Development at InVitria.

Rice-derived recombinant human transferrin, tradename Optiferrin™, is structurally and functionally similar to native transferrin. The results of this study show that effective and efficient methods of producing recombinant proteins enable products like Optiferrin to be cost effective and safe when compared to animal-derived transferrin.

 "In this paper, we describe the unrivaled efficiency that we have achieved in a plant-based production system. These expression yields are significantly higher than other systems, which is critical to achieving commercially attractive products like Optiferrin, recombinant human transferrin," said Deshui Zhang, InVitria Scientist and Lead Author.

InVitria has utilized Optiferrin to develop cell culture media supplements that avoid concerns about blood-borne pathogens found in animal or human serum while still optimizing performance in cell culture.  Optiferrin eliminates the nuisances of serum contamination and iron chelators in mammalian cell culture by providing a well defined, high performance and animal-free solution.

"Transferrin delivers necessary iron to cells, maintains iron balance, and avoids the toxic effects of iron compounds. Optiferrin outperforms iron chelators and provides a cost effective alternative to animal-derived transferrin," said Dr. Steve Pettit, Director of Cell Culture Research and Development at InVitria.

Optiferrin is suitable for all applications in mammalian cell culture, stem cells, regenerative medicine and biopharmaceutical drug delivery.