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Phenol

Phenol is a widely studied chemical compound with diverse applications in research, industry, and medicine.
It is a simple aromatic organic compound consisting of a hydroxyl group (-OH) attached to a benzene ring.
Phenol exhibits unique physical and chemical properties, including acidity, reactivity, and antimicrobial activity.
It is commonly used as a disinfectant, a preservative, and an intermediate in the synthesis of various pharmaceuticals and industrial chemicals.
Researchers utilize phenol in a variety of experimental protocols, ranging from extraction and purification to analytical techniques.
This MeSH term provides a concise overview of the key characteristics and applications of phenol, enabling researchers to eaasily locate and compare relevant protocols and products for their studies.

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Publication 2010
Alkaline Phosphatase Anti-Antibodies Buffers cDNA Library Cells chlorocarbonic acid Chloroform Embryo Endopeptidase K Ethanol G-substrate Genome, Human Homo sapiens hydroxybenzoic acid Intestines Kidney MicroRNAs Phenol Polynucleotide 5'-Hydroxyl-Kinase Proteins PUM2 protein, human Radioactive Tracers Ribonuclease T1 RNA, Messenger SDS-PAGE Ultraviolet Rays
Total RNAs were extracted using standard hot phenol RNA preparation method (51 (link)). For RT-PCR analysis, 1.5 µg of total RNAs were subjected to reverse transcription (RT) using gene-specific primers, and then the resulting cDNAs were analysed by standard PCR method or qPCR. Primers used are listed in Supplementary Table S3. The half-life of pre-mRNAs was determined as described previously (52 (link),53 (link)). For northern blotting, the procedures were as previously described (50 (link)) except that total RNAs (10 µg) were separated by 6% acrylamide gels. Sequences of oligonucleotide probes are listed in Supplementary Table S3. Band intensities were quantified using ImageJ densitometry software.
Publication 2013
Acrylamide Densitometry DNA, Complementary Gels Genes mRNA Precursor Oligonucleotide Primers Oligonucleotide Probes Phenol Reverse Transcription RNA Standard Preparations
To maximize transferability of the parameters, multidimensional structure scans were employed to generate conformational diversity. For smaller side chains, grid scans in dihedral space were used to generate side chain variety, including both α and β backbone conformations for each side chain rotamer. Grid scans were generated for Val in one dimension, as it only has χ1, at an interval of 10°. Grids were generated for Asp, Asn, Cys, Phe, His (δ-, ɛ-, and doubly-protonated), Ile, Leu, Ser, Thr, and Trp in two dimensions, as they have χ1 and χ2, at intervals of 20°, yielding 324 structures per amino acid.
We were unable to exhaustively explore side chain conformational space side chains with more than two rotatable bonds. Tyrosine has 3 rotatable χ bonds, but dihedral space is reduced as 180° rotation of either the phenol (χ2) or of the hydroxyl produce the same effect when accounting for symmetry of the ring. We therefore fully scanned each tyrosine dihedral when the other two were at a stable rotamer defined as any instance of that value in the rotamer library for this amino acid, rounded to the nearest 10° and limiting χ2 to (−90°, 90°] to account for symmetry. Stable rotamers for the hydroxyl, not in the rotamer library, were inferred from the QM energy profiles discussed above. Stable rotamers were 180° or ±60° for χ1, ±30° or 90° for χ2, and 0° or 180° for the hydroxyl. Conformations were generated using a full scan for each dihedral (at 20° increments), repeated for every combination of stable rotamer values for the other two dihedrals. As protonated aspartate has nearly the same dihedrals as Tyr (χ1, χ2 and hydroxyl), it was scanned in the same manner, but without χ2 restriction because aspartate does not have the same symmetry properties.
Cysteine presents a special case, as it can form disulfide bonds that bridge two amino acids. In addition to developing parameters for reduced Cys (no disulfide), a pair of Cys dipeptides with a disulfide bond was employed to scan the S-S energy profile. However, a disulfide between CysA and CysB has a total of five dihedrals: χ1A, χ2A, χSS, χ2B, and χ1B. As full sampling across five dihedrals is clearly intractable, conformation space was reduced by applying the same χ1 / χ2 values to both dipeptides. Using this symmetry, a two-dimensional scan was performed for all χ1 / χ2 combinations using 20° spacing; this scan was repeated with χSS restrained to 180°, ±60°, or ±90° (five 2D scans). Separately, the χSS profile was scanned with 20° spacing using χ1 of 180° or ±60° and χ2 of 180° or ±60° (nine 1D scans total). As with the other amino acids, the entire procedure was repeated with the backbone in α and β conformations; here, both dipeptides adopted the same backbone conformation.
The remaining side chains, Arg+, Gln, Glu (protonated), Glu,Lys+, and Met, have at least three side chain dihedrals (Table S1). Rather than performing a grid search, MD simulations were used to generate diverse conformations of these side chains. Each dipeptide was simulated twice, with α or β backbone restraints, for 100 ns each. To overcome kinetic traps, these simulations were performed at 500 K and the dielectric was set to 4r. Next, a diverse subset was generated by mapping each conformation to a multidimensional grid spaced 10° in each χ. The five lowest energy conformations at each grid point were saved. From each simulation grid, five hundred structures were randomly selected (comparable to the number generated by the grid procedure described above for Tyr). Because the longer, more flexible side chains of these amino acids can adopt conformations with strong interactions between backbone and side chain, conformations where we suspected the in vacuo MM description may produce fitting artifacts were excluded, using electrostatic and distance cutoffs defined in the Supporting Information.
Publication 2015
Amino Acids Aspartate Dipeptides Disulfides DNA Library Electrostatics Hydroxyl Radical Kinetics Phenol Radionuclide Imaging Tyrosine Vertebral Column
Escherichia coli strains and plasmids used in this study are listed in Supplementary Table S1. Escherichia coli strain MG1655 was grown in LB medium to OD600∼0.1 at 37°C and exposed to 0.5% α-methylglucoside (αMG) for 15 min. Escherichia coli strain CV104 harboring either pHDB3 or pLCV1 plasmids was grown in morpholinepropanesulfonic acid (MOPS) minimal medium supplemented with 0.2% D-glucose to OD600∼0.5 and exposed to 0.1 mM IPTG. Total RNA was extracted using the hot phenol method as described previously (17 (link)). RNA was treated with TURBO™ DNase (Ambion) according to the manufacturer’s protocol and resolved by electrophoresis on a 1.2% agarose gel to confirm integrity. Library construction and sequencing on the Illumina HiSeq2000 was performed at the W. M. Keck Center for Comparative and Functional Genomics at the University of Illinois at Urbana-Champaign. Ribo-Zero rRNA Removal Meta-Bacteria Kit (Epicentre Biotechnologies) was used to remove rRNA from 1 µg of total RNA. The mRNA-enriched fraction was converted to indexed RNAseq libraries with the ScriptSeq™ v2 RNA-Seq Library Preparation Kit (Epicentre Biotechnologies). The libraries were pooled in equimolar concentration and quantitated by quantitative PCR (qPCR) with the Library Quantification kit Illumina compatible (Kapa Biosystems). The pooled libraries were sequenced for 101 cycles plus 7 cycles for the index read on a HiSeq2000 using TruSeq SBS version 3 reagents. The fastq files were generated with Casava 1.8.2 (Illumina).
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Publication 2013
Acids Bacteria Deoxyribonucleases DNA Library Electrophoresis Escherichia coli Glucose Isopropyl Thiogalactoside methylglucoside Phenol Plasmids Ribosomal RNA RNA, Messenger RNA-Seq Sepharose Strains

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Publication 2011
Bicarbonate, Sodium Buffers Chloroform Chromatin Dot Immunoblotting Ethanol Formaldehyde Phenol Ribonuclease, Pancreatic Ribonuclease H Sodium Chloride

Most recents protocols related to «Phenol»

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Example 37

To improve inhibition potency relative to FAAH, various portions of the t-TUCB molecule were modified to identify potential FAAH pharmacophores. The 4-trifluoromethoxy group on t-TUCB was modified to the unsubstituted ring (A-3), 4-fluorophenyl (A-2) or 4-chlorophenyl (A-26). Potency on both sEH and FAAH increased as the size and hydrophobicity of the para position substituent increased, with 4-trifluoromethoxy being the most potent on both enzymes. Substituting the aromatic ring for a cyclohexane (A-3) or adamantane (A-4) resulted in a complete loss in activity against FAAH. Results are summarized in Table 1 below.

TABLE 1
Modification of the 4-trifluoromethoxy group of t-TUCB
[Figure (not displayed)]
Stereo-IC50 (nM)
R2—N(R3)—L1chemistryhsEHhFAAH
t-TUCB[Figure (not displayed)]
[Figure (not displayed)]
trans0.8140
A1-[Figure (not displayed)]
[Figure (not displayed)]
trans309,200
A-2[Figure (not displayed)]
[Figure (not displayed)]
trans184,600
A-26[Figure (not displayed)]
[Figure (not displayed)]
trans7380
A-3[Figure (not displayed)]
[Figure (not displayed)]
trans6>1,000
A-4[Figure (not displayed)]
[Figure (not displayed)]
trans3>10,000
A-10[Figure (not displayed)]
[Figure (not displayed)]
81,800

Next, the center portion of the molecule was modified to further investigate the specificity of t-TUCB on FAAH. Switching the cyclohexane linker to a cis conformation (A-5) resulted in a 20-fold loss of potency while removing the ring and replacing it with a butane chain (A-6) resulted in a completely inactive compound. While this suggests the compound must fit a relatively specific conformation in the active site to be active, we found the aromatic linker had essentially the same potency on FAAH (A-7). Although many potent urea-based FAAH inhibitors have a piperidine as the carbamoylating nitrogen, the modification to piperidine here reduced potency 13-fold. Results are summarized in Table 2 below.

TABLE 2
Modification of the central portion of t-TUCB
[Figure (not displayed)]
Stereo-IC50 (nM)
R2—N(R3)—L1chemistryhsEHhFAAH
t-TUCB[Figure (not displayed)]
[Figure (not displayed)]
trans0.8140
A-5[Figure (not displayed)]
[Figure (not displayed)]
cis22,800
A-6[Figure (not displayed)]
[Figure (not displayed)]
15>10,000
A-7[Figure (not displayed)]
[Figure (not displayed)]
7170

Since none of the modifications at this point improved potency towards FAAH, we focused on the benzoic acid portion of the molecule as shown in Table 3. To determine the importance of the terminal acid, the corresponding aldehyde (A-20) and alcohol (A-24) in addition to the amide (A-19) and nitrile (A-11) were tested. While the amide had slightly improved potency, the more reduced forms of the acid (A-20 and A-24) and amide (A-11) had substantially less activity on FAAH. Converting the benzoic acid to a phenol (A-21) increased potency while the anisole (A-22) was completely inactive. Since the amide and acid appeared to be active, the amide bioisostere oxadiazole (A-25) was tested and had 38-fold less potency than the initial compound.

TABLE 3
Modification of the benzoic acid portion of t-TUCB
[Figure (not displayed)]
IC50 (nM)
R1hsEHhFAAH
t-TUCB[Figure (not displayed)]
0.8140
A-11[Figure (not displayed)]
5>10,000
A-19[Figure (not displayed)]
270
A-20[Figure (not displayed)]
41,100
A-24[Figure (not displayed)]
35,800
A-21[Figure (not displayed)]
2120
A-22[Figure (not displayed)]
3>10,000
A-25[Figure (not displayed)]
45,300

Since the substrates for FAAH tend to be relatively hydrophobic lipids, we speculated that conversion of the acid and primary amide to the corresponding esters or substituted amides would result in improved potency. The methyl ester (A-12) had 4-fold improved potency relative to the acid. Improving the bulk of the ester with an isopropyl group (A-13) results in a 11-fold loss in potency relative to the methyl ester. However, the similar potency of the benzyl ester (A-14) to the methyl ester demonstrates the bulk but not the size affects potency. Reversing the orientation of the ester (A-23) reduces the potency 3.4-fold. Relative to the primary amide, the methyl (A-18), ethanol (A-15) and glycyl (A-16) amides were all slightly less potent; however, the benzyl amide (A-27) was substantially less potent (16-fold). Generating the methyl ester of the glycyl amide (A-17) increased the potency 4-fold compared to the corresponding acid.

TABLE 4
Potency of ester and amide conjugates of t-TUCB
[Figure (not displayed)]
IC50 (nM)
R1hsEHhFAAH
t-TUCB[Figure (not displayed)]
0.8140
A-12[Figure (not displayed)]
735
A-13[Figure (not displayed)]
5400
A-14[Figure (not displayed)]
324
A-23[Figure (not displayed)]
4120
A-18[Figure (not displayed)]
2170
A-15[Figure (not displayed)]
2100
A-16[Figure (not displayed)]
2130
A-17[Figure (not displayed)]
330
A-27[Figure (not displayed)]
51,100

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Patent 2024
Acids Adamantane Aldehydes Amides anisole Benzoic Acid Butanes Cyclohexane Dietary Fiber Enzymes Esters Ethanol inhibitors Lipids Nitriles Nitrogen Oxadiazoles Phenol piperidine Psychological Inhibition SOCS2 protein, human Urea

Example 1

Cephem Conjugates

Cephem ether linked β-lactam antibiotic cannabinoid conjugate components are synthesized according to the following Scheme. The CAS numbers for the two key building blocks is shown. Reaction conditions follow standard conditions for amine acylation in the first step to attach the cephem side chain, for alkylation of a phenol group of a cannabinoid in the second step with optional use of a catalyst or enhancer such as NaI, followed by standard removal of the p-methoxybenzyl protecting group in the third step to furnish the product. A di-alkylated product may also be obtained.

[Figure (not displayed)]

Carbacephem Conjugates

Carbacephem ether linked β-lactam antibiotic cannabinoid conjugate components are synthesized according to the following Scheme. The general starting material [177472-75-2] was reported in racemic form as [54296-34-3] (Journal of the American Chemical Society (1974), 96(24), 7584) and is elaborated to the iodide intermediate after installing a side chain of choice using a previously reported process (WO 96/04247). Alkylation of CBD with the iodide followed by deprotection, both steps under standard conditions, provides the desired product.

[Figure (not displayed)]

Penem Conjugates

Penem ether linked β-lactam antibiotic cannabinoid conjugate components are synthesized according to the following Scheme. The starting material [145354-22-9], prepared as reported (Journal of Organic Chemistry, 58(1), 272-4; 1993), is reacted with CBD under standard alkylating conditions. The silyl ether TBS protecting group is then removed followed by deallylation under known conditions to give the desired product.

[Figure (not displayed)]

Carbapenem Conjugates

Carbapenem ether linked β-lactam antibiotic cannabinoid conjugate components are synthesized according to the following Scheme. The starting material [136324-03-3] is reacted with CBD under standard alkylating conditions. The silyl ether TES protecting group is then removed followed by removal of the p-methoxybenzyl ester protecting group under known conditions to give the desired product.

[Figure (not displayed)]

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Patent 2024
Acylation Adjustment Disorders Alkylation Amines Cannabinoids carbacephems Carbapenems Esters Ethers Iodides Monobactams Penem Phenol

Example 6

Protocol: Place a 0.22 μm filter on center of the BHI agar plate with phenol red and measure the OD600 of overnight cultures of the different Rothia species or other candidate inhibitors. Dilute the bacterial cultures to OD600 0.5, spread them on filter and grow overnight in their respective growth conditions. This prevented bacteria from physically contacting the agar surface. After overnight growth, remove the filter bearing the bacterial cells and overlay the plate with 4 mL of BHI soft agar (0.5% agar) with phenol sred containing 200 uL of OD600 0.5 Sm Immersing the Sm cells in BHI soft agar and covering the surface of the plate with it allowed to separate Sm from the inhibitory bacteria both physically and temporally. When the soft agar solidifies, it was incubated overnight at 37° C. in aerobic +5% CO2 conditions. The next day pH values were taken at the center of the plate and the side of the plate. The experiments were performed in triplicate. The error bars represent the standard deviation and the statistical significance was determined using Studen't T-test.

Results: The Rothia successfully inhibited the acid production of both Sm UA140 and UA159 in this way (FIGS. 3B and 3C).

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Patent 2024
Acids Agar Bacteria Bacteria, Aerobic Figs Growth Disorders inhibitors Phenol Physical Examination Psychological Inhibition Technique, Dilution

Example 1

Graphene oxide (GO) was suspended in dimethylformamide (DMF) and thoroughly dispersed using a VWR Scientific Model 75T Aquasonic (sonic power ˜90 W, frequency ˜40 kHz) for 24 hours. The concentration of GO in the reaction mixture was held at 1 wt %. To the dispersed GO, a range of weight percentages 1-12 wt % Bisphenol F ethoxylate (2 EO/phenol) diacrylate (BisF) with average molar mass (Mn)˜484 (Sigma) and 4-11.5 wt % PEGDA of various Mn, 700 and 575, were added so that the total amount of polymer added equaled 12 wt %. To this mixture 0.02 g of the photo-initiator lithium phenyl(2,4,6-trimethylbenzoyl)phosphinate) (TPO-Li, Colorado Photopolymer Solutions) was dissolved.

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Patent 2024
Aquasonic ARID1A protein, human bisphenol A Dimethylformamide Graphene graphene oxide Hybrids Lithium Molar Phenol poly(ethylene glycol)diacrylate Polymers Resins, Plant
Total RNA was extracted from samples from 10 OS patients and 10 healthy controls using phenol-chloroform (TRIzol; Invitrogen; ThermoFisher Scientific, Inc., Waltham, MA, United States). The quality of RNA was assessed by capillary electrophoresis (Agilent Technologies, Inc., Santa Clara, CA, United States). Libraries for small RNA sequencing were prepared using NEB kits (New England Biolabs, Inc., Ipswich, MA, United States). qRT-PCR with SYBR-Green (Takara, Osaka, Japan) to detect CDC5L, CUL1, CXCL10, EIF2AK2, POLR2B, PTEN, STAT1, and TBP expression levels, GAPDH was applied as a house keeping gene. The reaction was performed via 40 amplification cycles using the following protocol: 95°C for 3 min, 95°C for 45 s, 55°C for 15 s, and 72°C for 50 s. Primers used in PCR were shown in Supplementary Table S1. Samples were analyzed in triplicate, and gene expression was quantified by normalizing target gene expression to that of the internal control using the 2−ΔΔCt formula.
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Publication 2023
Chloroform CUL1 protein, human Electrophoresis, Capillary GAPDH protein, human Gene Expression Genes, Housekeeping Oligonucleotide Primers Patients Phenol PTEN protein, human STAT1 protein, human SYBR Green I trizol

Top products related to «Phenol»

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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
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TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.
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Phenol, also known as carbolic acid, is a widely used chemical compound in various laboratory and industrial applications. It is a crystalline solid with a distinctive aromatic odor. Phenol serves as a core functional group in many organic compounds and plays a crucial role in chemical synthesis processes.
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Folin-Ciocalteu's phenol reagent is a laboratory reagent used for the colorimetric determination of phenolic compounds. It is a mixture of phosphomolybdic and phosphotungstic acid complexes. The reagent reacts with phenolic compounds, resulting in a blue-colored complex that can be measured spectrophotometrically.
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
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DNase I is an enzyme used in molecular biology laboratories to degrade DNA. It catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, effectively breaking down DNA molecules. This enzyme is commonly used to remove contaminating DNA from RNA preparations, allowing for more accurate downstream analysis of RNA.
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
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Turbo DNase is a laboratory equipment product designed for the efficient degradation of DNA molecules. It functions by rapidly and effectively removing any unwanted DNA from samples, ensuring the integrity and purity of subsequent analyses.
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Quercetin is a natural compound found in various plants, including fruits and vegetables. It is a type of flavonoid with antioxidant properties. Quercetin is often used as a reference standard in analytical procedures and research applications.

More about "Phenol"

Phenol, also known as carbolic acid or hydroxybenzene, is a widely studied and versatile chemical compound with diverse applications across research, industry, and medicine.
As a simple aromatic organic compound, phenol consists of a hydroxyl group (-OH) attached to a benzene ring, giving it unique physical and chemical properties.
Phenol exhibits a range of characteristics, including acidity, reactivity, and antimicrobial activity, making it a valuable component in many applications.
It is commonly used as a disinfectant, preservative, and an intermediate in the synthesis of various pharmaceuticals and industrial chemicals.
Researchers frequently utilize phenol in a variety of experimental protocols, including extraction, purification, and analytical techniques.
Related terms and compounds associated with phenol include TRIzol reagent, Gallic acid, Folin-Ciocalteu's phenol reagent, DPPH, DNase I, RNeasy Mini Kit, Turbo DNase, and Quercetin.
These substances often play complementary roles in research and applications involving phenol.
Phenol's versatility and importance in both academic and industrial settings have made it a well-studied and widely-used chemical.
Researchers can leverage the insights provided by the MeSH term description and metadescription to optimize their research protocols, enhance reproducibility, and explore the diverse applications of this remarkable compound.