850540P
Avanti
MEGA-8
Avanti Research™ - A Croda Brand
别名:
N-octanoyl-N-methylglucamine
产品名称
MEGA-8, Avanti Research™ - A Croda Brand 850540P, powder
方案
>99% (TLC)
表单
powder
包装
pkg of 1 × 1 g (850540P-1g)
制造商/商品名称
Avanti Research™ - A Croda Brand 850540P
应用
sample preservation
运输
dry ice
储存温度
−20°C
SMILES字符串
OCC(O)C(O)C(O)C(O)CN(C)C(CCCCCCC)=O
InChI
1S/C15H31NO6/c1-3-4-5-6-7-8-13(20)16(2)9-11(18)14(21)15(22)12(19)10-17/h11-12,14-15,17-19,21-22H,3-10H2,1-2H3/t11-,12+,14+,15+/m0/s1
InChI key
SBWGZAXBCCNRTM-CTHBEMJXSA-N
一般描述
Acyl-N-methylglucamide (MEGA) detergents are non-ionic detergents that provide a good starting point for your structural biology work. The hydrophilic head groups offer ample strength to extract proteins while still providing the capability to stabilize proteins in solution and promote crystal growth.
MEGA-8 is a neutral surfactant.
包装
20 mL Clear Glass Screw Cap Vial (850540P-1g)
法律信息
Avanti Research is a trademark of Avanti Polar Lipids, LLC
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Influence of N-octanoyl-N-methylglucamine and N-decanoyl-N-methylglucamine on the kinetics and mechanism of Zn2+ ions electroreduction
Nieszporek J and Dagci K
Electrochimica Acta, 125, 473-481 (2014)
J M Hierrezuelo et al.
Langmuir : the ACS journal of surfaces and colloids, 20(24), 10419-10426 (2004-11-17)
The mixed micellization between the nonionic surfactant decanoyl-N-methylglucamide (MEGA-10) and the common sodium dodecyl sulfate (SDS) in aqueous solutions of 0.1 M NaCl was investigated by the fluorescence probe method. The critical micelle concentrations were determined by the pyrene 1:3
J E Hildreth
The Biochemical journal, 207(2), 363-366 (1982-11-01)
N-d-Gluco-N-methylalkanamide detergents have been synthesized. The detergents, which were produced in high yield and at low cost, compared favourably in biochemical studies with commonly used non-ionic detergents, including a chemically related n-alkyl glucoside. The ease of removal by dialysis, high
Matthew A Churchward et al.
Proteome science, 3(1), 5-5 (2005-06-09)
The analysis of hydrophobic membrane proteins by two-dimensional gel electrophoresis has long been hampered by the concept of inherent difficulty due to solubility issues. We have optimized extraction protocols by varying the detergent composition of the solubilization buffer with a
Jen-Hua Chuang et al.
Analytical biochemistry, 418(2), 298-300 (2011-08-30)
We studied the extraction and analysis of integral membrane proteins possessing hydrophobic and hydrophilic domains and found that a nonionic detergent called MEGA-10, used in lysis buffers, had a superior extraction effect compared to most conventional detergents. A sodium dodecyl
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