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850542P

Avanti

MEGA-10

Avanti Research - A Croda Brand 850542P, powder

Synonyme(s) :

N-decanoyl-N-methylglucamine

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About This Item

Formule empirique (notation de Hill):
C17H35NO6
Numéro CAS:
Poids moléculaire :
349.46
Code UNSPSC :
12161902
Nomenclature NACRES :
NA.25

Pureté

>99% (TLC)

Forme

powder

Poids mol.

349.46 g/mol

Conditionnement

pkg of 1 × 1 g (850542P-1g)

Fabricant/nom de marque

Avanti Research - A Croda Brand 850542P

Conditions d'expédition

dry ice

Température de stockage

−20°C

Chaîne SMILES 

OCC(O)C(O)C(O)C(O)CN(C)C(CCCCCCCCC)=O

InChI

1S/C17H35NO6/c1-3-4-5-6-7-8-9-10-15(22)18(2)11-13(20)16(23)17(24)14(21)12-19/h13-14,16-17,19-21,23-24H,3-12H2,1-2H3/t13-,14+,16+,17+/m0/s1

Clé InChI

UMWKZHPREXJQGR-XOSAIJSUSA-N

Description générale

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-10/N-decanoyl-N-methylglucamine is a longer carbon chain or a sugar-based surfactant. It is a member of the fatty acid glucamides family.

Conditionnement

20 mL Clear Glass Screw Cap Vial (850542P-1g)

Informations légales

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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)
Light scattering and fluorescence studies of non-ionic surfactant binary mixtures formed by MEGA-10 and C12E8
Molina-Bolivar JA and Ruiz CC
Journal of Molecular Liquids, 155(2-3), 96-102 (2010)
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
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
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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