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Key Documents

L7880

Sigma-Aldrich

β-Lactoglobulin A from bovine milk

≥90% (PAGE)

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

Quality Level

assay

≥90% (PAGE)

form

powder

mol wt

18,363 Da by calculation

technique(s)

HPLC: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... LGB(280838)

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General description

A member of the lipocalin family, βLg is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da, featuring an eight-stranded β-barrel (strands A-H) succeeded by a three-turn a-helix and a final β-strand (strand I) that forms part of the dimerization interface.
Milk from dairy cows contains the protein β-lactoglobulin (BLG). It naturally occurs in a number of genetic variants, and the most prevalent bovine variants are known as BLG A and BLG B.

Application

β-Lactoglobulin A from bovine milk has been used:
  • as a calibrant for the calibration of the TriWave device
  • as a standard in the detection and quantification of β-lactoglobulin in bovine milk by reverse-phase high performance liquid chromatography (HPLC)
  • in the purification and molecular weight measurement of protease samples

β-Lactoglobulin was used in the identification of the genetic variants of κ-casein in milk by isoelectric focusing electrophoresis.

Biochem/physiol Actions

β-Lactoglobulin (β-lg) possesses heat-set gelation properties. It also exhibits antiviral, anticarcinogenic and hypocholesterolemic effects. β-lg can bind to retinol and long-chain fatty acids. It may participate in the absorption and metabolism of fatty acids.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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An Acid Protease Produced by Monilinia fructigena in vitro and in Infected Apple Fruits, and its Possible Role in Pathogenesis
Hislop EC, et al.
Microbiology, 128(4), 799-807 (1982)
Jeremy Pronchik et al.
The journal of physical chemistry. B, 112(36), 11422-11434 (2008-08-19)
We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, beta-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We
Bioactive milk proteins, peptides and lipids and other functional components derived from milk and bovine colostrum
Functional Foods, 471-511 (2011)
Detection and quantification of alphaS1-, alphaS2-, beta-, kappa-casein,alpha-lactalbumin, beta-lactoglobulin and lactoferrin in bovine milk by reverse-phase high-performance liquid chromatography
Maurmayr A, et al.
Agriculturae Conspectus Scientificus, 78(3), 201-205 (2013)
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Journal of the American Society For Mass Spectrometry, 30(1), 128-138 (2019)

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