TF 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 1 ion of ferric iron. The function of transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. In addition to its function in iron transport, transferrin may also have a physiologic role as granulocyte/pollen-binding protein (GPBP) involved in the removal of certain organic matter/allergins from serum.
Immunogen
Serotransferrin monoclonal antibody was raised against purified Serotransferrin (Human).
Recongizes an epitope located in the N-terminal domain of human serum transferrin, a 77 kDa single polypeptide chain glycoprotein (member of the iron binding family of proteins). It is synthesised in the liver and consists of two domains each having a high affinity reversible binding site for Fe3+. Transferrin (TF) is a glycoprotein with an approximate molecular weight of 76.5 kDa.
Serotransferrin antibody can be stored short term 4 ˚C. For long term storage aliquot and store at -20 ˚C. As with all antibodies avoid freeze/thaw cycles.