L8005
β-Lactoglobulin B from bovine milk
≥90% (PAGE)
Synonym(s):
β-LG, Bos d 5, beta-LG
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About This Item
biological source
bovine milk
Quality Level
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
Gene Information
bovine ... LGB(280838)
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.
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Casein polymorphism heterogeneity influences casein micelle size in milk of individual cows
Journal of Dairy Science, 98(6), 3633-3644 (2015)
Milk protein fractions strongly affect the patterns of coagulation, curd firming, and syneresis
Journal of Dairy Science, 102(4), 2903-2917 (2019)
Invited review: beta-lactoglobulin: binding properties, structure, and function
Journal of Dairy Science, 87(4), 785-796 (2004)
Analysis of alpha-lactalbumin, beta-lactoglobulin A and B in whey protein powder, colostrum, raw milk, and infant formula by CE and LC
Dairy science & technology, 91(2), 213-225 (2011)
Antimicrobial activity of bovine beta-lactoglobulin against mastitis-causing bacteria
Journal of Dairy Science, 94(1), 138-145 (2011)
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