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. _x000D_
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._x000D_
Purified by precipitation and chromatography
> 95% (by SDS-PAGE)
human, rabbit, pig/porcine
Store at 2-8°C. Do not freeze. Do not use after expiration date stamped on vial label.
The antibody HTF-14 recognizes 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+._x000D_
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