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L4040

Sigma-Aldrich

Lactoferrin human

recombinant, expressed in rice, Partially iron saturated, ≥90% (SDS-PAGE)

Synonym(e):

Growth-inhibiting protein 12, Lactotransferrin, Talalactoferrin

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About This Item

MDL-Nummer:
MFCD00164307
UNSPSC-Code:
12352202
NACRES:
NA.61

Biologische Quelle

human

Rekombinant

expressed in rice

Assay

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

Form

powder

Methode(n)

microbiological culture: suitable

Löslichkeit

H2O: soluble 10 mg/mL

UniProt-Hinterlegungsnummer

P02788

Lagertemp.

2-8°C

Angaben zum Gen

human ... LTF(4057)

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Anwendung

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. Wirkung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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
Qingsheng Kong et al.
Molecular and cellular biochemistry, 406(1-2), 293-299 (2015-05-20)
The metalloprotease lethal factor (LF) from Bacillus anthracis plays a vital role in anthrax toxin action, and thus becomes a target for anti-anthrax therapy. Following the guidelines based on existing metalloprotease inhibitors, we designed a 'first-generation' LF inhibitor R9LF-1. This
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
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