InVitria’s Recombinant Human Transferrin Production Technology Shown to be Significantly More Cost-effective Compared to Alternatives
Fort Collins, CO, USA, March 30, 2011 / b3c newswire / – InVitria was recently cited in a review article titled “Recombinant human transferrin: Beyond iron binding and transport”, published in Biotechnology Advances. The article describes the importance of utilizing recombinant human transferrin in therapeutic applications and as a means to eliminate the use of fetal bovine serum in biopharmaceutical manufacturing systems such as stem cells, regenerative medicine, cell-based vaccines and protein therapeutics. InVitria’s Optiferrin (recombinant human transferrin) and Lacromin (recombinant human lactoferrin) were identified in the review as commercial animal-free supplements that replace fetal bovine serum or blood plasma derived transferrin in serum-free media formulations.
The publication emphasizes the importance of maintaining an animal-free mammalian cell culture environment for the production of biopharmaceuticals. In the past, fetal bovine serum (FBS) was widely used to maintain the health of mammalian cell production systems and to improve growth and productivity. This practice has changed significantly due to performance problems encountered with FBS, including batch-to-batch variation associated with its intrinsically undefined nature leading to unpredictable results. There have also been serious concerns raised by the Food and Drug Administration (FDA) and other global regulatory agencies about prion (the infectious causative agent associated with Mad Cow Disease) and viral contamination risks associated with FBS and other animal-derived components used in biomanufacturing and cellular therapy. As a result, serum-free media that can maintain acceptable levels of growth and productivity for mammalian cell culture are vital to the biopharmaceutical production market. This article identifies transferrin as being essential to serum-free media formulations for optimal iron transport and delivery, critical aspects to cell survival and culture performance.
“It has long been recognized that serum and animal components are undesirable in biopharmaceutical manufacturing and are being phased out. InVitria has addressed this issue by creating a line of animal-free media supplements designed to improve serum-free media formulations,” said Shawn Smith, Vice President of Sales & Marketing at InVitria.
InVitria’s production system, called ExpressTec, was also identified as having significantly higher yield when compared with competing systems, such as yeast and E. coli. InVitria’s yield is forty percent of total soluble protein, which is many times higher than the next best system identified in the publication. “We are very pleased with the results achieved by ExpressTec and its ability to deliver cost-effective recombinant proteins at commercial volumes. It is a breakthrough for the biotechnology industry,” said Ning Huang, Vice President of Research and Development.
The article goes on to identify several direct human health indications as potential uses for recombinant transferrin, including use as a therapeutic agent for diseases such as diabetes and age related macular degeneration. Transferrin can also be used as a carrier for cancer drug delivery, gene delivery in gene therapy, and oral delivery of therapeutic proteins.
About InVitria - www.InVitria.com
InVitria develops, manufactures and markets a portfolio of animal component free products used in cell culture, diagnostics and bioproduction. InVitria’s products address customer needs for defined, safe and consistent cell culture supplements in stem cell technology, regenerative medicine, biomanufacturing, cell-based vaccines and life science research.
Brandsma, M., A. Jevnikar, S. Ma, Recombinant human transferrin: Beyond iron binding and transport. 2011. Biotechnology Advances. 29: 230-238.
Zhang, D., Nandi S, P. Bryan, S. Pettit, D. Nguyen, M. Santos, N. Huang, Expression, purification, and characterization of recombinant human transferrin from rice (Oryza sativa L.). 2010. Protein Expression and Purification. 74: 69-79.