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L4894

Sigma-Aldrich

Lactoferrin from human milk

powder, BioReagent, suitable for cell culture

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.75

product line

BioReagent

Assay

≥85% (SDS-PAGE)

form

powder

mol wt

82.4 kDa

technique(s)

cell culture | mammalian: suitable

color

white to light red

solubility

PBS, pH 7.4: 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)

UniProt accession no.

shipped in

ambient

storage temp.

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

InChI key

QCBUWCQOKPLTDZ-PKRULZLPSA-N

Gene Information

human ... LTF(4057)

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General description

Lactoferrin is mapped to human chromosome 3p21.31. It comprises globular lobes and undergoes post-translational modifications like phosphorylation and glycosylation. Lactoferrin belongs to the lactotransferrin family and has Ser‐Lys catalytic dyad like serine proteases.

Application

Lactoferrin from human milk has been used:
  • to test its neuroprotective effect on neuroblastoma cells and mouse mesencephalic dopaminergic cell lines MN9D
  • to test its antioxidative effect in Edible Bird′s Nest (EBN) induced toxicity in human neuroblastoma SH-SY5Y cells using oxygen radical absorbance capacity (ORAC) assay and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay
  • in the preparation of immobilized titanium substrate for testingMG-63 osteoblast activity
  • as a low-density lipoprotein (LDL) receptor-related protein (LRP1) ligand in vascular smooth muscle cells (VSMC)

Biochem/physiol Actions

Lactoferrin is blood-brain barrier (BBB) traversable and has therapeutic potential to regulate inflammation, immunity and apoptosis in Parkinson′s disease. It promotes the expression of brain-derived neurotrophic factor (BDNF) via various signaling pathways and aids protection in motor dysfunction. Lactoferrin favors osteogenic differentiation and proliferation of human adipose-derived stem cells (hADSCs). It exhibits proteolytic activity on Haemophilus influenzae colonization factors. Lactoferrin is also a nutraceutical and a potential marker in the pathophysiology of inflammatory bowel diseases, leukocytes
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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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D M Mann et al.
The Journal of biological chemistry, 269(38), 23661-23667 (1994-09-23)
Lactoferrin is an iron-binding protein which is synthesized by mucosal epithelium and neutrophils and released by these cells in response to inflammatory stimuli. It promotes neutrophil aggregation and manifests iron-dependent and -independent antimicrobial properties in vitro. Since lactoferrin binds to
W Bellamy et al.
Biochimica et biophysica acta, 1121(1-2), 130-136 (1992-05-22)
We report the existence of a previously unknown antimicrobial domain near the N-terminus of lactoferrin in a region distinct from its iron-binding sites. A single active peptide representing this domain was isolated following gastric pepsin cleavage of human lactoferrin, and
Linyuan Ma et al.
Scientific reports, 8(1), 7433-7433 (2018-05-11)
Efficient transgene expression in recipient cells constitutes the primary step in gene therapy. However, random integration in host genome comprises too many uncertainties. Our study presents a strategy combining bioinformatics and functional verification to find transgene integration sites in pig
Singleton, P., and Sainsbury, D.
Dictionary of Microbiology and Molecular Biology (1996)
Sung Eun Kim et al.
Colloids and surfaces. B, Biointerfaces, 123, 191-198 (2014-10-04)
The aim of this study was to develop a lactoferrin (LF)-immobilized titanium (Ti) substrate to enhance the osteoblast activity of MG-63 cells. Ti substrates were first modified through heparin-dopamine (Hep-DOPA) anchorage. Then, LF was immobilized on the Hep-Ti substrates via

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