Tartrates are a class of organic compounds derived from tartaric acid, a natural compound found in various fruits and wines.
These salts and esters exhibit a wide range of applications in the food, pharmaceutical, and chemical industries.
Tartrates play a crucial role in areas such as wine production, pharmaceuticals, and as chemical precursors.
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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.
The analyses presented here are based on 4257 isolates whose data has been submitted to http://mlst.ucc.ie/mlst/dbs/Senterica by ourselves and others. Of these, 1770 are maintained in the strain collection of MA at University College Cork, and 1042 in the strain collection of FXW at the Institut Pasteur, for a total of 2643 in either or both of those collections. Biotyping and serotyping were performed in multiple laboratories but most of the tests were performed under the supervision of FXW or MC. Serotyping and biotyping were according to the modified Kauffmann-White scheme [2] , except as described below. Basic information on all isolates can be downloaded from the website. In addition, a detailed description of strain properties for Paratyphi B and Java isolates is presented in Table S6. The distinction between Paratyphi B and Java was based on two tests, which gave concordant results after up to 7 days incubation: the lead acetate protocol 1 for d-tartrate fermentation described by Malorny et al. [58] (link) and the ability to grow on d-tartrate as the sole carbon source as described by Weill et al. [64] (link). The start codon of STM3356 was sequenced as described by Malorny et al. [58] (link). Table S7 gives detailed information on results with 6,7:c:1,5 isolates. These were assigned to serovars on the basis of the biochemical properties which are summarized in Table 3, and which are similar to the tests and recommendations by Le Minor et al. [65] . Mucate utilization, ducitol fermentation and H2S production were evaluated after 24 hrs incubation in standard media and tartrate fermentation was evaluated after 7 days, as described above. A separate manuscript is in preparation on differences between the contents of Selander's SARA and SARB collections. The conclusions drawn here were largely based on isolates stored by Kenneth E. Sanderson and corroborated by the collection of Fidelma Boyd. Serovar assignments were according to information uploaded to the website except that many atypical isolates and the Paratyphi B, Java and 6,7:c:1,5 isolates were retyped.
Achtman M., Wain J., Weill F.X., Nair S., Zhou Z., Sangal V., Krauland M.G., Hale J.L., Harbottle H., Uesbeck A., Dougan G., Harrison L.H, & Brisse S. (2012). Multilocus Sequence Typing as a Replacement for Serotyping in Salmonella enterica. PLoS Pathogens, 8(6), e1002776.
Mice with null mutation in the α5 nAChR subunit gene and their wildtype littermates, or male Wistar rats (Charles River Laboratories, Raleigh, NC), were surgically prepared with silastic catheters in the jugular vein and trained to respond on an “active” lever for food pellets under a fixed ratio 5 time-out 20 sec (FR5TO20) schedule of reinforcement. Mice and rats then responded for nicotine infusions on the FR5TO20 sec reinforcement schedule during 1 h daily testing sessions. Nicotine hydrogen tartrate salt was dissolved in sterile saline solution (0.9% w/v). Each nicotine reward earned resulted in the delivery of a nicotine infusion (0.033 ml injection volume delivered over 3-sec in mice; 0.1 ml delivered over 1-sec in rats) and initiated a 20-sec time-out period signaled by a light cue located above the active lever during which responding on the lever was without consequence.
Fowler C.D., Lu Q., Johnson P.M., Marks M.J, & Kenny P.J. (2011). Habenular α5* nicotinic receptor signaling controls nicotine intake. Nature, 471(7340), 597-601.
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.
Varenicline free base (7 g) was dissolved in methanol (140 ml) at 25-30° C. In a separate flask, tartaric acid (4.92 g) was dissolved in 70 ml water at 25-30° C. Varenicline solution was mixed with tartaric acid solution at 25-35° C. The resulting clear solution was stirred for 30 min at 25-35° C. to form the Varenicline tartrate salt solution. Maltodextrin (119.84 g) was dissolved in water (420.53 ml) at 25-35° C. separately and added this Maltodextrin solution into Varenicline tartrate solution prepared earlier. The resulting clear solution was stirred for 30 minutes, filtered through a micron filter and washed with water (2×70 ml). The clear filtrate was subjected to spray drying using a spray dryer to obtain the amorphous Varenicline Tartrate Maltodextrin Premix (1:10) API. Yield: 130.0 g. Purity by HPLC: 99.99%.
US11872234B2. Vareniciline compound and process of manufacture thereof (2024-01-16). Par Pharmaceutical, Inc. [US]. Inventors: Joseph Prabahar Koilpillai [IN], Sayuj Nath [IN], Satish Patil [IN], Somasundaram Muthuramalingam [IN], Selvakumar Viruthagiri [IN], Mohankumar Lakshmanan [IN].
Multinucleated osteoclast-like cells were stained for tartrate-resistant acid phosphatase (TRAP) using a TRAP/ALP Stain Kit (FUJIFILM, Tokyo, Japan) according to the manufacturer’s instructions. Multinucleated TRAP-positive cells with three or more nuclei were considered as osteoclasts.
Wang H., Tang H., Yuan S., Liang C., Li Y., Zhu S, & Chen K. (2024). IL-17A deficiency inhibits lung cancer-induced osteoclastogenesis by promoting apoptosis of osteoclast precursor cells. PLOS ONE, 19(2), e0299028.
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.
The tartrate-resistant acid phosphatase (TRAP) staining kit (MK300, Takara, Tokyo, Japan) was then used to stain for TRAP, an osteoclast marker, according to the manufacturer's instructions.27 (link) After culturing, stained TRAP-positive multinucleated cells with >3 nuclei were identified under an inverted microscope (C13220-01, NanoZoomer S360 Digital slide scanner, Hamamatsu, Shizuoka, Japan) and considered osteoclast-like cells. We analyzed and compared the number of TRAP-positive cells among all concentrations using an NDP.View2 Analyzer (Hamamatsu, Shizuoka, Japan). Three images were captured per well. These images were analyzed using ImageJ software.
Hsieh M.K., Wang C.Y., Kao F.C., Su H.T., Chen M.F., Tsai T.T, & Lai P.L. (2024). Local application of zoledronate inhibits early bone resorption and promotes bone formation. JBMR Plus, 8(5), ziae031.
Tartrate-resistant acid phosphatase (TRAP5b) activity via biochemical assay was measured in supernatants of the cultures after 14/1, 28/14, and 42/28 days in culture, as a marker of osteoclast differentiation and resorption activity [40 (link)]. Briefly, cells were rinsed twice with PBS and lysed with 100 μL lysis buffer (0.1% Triton-X in dH2O) and were subjected to two freeze–thaw cycles. An aliquot of 50 μL was mixed with 50 μL of TRAP reaction solution (2 mg/mL p-nitrophenyl phosphate in 0.1 M glycine with 20 mM sodium tartrate and 2 mM MgCl2 at pH 5). Afterwards, samples were left for 1 h at 37 °C and the absorbance of the reaction was measured at 405 nm in a spectrophotometer (Synergy HTX Multi-Mode Microplate Reader, BioTek, Winooski, VT, USA). The absorbance values were translated into pNP concentrations, with the use of a calibration curve constructed from known pNP values. Normalization was performed to total cellular protein, determined using the Bradford assay (Applichem, Darmstadt, Germany) in the cell lysates.
Kontogianni G.I., Bonatti A.F., De Maria C., Naseem R., Coelho C., Alpantaki K., Batsali A., Pontikoglou C., Quadros P., Dalgarno K., Vozzi G., Vitale-Brovarone C, & Chatzinikolaidou M. (2024). Cell Instructive Behavior of Composite Scaffolds in a Co-Culture of Human Mesenchymal Stem Cells and Peripheral Blood Mononuclear Cells. Journal of Functional Biomaterials, 15(5), 116.
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The Leukocyte acid phosphatase kit is a laboratory reagent designed to measure the activity of acid phosphatase enzyme in white blood cells (leukocytes). It provides a quantitative assessment of this enzyme, which is involved in cellular metabolism and can be used as an indicator of certain medical conditions.
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Nicotine hydrogen tartrate is a chemical compound used in various laboratory applications. It serves as a precursor for the synthesis of nicotine and other related compounds. The compound is a white, crystalline powder with a characteristic odor. It is soluble in water and certain organic solvents. Nicotine hydrogen tartrate is primarily utilized in research and development settings to facilitate the study and production of nicotine-based products.
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The TRAP staining kit is a laboratory product developed by Merck Group. It is used to detect and analyze tartrate-resistant acid phosphatase (TRAP) activity in cells. The kit provides the necessary reagents and protocols to perform TRAP staining, which is a widely used technique in various research applications.
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Nicotine hydrogen tartrate salt is a chemical compound that is used as a laboratory reagent. It is a crystalline solid and is soluble in water and various organic solvents. The compound is commonly used in scientific research and development applications.
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RANKL is a recombinant protein produced in mammalian cells. It is a member of the tumor necrosis factor (TNF) ligand family and plays a key role in the regulation of bone remodeling and immune function.
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M-CSF is a recombinant human protein that functions as a cytokine. It is involved in the differentiation and proliferation of monocytes and macrophages.
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture 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.
Butorphanol tartrate is a synthetic opioid analgesic used as a pharmaceutical ingredient. It functions as a mu-opioid receptor agonist and kappa-opioid receptor agonist.
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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.
