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Key Documents

L4040

Sigma-Aldrich

Lactoferrin human

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

Synonyme(s) :

Growth-inhibiting protein 12, Lactotransferrin, Talalactoferrin

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

human

Produit recombinant

expressed in rice

Pureté

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

Forme

powder

Technique(s)

microbiological culture: suitable

Solubilité

H2O: soluble 10 mg/mL

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

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.

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
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
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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