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
Form:
lyophilized powder
Assay:
≥90% (PAGE)
Biological source:
bovine milk
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)
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.
Preparation Note
Crystallized
Analysis Note
May not contain folate binding protein; not recommended for folate analysis.
Other Notes
Contains β-lactoglobulins A and B which can be isolated chromatographically.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| L0130-1G | 04061833945575 |
| L0130-5G | 04061833945582 |