810610P
Avanti
4-palmitamido-TEMPO
N-tempoyl palmitamide, powder
别名:
4-Palmitamido-2,2,6,6-tetramethylpiperidine-1-oxyl; 2,2,6,6-Tetramethyl-4-[(1-oxohexadecyl)amino]-1-piperidinyloxy; 2,2,6,6-tetramethyl-4-palmitamidopiperidinooxy; 2,2,6,6-Tetramethylpalmitoylamidopiperidine-1-oxyl; 4-(Palmitylimino)-2,2,6,6-tetramethyl-1
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About This Item
推荐产品
化驗
>99% (TLC)
形狀
powder
包裝
pkg of 1 × 1 mg (810610P-1mg)
製造商/商標名
Avanti Research™ - A Croda Brand 810610P
脂質類型
ESR probes
運輸包裝
dry ice
儲存溫度
−20°C
一般說明
4-palmitamido-TEMPO/N-tempoyl-palmitamide is a spin label, that is present in the polar head-group region of the membrane.
This amphiphilic compound binds strongly to membranes by virture of its long hydrocarbon chain, but the polarity of the amide linkage is expected to localize the nitroxide function in the aqueous phase adjacent to the membrane surface. The location of the nitroxide function allows one to investigate electrostatic potentials and lipid-protein interactions at the membrane surface.
應用
4-palmitamido-TEMPO/N-tempoyl palmitamide (N-TP) may be used:
- to enrich rod outer segment (ROS) membranes
- as a spin probe in vesicles/bilayer to prepare samples for electron spin resonance (ESR) experiments
- as a component in liposomes to assess the mobility of lipid headgroups
包裝
5 mL Amber Glass Screw Cap Vial (810610P-1mg)
法律資訊
Avanti Research is a trademark of Avanti Polar Lipids, LLC
儲存類別代碼
11 - Combustible Solids
Nature communications, 8, 14258-14258 (2017-02-22)
G-protein-coupled receptors are membrane proteins that are regulated by a small family of arrestin proteins. During formation of the arrestin-receptor complex, arrestin first interacts with the phosphorylated receptor C terminus in a pre-complex, which activates arrestin for tight receptor binding.
Biochimica et biophysica acta. Biomembranes, 1861(1), 75-82 (2018-11-06)
Curcumin, the main molecular ingredient of the turmeric spice, has been reported to exhibit therapeutic properties for varied diseases and pathological conditions. While curcumin appears to trigger multiple signaling pathways, the precise mechanisms accounting for its therapeutic activity have not
Selective Membrane Disruption Mechanism of an Antibacterial γ-AApeptide Defined by EPR Spectroscopy.
Biophysical journal, 110(8), 1789-1799 (2016-04-28)
γ-AApeptides are a new class of antibacterial peptidomimetics that are not prone to antibiotic resistance and are highly resistant to protease degradation. It is not clear how γ-AApeptides interact with bacterial membranes and alter lipid assembly, but such information is
Biophysical journal, 61(6), 1443-1453 (1992-06-01)
A new general method for the determination of electrostatic potentials at biological surfaces is presented. The approach is based on measurement of the collision frequency of a charged nitroxide in solution with a nitroxide fixed to the surface at the
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