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Merck
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Principaux documents

L3908

Sigma-Aldrich

β-Lactoglobulin from bovine milk

≥90% (PAGE), lyophilized powder

Synonyme(s) :

βLg, BLG, Bos d 5, beta-lactoglobulin

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About This Item

Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

bovine milk

Essai

≥90% (PAGE)

Forme

lyophilized powder

Technique(s)

ELISA: suitable

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

bovine ... LGB(280838)

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Description générale

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.

Actions biochimiques/physiologiques

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.

Autres remarques

Contains β-lactoglobulins A and B which can be isolated chromatographically.

Qualité

May not contain folate binding protein; not recommended for folate analysis.

Notes préparatoires

Chromatographically purified

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Wenhua Yang et al.
Journal of agricultural and food chemistry, 65(36), 8018-8027 (2017-08-13)
Bovine β-lactoglobulin (β-Lg) is one of major allergens in cow's milk. Previous study showed that ultrasound treatment induced the conformational changes of β-Lg and promoted the glycation in aqueous solutions, which is, however, less efficient compared with dry-state. In this
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
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

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