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Transferrin (TF) is a glycoprotein 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. Therefore, each Human TF molecule has the ability to carry two Iron ions in the Ferric form (Fe3+). The function of TF is to transport Iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. Human HOLO transferrin is iron saturated whereas APO transferrin is substantially iron-free. When human transferrin loaded with iron encounters a human transferrin receptor on the surface of a cell, it binds to it and is consequently transported into the cell in a vesicle. The cell will acidify the vesicle, causing human transferrin to release its iron ions.
Apotransferrin is an important transport factor used in defined culture media. Purified to have less than 0.01% iron and an iron-binding capacity of 1.25 ug/mg. Dissolves in water at 10 mg per ml.
Low endotoxin, bioprocessing grade in bulk quantity is available.