生物来源
bovine milk
质量水平
类型
Type III
检测方案
≥85% (PAGE)
形式
lyophilized powder
质量
calcium depleted
分子量
14,178 Da by calculation
技术
indirect ELISA: suitable
溶解性
H2O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow
痕量阳离子
Ca: ≤0.3 mol/mol
UniProt登记号
储存温度
−20°C
基因信息
cow ... LALBA(281894)
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相关类别
一般描述
may contain traces of (NH4)2SO4 and sodium phosphateL6010
应用
α-牛乳乳清蛋白已用于:
- 间接酶联免疫吸附测定(ELISA)和竞争性ELISA方法
- Hsp90和HSJ1b结合分析
- 抑制溶菌酶CAP-RAST测定体系
生化/生理作用
α-乳清蛋白是人乳中的主要蛋白。它由含有8个半胱氨酸(可形成二硫键)的单个多肽链组成。α-乳清蛋白可结合包括钙在内的几种金属离子,这被认为有助于从还原的变性形式α-乳清蛋白中再生天然形式的α-乳清蛋白。α-乳清蛋白还具有独特的锌结合位点,其被认为在乳糖合酶复合物的结合中起作用。其成熟蛋白由123个氨基酸残基(14kD)组成,具有1.7埃分辨率的三维结构,包含四个α-螺旋和三链反平行β-折叠。
其可通过改变半乳糖基转移酶的底物特异性以增加乳糖形成的速率;半乳糖基转移酶和α-乳白蛋白的复合物称为乳糖合酶。Asp87 或 Asp88 对 Ala 的定点诱变完全消除了强钙结合亲和力,并将乳糖合酶的刺激降低到最大速率的 <3.5%。
质量
可能含微量 (NH4)2SO4 和磷酸钠。
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
The Journal of dairy research, 81(1), 98-106 (2013-12-20)
Alpha-lactalbumin (α-la) is one of the major proteins in whey. When partially hydrolysed with Bacillus licheniformis protease, it produces nanotubular structures in the presence of calcium ions by a self-assembly process. This study presents investigation of α-la protein structure during
Effect of conjugation of cow milk whey protein with polyethylene glycol on changes in their immunoreactive and allergic properties
Food and agricultural immunology, 14(2), 155-162 (2002)
Prevalence of lysozyme sensitization in an egg-allergic population
Allergy, 52(2), 224-228 (1997)
Frontiers in physiology, 12, 687563-687563 (2021-10-09)
Lymphatic vascular permeability prevents lymph leakage that is associated with lymphedema, lymphatic malformations, obesity, and inflammation. However, the molecular control of lymphatic permeability remains poorly understood. Recent studies have suggested that adherens junctions and vesicle transport may be involved in
Life sciences, 67(12), 1455-1465 (2000-09-13)
The 90 kDa heat shock protein (Hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins. Both genetic and in vitro refolding experiments using reticulocyte lysate have suggested a functional interaction of Hsp90 with yeast human homologues of
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