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810142C

Avanti

4ME 16:0 NBD PE (NBD-DPhPE)

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

Sinónimos:

NBD-DPhPE

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About This Item

Fórmula empírica (notación de Hill):
C51H94N5O11P
Número de CAS:
Peso molecular:
984.29
UNSPSC Code:
12352211
NACRES:
NA.25

assay

>99% (TLC)

form

liquid

packaging

pkg of 1 × 1 mL (810142C-1mg)

manufacturer/tradename

Avanti Research - A Croda Brand 810142C

concentration

1 mg/mL (810142C-1mg)

shipped in

dry ice

storage temp.

−20°C

General description

4ME 16:0 NBD PE (NBD-DPhPE) is a headgroup labeled fluorescent phospholipid.
NBD-DPhPE preferentially partitions, although not entirely, into the fluid phase of the cell membrane rather than the more ordered cholesterol and sphingolipid-enriched microdomain known as a lipid "raft."NBD-DSPE preferentially partitions, although not entirely, into the more ordered cholesterol and sphingolipid-enriched microdomain known as a lipid "raft." - Personal communication, Dr. Erwin London, SUNY-Stony Brook

Application

4ME 16:0 NBD PE (NBD-DPhPE) or 1,2-diphytanoyl-sn-glycero-3-phosphoethanolamine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) (ammonium salt) may be used for fluorescence resonance energy transfer (FRET)experiments to determine raft affinity.

Packaging

5 mL Amber Glass Screw Cap Vial (810142C-1mg)

Legal Information

Avanti Research is a trademark of Avanti Polar Lipids, LLC

pictograms

Skull and crossbonesHealth hazard

signalword

Danger

Hazard Classifications

Acute Tox. 3 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3 - Carc. 2 - Eye Irrit. 2 - Repr. 2 - Skin Irrit. 2 - STOT RE 1 - STOT SE 3

target_organs

Central nervous system, Liver,Kidney

wgk_germany

WGK 3


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Transmembrane Protein (Perfringolysin O) Association with Ordered Membrane Domains (Rafts) Depends Upon the Raft-Associating Properties of Protein-Bound Sterol
Lin Q and LondonE
Biophysical Journal, 105(12), 2733-2742 (2013)
Qingqing Lin et al.
The Journal of biological chemistry, 288(2), 1340-1352 (2012-11-15)
The hypothesis that mismatch between transmembrane (TM) length and bilayer width controls TM protein affinity for ordered lipid domains (rafts) was tested using perfringolysin O (PFO), a pore-forming cholesterol-dependent cytolysin. PFO forms a multimeric barrel with many TM segments. The
Qingqing Lin et al.
Biophysical journal, 105(12), 2733-2742 (2013-12-24)
Because transmembrane (TM) protein localization, or nonlocalization, in ordered membrane domains (rafts) is a key to understanding membrane domain function, it is important to define the origin of protein-raft interaction. One hypothesis is that a tight noncovalent attachment of TM
Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O.
Lin Q and LondonE
Test, 288(2), 1340-1352 (2013)
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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