L4040
Lactoferrin human
recombinant, expressed in rice, Partially iron saturated, ≥90% (SDS-PAGE)
Sinónimos:
Growth-inhibiting protein 12, Lactotransferrin, Talalactoferrin
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About This Item
Productos recomendados
biological source
human
Quality Level
recombinant
expressed in rice
assay
≥70% protein basis (Bradford)
≥90% (SDS-PAGE)
form
powder
technique(s)
microbiological culture: suitable
solubility
H2O: soluble 10 mg/mL
UniProt accession no.
storage temp.
2-8°C
Gene Information
human ... LTF(4057)
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Application
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.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
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Los clientes también vieron
Chuang Guo et al.
Food & function, 11(8), 7183-7196 (2020-08-07)
Lactoferrin (Lf), an iron-binding glycoprotein, has been shown to possess antioxidant and anti-inflammatory properties and exert modulatory effects on lipid homeostasis and non-alcoholic fatty liver disease (NAFLD), but our understanding of its regulatory mechanisms is limited and inconsistent. We used
Thuy Nguyen Thi Dao et al.
Journal of extracellular vesicles, 11(2), e12195-e12195 (2022-02-22)
Cancer cell-derived extracellular vesicles (EVs) are promising biomarkers for cancer diagnosis and prognosis. However, the lack of rapid and sensitive isolation techniques to obtain EVs from clinical samples at a sufficiently high yield limits their practicability. Chimeric nanocomposites of lactoferrin
P Kragsbjerg et al.
Thorax, 50(12), 1253-1257 (1995-12-01)
The role of cytokines in the pathogenesis of pneumonia is still poorly understood. In a previous study the diagnostic value of measuring blood concentrations of interleukin 6 and interferon gamma was established. In the present study the value of blood
Shelton W Wright et al.
PLoS neglected tropical diseases, 14(8), e0008495-e0008495 (2020-08-09)
Melioidosis is an often-severe tropical infection caused by Burkholderia pseudomallei (Bp) with high associated morbidity and mortality. Burkholderia thailandensis (Bt) is a closely related surrogate that does not require BSL-3 conditions for study. Lactoferrin is an iron-binding glycoprotein that can
Mingi Kim et al.
mBio, 12(5), e0224821-e0224821 (2021-09-15)
The human pathogen Acinetobacter baumannii produces and utilizes acinetobactin for iron assimilation. Although two isomeric structures of acinetobactin, one featuring an oxazoline (Oxa) and the other with an isoxazolidinone (Isox) at the core, have been identified, their differential roles as
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