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2,6-Dihydroxyacetophenone Sale

(Synonyms: 2,6-二羟基苯乙酮) 目录号 : GC39767

2,6-Dihydroxyacetophenone 是一种内源性代谢产物。

2,6-Dihydroxyacetophenone Chemical Structure

Cas No.:699-83-2

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Sample solution is provided at 25 µL, 10mM.

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产品描述

2,6-Dihydroxyacetophenone is an endogenous metabolite.

Chemical Properties

Cas No. 699-83-2 SDF
别名 2,6-二羟基苯乙酮
Canonical SMILES CC(C1=C(O)C=CC=C1O)=O
分子式 C8H8O3 分子量 152.15
溶解度 DMSO : 100 mg/mL (657.25 mM; Need ultrasonic) 储存条件 Store at -20°C
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1 mM 6.5725 mL 32.8623 mL 65.7246 mL
5 mM 1.3145 mL 6.5725 mL 13.1449 mL
10 mM 0.6572 mL 3.2862 mL 6.5725 mL
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Research Update

AP-MALDI Mass Spectrometry Imaging of Gangliosides Using 2,6-Dihydroxyacetophenone

J Am Soc Mass Spectrom 2018 Jul;29(7):1463-1472.PMID:29549666DOI:10.1007/s13361-018-1928-8.

Matrix-assisted laser/desorption ionization (MALDI) mass spectrometry imaging (MSI) is widely used as a unique tool to record the distribution of a large range of biomolecules in tissues. 2,6-Dihydroxyacetophenone (DHA) matrix has been shown to provide efficient ionization of lipids, especially gangliosides. The major drawback for DHA as it applies to MS imaging is that it sublimes under vacuum (low pressure) at the extended time necessary to complete both high spatial and mass resolution MSI studies of whole organs. To overcome the problem of sublimation, we used an atmospheric pressure (AP)-MALDI source to obtain high spatial resolution images of lipids in the brain using a high mass resolution mass spectrometer. Additionally, the advantages of atmospheric pressure and DHA for imaging gangliosides are highlighted. The imaging of [M-H]- and [M-H2O-H]- mass peaks for GD1 gangliosides showed different distribution, most likely reflecting the different spatial distribution of GD1a and GD1b species in the brain. Graphical Abstract ᅟ.

Evaluation of 2,6-Dihydroxyacetophenone as matrix-assisted laser desorption/ionization matrix for analysis of hydrophobic proteins and peptides

Anal Biochem 2012 Jun 1;425(1):18-20.PMID:22406432DOI:10.1016/j.ab.2012.02.039.

Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is widely used for analysis of macromolecules like peptides and proteins. The analysis procedure is generally simple but must be adapted to the characteristics of the analytes. Therefore, specific matrices suitable for, e.g., hydrophobic proteins and peptides that are difficult to analyze would be preferable in order to optimize the outcome. In the present work, 2,6-Dihydroxyacetophenone (DHAP) was shown to be beneficial in comparison to DHB for intact bacteriorhodopsin (BR) as well as for chemically digested BR.

Use of 2,6-Dihydroxyacetophenone for analysis of fragile peptides, disulphide bonding and small proteins by matrix-assisted laser desorption/ionization

Rapid Commun Mass Spectrom 1996;10(5):529-36.PMID:9053038DOI:10.1002/(SICI)1097-0231(19960331)10:5<529::AID-RCM522>3.0.CO;2-9.

Several peptides were shown to undergo fragmentation during matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to a degree which complicated their analysis using alpha-cyano-4-hydroxycinnamic acid (CHCA) as a matrix, even at threshold laser irradiance. These peptides included synthetic peptides, peptides isolated from viral proteins and a phosphopeptide from beta-casein (residues 33-48). The excessive fragmentation occurred usually as a post-source phenomenon; however, in-source fragmentation was also observed. The combined effects of in-source and post-source fragmentation of one peptide studied led to a failure to observe the protonated molecule of this peptide in reflector mode analysis. The phosphopeptide studied exhibited a high degree of beta-elimination of phosphate. It was demonstrated that the fragility exhibited by these peptides in CHCA, including beta-elimination of phosphate from serine, was not evident with a matrix comprising 2,6-Dihydroxyacetophenone (DHAP) and di-ammonium hydrogen citrate (DAHC). The DHAP/DAHC matrix was also adapted for direct analysis of peptides from an acidic reducing milieu containing tris(2-carboxyethyl)phosphine. The molecular weight of equine cytochrome c was determined with a relatively high degree of accuracy (experimental M(r) = 12360.2 +/- 1.4 Da compared to the theoretical M(r) = 12360.09 Da) using DHAP/DAHC as a matrix for reflector mode analysis.

Inhibitors of hepatic mixed function oxidases. I. The metabolism of 2,6-dihydroxy-,2-hydroxy-6-methoxy- and 2,6-dimethoxyacetophenones

Xenobiotica 1975 Feb;5(2):65-72.PMID:1154800DOI:10.3109/00498257509056094.

1. 2,6-Dihydroxyacetophenone, its mono- and di-methyl ethers are inhibitors of hepatic mixed function oxidases. The dimethyl ether is a competitive inhibitor of aminopyrine demethylase with the others displaying mixed kinetics. The metabolism of all three ketones has been studied. 2. 2,6-Dihydroxyacetophenone is excreted unchanged and as conjugates. 3. 2-Hydroxy-6-methoxyacetophenone is largely excreted unchanged and conjugated but small amounts of the 3- and 5-hydroxylated derivatives are formed. 4. 2,6-Dimethoxyacetophenone is demethylated to 2-hydroxy-6-methoxy-acetophenone. In addition 3-hydroxy-2,5-dimethoxyacetophenone and 2,3-dihydroxy-6-methoxyacetophenone were identified as metabolites. 5. Quantitative data on the excretion of metabolites were obtained with 14C-labelled ketones.

Inhibitors of hepatic mixed function oxidase. 3. Inhibition of hepatic microsomal aniline hydroxylase and aminopyrine demethylase by 2,6- and 2,4-dihydroxyphenyl alkyl ketones and related compounds

J Med Chem 1977 Sep;20(9):1194-9.PMID:926120DOI:10.1021/jm00219a017.

A series of 2,6- and 2,4-dihydroxyphenyl alkyl ketones has been investigated as inhibitors of hepatic microsomal aniline hydroxylase and aminopyrine demethylase activities. Structural alterations in both series did little to enhance the inhibitory activity of the parent compounds 2,6-Dihydroxyacetophenone (3) and 2,4-dihydroxyacetophenone (27). In the 2,6 series activity against both microsomal systems varied only over a relatively narrow range, 6-allyloxy-2-hydroxyacetophenone (19) being the most potent inhibitor. In the 2,4 series, activity against aniline hydroxylase was poor or absent in most cases. tthe most potent inhibitor was 5-ethyl-2,4-dihydroxyacetophenone (31). In contrast, high activity against aminopyrine demethylase was frequently displayed in this series, 3,5-dibromo-2,4-dihydroxypropiophenone (36) showing greatest inhibitory potency. The effects of some compounds on hexobarbital sleeping times and zoxazolamine paralysis times in mice were also examined.