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L3770 Sigma

Lactoferrin from human milk

Iron saturated, ≥85% (SDS-PAGE)



Related Categories Biochemicals and Reagents, Casein and Other Milk Proteins, Proteins and Derivatives More...
assay   ≥85% (SDS-PAGE)
mol wt   mol wt 82.4 kDa
Iron content   0.15-1.0%
solubility   phosphate buffer: soluble10 mg/mL at 25 °C (0.01 M phosphate buffer, 0.0027 M potassium chloride and 0.137 M sodium chloride, pH 7.4)
storage temp.   2-8°C
Gene Information   human ... LTF(4057)


Biochem/physiol Actions

Lactoferrin is an iron binding protein. It is structurally similar to transferrin, the plasma iron transport protein; but lactoferrin has a much higher affinity for iron (250 fold). It is very abundant in colostrum and small amounts can also be found in tears, saliva, mucous secretions and in the secondary granules of neutrophils. It is made by mucosal epithelium and neutrophils and is released by these cells in response to inflammatory stimuli. Bacterial growth is inhibited by its ability to sequester iron and also permeabilize bacterial cell walls by binding to lipopolysaccharides through its N-terminus. Lactoferrin can inhibit viral infection by binding tightly to the viral envelope protein. This prevents cell-virus fusion by blocking the binding domain. Lactoferrin appears to activate host defense systems in part by stimulating the release of interleukin-8, a neutrophil activator. It may also be involved in antibody and interleukin synthesis, lymphocyte proliferation and complement activation.


5, 25, 100 mg in glass bottle


Lactoferrin was used to grow Streptococcus mutans in an iron-limiting medium. It was used to test if lactoferrin impedes epithelial cell adhesion in vitro. It was also used to test the diagnostic value of blood cytokine concentrations in acute pneumonia.

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Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

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Peer-Reviewed Papers


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