Na acetate

Manufactured by Merck Group

Sourced in Germany

Sodium acetate is a chemical compound with the formula CH3COONa. It is a white, crystalline salt that is commonly used as a buffer solution in various laboratory applications.

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α-naphthyl acetate (α-NA), (5 citations)

9 protocols using na acetate

Extraction and Analysis of Compounds

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The following reagents were used: hexane, chloroform, methanol, and acetone from RBM (Puebla, Mexico); dimethyl sulfoxide (DMSO), formamide (FA), HPLC-grade methanol, H₃PO₄, HCl, AlCl₃, Na acetate, H₃BO₃ were purchased from Sigma-Aldrich.

Vergara Barragán E., Bach H., Meza-Reyes S., Montiel-Smith S., Sánchez-Arreola E, & Hernández L.R. (2019). Bioactivities of Flavonoids from Lopezia racemosa. BioMed Research International, 2019, 3286489.

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Phytase Activity Assay of P. fortinii

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To identify the ability to hydrolyze organic phosphorus-containing compounds, P. fortinii DSE2 isolate was cultivated on potato-dextrose broth (PDB) at 20 ± 2 °C for 28 days. The isolate’s inoculation was performed by adding 3 plugs (d = 8 mm) with mycelium in 250 mL of PDB. On days 7, 14, 21, and 28, the mycelium was separated by filtration, and the filtrate was used as a crude enzyme preparation.
Phytase activity was determined according to [33 (link)]. The reaction mixture contained 500 nM of Na-phytate (Sigma Aldrich, St. Louis, MO, USA) solution, 100 mM of Na-acetate buffer (pH 4.5), and filtrate as a crude enzyme preparation. The mixture was incubated for 30 min at 37 °C. The enzyme activity was determined as the amount of released phosphate by adding the following reagent to the mixture: 10 mM ammonium molybdate solution, 5 N H₂SO₄ solution, and acetone at a ratio of 1:1:2. The optical density of the experimental sample was measured at λ = 355 nm on an Epoch spectrophotometer (Biotek, Santa Clara, CA, USA) against the control sample (contained buffer instead of filtrate).
Protein content in the filtrate was determined according to [34 (link)] using bovine serum albumin as a standard. The amount of phosphorus (μg) released in 1 min per 1 μg of protein was counted as 1 unit of phytase specific activity (1 U).

Mikheev V.S., Struchkova I.V., Ageyeva M.N., Brilkina A.A, & Berezina E.V. (2022). The Role of Phialocephala fortinii in Improving Plants’ Phosphorus Nutrition: New Puzzle Pieces. Journal of Fungi, 8(11), 1225.

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Tamoxifen-Induced Conditional Knockout and Lineage Tracing

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Tamoxifen (tmx) was used to activate CreER in conditional knockout and lineage-tracing models. For gene knockout, 6-8 week-old-mice (~18-25g) were intraperitoneally injected with tmx (Sigma, stock 20 mg/ml in corn oil) at a dose of 3 mg/d for three consecutive days. For lineage tracing experiments, mice were injected with a single 3 mg dose of tmx. For in vivo acetate treatment, drinking water was supplemented with either 150 mM NaCl (Sigma) as control or 150 mM Naacetate (Sigma). Sibling- or age-matched experimental and control animals were randomly allocated into experimental groups based only on genotype and date of birth. Both female and male mice were analyzed separately for each experiment. All results were consistent between sexes and combined when appropriate. All animal experiments were approved by the University of Pennsylvania’s Institutional Animal Care and Use Committee.

Stine R.R., Sakers A.P., TeSlaa T., Kissig M., Stine Z.E., Kwon C.W., Cheng L., Lim H.W., Kaestner K.H., Rabinowitz J.D, & Seale P. (2019). PRDM16 maintains homeostasis of the intestinal epithelium by controlling region-specific metabolism. Cell stem cell, 25(6), 830-845.e8.

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Glucose Uptake Assay for Cellular Metabolism

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Glucose uptake was determined via the glucose uptake assay as previously described (Murray 1971 (link)) Briefly, cells were exposed to DMSO (vehicle) or 50 μmol/L cytochalasin B in DMEM (both without glucose) and 5 μCi 3-O-Methyl-D-[³H]-Glucose for 60–90 sec. Cells were rapidly washed five times with ice-cold glucose assay wash buffer (100 mmol/L MgCl₂, 0.1 mmol/L Phloretin; Sigma-Aldrich, St. Louis, MO). Next, cells were lysed with 1 mL lysis buffer (200 mmol/L Na Acetate, 10% DMSO, 1% SDS; Sigma Aldrich, St. Louis, MO) and placed on ice until needed. Samples were transferred to disposable glass scintillation vials containing 6 mL Ready Safe™ liquid scintillation cocktail for aqueous samples (Beckman Coulter, Fullerton, CA). Radioactivity was measured by scintillation spectrometry on the LS 6500 Multi-Purpose Scintillation Counter (Beckman Coulter) for 1 min per sample. Protein concentration was determined by DC protein assay (Bio-Rad Laboratories, Hercules, CA) as per manufacturer’s instructions.

Viator R.J., Khader H., Hingorani N., Long S., Solodushko V, & Fouty B. (2015). Hypoxia-induced increases in glucose uptake do not cause oxidative injury or advanced glycation end-product (AGE) formation in vascular endothelial cells. Physiological Reports, 3(7), e12460.

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Quantifying Osteoclast Differentiation via TRAP 5b Assay

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Osteoclast differentiation was evaluated by measurement of TRAP 5b activity according to a modified protocol based on Janckila et al. [40 (link)]. Cell lysates were added to TRAP 5b reaction buffer as a substrate consisting of 2.5 mM N-ASBI-P (Sigma-Aldrich) in 100 mM Na acetate (Sigma-Aldrich) buffer containing 50 mM Na tartrate (Sigma-Aldrich), 2% NP-40 (Sigma-Aldrich), and 1% ethylene glycol monomethyl ether (EGME, Sigma-Aldrich) adjusted to pH 6.1. The mixtures were incubated at 37 °C for 1 h. The enzymatic reaction was stopped by adding 0.1 M NaOH. Fluorescence was measured at an excitation wavelength of 405 nm and an emission wavelength of 535 nm. The relative fluorescence units were correlated to a TRAP 5b standard.

Kruppke B., Heinemann C., Farack J., Weil S., Aflalo E.D., Sagi A, & Hanke T. (2020). Hemocyanin Modification of Chitosan Scaffolds with Calcium Phosphate Phases Increase the Osteoblast/Osteoclast Activity Ratio—A Co-Culture Study. Molecules, 25(19), 4580.

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Quantification of GAG Content in Samples

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GAG content in culture supernatants was assessed using the Barbosa method [40 (link)]. Briefly, 250 μL of collected supernatant was incubated with 1 mL of DMMB solution (16 mg/l dimethylmethylene blue, 6 mM sodium formate, 200 mM GuHCL, all from Sigma Aldrich, pH 3.0) on a shaker at room temperature for 30 min. After centrifugation, precipitated DMMB-GAG complexes were dissolved in decomplexion solution (4 M GuHCL, 50 mM Na-Acetate, 10% Propan-1-ol, all from Sigma Aldrich, pH 6.8) at 60 °C for 15 min. Absorption was measured at 656 nm and corresponding GAG concentrations were calculated using a standard curve prepared with purified bovine chondroitin sulfate (Sigma Aldrich).
For the measurement of GAG content in cartilage tissue, samples were preliminary digested overnight at 56 °C in 1 mL of proteinase K solution (Sigma Aldrich, P2308), and 100 µL of the resulting digested solution was used for the DMMB-GAG precipitation.

Pigeot S., Bourgine P.E., Claude J., Scotti C., Papadimitropoulos A., Todorov A., Epple C., Peretti G.M, & Martin I. (2020). Orthotopic Bone Formation by Streamlined Engineering and Devitalization of Human Hypertrophic Cartilage. International Journal of Molecular Sciences, 21(19), 7233.

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RNA and DNA Fragmentation for Sequencing

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Nucleic acids were isolated as described above. Total RNA (~400 μg), prepared in 0.1X TE buffer, at 0.5 μg/μl, were chemically fragmented in 50 mM Tris‐acetate pH 8.1, 100 mM CH₃CO₂K and 30 mM Mg(CH₃COO)₂ by incubating the samples at 96°C for 12 min. The reaction was stopped by transferring the samples to ice and the addition of 0.5 M EDTA to final concentration of 45 mM. Fragmented RNA samples were then mixed with 1/10 volume of Na‐acetate (3M, pH 5, Sigma) and 2.5 volumes of EtOH and incubated for 1 h at −80°C. Precipitated RNA was collected by centrifugation: 30 min at 12,000 g at +4°C and washed once in 75% EtOH before being air‐dried and dissolved in TE. Recovered RNA was spectrophotometrically quantified (NanoDrop, Thermo Fisher Scientific) and kept on ice until used. The average size of fragmented RNA was estimated from an aliquot analysed on a Bioanalyzer chip (RNA9000, Agilent Technologies), according to the manufacturer's instructions. Approximately 70% of the initial amount of RNA was recovered after fragmentation.
Genomic DNA, in TE buffer at 3 μg/μl, was fragmented by several rounds of sonication (Bioruptor, Diagenode) at RT until an average fragment length of approximately 200 bp was achieved.

Aarum J., Cabrera C.P., Jones T.A., Rajendran S., Adiutori R., Giovannoni G., Barnes M.R., Malaspina A, & Sheer D. (2020). Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates. EMBO Reports, 21(10), e49585.

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Sodium Oxalate Media Preparation

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Culture media containing 5, 10, 15 and 20 mmol/L sodium oxalate (MERK; Darmstadt, Germany) was prepared by adding 10 mL of the 0.46 μ filter sterilized sugar and ammonium oxalate solutions listed below to 10 mL base media proteose peptone no. 3 (MERK; Darmstadt, Germany), 10 g yeast extract (MERK; Darmstadt, Germany), 5 g Tween 80 (MERK; Darmstadt, Germany) 1 mL KH₂PO₄ (MERK; Darmstadt, Germany) 2 g Na acetate (MERK; Darmstadt, Germany) 5 g di-Ammonium hydrogen-citrate (MERK; Darmstadt, Germany) 2 g MgSO₄.7H₂O (MERK; Darmstadt, Germany) 0.05 g MnSO₄ (Merck) 0.05 g water to 500 mL and sterilized at 121°C for 15 min.
For the preparation of 5, 10, 15 and 20 mmol/L sodium oxalate solutions, 13.39 g of Na₂C₂O₄ (MW =133.96) transferred to a 100mL volumetric flask. Rinsed the boat into the flask through a funnel until the volume reaches to 100ml. It may need to heat this gently (NOT BOIL) to promote the dissolving. Then before autoclave sterilization of base media samples, a specified volume of sodium oxalate solution was added to the samples. The amount of sodium oxalate was derived from Eq 1:

C_{1} V_{1} = C_{2} V_{2}

C₁V₁ = Concentration/amount (start) and Volume (start)
C₂V₂ = Concentration/amount (final) and Volume (final)
The required volume of sodium oxalate solution with (20 mmol/L concentration) to the 10 ml base media derived from Eq. 1.

Karamad D., Khosravi-Darani K., Hosseini H, & Tavasoli S. (2019). Analytical procedures and methods validation for oxalate content estimation. Biointerface research in applied chemistry, 9(5), 4305-4310.

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Sodium Oxalate Media Preparation

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C_{1} V_{1} = C_{2} V_{2}

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