Trimethylamine N-oxide dihydrate
(Synonyms: 二水氧化三甲胺) 目录号 : GC61354
A metabolite of choline, phosphatidylcholine, and L-carnitine
Cas No.:62637-93-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Trimethylamine N-oxide (TMAO) is a metabolite of choline, phosphatidylcholine, and L-carnitine .1 It is formed by gut microbiota-mediated metabolism of choline, phosphatidylcholine, and L-carnitine to TMA followed by oxidation of TMA by flavin-containing monooxygenase 3 (FMO3) in the liver.1,2,3 Dietary administration of TMAO (0.12% w/w) increases renal tubulointerstitial fibrosis, collagen deposition, and Smad3 phosphorylation in mice and increases aortic lesion area in atherosclerosis-prone ApoE-/- mice.1,4 Plasma levels of TMAO are elevated in patients with chronic kidney disease and decreased in patients with active, compared with inactive, ulcerative colitis.1,2 Elevated plasma levels of TMAO are associated with increased risk of cardiovascular disease.4
1.Tang, W.H.W., Wang, Z., Kennedy, D.J., et al.Gut microbiota-dependent trimethylamine N-oxide (TMAO) pathway contributes to both development of renal insufficiency and mortality risk in chronic kidney diseaseCirc. Res.116(3)448-455(2015) 2.Wilson, A., Teft, W.A., Morse, B.L., et al.Trimethylamine-N-oxide: A novel biomarker for the identification of inflammatory bowel diseaseDig. Dis. Sci.60(12)3620-3630(2015) 3.Zhang, L.S., and Davies, S.S.Microbial metabolism of dietary components to bioactive metabolites: Opportunities for new therapeutic interventionsGenome Med.8(1)46(2016) 4.Wang, Z., Klipfell, E., Bennett, B.J., et al.Gut flora metabolism of phosphatidylcholine promotes cardiovascular diseaseNature472(7341)57-63(2011)
| Cas No. | 62637-93-8 | SDF | |
| 别名 | 二水氧化三甲胺 | ||
| Canonical SMILES | C[N+](C)([O-])C.O.O | ||
| 分子式 | C3H13NO3 | 分子量 | 111.14 |
| 溶解度 | Water: 100 mg/mL (899.77 mM) | 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 | 8.9977 mL | 44.9883 mL | 89.9766 mL |
| 5 mM | 1.7995 mL | 8.9977 mL | 17.9953 mL |
| 10 mM | 0.8998 mL | 4.4988 mL | 8.9977 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。
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of PhaA from Ralstonia eutropha
Acta Crystallogr F Struct Biol Commun 2014 Nov;70(Pt 11):1566-9.PMID:25372833DOI:10.1107/S2053230X14022778.
Polyhydroxybutyrate (PHB) is a biopolymer that is in the spotlight because of its broad applications in bioplastics, fine chemicals, implant biomaterials and biofuels. PhaA from Ralstonia eutropha (RePhaA) is the first enzyme in the PHB biosynthetic pathway and catalyzes the condensation reaction of two acetyl-CoA molecules to give acetoacetyl-CoA. RePhaA was crystallized using the hanging-drop vapour-diffusion method in the presence of 20% polyethylene glycol monomethyl ether 2K, 0.1 M Tris-HCl pH 8.5 and 0.2 M Trimethylamine N-oxide dihydrate at 295 K. X-ray diffraction data were collected to a maximum resolution of 1.96 Å on a synchrotron beamline. The crystal belonged to space group P2₁, with unit-cell parameters a=68.38, b=105.47, c=106.91 Å, α=γ=90, β=106.18°. With four subunits per asymmetric unit, the crystal volume per unit protein weight (VM) is 2.3 Å3 Da(-1), which corresponds to a solvent content of approximately 46.2%. The structure was solved by the molecular-replacement method and refinement of the structure is in progress.
Viscosity of magnetorheological fluids using Iron-silicon nanoparticles
J Nanosci Nanotechnol 2013 Sep;13(9):6055-9.PMID:24205598DOI:10.1166/jnn.2013.7638.
Fe-6.5Si fine particles were mechanically fabricated by a milling method for use in magnetorheological fluids. Oleic acid was used as a surfactant for the dispersed substance for preparing the hydrophobic fluid with silicon oil as a dispersing medium. Further, oleic acid and sodium dodecyl benzene sulfonate were used as surfactants, forming a bilayer structure, for preparing the hydrophilic fluid with polyethylene glycol as a dispersing medium. The adsorption of oleic acid onto the Fe-Si particles was achieved by oxidizing the particle surface with Trimethylamine N-oxide dihydrate. In order to make a comparative examination of the fluid properties, ferromagnetic nanoparticles were synthesized by chemical precipitation and the subsequent process was accompanied under the same conditions as applied for the magnetorheological fluid. The fluid particles were characterized by magnetization measurements. The viscosity of the fluids was obtained at various concentrations under an external field. The viscosity values of the magnetorheological fluid were higher than those of the ferromagnetic fluid. Moreover, they increased considerably by using silicon oil as the dispersing medium as well as under an applied magnetic field and at higher fluid concentrations. The magnetorheological fluids may be effectively resistant to a strong impact from outside when the appropriate fluid concentration is used and a magnetic field is applied for increasing the shear strength of the fluids.
Electron Acceptors Induce Secretion of Enterotoxigenic Escherichia coli Heat-Labile Enterotoxin under Anaerobic Conditions through Promotion of GspD Assembly
Infect Immun 2016 Sep 19;84(10):2748-57.PMID:27430271DOI:10.1128/IAI.00358-16.
Heat-labile enterotoxin (LT), the major virulence factor of enterotoxigenic Escherichia coli (ETEC), can lead to severe diarrhea and promotes ETEC adherence to intestinal epithelial cells. Most previous in vitro studies focused on ETEC pathogenesis were conducted under aerobic conditions, which do not reflect the real situation of ETEC infection because the intestine is anoxic. In this study, the expression and secretion of LT under anaerobic or microaerobic conditions were determined; LT was not efficiently secreted into the supernatant under anaerobic or microaerobic conditions unless terminal electron acceptors (Trimethylamine N-oxide dihydrate [TMAO] or nitrate) were available. Furthermore, we found that the restoration effects of TMAO and nitrate on LT secretion could be inhibited by amytal or ΔtorCAD and ΔnarG E. coli strains, indicating that LT secretion under anaerobic conditions was dependent on the integrity of the respiratory chain. At the same time, electron acceptors increase the ATP level of ETEC, but this increase was not the main reason for LT secretion. Subsequently, the relationship between the integrity of the respiratory chain and the function of the type II secretion system was determined. The GspD protein, the secretin of ETEC, was assembled under anaerobic conditions and was accompanied by LT secretion when TMAO or nitrate was added. Our data also demonstrated that TMAO and nitrate could not induce the GspD assembly and LT secretion in ΔtorCAD and ΔnarG strains, respectively. Moreover, GspD assembly under anaerobic conditions was assisted by the pilot protein YghG.
Effects of environmental factors on MSP21-25 aggregation indicate the roles of hydrophobic and electrostatic interactions in the aggregation process
Eur Biophys J 2014 Jan;43(1):1-9.PMID:24150738DOI:10.1007/s00249-013-0934-9.
Merozoite surface protein 2 (MSP2), one of the most abundant proteins on the merozoite surface of Plasmodium falciparum, is recognized to be important for the parasite's invasion into the host cell and is thus a promising malaria vaccine candidate. However, mediated mainly by its conserved N-terminal 25 residues (MSP21-25), MSP2 readily forms amyloid fibril-like aggregates under physiological conditions in vitro, which impairs its potential as a vaccine component. In addition, there is evidence that MSP2 exists in aggregated forms on the merozoite surface in vivo. To elucidate the aggregation mechanism of MSP21-25 and thereby understand the behavior of MSP2 in vivo and find ways to avoid the aggregation of relevant vaccine in vitro, we investigated the effects of agitation, pH, salts, 1-anilinonaphthalene-8-sulfonic acid (ANS), Trimethylamine N-oxide dihydrate (TMAO), urea, and sub-micellar sodium dodecyl sulfate (SDS) on the aggregation kinetics of MSP21-25 using thioflavin T (ThT) fluorescence. The results showed that MSP21-25 aggregation was accelerated by agitation, while repressed by acidic pHs. The salts promoted the aggregation in an anion nature-dependent pattern. Hydrophobic surface-binding agent ANS and detergent urea repressed MSP21-25 aggregation, in contrast to hydrophobic interaction strengthener TMAO, which enhanced the aggregation. Notably, sub-micellar SDS, contrary to its micellar form, promoted MSP21-25 aggregation significantly. Our data indicated that hydrophobic interactions are the predominant driving force of the nucleation of MSP21-25 aggregation, while the elongation is controlled mainly by electrostatic interactions. A kinetic model of MSP21-25 aggregation and its implication were also discussed.
Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
Biochemistry 2001 May 22;40(20):6036-46.PMID:11352739DOI:10.1021/bi002555c.
In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril formation were studied under different conditions using the fluorescent dye thioflavin T (ThT). The effect of insulin concentration, agitation, pH, ionic strength, anions, seeding, and addition of 1-anilinonaphthalene-8-sulfonic acid (ANS), urea, TMAO, sucrose, and ThT on the kinetics of fibrillation was investigated. The kinetics of the fibrillation process could be described by the lag time for formation of stable nuclei (nucleation) and the apparent rate constant for the growth of fibrils (elongation). The addition of seeds eliminated the lag phase. An increase in insulin concentration resulted in shorter lag times and faster growth of fibrils. Shorter lag times and faster growth of fibrils were seen at acidic pH versus neutral pH, whereas an increase in ionic strength resulted in shorter lag times and slower growth of fibrils. There was no clear correlation between the rate of fibril elongation and ionic strength. Agitation during fibril formation attenuated the effects of insulin concentration and ionic strength on both lag times and fibril growth. The addition of ANS increased the lag time and decreased the apparent growth rate for insulin fibril formation. The ANS-induced inhibition appears to reflect the formation of amorphous aggregates. The denaturant, urea, decreased the lag time, whereas the stabilizers, Trimethylamine N-oxide dihydrate (TMAO) and sucrose, increased the lag times. The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions. A kinetic model, involving the association of monomeric partially folded intermediates, whose concentration is stimulated by the air-water interface, leading to formation of the critical nucleus and thence fibrils, is proposed.