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840522P

Avanti

MGlc-DAG

1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol (E. coli), powder

Synonym(s):

Monoglucosyl Diacylglycerol (E. coli); MGlcDG

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About This Item

Empirical Formula (Hill Notation):
C43H80O10
CAS Number:
2021179-21-3
Molecular Weight:
757.09
UNSPSC Code:
12352211
NACRES:
NA.25

Assay

>99% (TLC)

form

powder

packaging

pkg of 1 × 5 mg (840522P-5mg)

manufacturer/tradename

Avanti Research™ - A Croda Brand 840522P

lipid type

neutral glycerides

shipped in

dry ice

storage temp.

−20°C

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

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

Storage Class Code

11 - Combustible Solids

Flash Point(F)

No data available

Flash Point(C)

No data available

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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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