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L4040

Sigma-Aldrich

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

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.61

origen biológico

human

recombinante

expressed in rice

Análisis

≥70% protein basis (Bradford)
≥90% (SDS-PAGE)

formulario

powder

técnicas

microbiological culture: suitable

solubilidad

H2O: soluble 10 mg/mL

Nº de acceso UniProt

temp. de almacenamiento

2-8°C

Información sobre el gen

human ... LTF(4057)

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Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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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
Snehal Kadam et al.
Biofilm, 3, 100047-100047 (2021-04-30)
Bacterial biofilms are a major cause of delayed wound healing. Consequently, the study of wound biofilms, particularly in host-relevant conditions, has gained importance. Most in vitro studies employ refined laboratory media to study biofilms, representing conditions that are not relevant
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
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

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