Serotransferrin (TF (or Tf))

Serotransferrin (TF, also commonly called transferrin) is a plasma glycoprotein and the principal iron transport protein in the blood, responsible for transferring iron from absorption and storage sites to tissues requiring iron, such as erythroid precursors in the bone marrow[1][3][7][8]. It consists of a single polypeptide chain with two homologous domains, each capable of binding one iron ion (typically Fe³⁺), and plays a central role in maintaining systemic iron homeostasis[1][4]. When loaded with iron, it binds the transferrin receptor on cell surfaces, allowing cellular uptake of iron via endocytosis; subsequent pH changes in the endosome facilitate iron release into the cell[1][2][5]. Beyond iron transport, TF may modulate cell proliferation and acts as a growth factor in some contexts[3]. Pathologically, it is implicated in anemia (low TF = increased anemia risk), infections (used as iron source by certain bacteria and parasites), and cancer (targeted for anti-tumor drug delivery and as a biomarker)[1][3]. TF-modified drug formulations exploit its receptor for enhanced specificity in tumor therapy, improve drug delivery, and overcome resistance, while its antimicrobial properties are under investigation for anti-infective therapy[1].

Other names

TransferrinTFTfBeta-1 metal-binding globulinSiderophilinBeta-globulin

Iron chelation/inhibition of iron transport, Targeted drug delivery through transferrin receptor-mediated endocytosis, Modulation of iron homeostasis for therapeutic effect