Lactoferrin is an iron binding glycoprotein with an approximate molecular weight of 80 kDa. The protein has two iron binding domains each housing one Fe³⁺ and the synergistic CO₃^2- ion. The crystal structure form of human lactoferrin at 2.2A resolution exhibits 5330 protein atoms, 2Fe²⁺, 2CO₃^2- and 98 carbohydrate atoms. Lactoferrin is absorbed from intestine by apical side of the membrane and localized to the nuclei. Intravenous infusion of lactoferrin is protective against lethal doses of E coli and induce bacterimia by a mechanism that downregulates neutrophil TNF alfa secretion. Recombinant human lactoferrin (rhLF), expressed and extracted from rice seed, is being evaluated for use as a dietary supplement to treat iron deficiency and/or iron deficiency induced anemia. Lactoferrin has been shown to have a role in the immune system and in early development of the embryo. A specific receptor for lactoferrin binding has been implicated in the human fetal intestine. Early embryonic localisation of lactoferrin by IHC has suggested its presence in various tissues including intestinal epitheliuem, kiney, and various regions of the brain.