Q exactive tandem mass spectrometer

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Q Exactive tandem mass spectrometer is an analytical instrument used for the detection, identification, and quantification of chemical compounds. It combines a quadrupole mass analyzer with an Orbitrap mass analyzer to provide high-resolution, accurate mass measurements. The Q Exactive is designed for a variety of applications, including proteomics, metabolomics, and small molecule analysis.

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Lab products found in correlation

Beh c18 column, by Waters Corporation (1 mentions) Dionex ultimate 3000 uhplc, by Thermo Fisher Scientific (1 mentions) Sep pak c18 cartridge, by Waters Corporation (1 mentions) Acclaim pepmap, by Thermo Fisher Scientific (1 mentions) U3000 hplc system, by Thermo Fisher Scientific (1 mentions) μ precolumn, by Thermo Fisher Scientific (1 mentions) Lc 20ad, by Shimadzu (1 mentions) Sequencing grade trypsin, by Promega (1 mentions)

Close spelling variants of this product

Q Exactive mass spectrometer Exactive mass spectrometer Q Exactive

5 protocols using q exactive tandem mass spectrometer

Metabolite Separation and Detection Protocol

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Waters 2D UPLC system (Waters Corp., Milford, MA, USA) and Q Exactive tandem mass spectrometer (Thermo Fisher Scientific, USA) were used for metabolite separation and detection. Chromatographic separation was conducted using a BEH C18 column (1.7 μm 2.1^*100 mm, Waters, USA). The linear gradient programme set as follows: 2% B, 0–1 min; 2–98% B, 1–9 min; 98% B, 9–12 min; 98–2% B, 12.0–12.1 min. 2% B, 12.1–15 min. Flow rate was set 0.35 mL/min and the column temperature was 45°C. The injection volume was 5 μl.
MS data were collected with a Q Exactive tandem mass spectrometer (Thermo Fisher Scientific, USA). The mass spectra was a range of 70–1,050 mass-to-charge ratio with primary resolution of 70,000 and secondary resolution of 17,500. The ion source was electrospray ionization. The sheath gas flow rate was 40 and the aux gas flow rate was 10. The capillary temp was 320°C and the aux gas heater temp was 350°C.

Duan L., Qiu W., Bai G., Qiao Y., Su S., Lo P.C., Lu Y., Xu G., Wang Q., Li M, & Mo Y. (2021). Metabolomics Analysis on Mice With Depression Ameliorated by Acupoint Catgut Embedding. Frontiers in Psychiatry, 12, 703516.

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Proteomic Analysis of Protein Samples

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15 µg of precipitate protein material was used for each individual sample. Samples were reduced for 1 h by addition of 200 mM dithiothreitol (DTT) followed by alkylation with 200 mM iodoacetamide (IAA) for 30 min. Trypsin digestion was performed overnight at 37 °C with gentle mixing using a 1:50 (trypsin:protein) ratio. Samples were acidified with 1 % FA or TFA. Peptide digests were then desalted using Sep-Pak C18 cartridges (Waters) and dried by Speed Vac centrifugation. Pellets were resuspended in 30 µl of buffer A (98 % Milli-Q-H2O, 2 % acetonitrile, 0.1 % formic acid) and kept at −20 °C until analysis. Peptides were analysed in duplicates by nano ultra-high performance liquid chromatography tandem mass spectrometry (nUHPLC–MS/MS) using a Dionex Ultimate 3000 UHPLC (C18 column with a 75 μm × 250 mm, 1.7 μm particle size, Thermo Scientific, Bremen, Germany) coupled to a Q Exactive tandem mass spectrometer (Thermo Scientific, Bremen, Germany) as described previously [21 (link)].

Kaisar M., van Dullemen L.F., Thézénas M.L., Zeeshan Akhtar M., Huang H., Rendel S., Charles P.D., Fischer R., Ploeg R.J, & Kessler B.M. (2016). Plasma degradome affected by variable storage of human blood. Clinical Proteomics, 13, 26.

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HPLC-MS/MS Peptide Separation and Analysis

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The extracted peptides were separated on a U 3000 HPLC system (Thermo Fisher Scientific). A PepMap Acclaim analytical column of 75 μm inner diameter × 50 cm length (2 μm C18 particles, Thermo Fisher Scientific) was used. The injected peptides were eluted at a flow rate of 300 nl/min with 5–40% acetonitrile gradient and subsequently ionized by on-line electrospray ionization at a potential of 2 kV, and sent into a Q Exactive tandem mass spectrometer (Thermo Fisher Scientific). In MS, the ionized peptides intact masses were measured in the Orbitrap mass analyser. In each scan, the top 10 peptides with more than a charge state of 2 + were passed on to high-energy collision cell and fragmented into y and b fragment to acquire MS/MS spectra in the orbitrap.

Kawasaki M., Meulendijks E.R., van den Berg N.W., Nariswari F.A., Neefs J., Wesselink R., Baalman S.W., Jongejan A., Schelfhorst T., Piersma S.R., Pham T.V., van Boven W.J., Driessen A.H., Jimenez C.R, & de Groot J.R. (2021). Neutrophil degranulation interconnects over-represented biological processes in atrial fibrillation. Scientific Reports, 11, 2972.

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Optimized Peptide Separation and Mass Spectrometry

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The dried fractionated peptides were re-dissolved in buffer C (2% ACN, 0.1% formic acid (FA)) and centrifuged at 20,000× g for 10 min to collect supernatants. Peptides were separated by Shimadzu LC-20AD, on which a 300 μm × 4 mm (μ-Precolumn, Thermo Scientific, Waltham, MA, USA) for peptide enrichment and a 75 μm × 15 cm in-house column for peptide separation were equipped. After enrichment and desalting in a trap column, each fraction was separated in in-house column by a 65-min gradient at 300 nl/min: 5% buffer D (98% ACN, 0.1% FA) for 8 min, 8–35% buffer D for 35 min, 35–60% buffer D for 5 min, 60–80% buffer D for 2 min, 80% buffer D for 5 min, and 5% buffer D for 10 min. Peptides were detected by the Q-Exactive tandem mass spectrometer (ThermoFisher Scientific, San Jose, CA, USA) that coupled to the Shimadzu LC-20AD at a data-dependent acquisition (DDA) mode. MS parameters were set as follows: spray voltage 1.6kv; scan range 350–1600 m/z; MS resolution 70,000; MS/MS resolution 17,500; dynamic exclusion duration 15s.

Chen X., Yi Y., You X., Liu J, & Shi Q. (2019). High-Throughput Identification of Putative Antimicrobial Peptides from Multi-Omics Data of the Lined Seahorse (Hippocampus erectus). Marine Drugs, 18(1), 30.

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Protein Identification by Mass Spectrometry

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The protein bands were excised from the one‐dimensional Coomassie blue‐stained polyacrylamide gel. The bands were digested in the gel with an excess of sequencing‐grade trypsin (Promega, USA).13 Each 4‐μg sample was loaded and separated on a C18 column (10 cm × 100 μm) using a nano‐liquid chromatograph (Dionex, Thermo Fisher). The separation procedure refers to our previous experimental conditions.12 The liquid phase‐separated peptide was introduced into a Q‐Exactive tandem mass spectrometer (ThermoFisher Scientific, San Jose, CA) equipped with an ESI ionization source.

Zhao Y., Fang X., Fang H., Feng Y., Chen F, & Xia Q. (2018). ATPR‐induced G0/G1 phase arrest in gastric cancer cells by regulating the binding of 14‐3‐3ε and filamin A. Cancer Medicine, 7(7), 3373-3384.

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