L7880
β-Lactoglobulin A from bovine milk
≥90% (PAGE)
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Doporučené produkty
biological source
bovine milk
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)
Osvědčení o analýze (COA)
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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
Agriculturae Conspectus Scientificus, 78(3), 201-205 (2013)
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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
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