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L0130

Sigma-Aldrich

β-乳球蛋白 来源于牛奶

≥90% (PAGE), lyophilized powder

别名:

β-LG, Bos d 5, beta-LG

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352202
NACRES:
NA.61

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生物源

bovine milk

品質等級

化驗

≥90% (PAGE)

形狀

lyophilized powder

UniProt登錄號

儲存溫度

2-8°C

基因資訊

bovine ... LGB(280838)

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一般說明

作为脂质运载蛋白家族的成员,β-乳球蛋白(βLg)是162个氨基酸的小蛋白质,分子量为∼18,400Da。它具有八链β-桶(链A-H),其后面是三转α-螺旋和最终 β-链(链I),其形成二聚化界面的一部分。[1]
来自奶牛的牛奶含有蛋白质 β-乳球蛋白(BLG)。它天然存在于许多遗传变异体中,最普遍的牛变体是BLG A和BLG B。[2]

應用

来自牛奶的β-乳球蛋白用于测试对牛′s 奶过敏的儿童过敏原反应性 CD4 + CD25 + 调节性 T细胞。[3]它还用于测试 Tween 20 从油 - 水和空气 - 水界面的β-乳球蛋白的竞争性置换。[4]

其他說明

含 β-乳球蛋白 A 和 B,可通过色谱法分离。

品質

可能不含叶酸结合蛋白;不推荐用于叶酸分析。

準備報告

结晶

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

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Isabella Pali-Schöll et al.
Clinical and translational allergy, 12(2), e12125-e12125 (2022-02-17)
Growing up on a cattle farm and consuming raw cow's milk protects against asthma and allergies. We expect a cattle-specific protein as active component in this farm effect. Dust was collected from cattle and poultry stables and from mattresses of
A Heinzmann et al.
International archives of allergy and immunology, 120(4), 280-286 (2000-01-21)
beta-Lactoglobulin (BLG) represents one of the major allergens causing cow's milk allergy (CMA) - a disease with a wide spectrum of clinical symptoms. The aim of this study was to evaluate sequential B cell epitopes of BLG by the Pin-ELISA
Rachana Pathak et al.
European biophysics journal : EBJ, 51(4-5), 335-352 (2022-05-17)
Amyloid crystals, a form of ordered protein aggregates documented relatively recently, have not been studied as extensively as amyloid fibres. This study investigates the formation of amyloid crystals with low frequency ultrasound (20 kHz) using β-lactoglobulin, as a model protein for
The Competitive Displacement of ?-Lactoglobulin by Tween 20 from Oil-Water and Air-Water Interfaces
Peter J. Wilde, David C. Clark
Journal of Colloid and Interface Science, 155, 48-54 (1993)
André C Dumetz et al.
Biophysical journal, 94(2), 570-583 (2007-12-28)
The aggregates and gels commonly observed during protein crystallization have generally been considered disordered phases without further characterization. Here their physical nature is addressed by investigating protein salting-out in ammonium sulfate and sodium chloride for six proteins (ovalbumin, ribonuclease A

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