MEGA-9
(Synonyms: Nonanoyl-N-Methylglucamide) 目录号 : GC44153
A detergent used to solubilize membrane proteins
Cas No.:85261-19-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
MEGA-9 is a nonionic detergent that can be used to solubilize membrane proteins. It has a critical micelle concentration (CMC) of 20 mM under no-salt conditions and CMCs ranging from 2 to 17.1 mM under high and low salt conditions for a variety of salts. It has been used to solubilize the melibiose transport carrier from E. coli membranes and reconstitute it into liposomes.
| Cas No. | 85261-19-4 | SDF | |
| 别名 | Nonanoyl-N-Methylglucamide | ||
| Canonical SMILES | OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CN(C)C(CCCCCCCC)=O | ||
| 分子式 | C16H33NO6 | 分子量 | 335.4 |
| 溶解度 | DMF: 30 mg/ml,DMSO: 30 mg/ml,DMSO:PBS (pH 7.2) (1:2): 0.33 mg/ml,Ethanol: 1 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 2.9815 mL | 14.9076 mL | 29.8151 mL |
| 5 mM | 0.5963 mL | 2.9815 mL | 5.963 mL |
| 10 mM | 0.2982 mL | 1.4908 mL | 2.9815 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
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
J Phys Chem B 2013 Jun 27;117(25):7578-92.PMID:23718221DOI:10.1021/jp400139d.
Self-aggregation of MEGA-9 (N-nonanoyl-N-methyl-D-glucamine), a nonionic sugar-based surfactant, was studied with respect to the effect of salt (NaCl) and ionic liquid (1-butyl-3-methylimidazolium tetrafluoroborate) on its critical micelle concentration (cmc), aggregation number, hydrodynamic dimensions, energetics of micellization, and micellar microenvironment. Fluorimetry (both steady state and time resolved) was used to understand the microenvironments under the influence of additives. NaCl was found to decrease cmc, increase aggregation number (N), increase micellar size, and decrease enthalpy of micelle formation; the IL effect on the parameters was mostly opposite. The microscopic properties of micelles were probed using two fluorophores: one nonpolar C-153 (2,3,5,6-1H,4H-tetrahydro-8-trifluormethylquinolizino-(9,9a,1-gh)coumarin) and the other fairly polar ANS (8-anilinonaphthalene-1-sulfonate); they delivered information on the palisade layer and the peripheral region of the micelle interface, respectively. Energy of activation and entropy of activation of the dynamics of the probes were evaluated from their decay time, lifetime, and rotational movements in the regions of residency in the micelles. Density functional theory (DFT) calculations showed that the ternary combination MEGA-9/IL/H2O had the maximum interaction energy compared to any of the binary combinations. Thus, the ionic liquid reduced MEGA-9 self-association to a large extent.
Solubility properties of the alkylmethylglucamide surfactants
Biochim Biophys Acta 1990 Nov 2;1029(1):67-74.PMID:2223813DOI:10.1016/0005-2736(90)90437-s.
The critical micelle concentration (CMC) and the ability to solubilize and form vesicles from phospholipids are important criteria for the selection of a surfactant for reconstitution protocols. The CMC and its temperature dependence were determined for an homologous series of alkylmethylglucamides (MEGA-8, MEGA-9, MEGA-10). Each detergent was added continuously from a concentrated solution to a saline buffer with the environment-sensitive fluorescent probe ANS, held in a thermojacketed cuvette; ANS fluorescence increases at the CMC. The CMCs at 25 degrees C were 51.3, 16.0 and 4.8 mM for MEGA-8, MEGA-9 and MEGA-10. The free energy change for transfer to a micellar environment per -CH2- was -740 cal/mol, similar to other alkyl series. The CMCs decreased slightly with increasing temperature (T = 5-40 degrees C) for MEGA-9 and MEGA-10 while that of MEGA-8 was virtually insensitive to temperature in this range. MEGA-9 solubilization of egg PC in aqueous solutions was determined as a function of [PC] and temperature. The lamellar-micellar phase boundaries were determined by simultaneous 90 degrees light scattering and the resonance energy transfer using the headgroup labeled lipid probes NBD-PE and Rho-PE. The [MEGA-9] at solubilization was linear with [PC]; the MEGA-9 to egg PC ratio in the structures at optical clarity was 2.3 while the monomeric [MEGA-9] was 14.3 mM or slightly lower than the CMC at 25 degrees C. Solubilization of egg PC by MEGA-9 was somewhat more temperature-dependent than the CMC of this detergent. Vesicles formed from MEGA-9 tended to be multilamellar. MEGA-9 is clearly different from octyl glucoside, despite its chemical similarity, in terms of its temperature sensitivity and vesicle forming characteristics.
Solubilization and characterization of the acceptor for Clostridium botulinum type B neurotoxin from rat brain synaptic membranes
Biochim Biophys Acta 1993 Nov 28;1158(3):333-8.PMID:8251534DOI:10.1016/0304-4165(93)90032-4.
The acceptor for Clostridium botulinum type B neurotoxin was solubilized from rat brain synaptic membrane with nonionic detergent, nonanoyl-N-methylglucamide (MEGA-9). The solubilized acceptor was assayed for the binding activity by precipitating the acceptor with acetone in the presence of phosphatidylcholine. 125Ilabeled neurotoxin specifically bound to the lipid vesicles having incorporated the acceptor together with gangliosides. The lipid vesicles having incorporated either the acceptor or gangliosides alone showed extremely low binding activity. The treatment of the solubilized acceptor with lysyl endopeptidase and glycopeptidase F but not with sialidase resulted in decreased toxin binding, indicating that the putative acceptor is a glycoprotein accompanying an N-linked carbohydrate moiety. The observations suggest also that a protein acceptor/ganglioside complex may be required to form the functional toxin receptor.
The photochemical reaction center of Chloroflexus aurantiacus is composed of two structurally similar polypeptides
Eur J Biochem 1987 Sep 15;167(3):595-600.PMID:3308462DOI:10.1111/j.1432-1033.1987.tb13377.x.
A method has been devised which allowed the isolation of highly purified reaction center from the thermophilic green bacterium, Chloroflexus aurantiacus. The procedure consisted of three chromatography steps. The final step was fast protein liquid chromatography on Mono Q in the presence of nonanoyl-N-methylglucamide (MEGA-9). The purified reaction center complex was photochemically active and had an A280/A813 of 1.4 or less. Under non-denaturing conditions, a pigmented protein band having a Mr of 52,000-55,000 was observed in sodium dodecyl sulfate gels. When the isolated complex was heat-dissociated in the presence of sodium dodecyl sulfate, just two polypeptides having very similar Mr (24,000 and 24,500) were observed. Two protein bands were also observed in two-dimensional isoelectric focusing/sodium-dodecyl-sulfate polyacrylamide gel electrophoresis; the PI values of the two polypeptides were 6.5 and 6.7. Partial peptide mapping of the two isolated subunits, using both enzymatic and chemical cleavage techniques, yielded almost identical patterns which indicated a high degree of sequence homology between the two polypeptides. The N-terminal amino acid sequences of the two polypeptides were identical and did not exhibit any homology to reaction center subunits of purple sulfur bacteria. The Chloroflexus reaction center is believed to be composed of one molecule of each polypeptide, the photoactive bacteriochlorophyll a dimer and, as accessory pigments, an additional bacteriochlorophyll a and three bacteriopheophytins. Hence, it appears to be the smallest photochemically active reaction center isolated to date.
Rapid and sensitive sandwich enzyme-linked immunosorbent assay for detection of staphylococcal enterotoxin B in cheese
Appl Environ Microbiol 1991 Mar;57(3):836-42.PMID:2039234DOI:10.1128/aem.57.3.836-842.1991.
A rapid and sensitive screening sandwich enzyme-linked immunosorbent assay (ELISA) was developed for the detection of staphylococcal enterotoxin B (SEB) in cheese by using a highly avid anti-SEB antibody (Ab) as the capture Ab (CAb) and as the biotinylated Ab conjugate. The glutaraldehyde fixation method for the immobilization of CAb on polystyrene dipsticks was superior to the adsorption fixation and the adsorption-glutaraldehyde fixation methods. The glutaraldehyde fixation method resulted in a higher surface-saturating CAb concentration as evaluated by the peroxidase saturation technique and by the ability of the CAb-coated dipstick to discriminate between positive and negative controls (index of discrimination). Of nine blocking agents used alone or in pairs, lysine-human serum albumin, bovine serum albumin, human serum albumin, and gelatin effectively saturated available sites on the CAb-coated dipsticks without causing interference with the antigen-Ab reactions. The addition of 1% polyethylene glycol to the diluent of the biotinylated anti-SEB Ab conjugate improved the detection of SEB. A concentration of 4% polyethylene glycol allowed a 5-min reaction time for the streptavidin-biotin-horseradish peroxidase conjugate. Cheddar cheese homogenate reduced the sensitivity of the SEB assay; however, the sensitivity was restored when 1.6% (wt/vol) of either a nonionic detergent (MEGA-9) or two zwitterionic detergents (Zwittergent 3-10 and 3-12 detergent) was added to the diluent. By using the rapid sandwich ELISA, a minimum of 0.5 to 1.0 ng of SEB per ml was detected within 45 min. The whole procedure for the analysis of the cheddar cheese samples was completed within 1 h.(ABSTRACT TRUNCATED AT 250 WORDS)