A recombinant partial protein sequence (within amino acids 311-445) from the human protein was used as the immunogen for the Transferrin antibody.
Iron (Fe) is a tightly metabolically controlled mineral and growth factor present in all living cells. Iron not bound in erythrocyte hemoglobin is transported by transferrin (Tf), the iron transport protein of vertebrate serum. The transferrin protein contains two homologous domains, each of which contain an Fe-binding site. The majority of transferrin is synthesized in the liver and secreted into the blood, but it is also produced in lower amounts in testis and brain as well as in oligodendrocytes, where transferrin is an early marker of oligodendrocyte differentiation. From the blood, transferrin is internalized by erythroblasts and reticulocytes upon binding the transferrin receptor (TfR), also designated CD71, through a system of coated pits and vesicles. After Fe release, transferrin is returned to the extracellular medium, where it can be reused. Defects in the transferrin gene results in atransferrinemia, a rare autosomal recessive disorder characterized by microcytic anemia and iron loading.
