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L3908

Sigma-Aldrich

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

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
Anwesha Sarkar et al.
Colloids and surfaces. B, Biointerfaces, 158, 137-146 (2017-07-09)
In this study, we designed emulsions with an oil-water interface consisting of a composite layer of whey protein isolate (WPI, 1wt%) and cellulose nanocrystals (CNCs) (1-3wt%). The hypothesis was that a secondary layer of CNCs at the WPI-stabilized oil-water interface
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

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