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840522P

Avanti

MGlc-DAG

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

Synonym(e):

Monoglucosyl Diacylglycerol (E. coli); MGlcDG

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About This Item

Empirische Formel (Hill-System):
C43H80O10
CAS-Nummer:
2021179-21-3
Molekulargewicht:
757.09
UNSPSC-Code:
12352211
NACRES:
NA.25

Assay

>99% (TLC)

Form

powder

Verpackung

pkg of 1 × 5 mg (840522P-5mg)

Hersteller/Markenname

Avanti Research™ - A Croda Brand 840522P

Lipid-Typ

neutral glycerides

Versandbedingung

dry ice

Lagertemp.

−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

Allgemeine Beschreibung

Monoglucosyl diacylglycerol (MGlcDAG) is a nonbilayer (NB)-prone[1] and a foreign neutral glycolipid.[2] It is mainly obtained from diacylglycerol (DAG).[1]

Biochem./physiol. Wirkung

Monoglucosyl diacylglycerol (MGlcDAG) is involved in the glucolipid pathway.[1] It is capable of restoring the transport activity of lactose permease (LacY) in the absence of phosphatidylethanolamine (PE).[3]

Verpackung

5 mL Clear Glass Sealed Ampule (840522P-5mg)

Rechtliche Hinweise

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Lagerklassenschlüssel

11 - Combustible Solids

Flammpunkt (°F)

No data available

Flammpunkt (°C)

No data available

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Analysenzertifikate (COA)

Lot/Batch Number

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Die Dokumentenbibliothek aufrufen

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
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

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