Human lactoferrin (Lf)

Human lactoferrin is an iron-binding glycoprotein (about 80 kDa) found extensively in human and mammalian milk, as well as in many exocrine secretions (saliva, tears, bile, and others) and in neutrophil granules[1][3][8]. Structurally, it comprises a single polypeptide chain (~691 amino acids) forming two homologous globular lobes (N-lobe and C-lobe), each containing one high-affinity iron-binding site[1][2][3][4][6]. It belongs to the transferrin family of iron transporters[2][3]. Its primary biological functions are sequestration of iron (to limit microbial growth), broad direct antimicrobial action, regulation of immune responses, and modulation of inflammation[3][5][8]. Lactoferrin's presence in neutrophils and release during infection or inflammation links it to innate immunity and host defense[5][8]. It is studied clinically for roles in infection, inflammation, and as a biomarker of disease activity, but it is not a classic pharmacological target for small molecule drugs, and is used mainly as a recombinant therapeutic protein or supplement[1][3][8]. Its supplementation is generally safe with minimal side effects[1][8].

Other names

LactotransferrinLactoferrinLTF

Iron sequestration deprives pathogens of essential iron, Direct microbicidal action, Modulation of immune cell activity