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생물학적 소스
bovine milk
분석
≥90% (PAGE)
양식
powder
분자량
18,276 Da by calculation
기술
HPLC: suitable
electrophoresis: suitable
UniProt 수납 번호
저장 온도
2-8°C
유전자 정보
bovine ... LGB(280838)
일반 설명
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[1] and optimum pH of 5.2.[1] It is present in high level in casein and is relatively low in raw bovine milk.[1] 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.[2]
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.[3]
애플리케이션
β-Lactoglobulin B from bovine milk has been used as:
- a protein standard in SDS-polyacrylamide electrophoresis for quantification of milk protein fractions[4]
- in the calibration of reversed phase- high-performance liquid chromatography (HPLC) for caseins quantification[5]
- for immobilization on the biosensor surface and a calibration standards in biosensor assay[6]
β-Lactoglobulin was used in the identification of the genetic variants of κ-casein in milk by isoelectric focusing electrophoresis.[7]
생화학적/생리학적 작용
β-Lactoglobulin B (β-LG B) show less inhibitory effect on the Staphylaococcus sp compared to β-LG A.[8]
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
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)
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)
Invited review: beta-lactoglobulin: binding properties, structure, and function
Kontopidis G, et al.
Journal of Dairy Science, 87(4), 785-796 (2004)
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
The beta-lactoglobulin content of bovine milk: Development and application of a biosensor immunoassay
Indyk HE, et al.
International dairy journal, 73, 68-73 (2017)
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