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Hydroquinone

Hydroquinone is a phenolic compound with the chemical formula C6H6O2.
It is used in a variety of applications, including as a reducing agent, antioxidant, and in the production of photographic developers.
Hydroquinone has also been studied for its potential therapeutic uses, such as in the treatment of skin conditions like hyperpigmentation.
Researchers can leverage AI-powered tools like PubCompare.ai to streamline their hydroquinone studies, locating and comparing protocols from literature, preprints, and patents to find the best approaches and products for their research.
This can help enhance the reproducibility and reliability of hydroquinone-related studies.
Experiene the future of hydroqunone research today with PubCompare.ai.

Most cited protocols related to «Hydroquinone»

1
Quantitative Evaluation of DNA Methylation
Cited 9 times
Three types of DNA targets were generated to address various issues surrounding the adaptation of the SNaPshot approach for the quantitative evaluation of C/T (G/A) ratios:

A fragment of the promoter region of the gene encoding human catecholamine O-methyltransferase (COMT) was amplified as follows. 10× PCR Buffer, 2 mM MgCl2, 2.5 mM dNTP, 1 M Betaine, 0.4 mM primers and 1 U of Taq polymerase (New England Biolabs), primers: comtF1 5′-agaccacaggtgcagtcagcacag-3′ and comtR1 5′-caccctatcccagtgttccacccta-3′ at 95°C for 5 min, 30 cycles (94°C for 1 min, 61°C for 1.5 min and 72°C for 1 min), and 72°C for 5 min. CCGG and GCGC sites of the amplicon were subsequently methylated using M-HpaII and M-HhaI, respectively, in two separate fractions. The third fraction of the amplicon was left unmethylated. Both methylated and unmethylated DNA samples were then subjected to bisulfite modification (21 (link)). Briefly, DNA was boiled for 5 min, cooled on ice and denatured for 15 min at 50°C after adding 4 μl of fresh 2 M NaOH in a total reaction volume of 25 μl. Two volumes of 2% LMP agarose in distilled water was added and 10 μl aliquots of this solution was pipetted into cold mineral oil and placed immediately back into dry ice to create beads. The mineral oil was removed and a solution of 1.9 g sodium metabisulfite in 2.5 ml H2O, 720 μl of 2 M NaOH and 500 μl of 1 mM hydroquinone was added. Samples were incubated on ice for 30 min followed by incubation at 50°C for 3.5 h. The agarose beads were washed four times for 15 min with 1 ml TE, two times for 15 min with 0.2 M NaOH, three times for 10 min with 1 ml TE and two times for 15 min with H2O. This was followed by semi-nested PCR using identical reaction and cycling conditions as above with semi-nested primers: BisF1, 5′-gaagggggttatttgtggttagaa-3′, BisF2 5′-gatttttgagtaagattagattaag-3′ and BisR1 5′-aacaaccctaactaccccaa-3′. C (metC in the amplicon) containing templates were mixed with the T (unmethylated C in the amplicon) containing fraction to create a standard curve from 100 to 0% of C signal in increments of 5%: (100% C: 0% T), (95% C: 5% T), (90% C: 10% T), …, (0% C: 100% T). This was done for those templates containing C at M-HpaII sites and M-HhaI sites separately. The M-HpaII sites were interrogated with three forward primers, while three primers for the M-HhaI sites were added as negative controls. In a similar way, M-HhaI sites were interrogated with all six forward primers (three of which were for the M-HpaII sites as negative controls) in one run and the three reverse primers in a second run (Figure 1). The interrogating primers were designed to have a Tm close to 50°C to allow for similar annealing dynamics in the multiplexed reaction. To vary the length of the primers, non-complementary tails were designed on the 5′ end of each primer by repeating the sequence GACT (shown in brackets): at least two sets of the GACT for oligos with the total length <40 nt and by one set of GACT for those >40 nt. The interrogating SNaPshot primers were

5′-agtaagattagattaagaggt-3′, 5′-[gact]1gatatttttatgaggatattt-3′ and 5′-[gact]6ttatggtttgtgtttgttat-3′ for the HpaII sites;

5′-[gact]4ggatattttggttattgttg-3′, 5′-[gact]6ttttgattttattttatttgttg-3′ and 5′-[gact]7agtgtttttttaatttttgtag-3′ for the HhaI sites (direct primers);

5′-ccacaataaatatccac-3′, 5′-[gact]2tataacaaacaaaatacaaaac-3′ and 5′-[gact]3acactacaaaaattaaaaaaac-3′ for the remaining three HhaI sites (reverse primers).

In order to investigate the effects of quantitative G/A and C/T polymorphisms in the SNaPshot primer binding region, sets of oligonucleotides containing variable C/T and G/A were synthesized. Five polymorphic positions were investigated: −2, −5, −10, −15 and −18 (A−2/G−2, A−5/G−5, T−10/C−10, A−15/G−15 and T−18/C−18) upstream of the nucleotide that was interrogated (‘target’ nucleotide, Ntarget) (Figure 2). SNaPshot primers in the experiment were named according to the polymorphic site, while the DNA template itself was named by the nucleotide in the polymorphic position and also the target nucleotide. Therefore, the primer T−2 is fully complementary to the templates A−2Atarget and A−2Gtarget, but not complementary at the −2 position to the templates G−2Atarget and G−2Gtarget. It is evident that the T−2 primer will preferentially bind to (and interrogate) the DNA sequence that contains A−2, in comparison to G−2 at the upstream position. The degree of such bias, however, is unknown as is the impact of the location of the mismatch proximal to the target nucleotide. To elucidate the degree of bias, DNA templates containing an upstream polymorphism, e.g. G−2Gtarget and A−2Atarget, were added in equal amounts which resulted in a polymorphic G/A site at the −2 position. This template mix was tested in two different primer scenarios: first with primer T−2, then with primer C−2. All other polymorphic sites at positions −5, −10, −15 and −18 were analyzed in the same way. For the mismatch bias correction, numerous DNA template combinations with varying percentages of polymorphic nucleotides in the primer binding site were tested using different primer combinations (see Results).

To verify that degenerative SNaPshot primers are able to interrogate numerous polymorphic C/T and A/G containing DNA sequence targets, two types of DNA templates were used:

Six oligonucleotide templates were synthesized with quantitative G/A polymorphisms in different positions of the SNaPshot primer annealing region (Figure 3). The target nucleotide A/G proportions were synthesized to be 50%:50% in each template while the upstream A/G ratios were synthesized according to Figure 3. SNaPshot primers contained a 50%:50% proportion of C/T at degenerative positions corresponding to polymorphic positions in the templates.

Two human genomic DNA samples from brain and placenta were bisulfite modified and subjected to both SNaPshot interrogation and to cloning plus sequencing-based measurement of metC density. The two selected CpG island regions were identified as exhibiting DNA methylation differences according to our microarray-based DNA methylation profiling (A. Schumacher, A. Petronis, et al., unpublished data). These regions are located between 28 and 276 bp upstream of known genes coding for LGALS1 (lectin, galactoside-binding, soluble, 1), otherwise referred to as galectin 1 and humanin, respectively. Three CpG positions were selected for each CpG island and will be referred to as gal1, gal2 and gal3 for galectin 1 and hum1, hum2 and hum3 for humanin (Figure 4).

Bisulfite modification reactions were performed as described above. Target sequences were amplified using fully nested PCR. PCR conditions were as follows: 10× PCR Buffer, 2 mM MgCl2, 2.5 mM dNTP, 0.4 mM primers and 1 U of Taq polymerase. The first PCR was performed using primers, for galectin 1: 22_f1 5′-gtagaatgttaattttgggtagaaataat-3′ plus 22_r1 5′-ctcaaccatcttctctaaacacc-3′; and for humanin: 52_f1 5′-agtttgtattaaggagatttataaggatag-3′ plus 52_r1 5′-aaccaacaaaacacacaaacc-3′. The second (nested) PCR used primers, for galectin 1: 22_f2: 5′-gttattgaggtttagaaaagagaaggtat-3′ plus 22_r2 5′-acttataaacctaactcatcatcaaactat-3′ and for humanin: 52_f2: 5′-aatttagattttgagtttttgaaag-3′ plus 52_r2 5′-aacacaacataacaacaaacaaaac-3′ site. Two successive rounds of touch down PCR were used with the following cycling conditions: 95°C for 3 min, 10 cycles [94°C for 1 min, 60°C for 30 s (minus 1°C/cycle), 72°C for 40 s], 30 cycles of (94°C for 1 min, 50°C for 30 s, 72°C for 40 s) and 72°C for 5 min. The sequences of the interrogating SNaPshot primers were gal1 5′-gttattgggggyggagtt-3′, gal2 5′-[gact]2gaggatgttttygggtagg-3′ and gal3 5′-[gact]4gatyggatygggtgagttt-3′. Primers for humanin were hum1 5′-acagttyggatttttygaaaggggg-3′, hum2 5′-aactcccaatatcrtacratac-3′ and hum3 5′-ygagggtgatagggaag-3′. Amplicons were cloned into the pDrive plasmid (Qiagen) that were used for transformation of DH5-α competent cells. Individual colonies were grown at 37°C for 15 h followed by plasmid purification using the Qiagen Spin Miniprep kit. Sequencing of 12–15 plasmid inserts per template was carried out with M13 reverse primer using ABI Big Dye Terminator kit 3.1. Six CpG positions were investigated using SNaPshot primers individually and five were multiplexed in two groups (gal1, gal2 and gal3, and hum1 and hum3). The differences in length of degenerative primers to be multiplexed were in accordance with the specifications recommended by the manufacturer (ABI). All SNaPshot experiments on bisulfite-modified DNA were repeated in quadruplicate.
Kaminsky Z.A., Assadzadeh A., Flanagan J, & Petronis A. (2005). Single nucleotide extension technology for quantitative site-specific evaluation of metC/C in GC-rich regions. Nucleic Acids Research, 33(10), e95.
Publication 2005
2
Enzymatic Activities of Dioxygenases
Cited 8 times
Activity of catechol 1,2-dioxygenase [EC 1.13.11.1] was measured spectrophotometrically by formation of cis,cis-muconic acid at 260 nm (λ260 = 16,800 M−1 cm−1). The reaction mixture contained 20 μl of catechol (50 mM), 67 μl Na2EDTA (20 mM), 893 μl of phosphoric buffer pH 7.4 (50 mM) and 20 μl of crude enzyme extracts in a total volume of 1 ml. When activity of catechol 2,3-dioxygenase was detected, crude enzyme extract was incubated with 5% H2O2 prior to determination of catechol 1,2-dioxygenase. In order to determine catechol 2,3-dioxygenase [EC 1.13.11.2] activity, formation of 2-hydroxymuconic semialdehyde was measured at 375 nm (λ375 = 36,000 M−1 cm−1). The reaction mixture contained 20 μl of catechol (50 mM), 960 μl of phosphoric buffer pH 7.4 (50 mM) and 20 μl of crude extract in a total volume of 1 ml (Hegeman 1966 (link)). Activity of protocatechuate 3,4-dioxygenase [EC 1.13.11.3] was measured by protocatechuate depletion at 290 nm in a reaction mixture containing 20 μl of protocatechuate (50 mM), 960 μl of Tris–HCl buffer pH 7.4 (50 mM) and 20 μl of crude extract in a total volume of 1 ml. A molar extinction coefficient of 2,300 M−1 cm−1 was used, which is the difference between λ290 of protocatechuate (3,890 M−1 cm−1) and λ 290 of the product 3-carboxy-cis cis-muconate (1,590 M−1 cm−1). Protocatechuate 4,5-dioxygenase [EC 1.13.11.8] activity was measured spectrophotometrically by formation of 2-hydroxy-4-carboxymuconic semialdehyde at 410 nm (λ410 = 9,700 M−1 cm−1). The reaction mixture contained 20 μl of protocatechuate (50 mM), 960 μl of Tris–HCl buffer pH 7.4 (50 mM) and 20 μl of crude extract in a total volume of 1 ml (Stanier and Ingraham 1954 (link)). In order to determine hydroxyquinol 1,2-dioxygenase [EC 1.13.11.37] activity, the formation of 4-hydroxymuconic semialdehyde was measured at 320 nm (λ320 = 11 mM−1cm−1). The reaction mixture contained 200 μl of hydroquinone (50 mM), 700 μl of K–Na phosphate buffer pH 6.6 (100 mM) and 100 μl of crude extract in a total volume of 1 ml (Zaborina et al. 1995 (link)). One unit of enzyme activity was defined as the amount of enzyme required to generate 1 μmol of product per minute. Protein concentrations of the crude extract from different inducer-cultured bacteria were determined by the Bradford method using bovine serum albumin (Bradford 1976 (link)).
Wojcieszyńska D., Guzik U., Greń I., Perkosz M, & Hupert-Kocurek K. (2010). Induction of aromatic ring: cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems. World Journal of Microbiology & Biotechnology, 27(4), 805-811.
Publication 2010
1,2,4-trihydroxybenzene A 300 Bacteria Buffers Catechols cis,cis-muconate cis-acid Complex Extracts Dioxygenases enzyme activity Enzymes Extinction, Psychological hydroquinone hydroxymuconic semialdehyde Molar Peroxide, Hydrogen Phosphates Phosphorus Proteins Serum Albumin, Bovine Tromethamine
3
MALDI-MS Analysis of DNA Adducts
Cited 7 times
Calf thymus DNA, 2´-deoxycytidine-5´-monophosphate, disodium salt (dCMP), hydroquinone, p-benzoquinone, nuclease P1, ferric chloride, triethylammonium acetate buffer (TEAA, 1M), 2-N-(morpholino)ethanesulfonic acid (MES), 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC), α-cyano-4-hydroxy-cinnamic acid (CCA), and ammonium citrate (dibasic) were from Sigma-Aldrich (St. Louis, MO). 5-Methyl-2´-deoxycytidine-5´-monophosphate, disodium salt (mdCMP) was a gift from Affymetrix (Cleveland, Ohio). Phosphodiesterase I was from Worthington (Lakewood, NJ). BIOMAX-5 Ultrafree MC centrifugal filter devices were from Millipore (Billerica, MA). Propanesulfonic acid silica was from J. T. Baker (Phillipsburg, NJ). Microcentrifuge tubes, pipetter tips, and HPLC grade acetonitrile (ACN) were from Fisher Scientific (Pittsburgh, PA). The OASIS columns were from Waters (Milford, MA). All materials were used as received. Benzoylhistamine (BH), benzoylhistamine-d4 (BH(d4), where the ethylene moiety is tetradeuteriated), and p-bromo-benzoylhistamine (Br-BH) were synthesized as described.9 Hydroquinone was reacted in the presence of ferric chloride with calf thymus DNA as described.10 (link) Our method for measuring DNA adducts, described before,8 (link),9 is summarized here. The digestion of the modified DNA to nucleotides was done with nuclease P1 at pH 5.5 followed with phosphodiesterase I at pH 9, 3 hours at 45 °C for both. The sample was purified with an OASIS column (186000383, Waters) and dried. The labeling reaction was performed by adding 3.5 μL of 12 mM BH (6 mM BH and 6 mM BH(d4)), or 12 mM Br-BH, and 3.5 μL of 80 mM EDC in 0.01 M MES buffer at pH 6, to the dried OASIS collection vial, and then, after mixing, the sample was kept at room temperature in the dark for 3 hours. The sample was separated on a capillary HPLC column (PepMap 180 μm I.D×150 mm, Dionex, Sunnyvale, CA) using a gradient flow from 3% to 60 % ACN in 40 min at 2.2 μL/min. A droplet was collected onto a MALDI plate every 20 sec with a Probot Fraction Collector (Dionex, Sunnyvale, CA). CCA matrix (0.5 μL, 5 mg/mL in ACN:water, 50:50, v/v, with 2.5 mM of ammonium citrate, dibasic) was deposited onto each dried spot, followed by air-drying for 5 min. Analysis was done on a Voyager DE STR MALDI-TOF-MS or a Model 5800 MALDI-TOF/TOF-MS (AB SCIEX, Foster City, CA) in a negative ion mode with a delay time of 150 ns. Each sample well was surveyed to find a “sweet spot”, and then 400 laser pulses were averaged to generate a spectrum. MS/MS was performed with a medium pressure of air and a mass resolution window of 400 with the metastable-ion suppressor on.
p-Benzoquinone was reacted with dCMP or mdCMP as described.13 (link) The nucleotide (8 mg of dCMP or 8.3 mg of mdCMP, 0.023 mmol) and p-benzoquinone (16 mg, 0.15 mmol) were allowed to react in 1 mL of 0.1 M sodium acetate buffer (pH 5) at 37 °C. After 17 h, the diluted reaction mixture (1:100 in water) was mixed with CCA matrix in a 1:5 ratio and subjected to MALDI-TOF-MS in a negative ion mode. Also, MS/MS in a positive ion mode was performed on the protonated modified nucleobase formed in MALDI ion source. Further, a combined sample (1 μL of each diluted reaction mixture) was labeled with Br-BH and subjected to MALDI analysis directly.
Wang P., Gao J., Li G., Shimelis O, & Giese R.W. (2012). Nontargeted Analysis of DNA Adducts by Mass-Tag MS: Reaction of p-Benzoquinone with DNA. Chemical research in toxicology, 25(12), 2737-2743.
Publication 2012
4
Quantitative VEGF-A and SP1 mRNA Expression
Cited 7 times

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Open the protocol to access the free full text link

Publication 2015
Actins Cells DNA, Complementary Genes Homo sapiens Hypersensitivity Nucleotides Oligonucleotide Primers Plasmids Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription RNA, Messenger Sp1 protein, human SYBR Green I Technique, Dilution Vascular Endothelial Growth Factors
5
Sodium Bisulfite-Based DNA Methylation Analysis
Cited 5 times
For methylation analyses, genomic DNA is modified by treatment with sodium bisulfite, which converts all unmethylated cytosines to uracil, then to thymidine during the subsequent PCR step (22 (link)). Briefly, 1 μg of DNA in 50 μl distilled H2O was incubated with 5.5 μl of 2 M NaOH at 37°C for 10 minutes, followed by 16 hours treatment at 50°C after adding 30 μl of freshly-prepared 10 mM hydroquinone (Sigma) and 520 μl of freshly-prepared 10mM sodium-bisulfite (Sigma) at pH 5.0. The bisulfite-treated DNA was purified using a DNA Wizard cleanup kit (Promega), by following manufacturer's instructions. The purified DNA was denatured at room temperature for 5 minutes with 5.5 μL of 3M NaOH, followed by ethanol precipitation with 33μL of 10M NH4Ac and 170μL of ethanol. After washing with 70% ethanol, the DNA pellet was resuspended in 50μL TE pH 7.5.
Vaissière T., Hung R., Zaridze D., Moukeria A., Cuenin C., Fasolo V., Ferro G., Paliwal A., Hainaut P., Brennan P., Tost J., Boffetta P, & Herceg Z. (2009). Quantitative analysis of DNA methylation profiles in lung cancer identifies aberrant DNA methylation of specific genes and its association with gender and cancer risk factors. Cancer research, 69(1), 243-252.
Publication 2008
Cytosine DNA, A-Form Ethanol Genome hydrogen sulfite hydroquinone Methylation Promega sodium bisulfite Thymidine Uracil

Most recents protocols related to «Hydroquinone»

1
Optimization of Arbutin Biotransformation
Hydroquinone (HQ), purchased from Merck (Darmstadt, Germany), was solubilized in bi-distilled water and aseptically administered to the cell suspension cultures through a 0.22 μm Millipore membrane filter. Two distinct HQ feeding protocols, at concentrations of 5 mM and 6 mM, were implemented for the biotransformation studies. The first approach, based on Coste et al. [29 ], involved a single HQ administration on the 14th culture day, followed by sample collection at intervals of 3, 6, 12, 24, and 48 h for both arbutin production and growth profiling. The second strategy, adapted from Yokoyama and Inomata [10 ], implied a sequential HQ addition commencing on the 10th culture day. For the 5 mM concentration, 1 mM HQ was added initially on the 10th day, followed by 2 mM HQ on each subsequent day. To achieve the 6 mM concentration, 2 mM HQ was added daily for three consecutive days, beginning on the 10th day. Evaluation of arbutin yield from dry biomass and liquid medium, as well as growth rate assessment, was carried out on the 14th culture day. All hydroquinone-supplemented cultures were maintained under agitation at 100 rpm at a temperature of 25 ± 1 °C and a 16 h photoperiod, illuminated by cool white, fluorescent light at an intensity of 30 μmol/m2/sec.
Pop C.E., Coste A., Vlase A.M., Deliu C., Tămaș M., Casian T, & Vlase L. (2024). Selection of a Digitalis purpurea Cell Line with Improved Bioconversion Capacity of Hydroquinone into Arbutin. Life, 14(1), 84.
Full text: Click here
Publication 2024
2
Optimizing Hydroquinone for Arbutin Production
Not available on PMC !
To determine the optimal concentration of hydroquinone for the production of arbutin in a liquid medium of production, different concentrations of hydroquinone (0.5, 1, 2, 3 and 4) % (w/v) were used to produce the bioactive compound (arbutin).
Noor M.I., & Mohammed N.S. (2024). Study of optimal nutritional conditions for Arbutin production from Bacillus subtilis NN2M. Plant Science Today.
Publication 2024
3
Quantification of Arbutin and Hydroquinone in Plants
Arbutin and hydroquinone determinations were performed based on the methodology described in the latest 7th edition of the European Pharmacopoeia [32 ]. A 0.800 g weighed amount of powdered plant material was placed in a 100 mL round-bottomed flask, 20 mL distilled water was added, and the flask was heated for 30 min in a water bath under a reflux condenser. After cooling, the extract was filtered through a wad of cotton wool and was extracted again, together with the residue in the flask, with another 20 mL of distilled water for 30 min in a water bath under a reflux condenser. After cooling, all the liquid was filtered through a paper filter and left to cool, then topped up with 50 mL of distilled water and filtered again, discarding the first 10 mL of the filtrate. The purified plant extracts were applied to conditioned Waters Sep-Pak (C18, 500 mg) syringe filter cartridges (Ireland). Phenolic compounds were leached from the columns with methanol in 10 mL round-bottomed flasks and were concentrated at 40 °C until the solvent was evaporated in a Hei-VAP Precision rotational vacuum evaporator from Heidolph (Schwabach, Germany). The leaf extracts in the round-bottomed flasks were dissolved with methanol and filtered through PTFE socket filters with a 0.45 µm pore size directly prior to chromatographic analysis. A standard solution was made by dissolving 50 mg of arbutin in 50 mL of mobile phase and 2.5 mg of hydroquinone in 10 mL of mobile phase, then mixed at the ratios specified in the methodology. The plant extracts were separated using a Thermo Scientific/Dionex UltiMate 3000 liquid chromatograph with a UV detector and a DAD-3000 (RS) diode matrix (ESA, Chelmsford, MA, USA). A HALO 90 A C18, 2.7 μm, 4.6 × 150 mm column was used for the separations at 25 °C. The mobile phase was methanol and water (10:90 v/w), the flow rate was 0.8 mL/min, and the assay time was 30 min, with detection at a wavelength of 280 nm. The injection volume was 10 µL. The average recovery for the highbush blueberry was 97%. The operation of the chromatographic set and processing of the obtained data were coordinated using the Thermo Scientific Dionex Chromeleon 7.2 Chromatography Data System.
Czernicka M., Sowa-Borowiec P., Puchalski C, & Czerniakowski Z.W. (2024). Content of Bioactive Compounds in Highbush Blueberry Vaccinium corymbosum L. Leaves as a Potential Raw Material for Food Technology or Pharmaceutical Industry. Foods, 13(2), 246.
Full text: Click here
Publication 2024
4
Benzoquinone Reduction with Sodium Dithionate
Not available on PMC !

Example 10

[Figure (not displayed)]

Sodium dithionate (18.7 g, 107.3 mmol, 7.3 equiv) was dissolved in 20 mL H2O and loaded into a separatory funnel. Next, a solution of benzoquinone (2 g, 14.7 mmol, 1 equiv) in 75 mL diethyl ether was added. The diphasic mix was stirred vigorously for 30 minutes and the organic layer changed color from orange to pale yellow. Organic phase was washed with brine, dried over MgSO4, and concentrated to yield a white solid (1.69 g, 83%).

US11867660B2. Electronic control of the pH of a solution close to an electrode surface (2024-01-09). Robert Bosch GmbH [DE]. Inventors: Christopher Johnson [US], Sam Kavusi [US], Nadezda Fomina [US], Habib Ahmad [US], Autumn Maruniak [US], Christoph Lang [US], Ashwin Raghunathan [US], Young Shik Shin [US], Armin Darvish [US], Efthymios Papageorgiou [US].
Full text: Click here
Patent 2024
1,4-benzoquinone brine Ethyl Ether hydroquinone sodium dithionate Sulfate, Magnesium
5
Danggui Shaoyao Powder and Hydroquinone for Skin
Patients in the DSP + H group took Danggui Shaoyao powder orally BID for twelve weeks and simultaneously used 4% hydroquinone cream topically twice a day. The H group used only 4% hydroquinone cream topically twice a day for 12 weeks.
Cheng Y.Y., Peng R.R., Luo H, & Zhao W. (2024). Comparison of the efficacy of Hydroquinone cream versus Hydroquinone cream plus Danggui Shaoyao powder in the treatment of melasma. Advances in Dermatology and Allergology/Postȩpy Dermatologii i Alergologii, 41(1), 66-71.
Publication 2024

Top products related to «Hydroquinone»

1
Hydroquinone by Merck Group
Sourced in United States, Germany, India, China, United Kingdom, Australia, Italy, Canada
Hydroquinone is a chemical compound used in various laboratory applications. It is a crystalline solid with the chemical formula C₆H₄(OH)₂. Hydroquinone is commonly used as a reducing agent, antioxidant, and in photographic development processes.
2
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
3
Hydrochloric acid (hcl) by Merck Group
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
4
Silver nitrate by Merck Group
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Silver nitrate is a chemical compound with the formula AgNO3. It is a colorless, water-soluble salt that is used in various laboratory applications.
5
Methanol by Merck Group
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
6
Sodium hydroxide (naoh) by Merck Group
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
7
Wizard dna clean up system by Promega
Sourced in United States, Norway
The Wizard DNA Clean-Up System is a laboratory equipment designed for the purification and concentration of DNA fragments from various sources, such as PCR reactions, restriction digests, or other enzymatic reactions. The system utilizes a silica-based resin to selectively bind DNA, allowing for the removal of unwanted salts, primers, enzymes, and other contaminants.
8
Sodium borohydride by Merck Group
Sourced in United States, Germany, Italy, France, Spain, United Kingdom, China, Canada, India, Poland, Sao Tome and Principe, Australia, Mexico, Ireland, Netherlands, Japan, Singapore, Sweden, Pakistan
Sodium borohydride is a reducing agent commonly used in organic synthesis and analytical chemistry. It is a white, crystalline solid that reacts with water to produce hydrogen gas. Sodium borohydride is frequently employed in the reduction of carbonyl compounds, such as aldehydes and ketones, to alcohols. Its primary function is to facilitate chemical transformations in a laboratory setting.
9
Ascorbic acid by Merck Group
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Ascorbic acid is a chemical compound commonly known as Vitamin C. It is a water-soluble vitamin that plays a role in various physiological processes. As a laboratory product, ascorbic acid is used as a reducing agent, antioxidant, and pH regulator in various applications.
10
Hydroquinone by Thermo Fisher Scientific
Sourced in United States, Belgium
Hydroquinone is a chemical compound commonly used in various laboratory applications. It serves as a reducing agent, antioxidant, and developer in photographic processes. The core function of hydroquinone is to facilitate chemical reactions and processes within a controlled laboratory environment.

More about "Hydroquinone"

Hydroquinone, also known as 1,4-dihydroxybenzene or quinol, is a versatile phenolic compound with the chemical formula C6H6O2.
This organic compound has a wide range of applications, including its use as a reducing agent, antioxidant, and in the production of photographic developers.
Researchers have also explored the potential therapeutic benefits of hydroquinone, particularly in the treatment of skin conditions like hyperpigmentation.
One of the key challenges in hydroquinone research is ensuring the reproducibility and reliability of studies.
Researchers can leverage AI-powered tools like PubCompare.ai to streamline their hydroquinone-related investigations.
These innovative platforms allow researchers to locate and compare protocols from literature, preprints, and patents, helping them identify the best approaches and products for their research.
By utilizing PubCompare.ai, researchers can enhance the reproducibility and reliability of their hydroquinone studies.
The AI-driven comparisons provided by the platform can help researchers optimize their protocols, leading to more consistent and trustworthy results.
This is particularly important when exploring the therapeutic applications of hydroquinone, such as its use in the treatment of skin conditions.
In addition to hydroquinone, researchers may also work with related compounds and materials, such as bovine serum albumin, hydrochloric acid, silver nitrate, methanol, sodium hydroxide, the Wizard DNA Clean-Up System, sodium borohydride, and ascorbic acid.
By leveraging the insights and capabilities of PubCompare.ai, researchers can streamline their investigations and unlock new discoveries in the field of hydroquinone research.
Experience the future of hydroqunone research today with PubCompare.ai and unlock the full potential of this versatile compound.