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840522P

Avanti

MGlc-DAG

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

同義詞:

Monoglucosyl Diacylglycerol (E. coli); MGlcDG

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About This Item

經驗公式(希爾表示法):
C43H80O10
CAS號碼:
分子量::
757.09
分類程式碼代碼:
12352211
NACRES:
NA.25

化驗

>99% (TLC)

形狀

powder

包裝

pkg of 1 × 5 mg (840522P-5mg)

製造商/商標名

Avanti Research - A Croda Brand 840522P

脂質類型

neutral glycerides

運輸包裝

dry ice

儲存溫度

−20°C

SMILES 字串

[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

一般說明

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).

包裝

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

法律資訊

Avanti Research is a trademark of Avanti Polar Lipids, LLC

儲存類別代碼

11 - Combustible Solids

閃點(°F)

No data available

閃點(°C)

No data available


分析證明 (COA)

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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
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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