Sodium tartrate, a salt of tartaric acid, is a chemical compound with a variety of applications in scientific research and industries.
It is commonly used as a buffer, a complexing agent, and a food additive.
Sodium tartrate has been studied for its potential applications in fields such as biochemistry, analytical chemistry, and materials science.
Researchers often need to find the most reliable and effective protocols for working with sodium tartrate, which can be challenging given the large volume of available literature.
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The α-amylase inhibition assay was performed using the 3,5-dinitrosalicylic acid (DNSA) method [8 (link)]. The leaf extract of A. pavonina was dissolved in minimum amount of 10% DMSO and was further dissolved in buffer ((Na2HPO4/NaH2PO4 (0.02 M), NaCl (0.006 M) at pH 6.9) to give concentrations ranging from 10 to 1000 μg/ml. A volume of 200 μl of α-amylase solution (2 units/ml) was mixed with 200 μl of the extract and was incubated for 10 min at 30 °C. Thereafter 200 μl of the starch solution (1% in water (w/v)) was added to each tube and incubated for 3 min. The reaction was terminated by the addition of 200 μl DNSA reagent (12 g of sodium potassium tartrate tetrahydrate in 8.0 mL of 2 M NaOH and 20 mL of 96 mM of 3,5-dinitrosalicylic acid solution) and was boiled for 10 min in a water bath at 85–90 °C. The mixture was cooled to ambient temperature and was diluted with 5 ml of distilled water, and the absorbance was measured at 540 nm using a UV-Visible spectrophotometer. The blank with 100% enzyme activity was prepared by replacing the plant extract with 200 μl of buffer. A blank reaction was similarly prepared using the plant extract at each concentration in the absence of the enzyme solution. A positive control sample was prepared using Acarbose (100 μg/ml–2 μg/ml) and the reaction was performed similarly to the reaction with plant extract as mentioned above. The α-amylase inhibitory activity was expressed as percent inhibition and was calculated using the equation given below: The % α-amylase inhibition was plotted against the extract concentration and the IC50values were obtained from the graph.
Wickramaratne M.N., Punchihewa J.C, & Wickramaratne D.B. (2016). In-vitro alpha amylase inhibitory activity of the leaf extracts of Adenanthera pavonina. BMC Complementary and Alternative Medicine, 16, 466.
BRIL-NOP was expressed in Spodoptera frugiperda (Sf9) insect cells. Ligand binding asays were performed as described in Methods online. Sf9 membranes were solubilized using 0.5% n-dodecyl-β-D-maltopyranoside (w/v) and 0.1% cholesteryl hemisuccinate (w/v), and purified by immobilized metal ion affinity chromatography (IMAC). Receptor crystallization was performed by the lipidic cubic phase (LCP) method. The protein-LCP mixture contained 40% (w/w) concentrated receptor solution, 54% (w/w) monoolein, and 6% (w/w) cholesterol. Crystals were grown in 40 nL protein-laden LCP bolus overlaid by 0.8 μL of precipitant solution (25–30% (v/v) PEG 400, 100–200 mM potassium sodium tartrate tetrahydrate, 100 mM BIS-TRIS propane [pH 6.4]) at 20 °C. Crystals were harvested directly from LCP matrix and flash frozen in liquid nitrogen. X-ray diffraction data were collected at 100 K on the 23ID-B/D beamline (GM/CA CAT) of the Advanced Photon Source at the Argonne National Laboratory using a 10 μm collimated minibeam. Diffraction data from 23 crystals were merged for the final dataset. Data collection, processing, structure solution and refinement are described in Methods online. Full Methods and any associated references are available in the online version of the paper at (web).
Thompson A.A., Liu W., Chun E., Katritch V., Wu H., Vardy E., Huang X.P., Trapella C., Guerrini R., Calo G., Roth B.L., Cherezov V, & Stevens R.C. (2012). Structure of the Nociceptin/Orphanin FQ Receptor in Complex with a Peptide Mimetic. Nature, 485(7398), 395-399.
Isolation and culture of canine BMSCs: Three healthy beagle dogs (male, 3 years old) were used in the present study. This study was conducted under Nihon University Animal Care and Use Committee approval (AP12B015). All dogs were premedicated intravenously with midazolam hydrochloride (0.2 mg/kg; Astellas Pharma Inc., Tokyo, Japan) and butorphanol tartrate (0.2 mg/kg; Meiji Seika Pharma Co., Ltd., Tokyo, Japan). Anesthesia was induced with an intravenous injection of propofol (4.0 mg/kg; Intervet K.K., Osaka, Japan) and maintained with 1.5 to 2.0% isoflurane (Intervet K.K.) in 100% oxygen given in an endotracheal tube. Butorphanol tartrate (0.2 mg/kg) was again administered intravenously for pain relief before awakening. Canine BMSCs were isolated as described previously [8 (link), 20 (link)]. Briefly, canine bone marrow was aspirated from the humerus, and mononuclear cells were separated by density gradient centrifugation using Histopaque-1077 (Sigma-Aldrich Inc., St. Louis, MO, U.S.A.). Following collection, the mononuclear cells were then transferred to a 75-cm2 plastic culture flask (Corning Inc. Life Sciences, Lowell, MA, U.S.A.) and static-cultured in an incubator at 5% CO2 and 37°C using α-modified Eagle minimum essential medium (Life Technologies Co., Carlsbad, CA, U.S.A.) with 10% fetal bovine serum (FBS; Life Technologies Co.). On the fourth day of culture, nonadherent cells were removed when the culture medium was replaced, thus isolating canine BMSCs. Canine BMSCs were harvested using 0.25% trypsin-ethylenediaminetetraacetic acid (Life Technologies Co.) once they reached approximately 90% confluence. Then, the collected cells were seeded at a density of 14,000 cells/cm2. The second-passage canine BMSCs were used for the following all experiments. Flow cytometry: Cultured canine BMSCs were characterized by flow cytometry analysis based on the previous report [31 (link)]. The cells were placed in 5 ml round-bottom tubes (BD Biosciences, Tokyo, Japan) at 1 × 105 cells/tube with phosphate buffered saline (PBS; Sigma-Aldrich Inc.) containing 0.5% FBS and incubated with antibodies, including the anti-human CD29 mouse monoclonal antibody (eBioscience Inc., San Diego, CA, U.S.A.), the PE-conjugated anti-canine CD34 mouse monoclonal antibody (eBioscience Inc.), the anti-human/mouse CD44 rat monoclonal antibody (eBioscience Inc.) and the FITC-conjugated anti-canine CD45 rat monoclonal antibody (eBioscience Inc.) at 4°C for 45 min. Alexa fluor® 488-conjugated goat anti-mouse or rat IgG antibody (Life Technologies Co.) was used to label anti-CD29 and anti-CD44 antibodies, respectively, in darkness at 4°C for 30 min. To exclude dying cells, propidium iodide (Life Technologies Co.) was added at a final concentration of 2.5 µg/ml. An equal number of cells incubated with respective isotype control antibodies or only secondary antibodies were used as a control sample. The data were analyzed by recording 10,000 events on BD FACS Canto™ (BD Biosciences) by means of BD FACS Diva™ software (BD Biosciences) and FLOWJO software (Tree star Inc., Ashland, OR, U.S.A.). Neuronal induction using bFGF: Canine BMSCs were placed in a 25-cm2 plastic culture flask (Corning Inc. Life Sciences) at a density of 4,000 cells/cm2. The neuronal induction using bFGF was conducted as described previously [10 (link), 37 (link)]. Briefly, the medium was changed to Neurobasal-A medium (Life Technologies Co.) supplemented with 2% B-27 supplement (Life Technologies Co.) and 100 ng/ml recombinant human bFGF (Immunostep, Salamanca, Spain) at 24 hr of passage. Neurobasal-A medium supplemented with 2% B-27 supplement without bFGF was used as the medium in the control group. The neuronal induction medium was changed every 3 days. The cells were harvested using 0.25% trypsin-ethylenediaminetetraacetic acid at 0, 3, 5 and 10 days after the treatment, and their viability was assessed by means of a trypan blue exclusion assay (Wako Pure Chemical Industries Ltd., Osaka, Japan). The morphology of these cells was evaluated under an inverted microscope at indicated time points. Real-time RT-PCR: Total RNAs were extracted from canine BMSCs before and after 3, 5, 10 days of the incubation with bFGF by using TRIzol® reagent (Life Technologies Co.). Canine BMSCs incubated in Neurobasal-A medium supplemented with 2% B-27 supplement without bFGF were used as a control group. The first-strand cDNA synthesis was carried out with 500 ng of total RNA using PrimeScript® RT Master Mix (TaKaRa Bio Inc., Otsu, Japan). Real-time RT-PCRs were performed with 2 µl of the first-strand cDNA in 25 µl (total reaction volume) with primers specific for canine neuronal (microtubule-associated protein 2 [MAP2], neurofilament light chain [NF-L] and neuron-specific enolase [NSE]), neural stem cells (nestin [NES]) and glial (glial fibrillary acidic protein [GFAP]) markers (Table 1
Primers for Real-time RT-PCR
Gene Name
Gene bank ID
Primer sequences
Microtubule-associated protein 2 (MAP2)
XM_845165.1
F: 5′-AAGCATCAACCTGCTCGAATCC-3′
R: 5′-GCTTAGCGAGTGCAGCAGTGAC-3′
Neurofilament light chain (NF-L)
XM_534572.2
F: 5′-TGAATATCATGGGCAGAAGTGGAA-3′
R: 5′-GGTCAGGATTGCAGGCAACA-3′
Neuron-specific enolase (NSE)
XM_534902.2
F: 5′-GCATCCAGGCAGAGCAATCA-3′
R: 5′-AATGGGTGGATGCAGCACAA-3′
Nestin (NES)
XM_547531.2
F: 5′-GGACGGGCTTGGTGTCAATAG-3′
R: 5′-AGACTGCTGCAGCCCATTCA-3′
Glial fibrillary acidic protein (GFAP)
XM_537614.2
F: 5′-GCAGAAGTTCCAGGATGAAACCA-3′
R: 5′-TCTCCAGATCCAGACGGGCTA-3′
Glucuronidase β (GUSB)
NM_001003191.1
F: 5′-ACATCGACGACATCACCGTCA-3′
R: 5′-GGAAGTGTTCACTGCCCTGGA-3′
) and SYBR® Premix Ex Taq™ II (TaKaRa Bio Inc.). The real-time RT-PCRs of no template controls were performed with 2 µl of RNase- and DNA-free water. In addition, real-time PCRs of no-reverse transcription controls were performed with 2 µl of each RNA sample. The PCRs were conducted using Thermal Cycler Dice® Real Time System II (TaKaRa Bio Inc.). The PCR reactions consisted of 1 cycle of denaturing at 95°C for 30 sec, 40 cycles of denaturing at 95°C for 5 sec and annealing and extension at 60°C for 30 sec. The specificity of each primer was verified using dissociation curve analysis and direct sequencing of each PCR product. The results were analyzed by means of the second derivative method and the comparative cycle threshold (ΔΔCt) method using TP900 DiceRealTime v4.02B (TaKaRa Bio Inc.). Amplification of β-glucuronidase [GUSB] from the same amount of cDNA was used as an endogenous control, and the amplification of the cDNA from non-treated canine BMSCs (0 day) was used as a calibrator standard. Western blotting: Canine BMSCs before and after 3, 5 and 10 days of the induction with or without bFGF were lysed with lysis buffer containing 100 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, 1 mM phenylmethanesulfonyl fluoride and complete mini EDTA-free protease inhibitor cocktail (Roche, Mannheim, Germany) at pH 7.4. Protein concentrations were adjusted using Bradford’s method [2 (link)]. Extracted proteins were boiled at 95°C for 5 min in sodium dodecyl sulfate buffer. Samples containing 10 µg of protein were loaded in each lane of 7.5% Mini-PROTEAN TGX gel (Bio-Rad, Hercules, CA, U.S.A.) and electrophoretically separated. Separated proteins were transferred to Immobilon-P Transfer Membranes (Merck Millipore, Billerica, MA, U.S.A.), treated with Block Ace (DS Pharma Biomedical, Osaka, Japan) for 50 min at room temperature and incubated for 120 min at room temperature with the primary antibodies: anti-human neurofilament light chain (NF-L) protein mouse monoclonal antibody (1:100; Thermo Fisher Scientific Inc., Rockford, IL, U.S.A.), anti-human neuron-specific enolase (NSE) mouse monoclonal antibody (1:200; DAKO North America Inc., Carpinteria, CA, U.S.A.) and anti-β-actin mouse monoclonal antibody (1:5,000; Sigma-Aldrich Inc.). After washing, the membranes were incubated with horseradish peroxidase-conjugated anti-mouse IgG (1:10,000; GE Healthcare, Piscataway, NJ, U.S.A.) for 90 min at room temperature. Immunoreactivity was detected using ECL Western blotting Analysis System (GE Healthcare). The chemiluminescent signals of the membranes were measured using ImageQuant LAS 4000 mini (GE Healthcare). Immunocytochemistry: Canine BMSCs were seeded on 35-mm glass base dish (Iwaki, Tokyo, Japan) and cultured for 24 hr. Before and after 10 days of the neuronal induction with or without bFGF, these cells were fixed in 4% paraformaldehyde (Nacalai Tesque Inc., Kyoto, Japan) for 15 min and processed for immunocytochemistry to examine the protein expression and the cellular localization of neuronal markers. The fixed cells were permeabilized by means of incubation in 0.2% Triton™ X-100 (Sigma-Aldrich Inc.) for 15 min at room temperature. Non-specific antibody reactions were blocked for 30 min with a serum-free blocking solution (DAKO North America Inc.). These cells were then incubated for 90 min at room temperature with primary antibodies: an anti-human NF-L protein mouse monoclonal antibody (Thermo Fisher Scientific Inc.) and an anti-human NSE mouse monoclonal antibody (DAKO North America Inc.). After a wash with PBS, these cells were incubated and visualized with Alexa fluor® 594-conjugated F (abʹ)2 fragments of goat anti-mouse IgG (H+L) (Life Technologies Co.), Alexa fluor® 488-conjugated phalloidin (Life Technologies Co.) and TO-PRO®-3-iodide (Life Technologies Co.) for 60 min in darkness at room temperature. The cells were also incubated with only secondary antibodies to control for nonspecific binding of the antibodies. Canine spinal cords were used as a positive control. These samples were washed 3 times with PBS, dried, mounted with ProLong® Gold Antifade Reagent (Life Technologies Co.) and observed with a confocal laser scanning microscope (LSM-510; Carl Zeiss AG, Oberkochen, Germany). Ca2+ imaging: Canine BMSCs were seeded on 35-mm glass base dishes at a density of 4,000 cells/cm2. After 10 days of the neuronal induction with or without bFGF, the cells were incubated in 1 ml of Neurobasal-A medium containing 2% B-27 supplement and 4.0 µM Fluo3-AM (Dojindo Lab., Kumamoto, Japan) with or without 100 ng/ml bFGF for 30 min at 37°C in the dark. Following incubation, the cells were washed twice in PBS. After washing, the culture medium was changed to a Ca2+ imaging buffer (containing 120 mM NaCl, 5 mM KCl, 0.96 mM NaH2PO4, 1 mM MgCl2, 11.1 mM glucose, 1 mM CaCl2, 1 mg/ml bovine serum albumin and 10 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid; pH 7.4). The glass base dishes with the fluorescent dye-loaded cells were placed at room temperature on the stage of a confocal laser scanning microscope (LSM510). Fluorescence of the dye was produced using excitation from a 75-W xenon arc lamp with appropriate filter sets (excitation 488 nm and emission 527 nm). Frames in a time lapse sequence were captured every 2 sec. After baseline images were acquired, the cells were stimulated with 50 mM KCl (Wako Pure Chemical Industries Ltd.) or 100 µM L-glutamate (Wako Pure Chemical Industries Ltd.). The relative changes in intracellular Ca2+ concentrations over time were expressed as relative change in baseline fluorescence. Inhibitor treatments: Canine BMSCs were placed in a 25-cm2 plastic culture flask at a density of 4,000 cells/cm2. The cells were pretreated with Neurobasal-A medium supplemented with 2% B-27 supplement containing the fibroblast growth factor receptor (FGFR) inhibitor SU5402 (25 µM; Sigma-Aldrich Inc.), the phosphoinositide 3-kinase (PI3K) inhibitor LY294002 (50 µM; Cell Signaling Technology Japan K.K., Tokyo, Japan) or the Akt inhibitor MK2206 (1 µM; Selleck chemicals Llc., Houston, TX, U.S.A.) for 1 hr as previously reported methods with slight modifications [37 (link)], and then, neuronal induction using bFGF (100 ng/ml) was performed. After 3 days of the neuronal induction using bFGF, total RNAs were extracted from each sample, and then, real-time RT-PCRs were performed to evaluate the mRNA expression of MAP2 as described above. Data analysis: The data for these experiments were calculated as mean ± standard error. Statistical analyses were performed using StatMate IV (ATMS, Tokyo, Japan). The comparison of the data between the bFGF group and the control group was analyzed by means of the unpaired t test. The data from the time course study by real-time RT-PCR were analyzed using two-way analysis of variance, and Tukey’s test was used as post hoc analysis. The data from the inhibitor study were analyzed using one-way analysis of variance, and Tukey’s test was used as post hoc analysis. The values of P less than 0.05 were considered significant.
NAKANO R., EDAMURA K., NAKAYAMA T., TESHIMA K., ASANO K., NARITA T., OKABAYASHI K, & SUGIYA H. (2014). Differentiation of canine bone marrow stromal cells into voltage- and glutamate-responsive neuron-like cells by basic fibroblast growth factor. The Journal of Veterinary Medical Science, 77(1), 27-35.
Following the standard protocol for the Micro BCA Protein Assay Kit (23235#, Pierce Company), the working reagent (WR) was prepared from 25 parts of MA (sodium carbonate, sodium bicarbonate and sodium tartrate in 0.2 N NaOH), 24 parts of MB (4% BCA in water) and 1 part of MC (4% cupric sulfate, pentahydrate in water). A series of WR with increasing BCA was prepared with varying MB present in 24, 36.5, 49, 74, and 124 parts. The volumes of all WR solutions were kept constant by adding pure water so that only the BCA concentration varied. The pH value of all WR solutions was 11.16±0.06 measured with an Orion 310 pH meter. Twelve BSA solutions with concentrations ranging from 0.02 to 40 mg/mL were prepared by dissolving BSA powder (purity ≥ 99.9%, purchased from Bailingke Company, Beijing) in pure water. After mixing one part BSA solution with seven parts WR, a total of sixty solutions with varying concentrations of protein or BCA were obtained. The concentration given in the experimental results is that in the final mixture, and only the concentration of copper ions was invariant, 0.4 mM in all sample solutions. Each measurement was performed in duplicate. The samples were incubated at 60 ˚C for one hour before cooling to room temperature in accordance with the standard procedures. All the absorbances were corrected by the corresponding blank replicate. The absorbance of the blank solution was 0.048±0.006. Absorbance at 562 nm was measured by spectrophotometer (Tianmei Company, Beijing) using glass cuvettes with optical path length of 0.1 cm.
Huang T., Long M, & Huo B. (2010). Competitive Binding to Cuprous Ions of Protein and BCA in the Bicinchoninic Acid Protein Assay. The Open Biomedical Engineering Journal, 4, 271-278.
Preparation of reagents: 10 g of 3,5-dinitrosalicylic acid plus 2 g of phenol, 0.5 g of sodium sulphite and 10 g of sodium hydroxide were dissolved in 800 mL of water. The volume was adjusted to 1 L and the solution stored in a sealed Duran bottle at room temperature (stable for >2 months). Rochelle’s salt solution was prepared by dissolving 80 g of potassium sodium tartrate in 120 mL of water and then adjusting the volume to 200 mL with water. The solution was stored in a sealed Duran bottle at room temperature and is stable for several years.
Preparation of substrate solutions: 1.0 g of beechwood xylan, birchwood xylan or wheat flour arabinoxylan was added to 90 mL of 100 mM sodium acetate buffer (pH 4.5) and dissolved by stirring at approximately 50 °C for 10 min on a magnetic stirrer hotplate. The volume was adjusted to 100 mL with 100 mM sodium acetate buffer (pH 4.5) and the solution stored in a well-sealed Duran bottle at room temperature. Substrate was also prepared in 100 mM sodium phosphate buffer (pH 6.0) using the same procedure. Two drops of toluene was added to each bottle to prevent microbial contamination.
Preparation of endo-xylanase preparations: Pure suspensions of endo-xylanase in ammonium sulphate (3.2 M) as supplied by Megazyme (see “Materials” section) were centrifuged in a microfuge at 13,000 rpm for 6 min and the supernatant solution removed with a micropipettor and discarded. The enzyme pellet was dissolved in 1 mL of either 100 mM sodium acetate buffer (pH 4.5) containing bovine serum albumin (BSA), (0.5 mg/mL) or 100 mM sodium phosphate buffer (pH 6.0) containing BSA (0.5 mg/mL), depending on the pH optima of the enzyme. This solution was then added to 9 mL of the same buffer and then further diluted in the same buffer to an enzyme concentration suitable for assay and stored on ice between use. A. niger and T. viride endo-xylanases were dissolved in acetate buffer at pH 4.5 whereas N. patriciarum and C. mixtus xylanases were dissolved in phosphate buffer at pH 6.0.
Assay procedure: Multiple aliquots of 1.8 mL of substrate solution in 16 × 120 mm glass test tubes were pre-equilibrated for 5 min at 40 °C. The reaction was initiated by adding 0.2 mL of pre-equilibrated, suitably diluted endo-xylanase solution and incubating the tubes at 40 °C. The reaction was terminated after various time intervals by adding 3 mL of DNSA reagent solution with vigorous stirring. Reagent blanks were prepared by adding 3 mL of DNSA reagent to 1.8 mL of substrate solution plus 0.2 mL of the buffer solution as used in the assay, and the tube contents were mixed immediately. Enzyme blanks were prepared by adding 3 mL of DNSA reagent to 1.8 mL of substrate solution plus 0.2 mL of the enzyme solution as used in the assay and the tube contents mixed immediately. The xylose/xylo-oligosaccharide standards were prepared by adding 3 mL of DNSA solution to 1.8 mL substrate solution plus 0.2 mL of xylose or xylo-oligosaccharide standard (0–2 μmoles/0.2 mL). All tubes (reaction, reagent blanks, enzyme blanks and xylose and xylo-oligosaccharide standards) were placed in a boiling water bath and incubated for 15 min. The tubes were removed from the boiling water bath, and 1 mL of 40 % Rochelles salt solution was added immediately and the tube contents mixed immediately on a vortex mixer. The tubes were cooled at room temperature over approximately 15 min, and the contents were then re-mixed. The absorbance of the xylose and xylo-oligosaccharide standards was measured against the reagent blank at 540 nm. Concurrently, the absorbance of the reaction solutions was measured against the enzyme blank at 540 nm. The rate of hydrolysis was calculated as micromoles of xylose reducing sugar equivalent released per minute. One unit of A. niger endo-xylanase activity is defined as the amount of enzyme required to release 1 μmole of xylose reducing sugar equivalents per minute from the xylan or arabinoxylan substrate at pH 4.5 and at 40 °C.
McCleary B.V, & McGeough P. (2015). A Comparison of Polysaccharide Substrates and Reducing Sugar Methods for the Measurement of endo-1,4-β-Xylanase. Applied Biochemistry and Biotechnology, 177(5), 1152-1163.
Tissue sections from each experimental group were stained by tartrate-resistant acid phosphatase (TRAP) to detect the activity of osteoclasts in the endplate of the lumbar disc cartilage in mice and to quantify the number of osteoclasts (N.Oc/TA) as previously described. Briefly, anhydrous sodium acetate, sodium tartrate and glacial acetic acid were prepared into a 200-mL base working solution and preheated at 37 °C. The slices were dewaxed and rehydrated into the base working solution with naphthol AS-BI phosphate and baked at 37 °C for 1 h. Then, transfer to another base working solution mixed with sodium nitrite and basic magenta and incubate for 5–10 min; the color appears to terminate the staining. Finally, alcohol-free hematoxylin staining was used as the background color.
Wang X., Zeng Q., Ge Q., Hu S., Jin H., Wang P.E, & Li J. (2024). Protective effects of Shensuitongzhi formula on intervertebral disc degeneration via downregulation of NF-κB signaling pathway and inflammatory response. Journal of Orthopaedic Surgery and Research, 19, 80.
For the staining of tartrate-resistant acid phosphatase (TRAP), lumbar spine paraffin sections from two-week-old mice were incubated in a substrate solution (40 mmol/L sodium acetate, 10 mmol/L sodium tartrate, 1.6 mmol/L fast red violet, 700 mmol/L naphthol, pH 5; all chemicals Sigma-Aldrich) for 90 min and counterstained with Mayer’s hematoxylin (Sigma-Aldrich). Quantification was performed using the Osteomeasure (OsteoMetrics, Inc.) system as follows: The hypertrophic zone and underlying primary spongiosa were marked as “bone” and TRAP-positive cells were marked as “osteoclasts”. The parameter number of osteoclasts per bone perimeter (N.Oc/B.Pm) was derived, which represents the number of TRAP-positive cells per tissue perimeter (TRAP+ cells/T.Pm in mm−1).
Brylka L.J., Alimy A.R., Tschaffon-Müller M.E., Jiang S., Ballhause T.M., Baranowsky A., von Kroge S., Delsmann J., Pawlus E., Eghbalian K., Püschel K., Schoppa A., Haffner-Luntzer M., Beech D.J., Beil F.T., Amling M., Keller J., Ignatius A., Yorgan T.A., Rolvien T, & Schinke T. (2024). Piezo1 expression in chondrocytes controls endochondral ossification and osteoarthritis development. Bone Research, 12, 12.
Ethyl acetate, chloroform, methanol, ethylene, n-hexane, gallic acid, sodium hydro-oxide, dimethyl sulfoxide, acarbose, buffer solution, potassium sodium tartrate, DNS (3,5-dinitrosalicylic acid), amylase (aspergillus), etc. were used in the experiments. Majority of the reagents were purchased from Sigma-Alrdich (Steinheim, Germany).
Ishtiaq H., Ahmad B., Zahid N., Bibi T., Khan I., Azizullah A., Ahmad K., Murshed A., Rehman S.U., Abdel-Maksoud M.A., El-Tayeb M.A., Lu J, & Zaky M.Y. (2024). Phytochemicals, Antioxidant, and Antidiabetic Effects of Ranunculus hirtellus Aerial Parts and Roots: Methanol and Aqueous Extracts. ACS Omega, 9(20), 21805-21821.
The total sugar content was determined by the phenol-sulfuric acid method. The determination of reducing sugar content was carried out using the sodium hydroxide, 3,5-dinitrosalicylic acid (DNS), potassium sodium tartrate method. The protein content was determined using the BCA method.
Xiao L., Sunniya H., Li J., Kakar M.U., Dai R, & Li B. (2024). Isolation and purification of polysaccharides from Bupleurum marginatum Wall.ex DC and their anti-liver fibrosis activities. Frontiers in Pharmacology, 15, 1342638.
The titanium monolithic electrode was purchased from Kunshan Guangjiayuan New Material Co., Ltd., China. Iron chloride (FeCl3·6H2O), potassium sodium tartrate (KNaC4H6O6), DMSO–d6, maleic acid (C4H4O4), sodium nitrate (NaNO3), potassium hydroxide (KOH), potassium nitrate (K15NO3) and ethanol were purchased from Sinopharm Chemical Regent Company. All chemicals were used without further purification.
Dai J., Tong Y., Zhao L., Hu Z., Chen C.T., Kuo C.Y., Zhan G., Wang J., Zou X., Zheng Q., Hou W., Wang R., Wang K., Zhao R., Gu X.K., Yao Y, & Zhang L. (2024). Spin polarized Fe1−Ti pairs for highly efficient electroreduction nitrate to ammonia. Nature Communications, 15, 88.
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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.
Sodium potassium tartrate is a chemical compound commonly used as a laboratory reagent. It is a white crystalline solid with the chemical formula KNaC₄H₄O₆. The compound acts as a buffer, maintaining a stable pH in various laboratory applications.
Naphthol AS-MX phosphate is a laboratory reagent used as a substrate in enzyme-linked immunosorbent assay (ELISA) and other biochemical assays. It is a chromogenic substrate that produces a colored product when cleaved by the enzyme alkaline phosphatase. The core function of Naphthol AS-MX phosphate is to serve as a detection system in various analytical techniques.
Fast red violet LB salt is a chemical compound used as a laboratory reagent. It is a diazonium salt that can be used in various biochemical and histological applications, such as the detection of alkaline phosphatase activity. The product's core function is to serve as a chromogenic substrate, allowing for the visualization of specific enzymatic reactions or the localization of target analytes.
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3,5-dinitrosalicylic acid is a chemical compound commonly used as a laboratory reagent. It is a yellow crystalline solid with the molecular formula C7H5N2O5. The primary function of 3,5-dinitrosalicylic acid is to serve as a colorimetric reagent for the detection and quantification of reducing sugars in various analytical applications.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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Sodium carbonate is a water-soluble inorganic compound with the chemical formula Na2CO3. It is a white, crystalline solid that is commonly used as a pH regulator, water softener, and cleaning agent in various industrial and laboratory applications.
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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.
Potassium sodium tartrate tetrahydrate is a chemical compound that serves as a crystalline solid. It is commonly used as a laboratory reagent and in the production of Rochelle salt.
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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.
Sodium tartrate is a versatile chemical compound with a variety of applications in scientific research and industries. It is commonly used as a buffer, a complexing agent, and a food additive. In biochemistry and analytical chemistry, sodium tartrate is often employed as a buffer to maintain a desired pH. It is also used as a complexing agent to improve the solubility and stability of other compounds. Additionally, sodium tartrate is utilized as a food additive, where it can serve as a preservative, a stabilizer, or a flavor enhancer.
Working with sodium tartrate can be challenging due to the large volume of available literature on the subject. Researchers often need to find the most reliable and effective protocols for their specific experiments, which can be time-consuming and error-prone. The sheer amount of information can make it difficult to identify the best practices and ensure reproducibility in their sodium tartrate-related studies.
PubCompare.ai's AI-driven research protocol comparison can help researchers streamline their sodium tartrate experiments and improve reproducibility. The platform allows users to easily locate the best protocols from literature, pre-prints, and patents, while its AI-powered comparisons ensure the most reliable and effective methods are identified. This can save researchers time, reduce errors, and enable them to focus on advancing their sodium tartrate-related studies. PubCompare.ai's platform can assist researchers in screening protocol literature more efficiently and leveraging AI to pinpoint critical insights, helping them identify the most effective protocols for their specific research goals.
Yes, there are different variations or types of sodium tartrate. The compound can exist in various hydration states, such as anhydrous sodium tartrate and sodium tartrate dihyclrate. Additionally, sodium tartrate can be found in different enantiomeric forms, including the D-isomer, the L-isomer, and the racemic mixture. The specific type of sodium tartrate used can depend on the application and the researchers' needs, as the different variations may have slightly different chemical and physical properties.
Sodium tartrate has a wide range of applications in scientific research and various industries. In biochemistry, it is used as a buffer to maintain pH in enzymatic reactions and protein purification processes. In analytical chemistry, sodium tartrate is employed as a complexing agent to improve the solubility and stability of analytes, enabling more accurate measurements. In materials science, sodium tartrate has been studied for its potential applications in areas such as catalysis, electrochemistry, and the synthesis of novel materials. Additionally, sodium tartrate is used as a food additive, where it can act as a preservative, a stabilizer, or a flavor enhancer.
More about "Sodium tartrate"
Sodium tartrate, also known as Rochelle salt, is a chemical compound with the chemical formula Na2C4H4O6.
It is a salt of tartaric acid and is widely used in scientific research and various industries.
Sodium tartrate is commonly employed as a buffer, complexing agent, and food additive due to its unique properties.
In biochemistry, sodium tartrate is often utilized as a buffer to maintain specific pH levels in experiments involving enzymes, proteins, and other biomolecules.
It is also used as a complexing agent to facilitate the extraction and purification of various compounds.
Within analytical chemistry, sodium tartrate plays a crucial role in colorimetric assays, such as the 3,5-dinitrosalicylic acid (DNS) assay, which is commonly used to measure the reducing sugars produced by enzymatic reactions.
Sodium tartrate can also be used in combination with other compounds, such as sodium hydroxide, potassium sodium tartrate tetrahydrate, and hydrochloric acid, to create buffer systems for various analytical applications.
In materials science, sodium tartrate has been investigated for its potential applications in areas like catalysis, energy storage, and the development of novel materials.
Researchers often explore the use of sodium tartrate as a precursor or template in the synthesis of advanced materials.
To ensure the reliability and effectiveness of their sodium tartrate-related experiments, scientists may consult the available literature, including scientific publications, preprints, and patents.
However, navigating the large volume of information can be challenging.
PubCompare.ai's AI-driven research protocol comparison can help researchers streamline their sodium tartrate experiments, improve reproducibility, and achieve better results by easily identifying the most reliable and effective protocols from the available literature.
By utilizing PubCompare.ai, researchers can save time, reduce errors, and focus on advancing their sodium tartrate-related studies, ultimately contributing to the progress in fields such as biochemistry, analytical chemistry, and materials science.
