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Key Documents

L3908

Sigma-Aldrich

β-Lactoglobulin from bovine milk

≥90% (PAGE), lyophilized powder

Synonim(y):

βLg, BLG, Bos d 5, beta-lactoglobulin

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About This Item

Numer CAS:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352202
NACRES:
NA.61

pochodzenie biologiczne

bovine milk

Poziom jakości

Próba

≥90% (PAGE)

Postać

lyophilized powder

metody

ELISA: suitable

numer dostępu UniProt

temp. przechowywania

2-8°C

informacje o genach

bovine ... LGB(280838)

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Opis ogólny

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.

Zastosowanie

β-Lactoglobulin was used in a cytologic assay for diagnosis of food hypersensitivity in patients with irritable bowel syndrome.

Działania biochem./fizjol.

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.

Inne uwagi

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

Jakość

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

Uwaga dotycząca przygotowania

Chromatographically purified
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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