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L4894

Sigma-Aldrich

Lactoferrin from human milk

powder, BioReagent, suitable for cell culture

CAS Number:
MDL number:
NACRES:
NA.75

product line

BioReagent

Quality Level

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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This Item
L0520L9507L4765
technique(s)

cell culture | mammalian: suitable

technique(s)

microbiological culture: suitable

technique(s)

fractionation: suitable

technique(s)

electrophoresis: suitable, ion chromatography: suitable

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)

solubility

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)

solubility

H2O: soluble 10 mg/mL

solubility

H2O: soluble 5 mg/mL

shipped in

ambient

shipped in

-

shipped in

-

shipped in

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

product line

BioReagent

product line

-

product line

-

product line

-

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


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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
Chuang Guo et al.
Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 42(13), 2504-2515 (2017-01-13)
Growing evidence suggests that lactoferrin (Lf), an iron-binding glycoprotein, is a pleiotropic functional nutrient. In addition, Lf was recently implicated as a neuroprotective agent. These properties make Lf a valuable therapeutic candidate for the treatment of Alzheimer's disease (AD). However
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
D R Hendrixson et al.
Molecular microbiology, 47(3), 607-617 (2003-01-22)
Lactoferrin is a member of the lactotransferrin family of non-haem, iron-binding glycoproteins and is found at high concentrations in all human secretions, where it plays a major role in mucosal defence. In recent work, we observed that lactoferrin has proteolytic
M C Harmsen et al.
The Journal of infectious diseases, 172(2), 380-388 (1995-08-01)
Native and chemically derivatized proteins purified from serum and milk were assayed in vitro to assess their inhibiting capacity on the cytopathic effect of human immunodeficiency virus (HIV)-1 and human cytomegalovirus (HCMV) on MT4 cells and fibroblasts, respectively. Only native

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