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Key Documents

L0520

Sigma-Aldrich

Lactoferrin from human milk

≥85% (SDS-PAGE), lyophilized powder

Sinonimo/i:

Growth-inhibiting protein 12, Lactotransferrin, Talalactoferrin

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About This Item

Numero CAS:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.61

Origine biologica

human milk

Livello qualitativo

Saggio

≥85% (SDS-PAGE)

Forma fisica

lyophilized powder

PM

82.4 kDa

Composizione

Protein, ≥90% biuret

tecniche

microbiological culture: suitable

Solubilità

phosphate buffer: 1 mg/mL, clear to slightly hazy (0.01 M phosphate buffer, 0.0027 M potassium chloride and 0.137 M sodium chloride, pH 7.4, at 25 °C)

N° accesso UniProt

Temperatura di conservazione

2-8°C

InChI

1S/C35H53N9O12/c1-16(2)27(43-33(53)23(14-26(47)48)41-25(46)15-38-29(49)18(5)39-31(51)21(36)13-24(37)45)34(54)40-19(6)30(50)42-22(12-20-10-8-7-9-11-20)32(52)44-28(17(3)4)35(55)56/h7-11,16-19,21-23,27-28H,12-15,36H2,1-6H3,(H2,37,45)(H,38,49)(H,39,51)(H,40,54)(H,41,46)(H,42,50)(H,43,53)(H,44,52)(H,47,48)(H,55,56)/t18-,19-,21-,22-,23-,27-,28-/m0/s1
QCBUWCQOKPLTDZ-PKRULZLPSA-N

Informazioni sul gene

human ... LTF(4057)

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Applicazioni

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.

Azioni biochim/fisiol

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.

Qualità

Contains iron, see certificate of analysis for lot specific information.

Nota sulla preparazione

Chromatographically purified.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Liisa Kautto et al.
Experimental eye research, 145, 278-288 (2016-02-07)
The human eye is constantly bathed by tears, which protect the ocular surface via a variety of mechanisms. The O-linked glycans of tear mucins have long been considered to play a role in binding to pathogens and facilitating their removal
Michał Zimecki et al.
Inflammation research : official journal of the European Histamine Research Society ... [et al.], 61(11), 1247-1255 (2012-07-20)
The aim of this study was to assess the utility of lactoferrin (LF), a natural immunomodulator, to restrain allergen-induced pleurisy in mice. BALB/c female mice, 8- to 10-week old, weighing 24 g on average, were used. Mice were immunized intraperitoneally
Jessica R Sheldon et al.
PLoS pathogens, 16(10), e1008995-e1008995 (2020-10-20)
Acinetobacter baumannii is an emerging pathogen that poses a global health threat due to a lack of therapeutic options for treating drug-resistant strains. In addition to acquiring resistance to last-resort antibiotics, the success of A. baumannii is partially due to
Growth of Streptococcus mutans in an iron-limiting medium.
Grace A. Spatafora, Meagan W. Moore
Methods in Cell Science : An Official Journal of the Society for In Vitro Biology, 20, 217-221 (1998)
M T Pöllänen et al.
Journal of periodontal research, 33(1), 8-16 (1998-04-03)
In the process of host defence against microbial challenge, neutrophils release granule contents with the potential side effect of damaging structural tissues. In the junctional epithelium such damage may contribute to the degeneration and renewal of the epithelial cells attached

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