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About This Item
Form:
lyophilized powder
Assay:
≥90% (PAGE)
Biological source:
bovine milk
biological source
bovine milk
assay
≥90% (PAGE)
form
lyophilized powder
technique(s)
ELISA: suitable
UniProt accession no.
storage temp.
2-8°C
Quality Level
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.
Preparation Note
Chromatographically purified
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Sirpa Jylhä et al.
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
Lena Wartosch et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 23(12), 4056-4068 (2009-08-08)
Mutations in either ClC-7, a late endosomal/lysosomal member of the CLC family of chloride channels and transporters, or in its beta-subunit Ostm1 cause osteopetrosis and lysosomal storage disease in mice and humans. The severe phenotype of mice globally deleted for
Tilman Barz et al.
Journal of chromatography. A, 1217(26), 4267-4277 (2010-05-07)
In this work, parameters of the steric mass-formalism SMA are optimally ascertained for a reliable determination of the adsorption isotherms of beta-lactoglobulin A and B under non-isocratic conditions. For this purpose, static batch experiments are used in contrast to the
Jonathan Vaneyck et al.
The Journal of biological chemistry, 296, 100358-100358 (2021-02-05)
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
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