Native Human Lactoferrin, Neutrophil

Human Lactoferrin plays an important role in iron transport and utilization in humans. A glycoprotein containing about 6% sugar, human lactoferrin is capable of binding two ferric ions with high affinity. Although lactoferrin binds iron tightly, the binding is reversible so that the metal is available upon demand to cells with a need for this essential element. Each human lactoferrin molecule has two iron-binding domains. Human Lactoferrin (hLF) is an iron-binding glycoprotein that facilitates the production of hydroxyl radicals and chelates iron, preventing its accessibility to microorganisms and thus inhibiting growth. Human Lactoferrin is found in secondary granules in polymorphonuclear neutrophils. Human Lactoferrin from human nuetrophil(s) lacks terminal fucose residues in the glycan chains that are required for binding to macrophages.

77 kDa