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Sodium Acetate
Sodium Acetate
Sodium acetate, a salt of acetic acid, is a widely used chemical in various scientific and industrial applications.
It serves as a buffering agent, preservative, and pH regulator in numerous experimental protocols.
PubCompare.ai's AI-driven platform can help researchers optimize their work with sodium acetate by providing access to the best published protocols, pre-prints, and patent information.
Users can locate reliable products and enhance the reproducibility of their experiments, streamlining the research process and improving their overall results.
It serves as a buffering agent, preservative, and pH regulator in numerous experimental protocols.
PubCompare.ai's AI-driven platform can help researchers optimize their work with sodium acetate by providing access to the best published protocols, pre-prints, and patent information.
Users can locate reliable products and enhance the reproducibility of their experiments, streamlining the research process and improving their overall results.
Most cited protocols related to «Sodium Acetate»
1,2-dihexadecyl-sn-glycero-3-phosphocholine
Alabaster
austin
Brain Stem
Buffers
Cells
Cerebellum
Chloroform
Cholinergic Agents
Cold Temperature
Cycloheximide
Deoxyribonucleases
Digestion
Dithiothreitol
Endoribonucleases
Ethanol
G-substrate
Goat
HEPES
inhibitors
Isopropyl Alcohol
Lipids
Magnesium Chloride
Mice, Laboratory
Mice, Transgenic
Motor Neurons
Nonidet P-40
Polyribosomes
Protease Inhibitors
Purkinje Cells
Ribosomal RNA
RNA, Messenger
Sodium Acetate
Sodium Chloride
Striatum, Corpus
Teflon
Tissues
trizol
2',5'-oligoadenylate
Cells
Codon
Deoxyribonuclease I
Ethanol
Lanugo
Neoplasm Metastasis
Oligonucleotide Primers
Oligonucleotides
Plasmids
Poly A
Proteins
RNA, Messenger
Simian virus 40
Sodium Acetate
Tail
Transcription, Genetic
Zebrafish
One hour after infecting the cell monolayers with 30–50 plaque forming units of the virus in 1 ml of maintenance medium without trypsin, we removed the virus inoculum, covered the cells with 3 ml of the different overlay media and incubated cultures at 35°C in 5% CO2 atmosphere. In the case of MC and Avicel overlays, care was taken not to disturb the plates during the incubation period in order to avoid formation of non-even plaques. After three days of incubation, we removed the overlays and fixed the cells. Agar overlay was removed using metal spatula; MC, Avicel, and liquid overlays were removed by suction. The cells were fixed with 4% paraformaldehyde solution in MEM for 30 min at 4°C and washed with PBS. All subsequent treatments of the cells were performed at room temperature. We permeabilized the cells and simultaneously blocked residual aldehyde groups by incubating the cells for 10–20 min with 1 ml/well of solution containing 0.5 % Triton-X-100 and 20 mM glycine in PBS. We immuno-stained virus-infected cells by incubating for 1 hr with monoclonal antibodies specific for the influenza A virus nucleoprotein (kindly provided by Dr. Alexander Klimov at Centers for Disease Control, USA) followed by 1 hr incubation with peroxidase-labeled anti-mouse antibodies (DAKO, Denmark) and 30 min incubation with precipitate-forming peroxidase substrates. Solution of 10% normal horse serum and 0.05% Tween-80 in PBS was used for the preparation of working dilutions of immuno-reagents. We washed the cells after the primary and secondary antibodies by incubating them three times for 3–5 min with 0.05% Tween-80 in PBS. As peroxidase substrates, we employed either ready to use True Blue™ (KPL) or solution of aminoethylcarbazole (AEC, Sigma) (0.4 mg/ml) prepared in 0.05 M sodium acetate buffer, pH 5.5 and containing 0.03% H2O2. Stained plates were washed with tap water to stop the reaction and dried. In the case of True Blue staining, which is relatively unstable in water solutions, plates were dried inverted in order to minimize bleaching. Stained plates were scanned on a flat bed scanner and the data were acquired by Adobe Photoshop 7.0 software.
As an alternative to immuno-staining, in some experiments we revealed plaques as areas of destroyed cells. To this end, after removing the overlays, we stained the cells with 1% crystal violet solution in 20% methanol in water.
As an alternative to immuno-staining, in some experiments we revealed plaques as areas of destroyed cells. To this end, after removing the overlays, we stained the cells with 1% crystal violet solution in 20% methanol in water.
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Agar
Aldehydes
Anti-Antibodies
Antibodies
Atmosphere
Avicel
Buffers
Dental Plaque
Equus caballus
Glycine
Metals
Methanol
Monoclonal Antibodies
Mus
NP protein, Influenza A virus
paraform
Peroxidase
Peroxide, Hydrogen
Senile Plaques
Serum
Sodium Acetate
Suction Drainage
Technique, Dilution
Triton X-100
true blue
Trypsin
Tween 80
Violet, Gentian
Virus
sgRNA DNA template was generated by fill in PCR (Supplementary Fig. 1c and d ). Briefly, a 52 nt oligo (sgRNA primer), containing the T7 promoter (Supplementary Table 1 #1), the 20 nt of the specific sgRNA DNA binding sequence and a constant 15 nt tail for annealing, was used in combination with a 80 nt reverse oligo to add the sgRNA invariable 3′ end (tail primer). A 117 bp PCR product was generated following these parameters: 3 minutes at 95°C, 30 cycles of 30 seconds at 95°C, 30 seconds at 45°C and 30 seconds at 72°C, and a final step at 72°C for seven minutes. PCR products were purified using Qiaquick (Qiagen) columns and approximately 120–150 ng of DNA were used as template for a T7 In vitro transcription (IVT) reaction (AmpliScribe-T7-Flash transcription kit from Epicentre) (Supplementary Fig. 1c ). In vitro transcribed sgRNAs were DNAse treated and precipitated with Sodium Acetate/Ethanol. Alternative sgRNAs were generated similarly using shorter (50 or 51 nt) and longer (53 or 54nt) sgRNA primers, with 18–22nt complementary to the target. SgRNAs beginning with GA sequences contained the SP6 promoter (Supplementary Table 1 #2) instead of the T7 promoter. A MAXIscript SP6 transcription Kit (Life technologies) was used for SP6 based IVT reactions.
Zebrafish codon-optimized protein from pT3TS-nCas9n (#2656)37 (link) was used in all experiments except for the pull down, where FLAG-Cas9 was employed. A N-terminal 3xFLAG-tag was cloned in pT3TS-nCas9n in the NcoI site. The resulting pT3TS-FLAG-nCas9n (#2722) plasmid is identical to one previously used for a similar experiment in cell lines4 (link), 12 (link). For the cas9-nanos 3′-UTR construct, the nanos 3′-UTR and SV40 late polyA signal was PCR amplified from a previous plasmid pCS2+GFP-nanos 3′UTR18 (link), 19 (link) using two oligos (Supplementary Table 1 #3 #4). The following PCR product was then digested in 3′ with NotI and ligated into the pCS2-nCas9n 37 (link) plasmid previously digested with SnaBI and NotI. The final pCS2-nCas9n-nanos 3′UTR (#2662) (addgene #62542) construct was confirmed by sequencing. Cas9 mRNA was in vitro transcribed from DNA linearized by either NotI (pCS2-nCas9n-nanos 3′UTR) or XbaI (pT3TS-nCas9n and pT3TS-FLAG-nCas9n) using the mMachine SP6 or T3 kit (Ambion), respectively. In vitro transcribed mRNAs were DNAse treated and purified using RNeasy Mini Kit (Qiagen).
Zebrafish codon-optimized protein from pT3TS-nCas9n (#2656)37 (link) was used in all experiments except for the pull down, where FLAG-Cas9 was employed. A N-terminal 3xFLAG-tag was cloned in pT3TS-nCas9n in the NcoI site. The resulting pT3TS-FLAG-nCas9n (#2722) plasmid is identical to one previously used for a similar experiment in cell lines4 (link), 12 (link). For the cas9-nanos 3′-UTR construct, the nanos 3′-UTR and SV40 late polyA signal was PCR amplified from a previous plasmid pCS2+GFP-nanos 3′UTR18 (link), 19 (link) using two oligos (
2',5'-oligoadenylate
Cells
Codon
Deoxyribonuclease I
Ethanol
Lanugo
Neoplasm Metastasis
Oligonucleotide Primers
Oligonucleotides
Plasmids
Poly A
Proteins
RNA, Messenger
Simian virus 40
Sodium Acetate
Tail
Transcription, Genetic
Zebrafish
Sequence tag preparation was done with Illumina's Digital Gene Expression Tag Profiling Kit according to the manufacturer's protocol (version 2.1B). A schematic overview of the procedure is given in Supplementary Figure 1 . One microgram of total RNA was incubated with oligo-dT beads to capture the polyadenlyated RNA fraction. First- and second-strand cDNA synthesis were performed while the RNA was bound to the beads. While on the beads, samples were digested with NlaIII to retain a cDNA fragment from the most 3′ CATG to the poly(A)-tail. Subsequently, the GEX adapter 1 was ligated to the free 5′ end of the RNA, and a digestion with MmeI was performed, which cuts 17 bp downstream of the CATG site. At this point, the fragments detach from the beads. After dephosphorylation and phenol extraction, the GEX adapter 2 was ligated to the 3′ end of the tag. A PCR amplifcation with 15 cycles using Phusion polymerase (Finnzymes) was performed with primers complementary to the adapter sequences to enrich the samples for the desired fragments. The resulting fragments of 85 bp were purified by excision from a 6% polyacrylamide TBE gel. The DNA was eluted from the gel debris with 1× NEBuffer 2 by gentle rotation for 2 h at room temperature. Gel debris were removed using Spin-X Cellulose Acetate Filter (2 ml, 0.45 µm) and the DNA was precipitated by adding 10 µl of 3 M sodium acetate (pH 5.2) and 325 µl of ethanol (–20°C), followed by centrifugation at 14 000 r.p.m. for 20 min. After washing the pellet with 70% ethanol, the DNA was resuspended in 10 µl of 10 mM Tris–HCl, pH8.5 and quantified the DNA with a Nanodrop 1000 spectrophotometer.
acetylcellulose
Anabolism
Centrifugation
DNA, Complementary
Ethanol
Fingers
oligo (dT)
Oligonucleotide Primers
Pepsin A
Phenols
Poly(A) Tail
polyacrylamide gels
Sodium Acetate
Strains
Tromethamine
Most recents protocols related to «Sodium Acetate»
Example 1
Cell-free fractions were prepared as previously described (25). Briefly, Lactobacillus acidophilus strain La-5 was grown overnight in modified DeMann, Rogosa and Sharpe medium. (mMRS; 10 g peptone from casein, 8 g meat extract, 4 g yeast extract, 8 g D(+)-glucose, 2 g dipotassium hydrogen phosphate, 2 g di-ammonium hydrogen citrate, 5 g sodium acetate, 0.2 g magnesium sulfate, 0.04 g manganese sulfate in 1 L distilled water) (MRS; BD Diagnostic Systems, Sparks, MD). The overnight culture was diluted 1:100 in fresh medium. When the culture grew to an optical density at 600 nm (OD600) of 1.6 (1.2×108 cells/ml), the cells were harvested by centrifugation at 6,000×g for 10 min at 4° C. The supernatant was sterilized by filtering through a 0.2-μm-pore-size filter (Millipore, Bioscience Division, Mississauga, ON, Canada) and will be referred to as cell-free spent medium (CFSM). Two litres of L. acidophilus La-5 CFSM was collected and freeze-dried (Unitop 600 SL, VirTis Co., Inc. Gardiner, NY., USA). The freeze-dried CFSM was reconstituted with 200 ml of 18-Ω water. The total protein content of the reconstituted CFSM was quantified using the BioRad DC protein assay kit II (Bio-Rad Laboratories Ltd., Mississauga, ON, Canada). Freeze-dried CFSM was stored at −20° C. prior to the assays.
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ammonium citrate
Biological Assay
casein peptone
Cells
Centrifugation
Diagnosis
Freezing
Glucose
Hydrogen
Lactobacillus acidophilus
L Cells
manganese sulfate
Meat
potassium phosphate, dibasic
Proteins
Sodium Acetate
Sulfate, Magnesium
Unitop
Yeast, Dried
Example 125
Methyl 4-((5-(benzyloxy)-2-methoxyphenyl)(ethyl)amino)butanoate (184). 5-(Benzyloxy)-N-ethyl-2-methoxyaniline (146) (0.681 g, 2.65 mmol), DIEA (0.92 mL, 5.3 mmol), and methyl 4-iodobutyrate (0.72 mL, 5.3 mmol) in DMF (5 mL) were stirred at 70° C. for 5 days. The reaction mixture was cooled to rt, diluted with EtOAc (60 mL), washed with water (4×50 mL), brine (75 mL), dried over Na2SO4 and evaporated. The residue was purified by chromatography on a silica gel column (2.5×30 cm bed, packed with CHCl3), eluant: 5% MeOH in CHCl3 to get compound 184 (0.72 g, 76%) as a dark amber oil.
Methyl 4-(ethyl(5-hydroxy-2-methoxyphenyl)amino)butanoate (186). Ester 184 (0.72 g, 2.0 mmol) was stirred under reflux with 6 mL of water and 6 mL of conc HCl for 1.5 hrs and then evaporated to dryness to give acid 185 as a brown gum. The crude acid was dissolved in 50 mL of methanol containing 1 drop (cat.) of methanesulfonic acid ant the solution was kept for 2 hrs at rt. After that the mixture was concentrated in vacuum and the residue was mixed with 20 mL of saturated NaHCO3. The product was extracted with EtOAc (3×40 mL). The extract was washed with brine (40 mL), dried over Na2SO4 and evaporated. The residue was purified by chromatography on a silica gel column (2.5×30 cm bed, packed with CHCl3), eluant: 5% MeOH in CHCl3 to get compound 186 (0.444 g, 83%) as a brown oil.
N-(6-(dimethylamino)-9-(4-(ethyl(4-methoxy-4-oxobutyl)amino)-2-hydroxy-5-methoxyphenyl)-3H-xanthen-3-ylidene)-N-methylmethanaminium chloride (187). To a stirred suspension of tetramethylrhodamine ketone 101 (0.234 g, 0.830 mmol) in 10 mL of dry chloroform was added oxalyl chloride (72 μL, 0.82 mmol) upon cooling to 0-5° C. The resulting red solution was stirred for 0.5 h at 5° C., and the solution of compound 186 (0.222 g, 0.831 mmol) in dry chloroform (5 mL) was introduced. The reaction was allowed to heat to rt, stirred for 72 h, diluted with CHCl3 (100 mL and washed with sat. NaHCO3 solution (2×30 mL) The organic layer was extracted with 5% HCl (3×25 mL). The combined acid extract was washed with CHCl3 (2×15 mL; discarded), saturated with sodium acetate and extracted with CHCl3 (5×30 mL). The extract was washed with brine (50 mL), dried over Na2SO4 and evaporated. The crude product was purified by chromatography on silica gel column (2×50 cm bed, packed with CHCl3/MeOH/AcOH/H2O (100:20:5:1)), eluant: CHCl3/MeOH/AcOH/H2O (100:20:5:1) to give the product 187 (0.138 g, 29%) as a purple solid.
4-((4-(6-(dimethylamino)-3-(dimethyliminio)-3H-xanthen-9-yl)-5-hydroxy-2-methoxyphenyl)(ethyl)amino)butanoate (188). Methyl ester 187 (0.136 g, 0.240 mmol) was dissolved in 5 mL of 1M KOH (5 mmol). The reaction mixture was kept at rt for 1.5 hrs and the acetic acid (1 mL) was added. The mixture was extracted with CHCl3 (4×30 mL), and combined extract was washed with brine (20 mL), filtered through the paper filter and. The crude product was purified by chromatography on silica gel column (2×50 cm bed, packed with MeCN/H2O (4:1)), eluant: MeCN/H2O/AcOH/(4:1:1) to give the product 188 (0.069 g, 98%) as a purple solid.
N-(6-(dimethylamino)-9-(4-((4-(2,5-dioxopyrrolidin-1-yloxy)-4-oxobutyl)(ethyl)amino)-2-hydroxy-5-methoxyphenyl)-3H-xanthen-3-ylidene)-N-methylmethanaminium chloride (189). To a solution of the acid 188 (69 mg, 0.12 mmol) in DMF (2 mL) and DIEA (58 μL, 0.33 mmol) was added N-hydroxysuccinimide trifluoroacetate (70 mg, 0.33 mmol). The reaction mixture was stirred for 30 min, diluted with chloroform (100 mL) and washed with water (5×50 mL), brine (50 mL), filtered through paper and concentrated in vacuum. The crude product was purified by precipitation from CHCl3 solution (5 mL) with ether (20 mL) to give compound 189 (55 mg, 67%) as a purple powder.
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Acetic Acid
Acids
Amber
Anabolism
Bicarbonate, Sodium
brine
Chlorides
Chloroform
Chromatography
Esters
Ethyl Ether
Hydroxyl Radical
Ketones
methanesulfonic acid
Methanol
N,N-diisopropylethylamine
N-hydroxysuccinimide
oxalyl chloride
Powder
Silica Gel
Sodium Acetate
tetramethylrhodamine
Trifluoroacetate
Vacuum
Example 6
The effect of direct plasma treatment time [min] with a distance of 2 mm on the activity of immobilized UPO (40 μL of 1 μM immobilized protein solution, over 60 min) is demonstrated in
The effect of enzyme immobilization and/or direct plasma treatment in comparison to free enzyme and/or samples without direct plasma treatment on the specific enzyme activity of UPO is illustrated in
Activity assay parameters: 5 nM UPO; 2.5 mM ABTS in 50 mM sodium acetate buffer, pH 5.5; 1 mM H2O2. Activity was calculated from linear slope in the absorption measurement.
In samples which were directly plasma-treated, the substrate conversion was determined by adding commercially available H2O2 to the sample after direct plasma treatment. The substrate used for the respective assay was added after direct plasma treatment.
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2-(4'-diethylaminophenyl)benzothiazole
Biocatalysis
Biological Assay
Buffers
enzyme activity
Enzymes
Immobilization
Peroxide, Hydrogen
Plasma
Proteins
Sodium Acetate
Specimen Handling
Example 101
Compound 104. To a stirred suspension of ketone 101 (94 mg, 0.333 mmol) in dry chloroform (10 mL), oxalyl chloride (30 μL, 0.33 mmol) was added upon cooling to 0-5° C. The resulted red solution was stirred for 1 h, then N,N-diethyl-m-anisidine (60 mg, 0.33 mmol) was added. The reaction was allowed to warm to rt, stirred for 16 h and diluted with CHCl3 (60 mL). Chloroform solution was shaken with sat. NaHCO3 (40 mL) until water layer turned almost colorless. The organic layer was washed with sat. NaHCO3 (20 mL) and extracted with 10% HCl (2×30 mL). The combined acid extract was washed with CHCl3 (2×15 mL; discarded), the aqueous solution was saturated with sodium acetate and extracted with CHCl3 (4×30 mL). The extract was washed with brine (30 mL), and evaporated. The crude product was purified by chromatography on silica gel column (2×40 cm bed, packed with 10% MeOH and 1% AcOH in CHCl3) eluant: 10% MeOH and 1% AcOH in CHCl3 to give the product 104 (3 mg, 2%) as a purple wax.
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3-anisidine
Acids
Anabolism
Bicarbonate, Sodium
brine
Chloroform
Chromatography
Ketones
oxalyl chloride
Silica Gel
Sodium Acetate
Example 8
This example provides an alternative in vitro activity assay for SGSH-Fc fusion proteins. The assay is adapted from Karpova et al., J. Inherit. Metab. Dis., 19:278-285 (1996).
The standard reaction mixtures consisted of 10-15 μg of protein and 20 μL MU-α-GlcNS (5 or 10 mmol/L, respectively) in Michaelis' barbital sodium acetate buffer, pH 6.5 (29 mmol/L sodium barbital, 29 mmol/L sodium acetate, 0.68% (w/v) NaCl, 0.02% (w/v) sodium azide; adjusted to pH 6.5 with HCl) and the reaction mixtures were incubated for 17 h at 37° C. MU-α-GcNS is available from Moscerdam Substrates. After the first incubation, 6 μl twice-concentrated McIlvain's phosphate/citrate buffer, pH 6.7, containing 0.02% sodium azide and 10 μl (0.1 U) yeast a-glucosidase (Sigma) in water were added and a second incubation of 24 h at 37° C. was carried out. Long incubations at 37° C. (17-24 h) were carried out in 96-well plates which were sealed airtight with broad sticky tape, limiting evaporation to <15%. Next, 200 μL 0.5 mol/L Na2CO3/NaHCO3, pH 10.7, was added, and the fluorescence of the released 4-methylumbelliferone (MU) was measured on a Fluoroskan (Titertek) fluorimeter. Protein was determined as described previously (van Diggelen et al., Clin. Chim. Acta., 187:131-139 (1990)).
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Barbital
Bicarbonate, Sodium
Biological Assay
Buffers
Citrate
Fluorescence
Glucosidase
Hymecromone
Phosphates
Proteins
Sodium
Sodium Acetate
Sodium Azide
Sodium Chloride
Yeast, Dried
Top products related to «Sodium Acetate»
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Sodium acetate is a chemical compound with the formula CH3COONa. It is a common salt that is widely used in various laboratory and industrial applications. Sodium acetate functions as a buffer solution, helping to maintain a specific pH level in chemical reactions and processes.
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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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Acetic acid is a colorless, vinegar-like liquid chemical compound. It is a commonly used laboratory reagent with the molecular formula CH3COOH. Acetic acid serves as a solvent, a pH adjuster, and a reactant in various chemical processes.
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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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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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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.
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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.
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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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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.
More about "Sodium Acetate"
Sodium acetate (CH3COONa) is a widely used chemical compound that serves various scientific and industrial applications.
It is a salt of acetic acid (CH3COOH), also known as ethanoic acid.
Sodium acetate is commonly employed as a buffering agent, preservative, and pH regulator in numerous experimental protocols and processes.
Sodium acetate is a versatile compound with a range of uses.
In scientific research, it is often utilized as a buffer to maintain a specific pH level in various experimental setups, such as in cell culture media, enzymatic assays, and biochemical analyses.
It can also act as a preservative, helping to extend the shelf-life of certain products or samples by inhibiting microbial growth.
Beyond its scientific applications, sodium acetate finds use in various industrial sectors.
It is employed as a food additive, where it functions as a pH regulator, preservative, and flavor enhancer.
In the pharmaceutical industry, sodium acetate is used in the formulation of certain drug products, leveraging its buffering and stabilizing properties.
Closely related compounds, such as acetic acid, hydrochloric acid, and sodium hydroxide, are also commonly utilized in scientific and industrial processes.
These substances can interact with sodium acetate, altering its properties and influencing its effectiveness in different applications.
Other compounds, like methanol, acetonitrile, quercetin, and ethanol, may be used in conjunction with sodium acetate, for example, in extraction, purification, or analytical procedures.
The combination of these chemicals can provide valuable insights and enable the optimization of various experimental protocols.
PubCompare.ai's AI-driven platform can assist researchers in navigating the complex landscape of sodium acetate and related compounds.
By providing access to the best published protocols, pre-prints, and patent information, the platform can help users locate reliable products and enhance the reproducibility of their experiments, streamlining the research process and improving their overall results.
It is a salt of acetic acid (CH3COOH), also known as ethanoic acid.
Sodium acetate is commonly employed as a buffering agent, preservative, and pH regulator in numerous experimental protocols and processes.
Sodium acetate is a versatile compound with a range of uses.
In scientific research, it is often utilized as a buffer to maintain a specific pH level in various experimental setups, such as in cell culture media, enzymatic assays, and biochemical analyses.
It can also act as a preservative, helping to extend the shelf-life of certain products or samples by inhibiting microbial growth.
Beyond its scientific applications, sodium acetate finds use in various industrial sectors.
It is employed as a food additive, where it functions as a pH regulator, preservative, and flavor enhancer.
In the pharmaceutical industry, sodium acetate is used in the formulation of certain drug products, leveraging its buffering and stabilizing properties.
Closely related compounds, such as acetic acid, hydrochloric acid, and sodium hydroxide, are also commonly utilized in scientific and industrial processes.
These substances can interact with sodium acetate, altering its properties and influencing its effectiveness in different applications.
Other compounds, like methanol, acetonitrile, quercetin, and ethanol, may be used in conjunction with sodium acetate, for example, in extraction, purification, or analytical procedures.
The combination of these chemicals can provide valuable insights and enable the optimization of various experimental protocols.
PubCompare.ai's AI-driven platform can assist researchers in navigating the complex landscape of sodium acetate and related compounds.
By providing access to the best published protocols, pre-prints, and patent information, the platform can help users locate reliable products and enhance the reproducibility of their experiments, streamlining the research process and improving their overall results.