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Potassium Acetate

Potassium Acetate: A versatile chemical compound with a wide range of applications in research and industry.
Potassium acetate is a salt of acetic acid and potassium, known for its ability to act as a buffer, preservative, and deicing agent.
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Most cited protocols related to «Potassium Acetate»

Preparation of cDNA for Illumina Sequencing

Preparation of cDNA followed the procedure described in Mortazavi et al.^{2 (link)}, with minor modifications as described below. Prior to fragmentation, a 7 uL aliquot (∼ 500 pgs total mass) containing known concentrations of 7 “spiked in” control transcripts from A. thaliana and the lambda phage genome were added to a 100 ng aliquot of mRNA from each time point. This mixture was then fragmented to an average length of 200 nts by metal ion/heat catalyzed hydrolysis. The hydrolysis was performed in a 25 uL volume at 94°C for 90 seconds. The 5X hydrolyis buffer components are: 200 mM Tris acetate, pH 8.2, 500 mM potassium acetate and 150 mM magnesium acetate. After removal of hydrolysis ions by G50 Sephadex filtration (USA Scientific catalog # 1415-1602), the fragmented mRNA was random primed with hexamers and reverse-transcribed using the Super Script II cDNA synthesis kit (Invitrogen catalog # 11917010). After second strand synthesis, the cDNA went through end-repair and ligation reactions according to the Illumina ChIP-Seq genomic DNA preparation kit protocol (Illumina catalog # IP102-1001), using the paired end adapters and amplification primers (Illumina Catalog # PE102-1004). Ligation of the adapters adds 94 bases to the length of the cDNA molecules.

Trapnell C., Williams B.A., Pertea G., Mortazavi A., Kwan G., van Baren M.J., Salzberg S.L., Wold B.J, & Pachter L. (2010). Transcript assembly and abundance estimation from RNA-Seq reveals thousands of new transcripts and switching among isoforms. Nature biotechnology, 28(5), 511-515.

Publication 2010

Acetate Anabolism Bacteriophage lambda Buffers Chromatin Immunoprecipitation Sequencing DNA, Complementary DNA Chips Filtration Genome Hydrolysis Ions Ligation magnesium acetate Metals Oligonucleotide Primers Potassium Acetate RNA, Messenger sephadex Tromethamine

Structural Probing of HIV-1 Genomic RNA

Full length HIV-1 genomic RNA was gently purified from NL4-3 virions (Genbank AF324493). The RNA was equilibrated in a native buffer [50 mM Hepes (pH 8.0), 200 mM potassium acetate (pH 8.0), 3 mM MgCl₂] at 37 °C for 15 min and treated with 1M710 (link). Sites of 2′-hydroxyl modification were identified over read lengths spanning several hundred nucleotides using 31 primer extension reactions resolved by fluorescence-detected capillary electrophoresis6 (link),11 (link). Pairing probabilities were determined using RNA-Decoder13 (link) and secondary structure models were developed by incorporating SHAPE reactivities as a pseudo-free energy change term, in conjunction with nearest-neighbor parameters, in an accurate thermodynamics-based prediction algorithm22 (link),23 (link).

Watts J.M., Dang K.K., Gorelick R.J., Leonard C.W., Bess JW J.r., Swanstrom R., Burch C.L, & Weeks K.M. (2009). Architecture and Secondary Structure of an Entire HIV-1 RNA Genome. Nature, 460(7256), 711-716.

Publication 2009

Buffers Capillaries Fluorescence Genome HEPES HIV-1 Hydroxyl Radical Magnesium Chloride Nucleotides Oligonucleotide Primers Potassium Acetate Virion

Flavonoid Content Quantification Method

The flavonoid contents of individual extracts were measured as per the Dowd method [46 (link)]. An aliquot of 1 mL of extract solution (25–200 µg/mL) or quercetin (25–200 µg/mL) were mixed with 0.2 mL of 10% (w/v) AlCl₃ solution in methanol, 0.2 mL (1 M) potassium acetate and 5.6 mL distilled water. The mixture was incubated for 30 min at room temperature followed with the measurement of absorbance at 415 nm against the blank. The outcome data were expressed as mg/g of quercetin equivalents in milligrams per gram (mg QE/g) of dry extract.

Aryal S., Baniya M.K., Danekhu K., Kunwar P., Gurung R, & Koirala N. (2019). Total Phenolic Content, Flavonoid Content and Antioxidant Potential of Wild Vegetables from Western Nepal. Plants, 8(4), 96.

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Publication 2019

Aluminum Chloride Flavonoids Methanol Potassium Acetate Quercetin

Quantifying Flavonoids in L. aromatica

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Publication 2013

Aluminum Chloride Colorimetry Flavonoids Methanol Potassium Acetate Quercetin

Structural Homogeneity Analysis of RNA Molecules

In order to check for structure homogeneity of the RNA molecules, all labeled transcripts were analyzed on 5–10% polyacrylamide gels (400/300/0.8 mm, acrylamide/bisakrylamide–29/1) in non-denaturing conditions. The electrophoresis was conducted at a constant power of 10 or 20 W for 4–6 h in 0.5 × TB buffer (45 mM Tris–borate) at 20°C (identical to the temperature of chemical and enzymatic structure probing reactions). Prior to gel electrophoresis, the ³²P-labeled transcripts were subjected to a denaturation/renaturation procedure in a solution containing 10 mM Tris–HCl (pH 7.2), 40 mM NaCl and 10 mM MgCl₂, by heating the sample at 90°C for 1 min. and slowly cooling it to 20°C (∼1°C/min), and mixed with an equal volume of 7% sucrose with dyes. Electrophoresis performed in the presence of 1–10 mM Mg²⁺ and constant buffer circulation did not reveal any significant differences in the formation of stable conformers. The specific conditions for the temperature and pH dependence experiments are described in the legend to the Supplementary Figure 2.
Two different electrophoretic migration standards were used: ds69 and ds107. The ds69 represents dsRNA molecule, 69 bp long, obtained by hybridization of two complementary RNA oligomers: 5′ GGG(CUG)₂₁CCC and 5′ GGG(CAG)₂₁ CCC. The second marker, ds107, was obtained by annealing of the fx4 transcript with its complementary molecule containing 23 CCG repeats.
A number of transcripts analyzed in this study migrated on the native gels as two distinct conformers. In all cases, the contribution of the less prevalent conformer was too high to be neglected in the structure studies. Two assays were used to obtain conformer-specific structural data. First, the preparative amount of intact conformers was separated on a native 8% polyacrylamide gel, exposed to the X ray film and then separately excised and eluted from the gel with 20 mM Tris–HCl, pH 7.2. The conformer-specific structure probing was performed without the initial denaturation/renaturation step as described below. Alternatively, structure probing reactions were performed on the mixture of coexisting stable conformers and partially nicked RNA molecules that were resolved on native polyacrylamide gels. Nicked transcripts (due to the nuclease or lead ion hydrolysis), which migrate on native gels at the same rate as intact conformers, were eluted from the gel (with 0.3 M potassium acetate, pH 5.1, 1 mM EDTA and 0.1% SDS), precipitated and analyzed on denaturing polyacrylamide gels. Although, both methods led to identical results, the first, more straightforward approach was used more frequently. In order to rule out the possibility of sequence heterogeneity between the stable coexisting conformers, RNA sequencing analysis of each conformer was conducted using RNA Sequencing Kit (Pharmacia Biotech Inc.) according to the manufacturer's recommendations.

Napierala M., Michalowski D., de Mezer M, & Krzyzosiak W.J. (2005). Facile FMR1 mRNA structure regulation by interruptions in CGG repeats. Nucleic Acids Research, 33(2), 451-463.

Publication 2005

Acrylamide Biological Assay Borates Buffers Complementary RNA Crossbreeding Dyes Edetic Acid Electrophoresis Enzymes Genetic Heterogeneity Hydrolysis Magnesium Chloride Molecular Structure polyacrylamide gels Potassium Acetate RNA, Double-Stranded Sequence Analysis Sodium Chloride Sucrose Tromethamine X-Ray Film

Most recents protocols related to «Potassium Acetate»

Generation and Characterization of Labeled DNA Probes

For generation of the labeled probe, 5ʹ-IRDye® 700 labeled oligonucleotides were purchased from IDT with the following sequences: ABE; 5ʹ-CGG TGT TGC ACG CGG *CGG GAC GCT CGC GGT AGT TTT* TTC CCA TGA TCA CG-3ʹ and 5ʹ-CGT GAT CAT GGG AAA *AAA CTA CCG CGA GCG TCC CGC CGC* GTG CAA CAC CG-3ʹ and scrambled control probes; 5ʹGTT TAC TAG GTC GAG GTA CTT CGA CGC GCG CCG TCT GCT AGC GCG GTC TG-3ʹ and 5ʹ-CA GAC CGC GCT AGC AGA CGG CGC GCG TCG AAG TAC CTC GAC CTA GTA AAC3ʹ. The AlpA binding element is indicated by asterisks. The oligonucleotides were annealed by mixing them in equimolar amounts in duplexing buffer (100 mM Potassium Acetate; 30 mM HEPES, pH 7.5) and heating to 100 °C for 5 min in a PCR cycler. The cycler was then turned off and the samples were allowed to cool to room temperature while still inside the block. The annealed product was then diluted with water to 6.25 nM for EMSA experiments.
For EMSAs fluorophore labeled DNA probes at a concentration of 0.3125 nM were incubated for 30 min at 20 °C in 20 µl reaction mix (Licor Odysee EMSA Kit) containing 33.4 mM Tris, 70.2 mM NaCl, 12.5 mM NaOAc, 3.75 mM HEPES, 50 mM KCl, 3.5 mM DTT, 0.25% Tween20 and 0.5 µg sheared salmon sperm DNA (ThermoFisher) with proteins. For resolving the reactions, 4% polyacrylamide gels containing 30% triethylene glycol were cast (For two gels: 2 ml ROTIPHORESE®Gel 30 37.5:1 (Roth), 4.5 ml triethylene glycol (Sigma-Aldrich), 1.5 ml 5x TBE-buffer, 7 ml ddH2O, 15 µl TEMED, 75 µl 10% APS). The gels were preequilibrated for 30 min at 130 V in 0.5x TBE-buffer. Samples with added 10x orange dye were then loaded onto the gel at 4 °C and the voltage set to 300 V until the samples entered the gel completely. The voltage was then turned down to 130 V and the gel was run until the migration front reached the end of the gel. The gels were imaged using the Licor Odyssey imaging system using the 700 nm channel. For generation of the figures, the scanned image was converted to greyscale and brightness and contrast adjusted. The unprocessed scan is available as Supplementary Fig. 15.

Eggers O., Renschler F.A., Michalek L.A., Wackler N., Walter E., Smollich F., Klein K., Sonnabend M.S., Egle V., Angelov A., Engesser C., Borisova M., Mayer C., Schütz M, & Bohn E. (2023). YgfB increases β-lactam resistance in Pseudomonas aeruginosa by counteracting AlpA-mediated ampDh3 expression. Communications Biology, 6, 254.

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Publication 2023

5'-chloroacetamido-5'-deoxythymidine AT 130 Buffers CD3EAP protein, human Electrophoretic Mobility Shift Assay Gels HEPES Oligonucleotides polyacrylamide gels Potassium Acetate Proteins Radionuclide Imaging Salmo salar Sodium Chloride Sperm triethylene glycol Tris-borate-EDTA buffer Tromethamine Tween 20

Dye Injection and Immunohistochemistry of Drosophila Nervous System

Dye injection and immunohistochemistry methods have previously been described in detail^{62 (link),63 (link)}. In brief, the ventral nerve cord of adult Drosophila was dissected and mounted dorsal side up on VECTABOND™ (Vector Labs) coated 0.9–1.1 mm etched slides. An 80–100 MΩ glass electrode filled with a dye solution of 10% w/v neurobiotin (Vector Labs) and tetramethyl rhodamine-labeled dextran (Invitrogen) and backfilled with 2 M potassium acetate was used to inject the dyes into the GF axons by passing depolarizing current. Samples were fixed in 4% paraformaldehyde and were prepared for confocal microscopy as described previously^{62 (link),63 (link)}. Streptavidin-Cy2 conjugate (Jackson ImmunoResearch; 1:750) was used to visualize neurobiotin. Samples were scanned at a resolution of 1024 × 1024 pixels, 2.5× zoom, and 0.5 μm step size with a Nikon C1si Fast Spectral Confocal system using a 60× oil immersion objective lens. Dye filling of the GFs with Lucifer Yellow was performed as described in ref. ^{15 (link)}.

Ermanoska B., Asselbergh B., Morant L., Petrovic-Erfurth M.L., Hosseinibarkooie S., Leitão-Gonçalves R., Almeida-Souza L., Bervoets S., Sun L., Lee L., Atkinson D., Khanghahi A., Tournev I., Callaerts P., Verstreken P., Yang X.L., Wirth B., Rodal A.A., Timmerman V., Goode B.L., Godenschwege T.A, & Jordanova A. (2023). Tyrosyl-tRNA synthetase has a noncanonical function in actin bundling. Nature Communications, 14, 999.

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Publication 2023

Adult Axon Cloning Vectors Cone-Rod Dystrophy 2 Drosophila Immunohistochemistry Lens, Crystalline lucifer yellow Microscopy, Confocal Nervousness neurobiotin paraform Potassium Acetate rhodamine-dextran-amine dye Streptavidin Submersion

Quantifying Flavonoids in Vernonia guineensis

The aluminum chloride colorimetric protocol described by Chang et al. [35 ] served as support to evaluate the total flavonoid contents in the hydroethanolic extract of V. guineensis. A mixture of extract (100 µl and 2 mg/ml), aluminum chloride (50 µl and 1.2%), and potassium acetate (50 µl and 120 mM) introduced into a tube was incubated (room temperature, 30 minutes) and the absorbance was read (415 nm, spectrophotometer). Various concentrations of quercetin (0.015 to 2 mg/ml) were used to plot the standard curve which allowed the calculation of the total flavonoid content in the extract.

Yousseu Nana W., Billong Mimb J.R., Atsamo A.D., Tsafack E.G., Djuichou Nguemnang S.F., Fagni Njoya Z.L., Matah Marthe V.M., Madjo Kouam Y.K., Mbiantcha M, & Ateufack G. (2023). In Vitro and In Vivo Anti-Inflammatory Properties of the Hydroethanolic Extract of the Roots of Vernonia guineensis (Asteraceae). International Journal of Inflammation, 2023, 7915367.

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Publication 2023

Aluminum Chloride Colorimetry Flavonoids Potassium Acetate Quercetin

Purification of ATP Synthase Complex

The strain expressing Atp6 subunit C-terminally tagged by HA-6xHis in the mitochondrial genome was characterized previously to cause no damage to the ATP synthase structure^{41 (link)}. This strain was used to pull down the whole ATP synthase complex by Ni-NTA agarose beads. Briefly, 5 mg of mitochondria were centrifuged and suspended in 1 mL of sonication buffer (250 mM sucrose, 50 mM NaH₂PO₄, 5 mM 6-aminocaproic acid, 1 mM EDTA, pH 7.5, protease inhibitors cocktail tablet (Roche), 1 µM PMSF) and sonicated 6 times 10 s, with 10 s intervals on ice. After centrifugation at 6000 × g 10 min at 4 °C, supernatant was ultracentrifuged at 268,526 × g for 1 h (Thermo Scientific™ Sorvall™ WX ultracentrifuge, TFT80.2 rotor). The pellet was washed twice with the sonication buffer without EDTA (without suspending it) and then suspended with the use of the potter in 500 µl MP extraction buffer (150 mM potassium acetate, 10% glycerol, 2 mM 6-aminocaproic acid, 30 mM HEPES, pH 7.4, 1% N-dodecyl-β-maltoside, 2 mM PMSF and protease inhibitors cocktail tablet, EDTA-free, Roche). After 20 min incubation on ice, the membranes were centrifuged for 30 min at 21,950 × g, 4 °C and the extract was incubated with 200 µL of the Ni–NTA agarose washed previously by Binding buffer (50 mM NaCl, 10% glycerol, 10 mM imidazole, 20 mM NaH₂PO₄, pH = 7.9, 0,1% n-dodecyl-β-maltoside, 2 mM PMSF, protease inhibitors cocktail tablet) for overnight. Next day the beads were washed twice with the Binding buffer, then suspended in 400 µL of Binding buffer, dosed and after addition of 100 µL of 5 × Laemmli sample buffer, boiled during 5 min. The 50 µg of the extract and 2 µg of bead eluate were loaded on the 15% SDS-PAGE gel. Then the gel was stained with Coomassie blue or silver staining according to manufacturer’s protocol (Pierce sliver stain kit, Thermo Fisher Scientific) to visualize the proteins.

Panja C., Wiesyk A., Niedźwiecka K., Baranowska E, & Kucharczyk R. (2023). ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast. Scientific Reports, 13, 3839.

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Publication 2023

6-Aminocaproic Acid ATP-sepharose Buffers Centrifugation Coomassie blue dodecyl maltoside Edetic Acid G 526 Genome, Mitochondrial Glycerin HEPES imidazole Laemmli buffer Mitochondria Nitric Oxide Synthase Potassium Acetate Protease Inhibitors Proteins Protein Subunits SDS-PAGE Sepharose Sodium Chloride Stains Strains Sucrose Tablet Tissue, Membrane

Mitochondrial ATP Synthase Complex Analysis

Two-dimensional gel electrophoresis was based on the protocol of Schamel^{43 (link)} with slight modifications. Briefly, the ATP synthase complexes were liberated from inner mitochondrial membrane of isolated mitochondria by incubation with 1–2% digitonin in extraction buffer (30 mM HEPES, 150 mM potassium acetate, 12% glycerol, 2 mM 6-aminocaproic acid, 1 mM EGTA, protease inhibitor cocktail tablets EDTA-free (Roche), pH 7.4) for different time intervals up to 60 min and separated using NativePAGE™ 3–12% Bis–Tris Gels (Thermo Fisher Scientific) to separate monomeric and dimeric ATP synthase complexes^{44 (link)}. For second dimensional analysis the lanes were cut from the gel and placed in SDS-PAGE running buffer (25 mM Tris, 192 mM Glycine, 0.1% SDS, pH 8.3 with 1% β-mercaptoethanol), heated in a microwave for 10 secs and incubated for another 10 min in a shaker. The gel strips were then loaded on the top of a 16% SDS-PAGE gel, and electrophoresis was conducted under denaturing conditions. Then the gel was stained with Coomassie blue or silver staining and bands cut-off were analyzed by mass spectrometry. For Western blotting proteins from the gel were transferred into PVDF or nitrocellulose membranes using iBlot system (Thermo Fisher Scientific). For SDS-PAGE analysis of steady state level of proteins, yeast cells were disrupted by alkaline lysis with NaOH/TCA^{45 (link)}. Western blot analysis was performed using the polyclonal rabbit anti-Mco10 antibody, anti-ATP synthase subunits antibodies (gifts from Marie-France Giraud, Bordeaux, France and Martin van der Laan, Germany), anti-Rip1 and Cob1 antibodies (provided by dr hab. Ulrike Topf, IBB PAS) or anti-Cox2 (Thermo Fisher Scientific).

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Publication 2023

2-Mercaptoethanol 6-Aminocaproic Acid Anti-Antibodies Antibodies Antibodies, Anti-Idiotypic Bistris Buffers Cells Coomassie blue Digitonin Edetic Acid Egtazic Acid Electrophoresis Electrophoresis, Gel, Two-Dimensional Gifts Glycerin Glycine HEPES Mass Spectrometry Microwaves Mitochondria Mitochondrial Membrane, Inner Nitric Oxide Synthase Nitrocellulose polyvinylidene fluoride Potassium Acetate Protease Inhibitors Proteins Protein Subunits PTGS2 protein, human Rabbits Saccharomyces cerevisiae SDS-PAGE Tissue, Membrane Tromethamine Western Blot

Top products related to «Potassium Acetate»

Potassium acetate by Merck Group

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Potassium acetate is a chemical compound commonly used in laboratory settings. It serves as a buffer, maintaining a desired pH level in various experiments and analytical procedures. The compound is a white, crystalline solid that is soluble in water and has a neutral to slightly basic pH. Potassium acetate is a versatile and widely used reagent in many scientific applications.

Quercetin by Merck Group

Sourced in United States, Germany, Italy, India, Spain, United Kingdom, France, Poland, China, Sao Tome and Principe, Australia, Brazil, Macao, Switzerland, Canada, Chile, Japan, Singapore, Ireland, Mexico, Portugal, Sweden, Malaysia, Hungary

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.

Gallic acid by Merck Group

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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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The Folin-Ciocalteu reagent is a colorimetric reagent used for the quantitative determination of phenolic compounds. It is a mixture of phosphomolybdic and phosphotungstic acid complexes that undergo a color change when reduced by phenolic compounds.

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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.

2 2 diphenyl 1 picrylhydrazyl (dpph) by Merck Group

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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.

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.

Aluminum chloride by Merck Group

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Aluminum chloride is a chemical compound with the formula AlCl3. It is a colorless crystalline solid that is soluble in water and organic solvents. Aluminum chloride is used as a catalyst in various chemical reactions and as a drying agent.

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Rutin is a laboratory reagent used for analytical and research purposes. It is a flavonoid compound derived from various plant sources. Rutin exhibits antioxidant and anti-inflammatory properties, and is commonly used in assays, chromatography, and other analytical techniques.

What are the common uses of Potassium Acetate?

Potassium Acetate has a wide range of applications in various industries and research fields. It is commonly used as a buffer, preservative, and deicing agent. In research, Potassium Acetate is often employed as a component in cell culture media, to maintain pH levels, and in cryopreservation solutions to protect cells during freezing. It also finds use in the production of pharmaceuticals, as a food preservative, and as an additive in de-icing fluids for aircraft and roads.

Are there different types or variations of Potassium Acetate?

Yes, there are several variations of Potassium Acetate available. The most common form is the anhydrous (water-free) Potassium Acetate, but there is also a hydrated version, Potassium Acetate Trihydrate, which contains three molecules of water per molecule of Potassium Acetate. The hydrated form is often preferred for certain applications, such as in cryoprotective solutions, where the additional water content can be beneficial.

What are some common challenges in using Potassium Acetate?

One of the main challenges with using Potassium Acetate is ensuring proper solubility and compatibility with other reagents or materials in your research setup. Potassium Acetate has a relatively high solubility in water, but its solubility can be affected by factors like temperature and pH. It's important to carefully consider the optimal conditions for your specific application to avoid precipitation or other issues. Additionally, Potassium Acetate can be hygroscopic, meaning it can absorb moisture from the air, which can impact its purity and handling.

How can PubCompare.ai help optimize the use of Potassium Acetate?

PubCompare.ai can be a valuable tool in optimizing the use of Potassium Acetate in your research. The platform's AI-driven analysis can help you efficiently screen protocol literature to identify the most effective methods and conditions for using Potassium Acetate. You can compare side-by-side protocols from scientific publications, preprints, and patents to pinpoint critical insights, such as the optimal pH, concentration, or temperature ranges for your specific application. This can help you choose the most reproducible and accurate protocols, saving you time and improving the quality of your research.

What are some specific applications of Potassium Acetate in research?

Potassium Acetate has a wide range of applications in research, including: 1) As a buffer in cell culture media to maintain optimal pH levels for cell growth and proliferation. 2) In cryopreservation solutions to protect cells during freezing and thawing. 3) In the formulation of pharmaceutical products, such as tablets or injections. 4) As a component in buffer systems for protein purification and characterization. 5) In the preparation of chemical reagents and standards for analytical techniques like chromatography and spectroscopy. The versatility of Potassium Acetate makes it a useful tool across many areas of scientific research.

More about "Potassium Acetate"

Potassium acetate, also known as acetic acid potassium salt, is a versatile chemical compound with a wide range of applications in research and industry.
This salt of acetic acid and potassium is known for its ability to act as a buffer, preservative, and deicing agent, making it a valuable tool in various scientific and industrial settings.
One of the key applications of potassium acetate is its use as a buffer in analytical and biochemical procedures.
Its buffering capacity helps maintain the desired pH levels in a variety of experiments, ensuring optimal conditions for chemical reactions and enzymatic activities.
In addition to its buffering properties, potassium acetate is also employed as a preservative, particularly in the food and pharmaceutical industries.
Its antimicrobial properties help extend the shelf life of products, making it an important ingredient in the formulation of various consumables and medical preparations.
Moreover, potassium acetate's ability to lower the freezing point of water has led to its widespread use as a deicing agent.
This makes it a valuable compound in winter maintenance, where it is used to clear roads, sidewalks, and other surfaces from ice and snow, improving safety and accessibility.
Beyond these core applications, potassium acetate has also found utility in other areas, such as in the synthesis of organic compounds, in the production of fertilizers, and as a component in various cleaning and personal care products.
To optimize your research workflows and elevate your studies, consider exploring the AI-driven platform PubCompare.ai.
This innovative tool helps researchers identify the best protocols and products, enabling them to compare research methods side-by-side and find the optimal conditions for their experiments.
Discover the power of potassium acetate and streamline your research process with PubCompare.ai.