产品名称
MGlc-DAG, 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol (E. coli), powder
packaging
pkg of 1 × 5 mg (840522P-5mg)
lipid type
neutral glycerides
manufacturer/tradename
Avanti Research™ - A Croda Brand 840522P
SMILES string
[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
assay
>99% (TLC)
form
powder
shipped in
dry ice
storage temp.
−20°C
General description
Monoglucosyl diacylglycerol (MGlcDAG) is a nonbilayer (NB)-prone and a foreign neutral glycolipid. It is mainly obtained from diacylglycerol (DAG).
Biochem/physiol Actions
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).
Packaging
5 mL Clear Glass Sealed Ampule (840522P-5mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
存储类别
11 - Combustible Solids
flash_point_f
No data available
flash_point_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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