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840522P

Avanti

MGlc-DAG

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

동의어(들):

Monoglucosyl Diacylglycerol (E. coli); MGlcDG

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모든 사진(2)

About This Item

실험식(Hill 표기법):
C43H80O10
CAS Number:
2021179-21-3
Molecular Weight:
757.09
UNSPSC 코드:
12352211
NACRES:
NA.25

분석

>99% (TLC)

양식

powder

포장

pkg of 1 × 5 mg (840522P-5mg)

제조업체/상표

Avanti Research™ - A Croda Brand 840522P

지질 유형

neutral glycerides

배송 상태

dry ice

저장 온도

−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

일반 설명

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

생화학적/생리학적 작용

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]

포장

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

법적 정보

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

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시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리 방문

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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