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Inositol

Inositol is a vitamin-like substance found naturally in various foods and produced by the body.
It plays a role in cellular signaling and may have potential therapeutic applications, such as in the management of polycystic ovary syndrome, mood disorders, and neurological conditions.
Researchers can leverage AI-powered tools like PubCompare.ai to enhance their inositol research by identifying the best protocols from the literature, pre-prints, and patents, and optimizing product selection to improve reproducibility and accuaracy.
With the power of AI, inositol research can be taken to new heights, leading to advancements in understanding its physiological functions and clinical utility.

Most cited protocols related to «Inositol»

1
Yeast Cultivation and Transformation Protocols
Saccharomyces cerevisiae CEN.PK102-5B (MATa ura3-52 his3Δ1 leu2-3/112 MAL2-8cSUC2) strain was obtained from Verena Siewers (Chalmers University). Yeast transformants were selected on synthetic complete (SC) drop-out media lacking the amino acids matching the auxotrophic markers on the plasmids used. These SC plates were made from premixed drop-out powders from Sigma-Aldrich. When yeast was grown in liquid media, it was either in SC, Delft, or standard yeast peptone dextrose (YPD) media. Delft contained (L−1): 7.5 g (NH4)2SO4, 14.4 g KH2PO4, 0.5 g MgSO4·7H2O, 22 g dextrose, 2 mL trace metals solution, and 1 mL vitamins. The pH of Delft medium was adjusted to 6 prior to autoclavation. Vitamin solution was added to Delft medium after autoclavation. Vitamin solution was added after autoclavation. The trace metals solution contained (L−1): 4.5 g CaCl2·2H2O, 4.5 g ZnSO4·7H2O, 3 g FeSO4·7H2O, 1 g H3BO3, 1 g MnCl2·4H2O, 0.4 g Na2MoO4·2H2O, 0.3 g CoCl2·6H2O, 0.1 g CuSO4·5H2O, 0.1 g KI, 15 g EDTA. The trace metals solution was prepared by dissolving all the components except EDTA in 900 mL ultra-pure water at pH 6. The solution was then gently heated and EDTA was added. In the end, the pH was adjusted to 4, and the solution volume was adjusted to 1 L and autoclaved (121 °C in 20 min). This solution was stored at + 4 °C. The vitamin solution had (L−1): 50 mg biotin, 200 mg p-aminobenzoic acid, 1 g nicotinic acid, 1 g Ca-pantothenate, 1 g pyridoxine-HCl, 1 g thiamine-HCl, 25 g myo-inositol. Biotin was dissolved in 20 mL 0.1 M NaOH and 900 mL water is added. pH was adjusted to 6.5 with HCl and the rest of the vitamins were added. pH was re-adjusted to 6.5 just before and after adding m-inositol. The final volume was adjusted to 1 L and sterile-filtered before storage at + 4 °C.
All standard cloning was carried out using Escherichia coli strain DH5α, which was grown in standard Luria–Bertani (LB) medium containing 100 μg mL−1 ampicillin. For the cloning of plasmid carrying the ccdB gene and chloramphenicol cassette, E. coli ccdB strain was used as a host strain and transformants were selected on LB medium containing 100 μg mL−1 ampicillin and 25 μg mL−1 chloramphenicol.
Jensen N.B., Strucko T., Kildegaard K.R., David F., Maury J., Mortensen U.H., Forster J., Nielsen J, & Borodina I. (2013). EasyClone: method for iterative chromosomal integration of multiple genes in Saccharomyces cerevisiae. Fems Yeast Research, 14(2), 238-248.
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Publication 2013
4-Aminobenzoic Acid Amino Acids Ampicillin Biotin Chloramphenicol Edetic Acid Escherichia coli Genes Glucose Inositol manganese chloride Metals Nicotinic Acids Peptones Plasmids Powder Pyridoxine Hydrochloride Saccharomyces cerevisiae sodium molybdate(VI) Sterility, Reproductive Strains Sulfate, Magnesium thiamine hydrochloride Vitamins
2
HEK-293T Cells Inositol Phosphate Assay
HEK-293T cells were maintained in DMEM supplemented with 10% fetal bovine serum (FBS), 100 IU/ml penicillin and 100 μg/ml streptomycin. Cells were transfected with 10 μg of receptor DNA per 15 cm cell culture dish and incubated overnight at 37°C in a humidified 5% CO2; the next day, cells were seeded into poly-L-lysine coated 96-well plates in 200 μl per well of DMEM supplemented with 1% dialyzed FBS, 100 IU/ml penicillin and 100 μg/ml streptomycin. After attaching to the plate, cells were incubated for 16 hours as above in inositol-free DMEM (United States Biological, Swampscott, MA) containing 1% dialyzed FBS, and 1 μCi/well of 3H-inositol. Next, cells were washed with 100 μl drug buffer (1X HBSS, 24 mM NaHCO3, 11 mM glucose, 15 mM LiCI, pH 7.4) and treated with 100 μl of drug buffer containing 10 μM drug in quadruplicate for 1 hour at 37°C in a 5% CO2 incubator. Alternatively, for concentration-response curves, cells were treated with a range of concentrations in quadruplicate in 100 μl of drug buffer and incubated for 1 hour at 37°C in a 5% CO2 incubator. Following treatment, drug solution was removed and 40 μl of 50 mM formic acid was added to lyse cells for 30 minutes at 4°C. After cell lysis, 40 μl of acid extracts were transferred to polyethylene terephthalate 96-well sample plate (PE#1450-401) and mixed with 75 μl of Perkin Elmer RNA Binding YSi SPA Beads (#RPNQ0013) at a concentration of 0.2 mg beads/well and incubated for 30 minutes at 4°C. Bead/lysate mixtures were then counted using a Perkin Elmer 2450 MicroPlate Counter.
Kroeze W.K., Sassano M.F., Huang X.P., Lansu K., McCorvy J.D., Giguere P.M., Sciaky N, & Roth B.L. (2015). PRESTO-TANGO: an open-source resource for interrogation of the druggable human GPCR-ome. Nature structural & molecular biology, 22(5), 362-369.
Publication 2015
Acids Bicarbonate, Sodium Biopharmaceuticals Buffers Cell Culture Techniques Cells DNA receptor Fetal Bovine Serum formic acid Glucose HEK293 Cells Hemoglobin, Sickle Hyperostosis, Diffuse Idiopathic Skeletal Inositol Lysine Penicillins Pharmaceutical Preparations Pharmaceutical Solutions Poly A Polyethylene Terephthalates Streptomycin
3
HEK-293T Cells Inositol Phosphate Assay
HEK-293T cells were maintained in DMEM supplemented with 10% fetal bovine serum (FBS), 100 IU/ml penicillin and 100 μg/ml streptomycin. Cells were transfected with 10 μg of receptor DNA per 15 cm cell culture dish and incubated overnight at 37°C in a humidified 5% CO2; the next day, cells were seeded into poly-L-lysine coated 96-well plates in 200 μl per well of DMEM supplemented with 1% dialyzed FBS, 100 IU/ml penicillin and 100 μg/ml streptomycin. After attaching to the plate, cells were incubated for 16 hours as above in inositol-free DMEM (United States Biological, Swampscott, MA) containing 1% dialyzed FBS, and 1 μCi/well of 3H-inositol. Next, cells were washed with 100 μl drug buffer (1X HBSS, 24 mM NaHCO3, 11 mM glucose, 15 mM LiCI, pH 7.4) and treated with 100 μl of drug buffer containing 10 μM drug in quadruplicate for 1 hour at 37°C in a 5% CO2 incubator. Alternatively, for concentration-response curves, cells were treated with a range of concentrations in quadruplicate in 100 μl of drug buffer and incubated for 1 hour at 37°C in a 5% CO2 incubator. Following treatment, drug solution was removed and 40 μl of 50 mM formic acid was added to lyse cells for 30 minutes at 4°C. After cell lysis, 40 μl of acid extracts were transferred to polyethylene terephthalate 96-well sample plate (PE#1450-401) and mixed with 75 μl of Perkin Elmer RNA Binding YSi SPA Beads (#RPNQ0013) at a concentration of 0.2 mg beads/well and incubated for 30 minutes at 4°C. Bead/lysate mixtures were then counted using a Perkin Elmer 2450 MicroPlate Counter.
Kroeze W.K., Sassano M.F., Huang X.P., Lansu K., McCorvy J.D., Giguere P.M., Sciaky N, & Roth B.L. (2015). PRESTO-TANGO: an open-source resource for interrogation of the druggable human GPCR-ome. Nature structural & molecular biology, 22(5), 362-369.
Publication 2015
Acids Bicarbonate, Sodium Biopharmaceuticals Buffers Cell Culture Techniques Cells DNA receptor Fetal Bovine Serum formic acid Glucose HEK293 Cells Hemoglobin, Sickle Hyperostosis, Diffuse Idiopathic Skeletal Inositol Lysine Penicillins Pharmaceutical Preparations Pharmaceutical Solutions Poly A Polyethylene Terephthalates Streptomycin
4
Quantitative Brain Metabolite Mapping by NMR
In vivo 1H NMR spectra were analyzed using LCModel (18 (link),19 (link)). The unsuppressed water signal measured from the same VOI without OVS was used as an internal reference for quantification, assuming 80% brain water content. LC-Model basis sets for 4T and 7T included spectra of 19 brain metabolites: alanine (Ala), ascorbate (Asc), aspartate (Asp), creatine (Cr), phosphocreatine (PCr), γ-aminobutyric acid (GABA), glucose (Glc), glutamate (Glu), glutamine (Gln), glutathione (GSH), glycerophosphorylcholine (GPC), phosphorylcholine (PCho), glycine, myo-inositol (myo-Ins), scyllo-inositol (scyllo-Ins), lactate (Lac), N-acetylaspartate (NAA), N-acetylaspartylglutamate (NAAG), phosphorylethanolamine (PE), and taurine (Tau). All spectra for both 4T and 7T basis sets were simulated using Varian spectrometer spin-simulation software (neglecting J-evolution for ultrashort TE) based on a recently updated database of chemical shifts and coupling constants (20 (link),21 ). Averaged spectra of fast relaxing macromolecules measured from five subjects at 4T and 7T using metabolite nulling inversion-recovery experiments with a short repetition time (TR = 2 s, TI = 0.675 s) were also included in the 4T and 7T LCModel basis sets. Before putting macromolecule spectra into the LCModel basis set, the residual signal of PCr with a short T1 was removed from FIDs and the high-frequency noise was suppressed by the Gaussian filter (σ= 0.05 s). The LCModel analysis was performed on spectra within the chemical shift range 0.5–4.2 ppm. The default value of the LCModel parameter DESDSH, controlling the uncertainty in referencing between in vivo spectra and spectra in the LCModel basis set, was decreased from 0.004 ppm to 0.002 ppm. All four parameters controlling the zero- and first-order phase correction and their deviations were set to zero. The hidden parameter DKNTMN, controlling the knot spacing for the spline baseline fitting, was set to 0.20. LCModel analysis was performed in chemical shift range 0.5–4.2 ppm.
Cramér-Rao lower bounds (CRLB) of LCModel analysis were used to eliminate meaningless fitting results with extremely high estimated errors. Metabolites quantified with CRLB above 100% were excluded from further analysis. If a metabolite was not quantified with CRLB < 100% in at least 50% of analyzed spectra of a given subject and a given number of summed transients, then this metabolite was eliminated from further analysis for this subject and NT. If a metabolite was not quantified from spectra with a given NT for at least five subjects, then this metabolite was eliminated from further analysis. Finally, if the average CRLB of a specific metabolite was higher than 50%, this metabolite was considered “not detectable” under these conditions (B0, NT). The correlation matrix from the detailed LCModel output was used to evaluate the correlation between fitted concentrations of metabolites with similar spectral patterns and high spectral overlap. t-Tests with and without corrections for multiple comparisons were used to evaluate the statistical significance of differences between 4T and 7T data. Average values are always reported as mean ± SD.
Tkáč I., Öz G., Adriany G., Uğurbil K, & Gruetter R. (2009). In Vivo 1H NMR Spectroscopy of the Human Brain at High Magnetic Fields: Metabolite Quantification at 4T vs. 7T. Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine, 62(4), 868-879.
Publication 2009
1H NMR Alanine Aspartate Biological Evolution Brain Creatine gamma Aminobutyric Acid Glucose Glutamate Glutamine Glycerylphosphorylcholine Glycine Inositol Inversion, Chromosome Lactates N-acetyl-aspartyl-glutamate N-acetylaspartate Phosphocreatine phosphoethanolamine Phosphorylcholine scyllitol Taurine Transients
5
Resolving Inositol Polyphosphates by PAGE
Inositol polyphosphates were resolved using 24×16×0.1 cm gel using 33.3% polyacrylamide gel in TBE (31.7 ml 40% Acr/Bis (19∶1); 3.8 ml 10× TBE; 2.2 ml H20; 270 µl 10% APS; 30 µl TEMED). Gels were pre-run for 20 minutes at 300 volts. Then 5–10 µl of 6× Dye (10 mM TrisHCl pH 7.0; 1 mM EDTA; 30% glycerol; 0.1% Orange G) was added to each sample prior to loading onto gels. Gels were run at 300–400 volts overnight at 4°C until the Orange G dye front reached 10 cm from the gel's bottom. To analyse in gel radioactivity distribution, serial, one cm gel fragments were cut after DAPI staining over a UV transilluminator. Gel fragments were incubated overnight with 1–2 ml of the gel solubilizer Solusol; 15–20 ml of Solucint-O cocktail was added and radioactivity was assessed with a β-counter.
Losito O., Szijgyarto Z., Resnick A.C, & Saiardi A. (2009). Inositol Pyrophosphates and Their Unique Metabolic Complexity: Analysis by Gel Electrophoresis. PLoS ONE, 4(5), e5580.
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Publication 2009
DAPI Edetic Acid Glycerin Inositol Orange G polyacrylamide gels Polyphosphates Radioactivity

Most recents protocols related to «Inositol»

1
Cultivation of NK92 and Pancreatic Cancer Cell Lines
Human natural killer cell line NK92 was purchased from the American Type Culture Collection and grown in α-MEM medium (Cat. No.12571089; Life Technologies, Carlsbad, CA, USA) supplemented with 12.5% fetal bovine serum (FBS; Cat. No.1614007; Gibco, Grand Island, NY, USA), 12.5% horse serum (Cat. No. 26050070; Gibco), 1.5 g/L sodium bicarbonate, 2 mM L-glutamine (Cat. No. 25030149; Gibco), 100 to 200 U/ml recombinant IL-2 (Cat. No. 200-02; PeproTech, Rocky Hill, NJ, USA,), 0.1 mM 2-mercaptoethanol, 0.2 mM inositol (Cat. No. I5125; Sigma-Aldrich, St. Louis, MO, USA), 0.02 mM folic acid, and 1% penicillin-streptomycin solution (Cat. No. SV30010; Solarbio, Beijing, China). Mouse pancreatic carcinoma cell line PAN02 and human pancreatic carcinoma cell line PANC28, PANC1, SW1990 were purchased from the American Type Culture Collection and cultured in DMEM medium contained 10% FBS (Gibco, Gaithersburg, MD, USA) at 37 °C in an atmosphere of 5% CO2.
Guo D., Jin C., Gao Y., Lin H., Zhang L., Zhou Y., Yao J., Duan Y., Ren Y., Hui X., Ge Y., Yang R, & Jiang W. (2023). GPR116 receptor regulates the antitumor function of NK cells via Gαq/HIF1α/NF-κB signaling pathway as a potential immune checkpoint. Cell & Bioscience, 13, 51.
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Publication 2023
2-Mercaptoethanol Atmosphere Bicarbonate, Sodium Cell Lines Culture Media Equus caballus Folic Acid Glutamine Homo sapiens Inositol Mus Natural Killer Cells Pancreatic Carcinoma Penicillins Serum Streptomycin
2
Molecular Weight Distribution and Monosaccharide Composition of Crude EPS
Molecular weight distributions of lyophilized crude EPS were determined by size exclusion chromatography. In brief, crude EPS powder was suspended in 0.1 M NaNO3 (0.5 mg/mL) and then filtered through a 0.45 μm pore diameter polyvinylidene fluoride membrane (Millipore Corporation, USA). The average molecular weight (MW) was determined by high-performance molecular exclusion chromatography (HPLC-SEC, Agilent 1,100 Series System, Hewlett-Packard, Germany) associated with a refractive index (IR) detector (Ibarburu et al., 2015 (link)). 50 μL of the samples were injected and eluted at a flow rate of 0.95 mL/min (pressure: 120:130 psi) at room temperature using 0.1 M NaNO3 as mobile phase. Dextrans (0.5 mg/mL) with a molecular weight between 103 and 2.106 Da (Sigma-Aldrich, USA) were used as standards.
Once the molecular weight distributions were determined, low and high molecular weight fractions that composed the crude EPS obtained at 20°C were separated. For this purpose, EPS solutions (0.2% w/v) were centrifuged through a Vivaspin™ ultrafiltration spin column 100 KDa MWCO, (Sartorious, Goettingen, Germany) for 20 min at 6000 g, eluting only the low MW fraction. Subsequently, high MW fraction retained in the column was eluted using hot distilled water. The eluted fractions were passed through a Vivaspin column (cut-off 30KDa) in order to separate the middle and low MW fraction of EPS.
Monosaccharide composition of crude EPS and their fractions were determined by gas chromatography as previously described (Notararigo et al., 2013 (link)). Briefly, 1–2 mg of EPS were hydrolyzed in 1 mL of 3 M trifluoroacetic acid (1 h at 120°C). The monosaccharides obtained were converted into alditol acetates by reduction with NaBH4 and subsequent acetylation. The samples were analyzed by gas chromatography in an Agilent 7890A coupled to a 5975C mass detector, using an HP5-MS column with helium as carrier gas at a flow rate of 1 mL/min. For each run, 1 μL of sample was injected (with a Split 1:50) and the following temperature program was performed: the oven was heat to 175°C for 1 min; the temperature was increased to 215°C at a rate of 2.5°C/min and then increased to 225°C at 10°C/min, keeping it constant at this temperature for 1.5 min. Monosaccharides were identified by comparison of retention times with standards (arabinose, xylose, rhamnose, galactose, glucose, mannose, glucosamine and galactosamine) analyzed under the same conditions. Calibration curves were also processed for monosaccharide quantification. Myo-inositol was added to each sample as internal standard.
Bengoa A.A., Dueñas M.T., Prieto A., Garrote G.L, & Abraham A.G. (2023). Exopolysaccharide-producing Lacticaseibacillus paracasei strains isolated from kefir as starter for functional dairy products. Frontiers in Microbiology, 14, 1110177.
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Publication 2023
Acetates Acetylation Arabinose Dextrans Division Phase, Cell Galactosamine Galactose Gas Chromatography Gel Chromatography Glucosamine Glucose Helium High-Performance Liquid Chromatographies Inositol Mannose Monosaccharides polyvinylidene fluoride Powder Pressure Retention (Psychology) Rhamnose Sugar Alcohols Tissue, Membrane Trifluoroacetic Acid Ultrafiltration Xylose
3
Extraction and Analysis of Striatal Proteins
Cytoplasmic and nuclear lysates were obtained from striatal samples using NE-PER nuclear and cytoplasmic extraction reagents (#78833, Thermo Fisher) per the manufacturer's instructions. Briefly, striatal tissues were washed with neutral pH phosphate-buffered saline (PBS) and centrifuged at 500   ×   g for 5 min. After discarding the supernatant, samples were homogenized with a Dounce homogenizer in ice-cold CER I buffer, vortexed for 15 s, and incubated on ice for 10 min. A 1×  solution of HALT protease and phosphatase inhibitor cocktail (Thermo Fisher) was added to all lysis reagents. Ice-cold CER II reagent was added to the homogenate, after which samples were vortexed and centrifuged at 16,000   ×   g for 5 min. The supernatant (containing the cytoplasmic fraction) was aliquoted and stored at −80oC. To obtain the nuclear fraction, the remaining pellet was resuspended in ice-cold NER solution, vortexed for 15 s every 10 min for a total of 40 min, then centrifuged at 16,000   ×   g for 10 min. Nuclear extracts were aliquoted and stored at −80oC. Protein concentration in lysates was determined by the bicinchoninic acid (BCA) method. 30 µg samples were electrophoresed on 10% Criterion TGX gels (Bio-Rad, Hercules, CA) and transferred to PVDF membranes. Non-specific binding sites on membranes were blocked for 1 h with Intercept blocking buffer (LI-COR, Lincoln, NE) for all kinase blots or 5% non-fat dry milk in Tris-buffered saline/Tween-20 (TBST) for pTDP-43/TDP-43 blots. Membranes were then incubated overnight in primary antibodies directed against pTDP-43 (Ser409/410) (1:1000, # 66318, Proteintech), CK2 (1:1,000, #10992, Proteintech), CK1δ (1:1,000, #14388, Proteintech), and inositol-triphosphate 3-kinase B (ITPKB) (1:1000, #12816, Proteintech) followed by incubation in species-specific HRP-conjugated secondary antibodies (for pTDP-43/TDP-43) or fluorescent-labeled secondary antibodies (for CK2, CK1δ, or ITPKB). For cytoplasmic extracts, GAPDH (# A303-878A; 1:2000; Bethyl Laboratories Inc., Montgomery, TX) was used to assess loading while LI-COR Total Protein Stain (# 92611011, LI-COR) was used to assess loading in nuclear extracts. Images of blots were obtained using a ChemiDoc Imager (Bio-Rad) and western blotting bands were analyzed with the Image Lab software (V6.0.1, Bio-Rad).
Ohene-Nyako M., Nass S.R., Richard H.T., Lukande R., Nicol M.R., McRae M., Knapp P.E, & Hauser K.F. (2023). Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia. ASN NEURO, 15, 17590914231158218.
Publication 2023
Antibodies bicinchoninic acid Binding Sites Cardiac Arrest Cold Temperature Cytoplasm Fluorescent Antibody Technique GAPDH protein, human Gels Inositol Milk, Cow's Peptide Hydrolases Phosphates Phosphoric Monoester Hydrolases Phosphotransferases polyvinylidene fluoride Proteins protein TDP-43, human Saline Solution Stains Striatum, Corpus Tissue, Membrane Tissues triphosphate Tween 20
4
Klebsiella Surveillance in Fattening Pigs
In 2019, caecal samples from fattening pigs sampled at slaughter were included in the NORM-VET surveillance programme [17 ]. Only one pig per herd was included. These samples were available for the current study, and were screened for the presence of Klebsiella spp. Each sample was plated directly onto Simmons citrate agar with 1 % inositol (SCAI; Oxoid) and incubated at 37 °C for 48 h. Presumptive Klebsiella spp. colonies were selected based on morphology, and confirmed as Klebsiella spp. with a MALDI-TOF instrument (Bruker Daltonik).
Kaspersen H., Franklin-Alming F.V., Hetland M.A., Bernhoff E., Löhr I.H., Jiwakanon J., Urdahl A.M., Leangapichart T, & Sunde M. (2023). Highly conserved composite transposon harbouring aerobactin iuc3 in Klebsiella pneumoniae from pigs. Microbial Genomics, 9(2), mgen000960.
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Publication 2023
Agar Cecum Citrate Inositol Klebsiella Pigs Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
5
Metabolic Labeling for GPI-Anchored Proteins
The process of labeling experiments followed a previous protocol (Wang et al., 2020 (link)). For mannose labeling, ∼2 × 106 PIGS-KO, PIGS-HRD1-DKO, and PIGS-HRD1-CD55-TKO cells, and PIGS-HRD1-CD55-TKO cells stably expressing HA-CD55 were precultured in normal medium overnight, washed with wash medium (glucose-free DMEM buffered with 20 mM Hepes, pH 7.4), and incubated for 1 h at 37°C in 1 ml of reaction medium (wash medium supplemented with 10% dialyzed FBS (Gibco), 10 μg ml−1 tunicamycin (Wako), and 100 μg ml−1 glucose). [2-3H] Mannose (American Radiolabeled Chemicals) was added to 25 Ci ml−1 and the cells were incubated for 1 h at 37°C in 5% CO2. The cells were pelleted and washed with 1 ml of cold PBS. Radiolabeled GPIs were extracted with 1-butanol, separated by high-performance thin-layer chromatography (HPTLC; Merck), and visualized using an FLA 7000 analyzer (Fujifilm).
To detect GlcN-PI or GlcN-(acyl)-PI after inositol-labeling, PIGW-KO, PIGS-KO, PIGS-HRD1-DKO, PIGS-HRD1-ARV1-TKO, PIGS-HRD1-CD55-TKO, and HA-CD55 rescued cells were washed with inositol-free DMEM and then incubated in 1 ml of reaction medium B (inositol-free DMEM buffered with 20 mM Hepes, pH 7.4) supplemented with 10% dialyzed FBS in the presence of 10 μCi of myo-[2-3H] inositol (PerkinElmer) for 24 h. After metabolic labeling, the cells were washed twice with 1 ml of cold PBS and pelleted by centrifugation. Lipids and radiolabeled GPIs were extracted with 1-butanol partitioning, separated by HPTLC (Merck), and visualized using an FLA 7000 analyzer.
Liu Y.S., Wang Y., Zhou X., Zhang L., Yang G., Gao X.D., Murakami Y., Fujita M, & Kinoshita T. (2023). Accumulated precursors of specific GPI-anchored proteins upregulate GPI biosynthesis with ARV1. The Journal of Cell Biology, 222(5), e202208159.
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Publication 2023
Butyl Alcohol Cells Centrifugation Cold Temperature Glucose HEPES Inositol Lipids Mannose Pigs Thin Layer Chromatography Tunicamycin

Top products related to «Inositol»

1
Myo inositol by Merck Group
Sourced in United States, Germany, Italy, Spain
Myo-inositol is a naturally occurring sugar alcohol found in various foods and tissues. It serves as a core component in cellular structures and signaling pathways. Myo-inositol is a versatile compound used in laboratory applications and research.
2
Inositol by Merck Group
Sourced in United States, Germany, China, France
Inositol is a naturally occurring sugar alcohol found in various plant and animal tissues. It plays a crucial role in cellular function and signaling processes. Inositol is commonly used as a laboratory reagent and research tool to study these cellular mechanisms.
3
Folic acid by Merck Group
Sourced in United States, Germany, India, Switzerland, Italy, Macao, Sao Tome and Principe, Brazil, United Kingdom, Canada, Poland
Folic acid is a laboratory reagent used in various scientific applications. It is a water-soluble vitamin that plays a crucial role in cellular function and development. Folic acid is an essential component in many biochemical processes, including DNA synthesis and cell growth.
4
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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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.
5
Horse serum by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, New Zealand, Japan, China, France, Australia, Italy, Spain, Switzerland, Canada, Netherlands, Denmark, Austria, Belgium, Ireland, Israel, Brazil
Horse serum is a biological fluid derived from the blood of horses. It contains a complex mixture of proteins, including immunoglobulins, hormones, and other biomolecules. Horse serum is commonly used as a supplement in cell culture media to support the growth and maintenance of various cell types.
6
Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
7
L glutamine by Thermo Fisher Scientific
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L-glutamine is an amino acid that is commonly used as a dietary supplement and in cell culture media. It serves as a source of nitrogen and supports cellular growth and metabolism.
8
α mem by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, China, Japan, Australia, France, Italy, Canada, Switzerland, New Zealand, Netherlands, Denmark, Israel, Thailand, Holy See (Vatican City State), Argentina, Ireland
α-MEM is a cell culture medium formulated for the growth and maintenance of mammalian cells. It provides a balanced salt solution, amino acids, vitamins, and other nutrients required for cell proliferation.
9
2 mercaptoethanol by Merck Group
Sourced in United States, Germany, United Kingdom, Japan, France, Canada, Australia, China, Italy, Sao Tome and Principe, Switzerland, Denmark, Austria, Macao, Poland, Spain, Israel, Ireland, Gabon, Belgium, Czechia, Sweden, Argentina
2-mercaptoethanol is a clear, colorless liquid that is commonly used as a reducing agent in various laboratory applications. It is a small organic molecule with the chemical formula C2H6OS. 2-mercaptoethanol plays a crucial role in maintaining the proper conformation and disulfide bond formation of proteins during sample preparation and analysis.

More about "Inositol"

Inositol, also known as myo-inositol, is a vitamin-like substance that plays a crucial role in various physiological processes.
This cyclitol is found naturally in many foods, including fruits, grains, legumes, and nuts, and can also be produced by the human body.
Inositol is involved in cellular signaling pathways, contributing to the regulation of a wide range of bodily functions.
Researchers have been exploring the potential therapeutic applications of inositol, particularly in the management of conditions such as polycystic ovary syndrome (PCOS), mood disorders, and neurological conditions.
PCOS, a common endocrine disorder affecting women, has been a focus of inositol research, with studies suggesting its potential to improve insulin sensitivity and regulate hormonal imbalances.
The field of inositol research has benefited greatly from the advent of AI-powered tools like PubCompare.ai.
These tools enable researchers to efficiently identify the best protocols from the existing literature, preprints, and patents, enhancing the reproducibility and accuracy of their studies.
By leveraging the power of AI, researchers can optimize product selection and take their inositol research to new heights, leading to a deeper understanding of its physiological functions and clinical utility.
In addition to inositol, other related substances such as folic acid, which is often supplemented alongside inositol, and culture media components like fetal bovine serum (FBS), horse serum, penicillin/streptomycin, L-glutamine, and α-MEM, are also important considerations in inositol research.
These elements can play a crucial role in the in vitro study of inositol's effects and the development of potential therapeutic interventions.
By incorporating the insights gained from the MeSH term description and metadescription, as well as relevant information from related terms, this comprehensive text provides a robust foundation for understanding the importance of inositol and the advancements in its research, enabled by the powerful tools of AI.
With this knowledge, researchers and healthcare professionals can explore the full potential of inositol in improving human health and well-being.