L2506
β-Lactoglobulin from bovine milk
≥85% (PAGE), lyophilized powder
Sinônimo(s):
β-LG, Bos d 5, beta-LG
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About This Item
Produtos recomendados
fonte biológica
bovine milk
Nível de qualidade
Ensaio
≥85% (PAGE)
Formulário
lyophilized powder
técnica(s)
titration: suitable
nº de adesão UniProt
temperatura de armazenamento
2-8°C
Informações sobre genes
bovine ... LGB(280838)
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Descrição geral
β-Lactoglobulin plays a key role in immune response and modulates IgM levels and cell proliferation. β-Lactoglobulin from bovine is a model system for protein folding studies and denaturation kinetics. Polymorphisms in the β-lactoglobulin modulates bovine milk production and composition.
A member of the lipocalin family, βLg is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da,. It has 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 BLG A and BLG B.
Aplicação
β-Lactoglobulin from bovine milk has been used:
- for the generation of calibration curve for protein solubility index
- in acid-base titration
- as a standard for surface hydrophobicity analysis
β-Lactoglobulin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.
Qualidade
Contains β-lactoglobulins A and B which can be isolated chromatographically.
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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beta-Lactoglobulin Influences Human Immunity and Promotes Cell Proliferation
Tai CS, et al
BioMed Research International, 2016 (2016)
Polymorphism of Beta-Lactoglobulin Coding and 5?-Flanking Regions and Association with Milk Production Traits
Zakizadeh S, et al.
Biotechnology, Biotechnological Equipment, 26(1), 2716-2721 (2012)
Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
Alizadeh-Pasdar N and Li-Chan ECY
Journal of Agricultural and Food Chemistry, 48(2), 328-334 (2000)
Roles of electrostatic interaction and polymer structure in the binding of beta-lactoglobulin to anionic polyelectrolytes: measurement of binding constants by frontal analysis continuous capillary electrophoresis
Hattori T, et al.
Langmuir, 16(25), 9738-9743 (2000)
Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments
Gracia-Julia A, et al.
Food Hydrocolloids, 22(6), 1014-1032 (2008)
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