Serotransferrin (TF)

Serotransferrin, commonly referred to as transferrin, is a 77-kDa glycoprotein primarily synthesized in the liver that serves as the principal iron-transport protein in human plasma (UniProt P02787). Its primary biological function is to sequester ferric iron (Fe3+), maintaining it in a soluble form and preventing the formation of reactive oxygen species while delivering it to cells via receptor-mediated endocytosis (StatPearls, Physiology, Transferrin). In the therapeutic context, transferrin is targeted by iron-replacement therapies such as ferric maltol and iron sucrose to treat iron-deficiency anemia (DrugBank DB09143). Additionally, because many cancer cells overexpress transferrin receptors to meet high iron demands, transferrin is extensively researched as a ligand for targeted drug delivery systems (PubMed, PMID: 30107145). Clinically, transferrin levels and saturation are essential biomarkers for diagnosing iron-related disorders like hemochromatosis and atransferrinemia (NCBI Gene 7018). The protein also plays a role in the innate immune system by withholding iron from invading pathogens, thereby exhibiting antimicrobial properties (UniProt P02787).

Other names

TransferrinSiderophilinBeta-1-metal-binding globulinPRO1557PRO2086

Binds and transports ferric iron (Fe3+) to cells via receptor-mediated endocytosis through the transferrin receptor (UniProt P02787).