N1138
N-Nonanoyl-N-methylglucamine
≥98%
别名:
N-(D-Glucityl)-N-methylnonanamide, N-Methyl-N-nonanoyl-D-glucamine, MEGA-9
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关于此项目
经验公式（希尔记法）:
C16H33NO6
化学文摘社编号:
分子量:
335.44
UNSPSC Code:
12352116
PubChem Substance ID:
NACRES:
NA.32
SMILES string
CCCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO
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
InChI key
GCRLIVCNZWDCDE-SJXGUFTOSA-N
description
non-ionic
assay
≥98%
form
powder
mol wt
335.44 g/mol
technique(s)
protein expression: suitable
CMC
19-25 mM (20-25°C)
suitability
suitable for molecular biology
application(s)
life science and biopharma
Quality Level
Application
Non-ionic, dialyzable detergent
N-Nonanoyl-N-methylglucamine has been used to reconstitute proteins into liposomes. It has also been used to study its effects on the oligomerization of Bacillus thuringiensis Cry4Ba toxin.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Conserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85*
Patrick Koenig
The Journal of Biological Chemistry (2010)
Functional assembly of 260-kDa oligomers required for mosquito-larvicidal activity of the Bacillus thuringiensis Cry4Ba toxin
Narumol Khomkhum
Peptides (2015)
K Häsler et al.
Biochemistry, 38(41), 13759-13765 (1999-10-16)
ATP synthase is conceived as a rotary enzyme. Proton flow drives the rotor (namely, subunits c12 epsilon gamma) relative to the stator (namely, subunits ab2 delta(alpha beta)3) and extrudes spontaneously formed ATP from three symmetrically arranged binding sites on (alpha
B Norling et al.
Biochimica et biophysica acta, 935(2), 123-129 (1988-09-14)
Isolation of F1-ATPase from Rhodospirillum rubrum by chloroform extraction of chromatophores, followed by purification on a glycerol gradient, results in a very pure enzyme preparation containing five subunits with high Ca2+-ATPase activity (15 mumol per min per mg protein). Furthermore
E V Yurkova et al.
Biomedical science, 1(6), 585-590 (1990-01-01)
The conditions for crystallization of the integral membrane protein bovine rhodopsin were determined. Crystals form over a wide range of protein concentration (0.4-15 mg ml-1) and pH (5.5-7.5) in detergent solutions of octyl-polyoxyethylene (o-POE) that contain inorganic salts as precipitants.
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