L3908
β-Lactoglobulin from bovine milk
≥90% (PAGE), lyophilized powder
Synonym(s):
βLg, BLG, Bos d 5, beta-lactoglobulin
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About This Item
Recommended Products
biological source
bovine milk
Assay
≥90% (PAGE)
form
lyophilized powder
technique(s)
ELISA: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LGB(280838)
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General description
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 was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.
Biochem/physiol Actions
A member of the lipocalin family, 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.
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
Chromatographically purified
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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Journal of immunological methods, 350(1-2), 63-70 (2009-08-04)
Cow's milk allergy (CMA) is a common food allergy, especially among infants and young children. Approximately 85% of milk-allergic children outgrow their allergy by the age of three but the remaining 15% remain allergic. Bovine beta-lactoglobulin (BLG) is one of
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The aggregation of the protein α-synuclein (aSyn) into amyloid fibrils in the human brain is associated with the development of several neurodegenerative diseases, including Parkinson's disease. The previously observed prion-like spreading of aSyn aggregation throughout the brain and the finding
Junzhen Zhong et al.
Food chemistry, 278, 491-496 (2018-12-26)
Previous work indicated that conformational changes of β-lactoglobulin (β-LG) induced by dynamic high pressure microfluidization (DHPM) was related to the increase of antigenicity. In this study, β-LG glycated with 1-kestose and combined with DHPM decreased the antigenicity of β-LG. The
Özge Dönmez et al.
Food & function, 11(7), 6038-6053 (2020-06-20)
The effect of binding of flavonoids, (-)-epigallocatechin-3-gallate (EGCG) and green tea extract (GTE), to beta-lactoglobulin (β-Lg) and micellar casein (micellar casein isolate, MCI) on protein digestibility was investigated. β-Lg resisted digestion by pepsin, but in the presence of EGCG the
Leonor Pérez-Fuentes et al.
Soft matter, 13(6), 1120-1131 (2017-01-18)
In this study we have investigated how different proteins interact with big organic ions. Two ions that are similar in size and chemical structure (Ph
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