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810141P

Avanti

18:0 NBD PE (NBD-DSPE)

Avanti Research™ - A Croda Brand

Synonym(s):

NBD-DSPE

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About This Item

Empirical Formula (Hill Notation):
C47H86N5O11P
CAS Number:
1246303-01-4
Molecular Weight:
928.19
UNSPSC Code:
12352211
NACRES:
NA.25

description

1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) (ammonium salt)

Assay

>99% (TLC)

form

powder

packaging

pkg of 1 × 1 mg (810141P-1mg)
pkg of 5 × 2 mg (810141P-10mg)

manufacturer/tradename

Avanti Research™ - A Croda Brand

shipped in

dry ice

storage temp.

−20°C

General description

18:0 NBD PE (NBD-DSPE) is a light sensitive lipid which is not hygroscopic. It has saturated acyl chains.
NBD-DSPE preferentially partitions, although not entirely, into the more ordered cholesterol and sphingolipid-enriched microdomain known as a lipid "raft".

Application

18:0 NBD PE (NBD-DSPE) has been used as NBD-labeled lipids to study the partitioning behavior in vesicles.

Packaging

5 mL Amber Glass Screw Cap Vial (810141P-10mg)
5 mL Amber Glass Screw Cap Vial (810141P-1mg)

Legal Information

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Storage Class Code

11 - Combustible Solids

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Ordered raft domains induced by outer leaflet sphingomyelin in cholesterol-rich asymmetric vesicles
Lin Q and London E
Biophysical Journal, 2212-2222 (2015)
Ordered raft domains induced by outer leaflet sphingomyelin in cholesterol-rich asymmetric vesicles
Lin Q and London E
Biophysical Journal (2015)
Ordered raft domains induced by outer leaflet sphingomyelin in cholesterol-rich asymmetric vesicles
Lin Q and London E
Biophysical Journal (2015)
Peter J Quinn
Progress in lipid research, 49(4), 390-406 (2010-05-19)
Domains in cell membranes are created by lipid-lipid interactions and are referred to as membrane rafts. Reliable isolation methods have been developed which have shown that rafts from the same membranes have different proteins and can be sub-fractionated by immunoaffinity

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