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Key Documents

850541P

Avanti

MEGA-9

Avanti Research - A Croda Brand 850541P, powder

Sinônimo(s):

N-nonanoyl-N-methylglucamine

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About This Item

Número CAS:
Código UNSPSC:
12161902
NACRES:
NA.25

Ensaio

>99% (TLC)

forma

powder

embalagem

pkg of 1 × 1 g (850541P-1g)

fabricante/nome comercial

Avanti Research - A Croda Brand 850541P

aplicação(ões)

microbiology

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

cadeia de caracteres 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

chave InChI

GCRLIVCNZWDCDE-SJXGUFTOSA-N

Descrição geral

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.

Aplicação

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

Embalagem

20 mL Clear Glass Screw Cap Vial (850541P-1g)

Informações legais

Avanti Research is a trademark of Avanti Polar Lipids, LLC

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (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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