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L4765

Sigma-Aldrich

Lactoferrin from bovine colostrum

≥85% (SDS-PAGE)

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CAS Number:
MDL number:
NACRES:
NA.61

biological source

bovine colostrum

Quality Level

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

Gene Information

cow ... LTF(280846)

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This Item
L4894L3770L0520
Lactoferrin from bovine colostrum ≥85% (SDS-PAGE)

L4765

Lactoferrin from bovine colostrum

Lactoferrin from human milk powder, BioReagent, suitable for cell culture

L4894

Lactoferrin from human milk

Lactoferrin from human milk Iron saturated, ≥85% (SDS-PAGE)

L3770

Lactoferrin from human milk

Lactoferrin from human milk ≥85% (SDS-PAGE), lyophilized powder

L0520

Lactoferrin from human milk

technique(s)

electrophoresis: suitable, ion chromatography: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

microbiological culture: suitable

technique(s)

microbiological culture: suitable

biological source

bovine colostrum

biological source

-

biological source

human milk

biological source

human milk

form

powder

form

powder

form

powder

form

lyophilized powder

mol wt

~90 kDa

mol wt

82.4 kDa

mol wt

82.4 kDa

mol wt

82.4 kDa

Gene Information

cow ... LTF(280846)

Gene Information

human ... LTF(4057)

Gene Information

human ... LTF(4057)

Gene Information

human ... LTF(4057)

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.
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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Structural and functional characteristics of bovine milk protein glycosylation
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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
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
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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