serotransferrin is a member of transferrin family. TF (transferrin) is a 80kDa monomeric blood plasma glycoprotein with iron bindinding property. It is braodly divded into two regions with two iron binding sites. Both the N-terminal and C-terminal domains consist of two sub domains (N1 and N2, C1 and C2) connected by a hinge region.

Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron (Fe) in biological fluids.Transferrin glycoproteins bind iron tightly, but reversibly. The affinity of transferrin for Fe(III) is extremely high (association constant is 1020 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.

plays a role iin iron transport and homeostasis [RGD, Feb 2006]

Transferrin (TF) is a glycoprotein with an approximate molecular weight of 76.5 kDa. It is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of Transferrin (TF) is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. Transferrin (TF) may also have a physiologic role as granulocyte/pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum.

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.