Transferrin is a protein found in the blood plasma, a glycoprotein that is specific for controlling free iron in the bodies' biological fluids. Transferrin has two binding sites that are specific for very tight and reversible iron binding. The binding of iron to transferrin can be related to pH levels, among other things, with a high binding affinity for a more acidic pH and decreasing levels as the blood pH becomes more basic. This binding affinity is the basis for the transport mechanism of Transferrin. When the protein, attached to iron, encounters a cell with a transferring receptor, it is transported in a vesicle. While traveling in the vesicle, the pH is reduced by hydrogen ion pumps to a more basic level, around 5.5, causing Transferrin to release the iron ions. The receptor is then transported via vesicle back to the cell surface, and the whole process repeats itself.
Transferrin was discovered over 30 years ago, with credit going to Dessauer and Zwiefel who looked at genes of kingsnakes to determine that Transferrin is inherited as a co-dominant trait. Transferrin and Serum Transferrin Receptor have been used to discriminate between iron deficiency anemia and anemia of inflammation, which can be found in infants at a prevalence of 10-40%. Because of the novel uses of this protein, it is instrumental in a great deal of research. Among its many uses, Transferrin is a staple in cell culture media when the investigator is concerned with regulating cellular iron uptake, utilization and transport. But due to a common contamination of blood borne pathogens, it is essential that it be free from contamination. Therefore, recombinant Transferrin is preferred over human or animal plasma-derived transferrin. Fortunately, there is a fully functional Transferrin protein available in a purified, recombinant form right from Novus Biologicals!
This guest blog was submitted by Novus customer, Shannon Cain of the University of Colorado Denver.
Novus Biologicals offers Transferrin reagents for your research needs including:
