In routine cell culture, transferrin is customarily supplied as a natural component of fetal bovine serum (FBS). The growing use of serum-free, chemically defined media in the culture of cells destined for downstream clinical therapeutic applications, however, necessitates use of a purified, recombinant form of this essential component.
InVitria’s recombinant human transferrin, Optiferrin, is completely free of animal and human components and is produced in a scalable, non-mammalian expression system. It is fully human in primary sequence, is ⍺-glycosylated during expression in the host, and shares secondary and higher-order structural equivalence with naturally occurring human holo-transferrin. Its functional performance in cell culture is equivalent to human holo-transferrin in terms of reversible iron binding, transferrin-receptor binding, and promoting cell growth and productivity.
Optiferrin is naturally free of prion agents and carries a far lower potential risk of contamination with other human or mammalian adventitious agents compared to serum-derived components and recombinant proteins produced in other systems. Its purity makes it ideal for demanding research and commercial applications.