产品名称
α-乳清蛋白 来源于牛奶, Marker for non-denaturing PAGE
Quality Level
biological source
bovine milk
form
lyophilized powder
mol wt
~14.2 kDa
concentration
0.9—1.4 mg per vial protein (biuret)
technique(s)
microbiological culture: suitable
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... LALBA(281894)
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Biochem/physiol Actions
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。
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%。
α-乳清蛋白是母乳中的主要蛋白质。它由单个多肽链组成，含有通过二硫键连接的8个半胱氨酸。α- 乳清蛋白可结合多种金属离子，包括钙，被认为在从还原的变性形式再生成天然α-乳清蛋白的过程中发挥重要作用。α-乳清蛋白还具有独特的锌结合位点，该位点被认为在乳糖合酶复合物的结合中起作用。 成熟蛋白由 123 个氨基酸残基（14 kD） 组成，具有 1.7Α° 分辨率的三维结构，显示出四 α-螺旋和三链反平行 β-折叠。
General description
α-乳清蛋白是一种小球状乳清蛋白，存在于迄今为止已研究的所有乳汁中。它是在乳腺中产生的约14kDa的金属蛋白。
Preparation Note
用 1 mL 水复溶后为 0.9-1.4 mg/mL
Application
α-乳清蛋白用于分离和分析来自副结核分枝杆菌和其他分枝杆菌物种的染色体 DNA 的限制性核酸内切酶消化模式。它还用于一项研究，以测试神经内分泌蛋白 7B2 是否抑制神经退行性疾病相关蛋白的聚集。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Michael Helwig et al.
The Journal of biological chemistry, 288(2), 1114-1124 (2012-11-23)
Neurodegenerative diseases such as Alzheimer (AD) and Parkinson (PD) are characterized by abnormal aggregation of misfolded β-sheet-rich proteins, including amyloid-β (Aβ)-derived peptides and tau in AD and α-synuclein in PD. Correct folding and assembly of these proteins are controlled by
Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme.
K Brew et al.
The Journal of biological chemistry, 242(16), 3747-3749 (1967-08-25)
D B Veprintsev et al.
FEBS letters, 412(3), 625-628 (1997-08-04)
The thermal denaturation of bovine and human apo-alpha-lactalbumins at neutral pH has been studied by intrinsic protein fluorescence, circular dichroism (CD), and differential scanning microcalorimetry (DSC) methods. Apo-alpha-lactalbumin possesses a thermal transition with a midpoint about 25-30 degrees C under
J Ren et al.
The Journal of biological chemistry, 268(26), 19292-19298 (1993-09-15)
It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A
D L Whipple et al.
Journal of clinical microbiology, 25(8), 1511-1515 (1987-08-01)
A relatively rapid and efficient method for the extraction of chromosomal DNA from Mycobacterium paratuberculosis and other mycobacteria was developed. Approximately 25 to 50 micrograms of DNA could be extracted from 100 mg (wet weight) of cells, which was sufficient
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