L0130
β-Lactoglobulin from bovine milk
≥90% (PAGE), lyophilized powder
Synonym(s):
β-LG, Bos d 5, beta-LG
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About This Item
Recommended Products
biological source
bovine milk
Quality Level
Assay
≥90% (PAGE)
form
lyophilized powder
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LGB(280838)
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General description
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.
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.
Application
β-Lactoglobulin from bovine milk was used to test the allergen-responsive CD4+ CD25+ regulatory T cells in children who have outgrown cow′s milk allergy. It is also used to test the competitive displacement of β-lactoglobulin by Tween 20 from oil-water and air-water interfaces.
Other Notes
Contains β-lactoglobulins A and B which can be isolated chromatographically.
Quality
May not contain folate binding protein; not recommended for folate analysis.
Preparation Note
Crystallized
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Customers Also Viewed
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
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
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
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)
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