810331P
Avanti
18:1 Pyrene PE
Avanti Research™ - A Croda Brand 810331P, powder
Synonym(s):
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(1-pyrenesulfonyl) (ammonium salt)
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About This Item
Recommended Products
Assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 1 mg (810331P-1mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand 810331P
shipped in
dry ice
storage temp.
−20°C
General description
Pyrene is made up of four fused benzol rings. It is an apolar molecule. Phosphatidylethanolamine (PE), a phospholipid is found abundantly in mammalian cells. In mammals, 15-25% of the total lipid comprises of PE. It is enriched in the inner leaflet of membranes and is abundant in the inner mitochondrial membrane.
Application
18:1 Pyrene PE may be used:
- as a quencher of protein intrinsic emission in intrinsic tryptophan quenching assays of membrane proximity
- to incorporate in vesicle membranes
- to label vesicles to confirm the presence of hybrid vesicles in flow-cytometric analysis
Biochem/physiol Actions
Phosphatidylethanolamine (PE) can serve as a lipid chaperone that supports in the folding of membrane proteins. It plays a key role in the activity of respiratory complexes. PE also participates in the initiation of autophagy.
Packaging
5 mL Amber Glass Screw Cap Vial (810331P-1mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
Storage Class Code
11 - Combustible Solids
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
beta-Carotene-Lipid Interactions in Liposomes with Different Lipid Composition
Advances in pharmacognosy and phytomedicine, 14, 293-307 (2011)
Ethanolamine and phosphatidylethanolamine: partners in health and disease
Oxidative Medicine and Cellular Longevity (2017)
Hybrid, Nanoscale Phospholipid/Block Copolymer Vesicles
Polymers, 5(3), 1102-1114 (2020)
Membrane Fluidity Is a Key Modulator of Membrane Binding, Insertion, and Activity of 5-Lipoxygenase
Biophysical Journal, 88(6), 4084-4094 (2005)
MT1-MMP Binds Membranes by Opposite Tips of Its beta Propeller to Position It for Pericellular Proteolysis
Structure, 27(2), 281-292 (2019)
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