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Study Demonstrates a Safe and Cost Effective Source of Recombinant Human Transferrin
Date:6/17/2010

Optiferrin, InVitria’s recombinant human transferrin, outperforms iron chelators and provides a cost-effective cell culture media supplement that is consistent and animal component free.

Fort Collins, CO (PRWEB) June 17, 2010 -- 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 OptiferrinTM, 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 s
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