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850541P

Avanti

MEGA-9

Avanti Polar Lipids 850541P, powder

Synonyme(s) :

N-nonanoyl-N-methylglucamine

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About This Item

Numéro CAS:
85261-19-4
Code UNSPSC :
12161902
Nomenclature NACRES :
NA.25

Pureté

>99% (TLC)

Forme

powder

Conditionnement

pkg of 1 × 1 g (850541P-1g)

Fabricant/nom de marque

Avanti Polar Lipids 850541P

Application(s)

microbiology

Conditions d'expédition

dry ice

Température de stockage

−20°C

Chaîne SMILES 

OCC(O)C(O)C(O)C(O)CN(C)C(CCCCCCCC)=O

InChI

1S/C16H33NO6/c1-3-4-5-6-7-8-9-14(21)17(2)10-12(19)15(22)16(23)13(20)11-18/h12-13,15-16,18-20,22-23H,3-11H2,1-2H3/t12-,13+,15+,16+/m0/s1

Clé InChI

GCRLIVCNZWDCDE-SJXGUFTOSA-N

Catégories apparentées

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-9 (N-nonanoyl-N-methyl-D-glucamine) is a nonionic sugar-based surfactant. It is a membrane solubilizer and can forms vesicles.

Application

MEGA-9 may be used as a component of PBS.

Conditionnement

20 mL Clear Glass Screw Cap Vial (850541P-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

Certificats d'analyse (COA)

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Self-aggregation of MEGA-9 (N-nonanoyl-N-methyl-d-glucamine) in aqueous medium: physicochemistry of interfacial and solution behaviors with special reference to formation energetics and micelle microenvironment
Pan A, et al.
The Journal of Physical Chemistry B, 117(25), 7578-7592 (2013)
Hb (64-76) epitope binds in different registers and lengths to I-Ek and I-Ak
Vidal K, et al.
Molecular Immunology, 37(5), 203-212 (2000)
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
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
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