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安全信息

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 号:
MDL编号:
UNSPSC代码:
12352202
NACRES:
NA.61

生物来源

bovine milk

质量水平

检测方案

≥90% (PAGE)

形式

lyophilized powder

UniProt登记号

储存温度

2-8°C

基因信息

bovine ... LGB(280838)

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一般描述

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。
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。

应用

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。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。

其他说明

含 β-乳球蛋白 A 和 B,可通过色谱法分离。

质量

可能不含叶酸结合蛋白;不推荐用于叶酸分析。

制备说明

结晶

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

动植物源性产品

分析证书(COA)

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Nicholas A Smith et al.
Brain, behavior, and immunity, 95, 122-141 (2021-03-12)
A number of studies have reported comorbidity of food allergies with various neuropsychiatric disorders, such as anxiety, depression, attention-deficit hyperactivity disorder, and autism. However, inconsistent results across clinical studies have left the association between food allergy and behavioral disorders inconclusive.
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)
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
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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