The Transferrin Receptor (TfR), also known as TfR-1 or CD71, is a type II transmembrane glycoprotein that plays a crucial role in iron homeostasis. It is primarily responsible for the uptake of transferrin-bound iron into cells. The receptor is expressed on the surface of various cell types, including erythroid progenitors, muscle cells, and proliferating cells .
The Transferrin Receptor is a homodimer, consisting of two 95 kDa monomers linked by disulfide bonds, forming a 188 kDa dimer . Each monomer has an extracellular domain that binds to transferrin, a plasma protein that transports iron throughout the body. The binding of transferrin to TfR facilitates the internalization of the complex via receptor-mediated endocytosis .
Recombinant human transferrin receptor is produced using various expression systems, including mammalian cell lines such as HEK293 and NS0 cells . The recombinant protein is typically tagged with a polyhistidine (His) tag to facilitate purification. The recombinant form retains the functional properties of the native receptor, including its ability to bind transferrin and mediate iron uptake.
Recombinant human transferrin receptor is widely used in research to study iron metabolism, receptor-mediated endocytosis, and related cellular processes. It is also employed in the development of therapeutic strategies for diseases associated with iron dysregulation, such as anemia and hemochromatosis .