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
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NBD-DPhPE
C51H94N5O11P
Recommended Products
Assay
>99% (TLC)
form
liquid
packaging
pkg of 1 × 1 mL (810142C-1mg)
manufacturer/tradename
Avanti Polar Lipids 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)
Signal Word
Danger
Hazard Statements
Precautionary Statements
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
WGK 3
Regulatory Information
易制毒化学品(2类)
危险化学品
Certificates of Analysis (COA)
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Transmembrane Protein (Perfringolysin O) Association with Ordered Membrane Domains (Rafts) Depends Upon the Raft-Associating Properties of Protein-Bound Sterol
Biophysical Journal, 105(12), 2733-2742 (2013)
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
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.
Test, 288(2), 1340-1352 (2013)
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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