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Ammonium peroxydisulfate

Ammonium peroxydisulfate is a chemical compound with the formula (NH4)2S2O8.
It is a strong oxidizing agent used in various applications, such as bleaching and disinfection.
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Most cited protocols related to «Ammonium peroxydisulfate»


ClustalW alignment In order to perform the alignment, amino acid sequences from different vertebrate species annotated as Bax isoform alpha [human (Q07812), rat (Q63690), mouse (Q07813), bovine (O022703)] or complete sequences having an equivalent start codon assignment [cat (Q8SQ43), dog (Q8HYUS), zebra fish (Q919N4)] as well as having only a short extension [xenopus (Q98U13)] were used. Sequences with N-terminal extensions or deletions within the sequence were excluded, e.g. the sequence from Pan troglodytes (chimpanzee), which shows only two differences in the part homologous to the human Bax alpha, but is elongated by 70 amino acids at the N-terminus.
Expression and purification of human Bax alpha We essentially followed the procedure described by Suzuki et al. (2000) (link). The purity of the protein was analyzed by SDS-PAGE and LC-MS (calculated mass: 21,184 Da; determined mass: 21,183 Da).
Bax reconstitution in liposomes Lipid mixtures from E. coli or bovine heart extracts (Avanti polar lipids Inc. Alabaster, AL) were dissolved in chloroform, dried by evaporation to form a thin film, and resuspended in buffer 1 (20 mM Tris-HCl, 100 mM NaCl; pH 7.5) by repeatedly vortexing, freezing and thawing. The final lipid concentration was 20 mg/ml. The solution was passed through a membrane with 200 or 400 nm pores (Avestin Inc. Ottawa, Canada) for at least 25 times. Bax pre-incubated with 0.1% DDM was mixed with the vesicles pre-incubated with 0.1% DDM to a final concentration of 0.25 mg/ml protein and 12 mg/ml lipid. Biobeads (BioRAD, Hercules, CA) were added to remove excess detergent. For protein insertion the solution was incubated for 3 h at 30 °C at 300 rpm. To remove free protein as well as aggregates, a nycodenz gradient was used. The gradient was layered as followed: the liposome/Bax solution in 10% nycodenz (dissolved in buffer 1) was overlaid with 5% nycodenz in buffer 1 and finally pure buffer 1. The gradient was spun at 200,000×g for 30 min at 10 °C. A pellet and a swimming lipid band (fuzzy when bovine heart lipids were used) were separated. The latter was mixed with buffer 1 and centrifuged under identical conditions to remove the nycodenz by sedimentation.
Secondary structure determination by circular-dichroism spectroscopy The concentration of Bax (in buffer 2; 20 mM Tris, pH 8.8) was adjusted to 0.1 mg/ml. The CD-spectra and melting curves were recorded on a Jasco J715 spectropolarimeter (Jasco, Gross Umstadt, Germany) with a Jasco PFD 350S Peltier type FDCD attachment for temperature control using a 0.1 mm quartz cuvette. Two spectra were accumulated per measurement using a data pitch of 0.1 nm, a scan speed of 20 nm s−1 and 1 nm slit width. The content of secondary structure was calculated using the program CDNN (Bohm et al. 1992 (link)). Notably, samples of Bax did not show any precipitation during the temperature increase which was tested by UV-spectroscopy. If buffer 1 was used instead of buffer 2, only neglectable differences were visible in the spectra.
Protease digestion Monomeric and oligomeric Bax samples were mixed with subtilisin or proteinase K at a stoichiometry of 1:200 and incubated for one hour on ice. The reaction was stopped either by (a) treatment with the denaturing SDS-gel loading buffer and subsequent boiling for 5 min or (b) freezing in liquid nitrogen and storage at −80 °C before further analysis. Protein samples were subjected to SDS-PAGE and blotted onto a PVDF membrane (transfer buffer: 25 mM Tris-HCl, 192 mM glycine, 20% methanol) for subsequent N-terminal sequencing of individual bands (using a gas-phase sequencer Procise 492cLC, Applied Biosystems, Foster City, CA). Sample mixtures were also analyzed by ESI-MS. After Bax reconstitution in liposomes, the protein concentration was estimated by the band intensity on a SDS-gel. Consequently, the estimation was less accurate than the estimation by UV spectroscopy. Furthermore, since ESI-MS did not work with Bax liposomes only N-terminal sequencing was performed.
Tryptophan fluorescence Fluorescence emission spectra were recorded on a Perkin-Elmer spectrometer (LS50B, Waltham MA). Bax (concentrations of 0.25 to 1 µM), and free acetylated-tryptophan (4 µM) were excited at 280 nm at a slit width of 5 nm to detect the emitted fluorescence in the range between 300 and 400 nm.
Cross-link experiments Protein samples were adjusted to a concentration of about 0.5 mg/ml in the presence or absence of 0.5% DDM. These samples were slowly heated to 50–90 °C and the temperature was kept constant for 600 s. Afterwards, the samples were immediately cooled on ice. 10 µl samples were mixed with 1 µl ammonium peroxydisulfate (APS, 25 mM) and 2 µl ruthenium (II) Tris-bipyridyldication (5 mM Sigma-Aldrich) in the dark and then immediately exposed to illumination with visible light (400 to 700 nm, generated by a Xenon lamp, 100 W Leica, filters: KG4, GG 395 nm). The photo-induced reaction was stopped by the addition of 5 µl SDS-gel loading buffer.
Miscellaneous To induce oligomerization, Bax was mixed with 0.5% DM (Anatrace), 0.5% DDM (Anatrace) or 2% OG (Anatrace) in buffer 1. The samples were incubated under shaking for at least 8 h at 4 °C. The oligomerization was analyzed by size exclusion chromatography on a Superdex 200 column using SMART FPLC (GE Healthcare). ESI-MS was performed on a micrOTOF LC (Bruker Daltonics, Billerica, MA). Absorption spectra were collected on a Shimadzu UV-1700 UV-visible spectrophotometer. Bax structure was illustrated with Pymol using the PDB file 1F16 of monomeric Bax (Suzuki et al. 2000 (link)). Data were plotted using origin 6.1.
Publication 2009
PANI synthesis was
adapted from a one-pot synthetic procedure reported by Li et al.25 (link) An ammonium peroxydisulfate precursor solution
was created by dissolving APS (0.799 mmol) in 10 mL of 1 M hydrochloric
acid. Aniline (306 mmol) was dissolved in a separate vial containing
10 mL of 1 M hydrochloric acid. The APS precursor solution was then
rapidly added to the aniline precursor solution. The vial was shaken
for approximately 30 s and then left undisturbed to polymerize for
24 h at room temperature. PANI was then centrifuged and washed three
times with 1 M HCl to remove excess APS.29
Publication 2020
ammonium peroxydisulfate Anabolism aniline Hydrochloric acid
The reagents used in this study were as follows: liposomes were purchased from Invitrogen (Carlsbad, CA, USA); glycine, lauryl sodium sulfate, tetramethylethylenediamine, TRIzol, and tris(hydroxymethyl)aminomethane were purchased from Amresco (Solon, OH, USA); acrylic amide was purchased from Merck (Darmstadt, Germany); bovine serum albumin (BSA) was purchased from Roche (Basel, Switzerland); fluorescent protein solutions were purchased from Pierce (Rockford, IL, USA); ammonium peroxydisulfate, dimethyl sulfoxide (DMSO), N, N’-methylenebisacrylamide, and puromycin were purchased from Sigma (St. Louis, MO, USA); trypsin, Dulbecco’s modified Eagle’s medium (DMEM) with high glucose, and fetal bovine serum were purchased from HyClone (Logan, UT, USA); PrimeSTAR DNA polymerase and T4 DNA ligase were purchased from TaKaRa (Tokyo, Japan); GAPDH, P62, CHK1, CHK2, MYTl, WEEl, CDC25, CDC25C, ATM, CDK1, LC3, p68-CHK1, p216-CDC25C, p15-CDK1, p1981-ATM, SQSTM1/P62, pCHK2, pCHK1, CDC, pCDC25C, and MPM2 antibodies were purchased from Santa Cruz Biotechnology (Dallas, TX, USA), Cell Signaling Technology (Danvers, MA, USA), or Millipore/Upstate(NY, USA); and the pLKO.1 plasmid was purchased from Sigma (Darmstadt, Germany).
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Publication 2020
Amides ammonium peroxydisulfate Antibodies CDC25C protein, human CDK1 protein, human DNA-Directed DNA Polymerase dodecyl sulfate Eagle Fetal Bovine Serum GAPDH protein, human Glucose Glycine Liposomes methylamine N,N'-methylenebisacrylamide Plasmids Proteins Puromycin RASGRF1 protein, human Serum Albumin, Bovine Sodium sodium sulfate Solon Sulfoxide, Dimethyl T4 DNA Ligase tetramethylethylenediamine trizol Tromethamine Trypsin
Approximately, 10 ng of template DNA was added to a 10-µL PCR mix containing 1×PCR buffer with MgCl2 (Perkin-Elmer), 250 µM dNTPs, 0.2 µM primers (forward and reverse), and 0.5 units of TaqGold DNA Polymerase (Perkin-Elmer). The PCR reaction profile comprised a 10-min incubation at 94°C, then a cycle of 94°C for 30 s, 50–60°C for 30 s and 72°C for 40 s, repeated 35 times. Following cycling, the reaction was held at 72°C for 10 min, before a final 4°C hold. The entire reaction is carried out in the BioRAD S1000 Thermal cycler. The PCR product quality was checked in a 1.0% agarose gel, using 3 µL of the PCR reaction and the remaining reaction was then subjected to electrophoresis on a 8% polyacrylamide gel, consisting of 30% PA (acrylamide+N, N-methylene bisacrylamide, Biosharp) 12 mL, 10×TBE 4 mL, TEMED 50 µL, 10% APS (ammonium peroxydisulfate, Biosharp) 950 µL, and ddH2O to a total volume of 45 mL. Electrophoresis was carried out in 1×TBE buffer at 220 U for 90 min. Gels were stained with 0.1% silver nitrate following a chromogenic reaction with 1.5% NaOH (including 1% formaldehyde), and finally photographed in white light. We screened 24 typical cannabis varieties to assess the usefulness of the SSR primer pairs developed in this study.
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Publication 2014
Acrylamide ammonium peroxydisulfate ARID1A protein, human azo rubin S Buffers Cannabis DNA-Directed DNA Polymerase Electrophoresis Formaldehyde Gels Light Magnesium Chloride N,N'-methylenebisacrylamide Oligonucleotide Primers polyacrylamide gels Sepharose Tris-borate-EDTA buffer
Western blotting was conducted basically as reported15. Cells cultured in 6-well plates were washed twice with 2 mL iced-cold PBS, lysed by adding 100–200 μL of ice-cold lysis buffer [50 mM Tris-HCl (pH7.5) 150 mM NaCl, 1% Triton X-100] containing complete protease inhibitor cocktail (11873580001, Roche) and placed on ice for 20 min. Cell extracts were sedimented by centrifugation at 20,400 g for 10 min at 4°C. Protein concentration of supernatants was measured using the Protein Assay Bicinchoninate kit (06385–00, Sigma-Aldrich). Supernatants were mixed with 100–200 μL of sample buffer (2% SDS, 100 mM DTT, 50 mM Tris-HCl [pH 6.8], 5% glycerol, 0.001% bromophenol blue), incubated at 98°C for 5 min, and separated by SDS-PAGE. LC3 protein was detected using 15% polyacrylamide SDS-PAGE gels, which were made using the following regents: H2O 1.4 mL, 1.5 M Tris-HCl (pH 8.8) 1.5 mL, 30% acrylamide/bis-acrylamide 3 mL, 10% SDS 60 μL, 10% ammonium peroxydisulfate: (APS) 50 μL, tetramethyl ethylenediamine: (TEMED) 5 μL. Stacking gel was prepared using the following reagents: H2O 1.8 mL, 0.5 M Tris-HCl (pH 6.8) 750 μL, 30% acrylamide/bis-acrylamide 375 μL, 10% SDS 30 μL, 10% APS 30 μL, TEMED 5 μL). TFEB, S6K and 4EBP1 proteins detected using 10% polyacrylamide SDS-PAGE gels, which were made using the following reagents: H2O 2.4 mL, 1.5 M Tris-HCl (pH 8.8), 1.5 mL, 30% acrylamide/bis-acrylamide 2 mL, 10% SDS 60 μL, 10% APS 50 μL, TEMED 5 μL. ULK1 protein detected using 7.5% polyacrylamide SDS-PAGE gels, which were made using the following regents: H2O 2.9 mL, 1.5 M Tris-HCl (pH 8.8) 1.5 mL, 30% acrylamide/bis-acrylamide 1.5 mL, 10% SDS 60 μL, 10% APS 50 μL, TEMED 5 μL. The separated proteins were transferred to PVDF membranes (LC3: Immobilon-P, Merck Millipore; ULK1, TFEB, S6K, and 4EBP1: Hybond-P, Amersham) using transfer buffer (24 mM Tris base, 190 mM glycine, 20% methanol) by the wet transfer system (NA-1510B S/N 15J01, EIDO) at 150 mA for 1 hour. The membranes were blocked for 1 hour at room temperature in 1.0% skim milk in TBS-T (25 mM Tris base, 137 mM NaCl, 2.7 mM KCl, 0.16% HCl, 0.08% Tween 20, pH adjusted to 7.4). For phosphorylated proteins, 2.5% bovine serum albumin (A7906-50G, Sigma-Aldrich) in TBS-T was used as the blocking buffer. After blocking, the membrane was incubated for 1 hour with each primary antibody in blocking buffer at room temperature. The membrane was washed three times with TBS-T for 10 min and incubated at room temperature for 40 min with HRP-conjugated secondary antibody in blocking buffer, and then washed three times with TBS-T for 10 min. The membrane was incubated in the ECL Select western blotting detection reagent (GE Healthcare) for 5 min at room temperature. Signals were detected on a Gene Gnome-5 chemiluminescence detector (Syngene).
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Publication 2020

Most recents protocols related to «Ammonium peroxydisulfate»

TC (0.005 mmol, 2.5 mg), catalyst (15 mg), and H2O (50 mL) were poured into an Erlenmeyer flask and stirred for 3 min, and then ammonium peroxydisulfate (1 mmol, 240 mg) was added to the mixture. Again, the course of the reaction was monitored every 10 min through UV–Visible spectroscopy.
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Publication 2024
Six pooled saliva samples from different participants were used for testing analytical recovery by adding 10, 20, 40 and 120 µL of intermediate standard with iodine concentration of 1000 µg/L to 500 µL of saliva sample before the digestion step. Samples were measured 8 times and recovery was expressed as the percentage of the measured amount of iodine over the expected amount of iodine.
Three pooled saliva samples from different participants were tested for the potential influence of the molarity of ammonium peroxydisulfate to the final result. For UIC determination, 1 mL of 1.0 mol/L of ammonium peroxydisulfate was used, therefore we tested the same volume of ammonium peroxydisulfate with different concentrations, below and above proposed concentration: 1 mL of 0.5 mol/L, 1.0 mol/L, and 1.5 mol/L. Linearity of the method was tested using 4 saliva samples, each measured 8 times, in the range up to 165 µg/L. Higher concentrations were not available for linearity testing. Distilled water was used as diluent in ratios of 1:2, 1:4, 1:8, and 1:16. Test was considered as linear, if the recovery was in the range of 80-120%.
The interferences of some potential substances such as thiocyanate and caffeine in the introduced method were tested by adding 19.6, 38.5, 74.1, and 193.5 mg/L of both, potassium thiocyanate and caffeine, to 6 saliva samples. Samples were measured 8 times and results are reported as recoveries expressed as the percentage of the measured over expected amount of iodine. The result was considered as no influences of interferences, if the recovery was in the range of 80-120%.
Limit of blank (LoB) and limit of detection (LoD) of the method were determined. Eighty-eight measurements for LoB from 8 samples on two microplates using two different standard curves were analysed. To test LoB, dH 2 O was used. An F-test was used to compare values of measurements between both microplates. For LoD 180 measurements from 12 samples were analysed on five microplates using five different standard curves. LoD samples were in the concentration range between LoB and 4times LoB value.
For intra-and inter-assay precision, two different types of samples were prepared. Intra-assay precision was assessed on one microplate where 40 replicates were measured, whereas inter-assay precision was measured on 15 microplates, where at least 5 replicates on each microplate were measured. Reproducibility was assessed by using 4 samples, 3 of which were prepared in water solution at concentration levels 20, 100, and 350 µg/L to cover the range of the assay standard curve, and one was prepared as pooled saliva sample, which was pooled from random saliva samples and final concentration was 165 µg/L. Precisions were measured as coefficients of variation (CV (%)). Procedure of the method All reagents reached room temperature and were gently mixed before use. To 250 µL of standards, CSs, and samples, 1 mL of 1 mol/L ammonium peroxydisulfate solution was added. Oxidation of all samples, including standards and CSs, was performed manually in 13 × 100 mm glass tubes. Solution was then mixed and incubated for 1 h on 95°C on dry bath (ScientificTM IsotempTM Digital Dry Bath/Block Heater, Fisher Scientific, UK). After cooling down to room temperature, 50 µL of standards, CSs, and samples were transferred in duplicate to microplate (Nunc Multiwell plate -96 well solid flat bottom, Merck, Germany). To each well 100 µL of arsorous acid solution was added. Microplate was sealed and incubated for 60 s on a microplate shaker. Afterwards 50 µL of ammonium cerium(IV) sulfate solution was added to each well within 40 s with an 8-channel semi-automatic pipette. Microplate was sealed and put on the microplate shaker for exactly 30 min. Immediately after shaking, an absorbance measurement at 405 nm on a spectrophotometer (SunriseTM, Tecan, Switzerland) was performed. The results were calculated by plotting the linear optical density (OD) data on Y-axis and linear iodide ion concentration on X-axis. Concentration was inversely proportional to absorbance. Standard curves were developed for each microplate separately. A quadratic polynomial was used to calculate concentration from OD.
Publication 2024
Prior to laser processing, electronic
grade single-crystal diamond samples (Chenguang Machinery & Electric
Equipment Co. Ltd., China, 4 × 4 × 0.5 mm) were cleaned
using the process described in Baral et al.49 (link) Briefly, substrates were submerged in a saturated solution of sulfuric
acid and ammonium peroxydisulfate at 200 °C for 20 min, followed
by a rinse solution of hydrogen peroxide and ammonium hydroxide (1:1)
for 10 min. This process works both to remove any surface contaminants
and to etch any sp2 carbon species present on the substrate
surface. To check for reproducibility, several tracks were drawn on
the same substrate under the conditions described below, and subsequently,
the measurements were repeated on other single-crystal diamond substrates
following this type of laser processing. At all times, the observations
were repeatable. Further, repeat measurements made about one year
later on the original laser-processed material showed no change in IV measurements, indicating the
long-term stability of the electrical properties reported here.
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Publication 2024
Not available on PMC !
The coupling assays were performed based on the methods described by Davin et al. (1997) (link) and Zheng et al. (2011) (link). The reaction mixture consisted of coniferyl alcohol (10 μmol/mL), ammonium peroxydisulfate (2 μmol/ mL), and ScDIR proteins (1.5 nmol/mL). After incubation for 3 h at 30°C, the mixture was extracted three times with ethyl acetate. The extract was evaporated to dryness under vacuum, and the residue was redissolved in 50% methanol. A high-performance liquid chromatography (HPLC) analysis of each extract was performed under the following conditions: column temperature, 25°C; flow rate, 1.0 mL/min; chromatogram, 280 nm (Zheng et al., 2011) (link). HPLC analysis was performed on a Waters e2695 system (Milford, MA, USA) equipped with a Symmetry300 ™ C18 column (250 mm × 4.6 mm, 5 μm i.d., Ireland).
Publication 2024
Chemicals: potassium iodate(V) (KIO 3 ) (Sigma-Aldrich, Germany), ammonium peroxydisulfate ((NH 4 ) 2 S 2 O 8 ) (Sigma-Aldrich, Germany), deionized water (dH 2 O) (BRAUN, Aqua B. Braun, Sterile, Ecotainer®, Germany), sodium hydroxide (NaOH) (Merck, Germany), arsenic(III) oxide (As 2 O 3 ) (Sigma-Aldrich, Germany), sodium chloride (NaCl) (Sigma-Aldrich, Germany), concentrated sulfuric(VI) acid (H 2 SO 4 ) (Sigma-Aldrich, Germany), ammonium cerium(IV) sulfate dihydrate ((NH 4 ) 4 Ce(SO 4 ) 4 ×2H 2 O) (Sigma-Aldrich, Germany), 65% nitric(V) acid (HNO 3 ) (Honeywell, USA).
All laboratory equipment was treated with 65% nitric(V) acid before preparation of reagents to remove any additional iodine from environment. Preparation of reagents as well as digestion processes and analyses took place in a ventilating fume hood. Reagents were prepared in volumetric flasks. Brief summary of preparation: 1 mol/L ammonium peroxydisulfate solution: dissolution of 228.2 g of (NH 4 ) 2 S 2 O 8 in 1 L of dH 2 O, 0.875 mol/L sodium hydroxide solution: dissolution of 8.75 g of NaOH in 0.25 L of dH 2 O, 0.05 mol/L arsorous acid (H 3 AsO 3 ) solution: dissolution of 5 g of As 2 O 3 in 0.1 L of 0.875 mol/L NaOH on magnetic stirrer. Afterwards, the solution was put in an ice-cold bath and 16 mL of concentrated H 2 SO 4 was added while stirring on magnetic stirrer. After cooling, 12.5 g of NaCl was added and diluted with dH 2 O up to 0.5 L. Solution was then mixed for 90 min at 60°C. Afterwards the solution was filtrated, 1.75 mol/L sulfuric acid solution: on an ice bath 97 mL of concentrated H 2 SO 4 was slowly added to 0.5 L of dH 2 O and filled with dH 2 O up to 1 L, 0.019 mol/L ammonium cerium(IV) sulfate solution: dissolution of 6 g of (NH 4 ) 4 Ce(SO 4 ) 4 ×2H 2 O in 0.5 L of 1.75 mol/L H 2 SO 4 .
All reagents were stored in amber bottles in the dark at room temperature except for ammonium peroxydisulfate solution, which was stored in the dark at 2-8°C.
We followed all Clinical Laboratory Standard Institute (CLSI) protocols for method establishment, namely EP06, EP07, EP09, EP15-A3, EP17-A2.
Preparation of standards 1.68 g of KIO 3 was dissolved in 1 L of dH 2 O. The solution was then used for preparation of intermediate standard with iodine concentration of 1000 µg/L, which was used later for preparation of standards and control samples (CSs).
Standards were prepared with two different matrices, i.e. as artificial saliva to retain properties comparable to real saliva and as a water solution of iodine, which is used in UIC determination, in order to test appropriateness of matrix for standard curve.
Artificial saliva was prepared according to commercially available products that are available for patients after head and neck cancer treatment for moistening mouth and throat. Ingredients used for the preparation of a 100 mL of artificial saliva were 30.45 mg/mL of sorbitol, 10.15 mg/mL of sodium carboxymethylcellulose, 1.218 mg/mL of potassium chloride, 0.856 mg/mL of sodium chloride, 0.348 mg/mL of potassium hydrogen phosphate, 0.148 mg/mL of calcium chloride dihydrate, 0.052 mg/mL of magnesium chloride hexahydrate, and water for injections as solution with pH set at 7.0. Cellulose was added for adjusting viscosity of matrix retaining properties comparable to real saliva.
Both standards and CSs were prepared and stored according to previously published method for UIC determination. 12 Briefly, 6 working standards were prepared at concentrations of iodide: 0, 40, 80, 120, 200, and 400 µg/L. For comparison, both standards were measured on six microplates with S-K reaction. Each standard was measured in 6 replicates on each microplate and the mean concentration was calculated, whereas standards in artificial saliva were also analysed by ICP-MS. CSs were prepared at two different levels: 160 and 280 µg/L.
Publication 2024

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Ammonium peroxydisulfate is a chemical compound with the formula (NH4)2S2O8. It is a white crystalline solid that is commonly used as an oxidizing agent, initiator, and catalyst in various industrial and laboratory applications.
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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.
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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.
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Aniline is a chemical compound that serves as a raw material for the production of various other chemicals and materials. It is a colorless to pale-yellow liquid with a distinctive, unpleasant odor. Aniline is used as a precursor in the synthesis of a wide range of other organic compounds, including dyes, pesticides, and pharmaceuticals.
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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.
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Potassium peroxydisulfate is an inorganic chemical compound with the formula K2S2O8. It is a white crystalline solid that is commonly used as an oxidizing agent in various industrial and laboratory applications.
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Ethanol is a clear, colorless liquid chemical compound commonly used in laboratory settings. It is a key component in various scientific applications, serving as a solvent, disinfectant, and fuel source. Ethanol has a molecular formula of C2H6O and a range of industrial and research uses.
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Ammonium peroxydisulfate is a commonly used laboratory chemical. It functions as an oxidizing agent and is utilized in various chemical processes and analyses.
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Pyrrole is a heterocyclic organic compound with the chemical formula C₄H₅N. It is a colorless liquid with a slightly unpleasant odor. Pyrrole is a key building block in the synthesis of various organic compounds, including pharmaceuticals, agrochemicals, and materials science applications.
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NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.

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