Anti-Transferrin Monoclonal Antibody (Clone:HTF-14)

Transferrin is a monomeric glycoprotein of approximately 77 kDa, which serves as an iron-transporter. In normal plasma, transferrin has a concentration of 25-50 µmol / liter, and is usually about one-third saturated with iron, thus providing a large buffering capacity in case of an acute increase in plasma iron levels. Cells take up transferrin-iron complexes (holotransferrin) using transferrin receptor dimers. Upon binding of holotransferrin, the receptor is internalized by clathrin-mediated endocytosis. Acidification of endosomes by vesicular membrane proton pumps leads to dissociation of iron ions, whereas transferrin (apotransferrin) remains associated with its receptor (CD71) and recycles to the cell surface, where apotransferrin is released upon exposure to normal pH. Internalization of labeled transferrin thus represents an usefull approach to study endocytosis. Serum concentration rises in iron deficiency and pregnancy and falls in iron overload, infection and inflammatory conditions. Iron/transferrin complex is essential in haemoglobin synthesis and for certain types of cell division. Protein function: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). [The UniProt Consortium]