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A propos de cet article
Form:
powder
Assay:
≥70% protein basis (Bradford), ≥90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in rice
Service technique
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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.
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.
Other Notes
rhLactoferrin manufactured in the USA by InVitria.
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Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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