13c labeled glucose

Manufactured by Cambridge Isotopes

Sourced in United States

13C-labeled glucose is a stable isotope-labeled chemical compound used in research and analytical applications. It is produced by incorporating the 13C isotope of carbon into the glucose molecule. This product serves as a tracer for metabolic studies and other analytical techniques requiring the use of labeled substrates.

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Lab products found in correlation

15nh4cl, by Cambridge Isotopes (7 mentions) 15n labeled ammonium chloride, by Cambridge Isotopes (4 mentions) Dmso d6, by Cambridge Isotopes (2 mentions) Chelex 100, by Bio-Rad (2 mentions) Chitin column, by New England Biolabs (2 mentions) Bl21 ai cells, by Thermo Fisher Scientific (2 mentions) M9 minimal media, by Cambridge Isotopes (2 mentions) Cngb1, by GenScript (2 mentions) Luria broth, by Avantor (1 mentions) β mercaptoethanol, by Merck Group (1 mentions) Sw480 cells, by American Type Culture Collection (1 mentions) Ccl 228, by American Type Culture Collection (1 mentions) Bl21 codonplus de3 ripl, by Agilent Technologies (1 mentions) Dynamag 2 magnet, by Thermo Fisher Scientific (1 mentions) Rpmi 1640 medium without glucose, by Thermo Fisher Scientific (1 mentions) Anti cd3 cd28 dynabeads, by Thermo Fisher Scientific (1 mentions) Penicillin streptomycin, by Merck Group (1 mentions) L glutamine, by Merck Group (1 mentions) Restriction enzyme, by New England Biolabs (1 mentions) Pymol molecular graphics system, by Schrödinger (1 mentions)

Spelling variants of this product

13C-glucose (50 citations) Uniformly labeled 13C glucose (5 citations) 13C-labeled d-glucose (3 citations) U−13C-labeled glucose (2 citations)

18 protocols using 13c labeled glucose

Trace Metal-Free Reagent Preparation

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All chemical reagents were ACS grade or higher unless otherwise indicated. All buffers were passed through Chelex-100 (Bio-Rad, Hercules, CA) to remove trace metals. The D₂O, d₆-DMSO, ¹⁵NH₄Cl, and ¹³C-labeled glucose were purchased from Cambridge Isotope Laboratories, Inc. (Andover, MA).

Lanning M.E., Yu W., Yap J.L., Chauhan J., Chen L., Whiting E., Pidugu L.S., Atkinson T., Bailey H., Li W., Roth B.M., Hynicka L., Chesko K., Toth E.A., Shapiro P., MacKerell AD J.r., Wilder P.T, & Fletcher S. (2016). Structure-Based Design of N-Substituted 1-Hydroxy-4-sulfamoyl-2-naphthoates as Selective Inhibitors of the Mcl-1 Oncoprotein. European journal of medicinal chemistry, 113, 273-292.

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Quantifying Cellular Glucose Metabolism

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Cells were grown as described above. The day before harvesting, cells were transferred into six-well plates at 400,000 cell/well density; each sample group was seeded in triplicate. The old culture medium was substituted by a new one with the same composition, but containing 10 mM ¹³C-labeled glucose (Cambridge Isotope Laboratories) instead of 10 mM glucose. After overnight incubation, cells were harvested and lysed as before. The CHCl₃ was evaporated, and the lipids were saponified by addition of 500 μl 1.5 M NaOH and incubated for 4 h at 80°C and 100g. Afterward, 500 μl 2 M HCl was added and fatty acids were extracted by adding 500 μl CHCl₃. After centrifugation (5 min, 15,000g, 4°C), 400 μl of the CHCl₃ phase was evaporated and derivatized for gas chromatography–electron ionization–mass spectrometry analysis by 20 μl pyridine and 50 μl N-methyl-N-trimethylsilyltrifluoroacetamide for 30 min at 37°C and 100g. Extracted ion chromatograms for the isotopologues for the different fatty acids (trimethylsilylated fatty acids –CH₃) were generated, integrated, and corrected for natural isotopic abundance. Relative abundance was calculated by dividing each isotopologue by the sum of the isotopologues of each fatty acid.

Ferrarese R., Izzo A., Andrieux G., Lagies S., Bartmuss J.P., Masilamani A.P., Wasilenko A., Osti D., Faletti S., Schulzki R., Yuan S., Kling E., Ribecco V., Heiland D.H., Tholen S., Prinz M., Pelicci G., Kammerer B., Boerries M, & Carro M.S. (2022). ZBTB18 inhibits SREBP-dependent lipid synthesis by halting CTBPs and LSD1 activity in glioblastoma. Life Science Alliance, 6(1), e202201400.

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Preparation of Isotopically-Labeled Luria Broth

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The reagents for Luria broth were obtained from AMRESCO. ¹⁵NH₄Cl, ¹³C-labeled glucose, and D₂O were purchased from Cambridge Isotope Laboratories, and β-mercaptoethanol was obtained from Sigma. SW-480 cells were purchased from the American Type Culture Collection (ATCC; CCL-228).

Penumutchu S.R., Chou R.H, & Yu C. (2014). Structural Insights into Calcium-Bound S100P and the V Domain of the RAGE Complex. PLoS ONE, 9(8), e103947.

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Isotopic Protein Labeling in E. coli

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To generate isotopically-labeled, purified protein, target constructs were transformed into BL21-CodonPlus (DE3)-RIPL (Agilent). Cultures were then grown in M9 media supplemented with ¹⁵NH₄Cl and/or ¹³C-labeled glucose (Cambridge Isotopes) at 37°C to a culture density of approximately 0.7. Protein expression was induced with 1 mM IPTG (final concentration) and proceeded for 3.5 hours.

Ipsaro J.J., O’Brien P.A., Bhattacharya S., Palmer AG I.I.I, & Joshua-Tor L. (2021). Asterix/Gtsf1 links tRNAs and piRNA silencing of retrotransposons. Cell reports, 34(13), 108914.

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Recombinant CaM Protein Purification

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Recombinant human CaM was subcloned into pET11b expression vector (Novagen) and overexpressed in E. coli strain BL21(DE3) as described previously (Turner et al. 2020 (link)). Uniformly ¹³C/¹⁵N-labeled CaM samples were overexpressed in M9 minimal media, containing 1 g/L ¹⁵NH₄Cl and 3 g/L ¹³C-labeled glucose (Cambridge Isotopes Laboratories) as the sole nitrogen and carbon sources, respectively. The soluble fraction of the cell lysate was loaded onto a HiPrep Phenyl Sepharose 6 column that was pre-equilibrated with equilibration buffer, containing 20 mM Tris (pH 7.5), 200 mM KCl, 2 mM CaCl₂. The CaM protein was eluted from the column using a buffer that contained 20 mM Tris (pH 7.5), 50 mM KCl, 2 mM EGTA. The eluted protein fraction was further loaded onto a HiPrep Q Sepharose anion exchange column that was pre-equilibrated with 50 mM Tris (pH 7.5), 25 mM KCl, 1 mM EGTA and eluted by a KCl gradient up to 625 mM. The purity and identity of the eluted protein fractions were confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis.

Bej A, & Ames J.B. (2022). Chemical shift assignments of calmodulin under standard conditions at neutral pH. Biomolecular Nmr Assignments, 16(2), 213-218.

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Trace Metal-Free Biochemical Protocols

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All chemical reagents were American Chemical Society grade or higher unless otherwise indicated. The D₂O, D₆-DMSO, ¹⁵NH₄Cl, and ¹³C-labeled glucose were purchased from Cambridge Isotope Laboratories, Inc. (Andover, MA). All buffers were passed through and/or stored with dialysis bags containing Chelex-100 (Bio-Rad, Hercules, CA) to remove trace metals. The Chelex-100 treated reagents were stored in plastic containers, transferred minimally, and contacted only plastic or quartz cuvettes that had been acid washed to minimize contaminating calcium.

Young B.D., Varney K.M., Wilder P.T., Costabile B.K., Pozharski E., Cook M.E., Godoy-Ruiz R., Clarke O.B., Mancia F, & Weber D.J. (2021). Physiologically relevant free Ca2+ ion concentrations regulate STRA6-calmodulin complex formation via the BP2 region of STRA6: Calcium regulation of the calmodulin-STRA6 complex. Journal of molecular biology, 433(22), 167272.

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CD8+ T Cell Differentiation Kinetics

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For in vitro differentiation, naïve CD8⁺ T cells (1.5 x 10⁶ cells/mL and 1 x 10⁶ cells/mL) were distributed into four wells of a 24-well plate and activated for 8 days by adding prewashed anti-CD3/CD28 Dynabeads at a 1:1 bead-to-cell ratio (Invitrogen/Thermo Fisher Scientific, Massachusetts, USA) and human rIL-2 (30 U/mL) (Roche/Merck, Darmstadt, Germany) to the culture. To generate effector memory T cells, 1 x 10⁶ cells/mL were restimulated on day 7 by adding prewashed anti-CD3/CD28 Dynabeads at a 1:1 bead-to-cell ratio and human rIL-2 (30 U/mL) a second time to the culture. The cells were cultured in RPMI 1640 medium without glucose (Gibco/Life Technologies, Carlsbad, USA) where 11 mM D-glucose was added to 10% FBS, 2 mM L-glutamine and 1% penicillin-streptomycin (all from Sigma Aldrich, St.Louis, USA). 24 h before collection, culture medium was replaced with RPMI 1640 medium containing 11 mM of ¹³C labeled-glucose (Cambridge Isotope Laboratories, Massachusetts, USA). At indicated time points, naïve T cells (T_N, day 1), stem cell memory T cells (T_SCM, day 2), central memory T cells (T_CM, day 5) and effector memory T cells (T_EM, day 8) were collected and anti-CD3/CD28 beads were removed by using a DynaMag-2 magnet (Thermo Fisher Scientific, Massachusetts, USA) before further processing for flow cytometry, RNA sequencing and metabolomics analyses.

Kirchmair A., Nemati N., Lamberti G., Trefny M., Krogsdam A., Siller A., Hörtnagl P., Schumacher P., Sopper S., Sandbichler A., Zippelius A., Ghesquière B, & Trajanoski Z. (2023). 13C tracer analysis reveals the landscape of metabolic checkpoints in human CD8+ T cell differentiation and exhaustion. Frontiers in Immunology, 14, 1267816.

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Homology Modeling of Ssa1 and DnaK

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All chemicals used in this study were purchased from Sigma-Aldrich (St. Louis, MO) unless noted otherwise. Restriction enzymes were purchased from New England BioLabs (Ipswich, MA). The ¹³C labeled glucose and ¹⁵N labeled ammonium chloride were purchased from Cambridge Isotope Laboratories, Inc. (Andover, MA). Homology modeling of Ssa1 structures in ATP and ADP state were prepared using SWISS-MODEL [88 (link)] and DnaK structures (PDB: 4NJ4 and 2KHO, respectively) as templates. Structural images were prepared with the PyMOL Molecular Graphics System, Version 1.5 Schrödinger, LLC.

Schilke B.A., Ciesielski S.J., Ziegelhoffer T., Kamiya E., Tonelli M., Lee W., Cornilescu G., Hines J.K., Markley J.L, & Craig E.A. (2017). Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. PLoS Genetics, 13(10), e1007084.

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Labeling Compounds for Microbial Growth

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¹⁵N-labeled ammonium chloride and ¹³C-labeled glucose were purchased from Cambridge Isotope Laboratories, Inc. (Tewksbury, MA, USA). Thermanox substrate-coated cover slips were purchased from Thermo Fisher Scientific (Waltham, MA, USA). Sabouraud dextrose (SD) broth and SD agar were purchased from Becton, Dickinson, and Company (Franklin Lakes, NJ, USA). All other chemicals used in this study were obtained from Sigma-Aldrich (St. Louis, MO, USA).

Cheng K.T., Wu C.L., Yip B.S., Chih Y.H., Peng K.L., Hsu S.Y., Yu H.Y, & Cheng J.W. (2020). The Interactions between the Antimicrobial Peptide P-113 and Living Candida albicans Cells Shed Light on Mechanisms of Antifungal Activity and Resistance. International Journal of Molecular Sciences, 21(7), 2654.

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Affinity Purification of NpR6012g4 Protein

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The protein sample in this study consists of 180 native residues (M583-G762, Fig. 1) after removal of a C-terminal intein-CBD tag used for affinity purification (Kim et al, 2012 (link)). NpR6012g4 was expressed in BL21-AI cells (Invitrogen) grown in M9 minimal media supplemented with ALA (100 μM), ¹⁵N-labeled ammonium chloride, and/or ¹³C-labeled glucose (Cambridge Isotopes) using a published system for induction of protein expression and chromophore biosynthesis (Gambetta & Lagarias, 2001 (link)). Affinity purification of NpR6012g4 using a chitin column (NEB) followed our previous procedure (Kim et al, 2012 (link); Rockwell et al, 2012 (link); Rockwell et al, 2015a (link); Rockwell et al, 2015b (link)). Peak eluted fractions were pooled for overnight dialysis into 10 mM sodium phosphate (pH 7.4) supplemented with 1 mM EDTA to remove residual metal ions followed by final overnight dialysis into 10 mM sodium phosphate (pH 7.4). The protein was concentrated to approximately 0.7 mM, and D₂O was added to 7% (v/v). Dark reversion of the metastable green-absorbing state under these conditions was < 10% after 24 hours at 298 K as reported previously (Rockwell et al, 2015b (link)). All subsequent manipulations were performed on samples kept in darkness.

Lim S., Yu Q., Rockwell N.C., Martin S.S., Clark Lagarias J, & Ames J.B. (2015). 1H, 13C, and 15N Chemical Shift Assignments of Cyanobacteriochrome NpR6012g4 in the Green-Absorbing Photoproduct State. Biomolecular NMR assignments, 10(1), 157-161.

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