检测方案
>99% (TLC)
形式
liquid
包装
pkg of 1 × 1 mL (810142C-1mg)
制造商/商品名称
Avanti Research™ - A Croda Brand 810142C
浓度
1 mg/mL (810142C-1mg)
运输
dry ice
储存温度
−20°C
一般描述
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
应用
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.
包装
5 mL Amber Glass Screw Cap Vial (810142C-1mg)
法律信息
Avanti Research is a trademark of Avanti Polar Lipids, LLC
警示用语：
Danger
危险分类
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
靶器官
Central nervous system, Liver,Kidney
WGK
WGK 3
法规信息
易制毒化学品（2类）
危险化学品
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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