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.
Lactoferrin exhibits antimicrobial activity against a variety of microorganisms and is also a useful cell culture growth factor that furnishes a source of iron to certain cell lines.
Cell culture applications | Antimicrobial Treatment
|Application Notes||Lactoferrin exhibits antimicrobial activity against a variety of microorganisms and is also a useful cell culture growth factor that furnishes a source of iron to certain cell lines.|
|Concentration||Protein Content: ≥96%|
|Gene ID||cow ... LTF(280846)|
|Applications||Cell culture applications | Antimicrobial Treatment|
|Pack Size||10 mg|
|Physical Appearance||Peach-colored Solid|
|Protein or Enzyme Type||Growth Factors|
|Research Areas||Growth Factors Receptors|
|Solubility||Soluble in water 10 mg/mL.|
|Storage and Handling||Store at +4°C.|