L4765
Lactoferrin from bovine colostrum
≥85% (SDS-PAGE)
Lactoferrin from bovine colostrum
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10 MG
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50 MG
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Informacje o tej pozycji
Form:
powder
Assay:
≥85% (SDS-PAGE)
Biological source:
bovine colostrum
Mol wt:
~90 kDa
Przejdź do
Pomoc techniczna
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Pozwól nam pomócbiological source
bovine colostrum
assay
≥85% (SDS-PAGE)
form
powder
mol wt
~90 kDa
technique(s)
electrophoresis: suitable, ion chromatography: suitable
impurities
salt, essentially free
solubility
H2O: soluble 5 mg/mL
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
cow ... LTF(280846)
1 of 4
Ta pozycja | |||
|---|---|---|---|
| technique(s) electrophoresis: suitable, ion chromatography: suitable | technique(s) - | technique(s) - | technique(s) microbiological culture: suitable |
| assay ≥85% (SDS-PAGE) | assay ~80% (GE) | assay ≥85% (GE) | assay ≥85% (SDS-PAGE) |
| biological source bovine colostrum | biological source human milk | biological source human milk | biological source human milk |
| form powder | form solid | form solid | form powder |
| mol wt ~90 kDa | mol wt 82.4 kDa | mol wt 82.4 kDa | mol wt 82.4 kDa |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
General description
Lactoferrin from bovine colostrum corresponds to a molecular weight of 80 kDa. It is a glycosylated protein and belongs to the transferrin family. Bovine lactoferrin has N and C-terminal lobes homologous to human lactoferrin.
Application
Lactoferrin from bovine colostrum has been used as standard protein in sodium dodecyl sulfate (SDS)- polyacrylamide gel electrophoresis (PAGE) for the quantification of IgG samples. It has also been used to test its effect in inducing autoimmune pancreatitis.[1]
Lactoferrin from bovine colostrum was used in the characterization of lactoferrin (lf) from colostral whey using anti-lf antibody immunoaffinity chromatography. It was used in the isolation of lactoferrin from bovine colostrum using ultrafiltration coupled with strong cation exchange chromatography.
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.
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Klasa składowania
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Andrew S Cooke et al.
PeerJ, 8, e8631-e8631 (2020-05-06)
Promoting and maintaining health is critical to ruminant welfare and productivity. Within human medicine, faecal lactoferrin is quantified for routine assessment of various gastrointestinal illnesses avoiding the need for blood sampling. This approach might also be adapted and applied for
Structural and functional characteristics of bovine milk protein glycosylation
O Riordan N, et al.
Glycobiology, 24(3), 220-236 (2014)
Isolation of lactoferrin from bovine colostrum by ultrafiltration coupled with strong cation exchange chromatography on a production scale
Lu RR, et al.
Journal of Membrane Science , 297(1-2), 152-161 (2007)
Erika N Biernbaum et al.
JDS communications, 2(3), 92-97 (2021-03-12)
Improper storage conditions or processing of milk leads to potential spoilage and illness, due in part to temperature abuse, allowing bacteria present to grow and spoil the product. However, certain proteins naturally found in raw milk, such as lactoferrin, have
Serena Belegrinou et al.
Langmuir : the ACS journal of surfaces and colloids, 24(14), 7251-7261 (2008-06-14)
The interaction of the proteins bovine serum albumin (BSA), lysozyme (Lys), lactoferrin (Lf), and fibronectin (Fn) with surfaces of protein-resistant poly(ethylene oxide) (PEO) and protein-adsorbing poly(acrylic acid) (PAA) fabricated by plasma-enhanced chemical vapor deposition has been studied with quartz crystal
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