840522P
Avanti
MGlc-DAG
Avanti Research™ - A Croda Brand
别名:
Monoglucosyl Diacylglycerol (E. coli); MGlcDG
产品名称
MGlc-DAG, 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol (E. coli), powder
方案
>99% (TLC)
表单
powder
包装
pkg of 1 × 5 mg (840522P-5mg)
制造商/商品名称
Avanti Research™ - A Croda Brand 840522P
脂质类型
neutral glycerides
运输
dry ice
储存温度
−20°C
SMILES字符串
[H][C@@](CO[C@@H](O1)[C@H](O)[C@@H](O)[C@@H]([C@H]1CO)O)(OC(CCCCCCC/C=C\CCCCCCCC)=O)COC(CCCCCCCCCCCCCCC)=O
一般描述
Monoglucosyl diacylglycerol (MGlcDAG) is a nonbilayer (NB)-prone and a foreign neutral glycolipid. It is mainly obtained from diacylglycerol (DAG).
生化/生理作用
Monoglucosyl diacylglycerol (MGlcDAG) is involved in the glucolipid pathway. It is capable of restoring the transport activity of lactose permease (LacY) in the absence of phosphatidylethanolamine (PE).
包装
5 mL Clear Glass Sealed Ampule (840522P-5mg)
法律信息
Avanti Research is a trademark of Avanti Polar Lipids, LLC
储存分类代码
11 - Combustible Solids
闪点(°F)
No data available
闪点(°C)
No data available
法规信息
涉药品监管产品
此项目有
Malin Wikström et al.
The Journal of biological chemistry, 279(11), 10484-10493 (2003-12-23)
The mechanisms by which lipid bilayer properties govern or influence membrane protein functions are little understood, but a liquid-crystalline state and the presence of anionic and nonbilayer (NB)-prone lipids seem important. An Escherichia coli mutant lacking the major membrane lipid
L Li et al.
The Journal of biological chemistry, 272(47), 29602-29606 (1997-12-31)
1,2-Diacylglycerol 3-glucosyltransferase synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol (MGlcDAG) in the membrane of Acholeplasma laidlawii, which is important for the spontaneous curvature, and is a regulatory site for the lipid surface charge density. A potential connection between activity and a
Jun Xie et al.
The Journal of biological chemistry, 281(28), 19172-19178 (2006-05-16)
To determine the specific role lipids play in membrane protein topogenesis in vivo, the orientation with respect to the membrane bilayer of Escherichia coli lactose permease (LacY) transmembrane (TM) domains and their flanking extramembrane domains was compared after assembly in
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