L0130
β-Lactoglobulin from bovine milk
≥90% (PAGE), lyophilized powder
Sinônimo(s):
β-LG, Bos d 5, beta-LG
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1 G
R$ 1.508,00
5 G
R$ 5.489,00
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1 G
R$ 1.508,00
5 G
R$ 5.489,00
About This Item
Produtos recomendados
fonte biológica
bovine milk
Nível de qualidade
Ensaio
≥90% (PAGE)
Formulário
lyophilized powder
nº de adesão UniProt
temperatura de armazenamento
2-8°C
Informações sobre genes
bovine ... LGB(280838)
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Descrição geral
A member of the lipocalin family, β-Lactoglobulin (βLg) is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da. It features 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.[1]
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 BLG A and BLG B.[2]
Aplicação
Outras notas
Contains β-lactoglobulins A and B which can be isolated chromatographically.
Qualidade
May not contain folate binding protein; not recommended for folate analysis.
Nota de preparo
Crystallized
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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Isabella Pali-Schöll et al.
Clinical and translational allergy, 12(2), e12125-e12125 (2022-02-17)
Growing up on a cattle farm and consuming raw cow's milk protects against asthma and allergies. We expect a cattle-specific protein as active component in this farm effect. Dust was collected from cattle and poultry stables and from mattresses of
A Heinzmann et al.
International archives of allergy and immunology, 120(4), 280-286 (2000-01-21)
beta-Lactoglobulin (BLG) represents one of the major allergens causing cow's milk allergy (CMA) - a disease with a wide spectrum of clinical symptoms. The aim of this study was to evaluate sequential B cell epitopes of BLG by the Pin-ELISA
Rachana Pathak et al.
European biophysics journal : EBJ, 51(4-5), 335-352 (2022-05-17)
Amyloid crystals, a form of ordered protein aggregates documented relatively recently, have not been studied as extensively as amyloid fibres. This study investigates the formation of amyloid crystals with low frequency ultrasound (20 kHz) using β-lactoglobulin, as a model protein for
The Competitive Displacement of ?-Lactoglobulin by Tween 20 from Oil-Water and Air-Water Interfaces
Peter J. Wilde, David C. Clark
Journal of Colloid and Interface Science, 155, 48-54 (1993)
André C Dumetz et al.
Biophysical journal, 94(2), 570-583 (2007-12-28)
The aggregates and gels commonly observed during protein crystallization have generally been considered disordered phases without further characterization. Here their physical nature is addressed by investigating protein salting-out in ammonium sulfate and sodium chloride for six proteins (ovalbumin, ribonuclease A
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