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Laissez-nous vous aiderNom du produit
β-Lactoglobulin B from bovine milk, ≥90% (PAGE)
biological source
bovine milk
assay
≥90% (PAGE)
form
powder
mol wt
18,276 Da by calculation
technique(s)
HPLC: suitable
electrophoresis: suitable
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
bovine ... LGB(280838)
Application
β-Lactoglobulin B from bovine milk has been used as:
- a protein standard in SDS-polyacrylamide electrophoresis for quantification of milk protein fractions
- in the calibration of reversed phase- high-performance liquid chromatography (HPLC) for caseins quantification
- for immobilization on the biosensor surface and a calibration standards in biosensor assay
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 B (β-LG B) show less inhibitory effect on the Staphylaococcus sp compared to β-LG A.
General description
β-Lactoglobulin B (β-LG B), a isoform of β-Lactoglobulin, is a small protein of 162 amino acids with a molecular mass of 18.2 kDa and optimum pH of 5.2. It is present in high level in casein and is relatively low in raw bovine milk. β-LG has eight-stranded β-barrel (strands A-H) succeeded by a three-turn α-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.
Classe de stockage
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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Milk protein fractions strongly affect the patterns of coagulation, curd firming, and syneresis
Amalfitano N, et al.
Journal of Dairy Science, 102(4), 2903-2917 (2019)
Invited review: beta-lactoglobulin: binding properties, structure, and function
Kontopidis G, et al.
Journal of Dairy Science, 87(4), 785-796 (2004)
Casein polymorphism heterogeneity influences casein micelle size in milk of individual cows
Day L, et al.
Journal of Dairy Science, 98(6), 3633-3644 (2015)
Antimicrobial activity of bovine beta-lactoglobulin against mastitis-causing bacteria
Chaneton L, et al.
Journal of Dairy Science, 94(1), 138-145 (2011)
Huaying Zhao et al.
Current protocols in protein science, 101(1), e109-e109 (2020-07-03)
Sedimentation velocity analytical ultracentrifugation is a powerful classical method to study protein self-association processes in solution based on the size-dependent macromolecular migration in the centrifugal field. This technique can elucidate the assembly scheme, measure affinities ranging from picomolar to millimolar
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