840027P
Avanti
E. coli PE
Avanti Research™ - A Croda Brand 840027P, powder
Synonym(s):
L-α-phosphatidylethanolamine (E. coli)
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About This Item
Recommended Products
assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 25 mg (840027P-25mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand 840027P
lipid type
phosphoglycerides
shipped in
dry ice
storage temp.
−20°C
SMILES string
[O-]P(OCC[NH3+])(OC[C@@]([H])(COC(CCCCCCCCCCCCCCC)=O)OC(CCCCCCC/C=C/CCCCCCCC)=O)=O
General description
L-α-phosphatidylethanolamine (E. coli) is the major phospholipid constituting around 70-80%, present in the inner membrane of E. coli. PE in E. coli tends to form non-bilayer structure.
Application
E. coli PE may be used to study the physical states and thermodynamic properties extracted from E. coli.
Biochem/physiol Actions
L-α-phosphatidylethanolamine (E. coli) plays a vital role in cytoskeletal organization during cytokinesis. It also interacts with several membrane proteins such as lactose permease.
Packaging
5 mL Clear Glass Sealed Ampule (840027P-25mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
also commonly purchased with this product
Storage Class
11 - Combustible Solids
Certificates of Analysis (COA)
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Physical states and thermodynamic properties of model gram-negative bacterial inner membranes
Chemistry and Physics of Lipids, 218, 57-64 (2019)
Phosphatidylethanolamine-phosphatidylglycerol bilayer as a model of the inner bacterial membrane
Biophysical Journal, 88(2), 1091-1103 (2005)
The Journal of cell biology, 149(6), 1215-1224 (2000-06-13)
Phosphatidylethanolamine (PE) is a major membrane phospholipid that is mainly localized in the inner leaflet of the plasma membrane. We previously demonstrated that PE was exposed on the cell surface of the cleavage furrow during cytokinesis. Immobilization of cell surface
Depletion of phosphatidylethanolamine affects secretion of Escherichia coli alkaline phosphatase and its transcriptional expression
Febs Letters, 493(2-3), 85-90 (2001)
Proceedings of the National Academy of Sciences of the United States of America, 107(34), 15057-15062 (2010-08-11)
Phosphatidylcholine (PC) has been widely used in place of naturally occurring phosphatidylethanolamine (PE) in reconstitution of bacterial membrane proteins. However, PC does not support native structure or function for several reconstituted transport proteins. Lactose permease (LacY) of Escherichia coli, when
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