The specification sheets for products SRP and L4894 do not mention testing for iron. The product SRP6519 undergoes basic testing, including appearance and SDS Page electrophoresis. On the other hand, product L4894 undergoes more detailed testing, including appearance, solubility, protein by biuret, SDS Page electrophoresis, as well as additional testing for infectious agents and use in cell culture. While iron is expected to be present, there are no confirmatory tests performed to document the amount of iron on a batch-to-batch basis.
L4894
Lactoferrin from human milk
powder, BioReagent, suitable for cell culture
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$474.00
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SMILES string
N([C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C(=O)O)C(=O)[C@@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)CC(=O)N)C)CC(=O)O
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
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
Quality Level
Gene Information
human ... LTF(4057)
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This Item | |||
|---|---|---|---|
| form powder | form lyophilized powder | form powder | form powder |
| technique(s) cell culture | mammalian: suitable | technique(s) microbiological culture: suitable | technique(s) microbiological culture: 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 phosphate buffer: 10 mg/mL at 25 °C (0.01 M phosphate buffer, 0.0027 M potassium chloride and 0.137 M sodium chloride, pH 7.4) | 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 |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
Application
Lactoferrin from human milk has been used:
- to test its neuroprotective effect on neuroblastoma cells and mouse mesencephalic dopaminergic cell lines MN9D [3]
- 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[4]
- in the preparation of immobilized titanium substrate for testingMG-63 osteoblast activity[5]
- as a low-density lipoprotein (LDL) receptor-related protein (LRP1) ligand in vascular smooth muscle cells (VSMC)[6]
Biochem/physiol Actions
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.
Lactoferrin is blood-brain barrier (BBB) traversable and has therapeutic potential to regulate inflammation, immunity and apoptosis in Parkinson′s disease.[1] It promotes the expression of brain-derived neurotrophic factor (BDNF) via various signaling pathways and aids protection in motor dysfunction.[1] Lactoferrin favors osteogenic differentiation and proliferation of human adipose-derived stem cells (hADSCs).[3] It exhibits proteolytic activity on Haemophilus influenzae colonization factors.[2] Lactoferrin is also a nutraceutical and a potential marker in the pathophysiology of inflammatory bowel diseases, leukocytes[1]
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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José M Fernández-Real et al.
Obesity (Silver Spring, Md.), 18(3), 482-488 (2009-08-22)
Lactoferrin is an innate immune system protein with anti-inflammatory and antioxidant activities. We aimed to evaluate circulating lactoferrin levels in association with lipid concentrations, and parameters of oxidative stress and inflammation in subjects with morbid obesity after an acute fat
Lactoferrin: a multifunctional immunoregulatory protein?
J Brock
Immunology today, 16(9), 417-419 (1995-09-01)
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
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
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
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Could you confirm whether products SRP6519 and L4894 Lactoferrin derived from human milk have confirmed iron content?
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