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Lumos tribrid mass spectrometer

Manufactured by Thermo Fisher Scientific
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The Lumos Tribrid mass spectrometer is an analytical instrument designed for high-performance mass spectrometry. It features a Tribrid architecture, which combines multiple mass analyzers for enhanced performance and versatility. The core function of the Lumos Tribrid is to accurately measure and analyze the mass-to-charge ratio of ionized molecules, enabling researchers to identify and characterize complex samples.

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Lab products found in correlation

Easy nlc 1200, by Thermo Fisher Scientific (1 mentions) Ultimate 3000 rslc nano uphlc system, by Thermo Fisher Scientific (1 mentions) Ultimate 3000, by Thermo Fisher Scientific (1 mentions) Proswift rp 4h column, by Thermo Fisher Scientific (1 mentions) Pepswift monolith trap, by Thermo Fisher Scientific (1 mentions) Easy spray column, by Thermo Fisher Scientific (1 mentions) Ultimate 3000 rslcnano system, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Orbitrap Fusion Lumos Tribrid mass spectrometer (204 citations) Fusion Lumos Tribrid mass spectrometer (10 citations) Orbitrap Lumos Tribrid mass spectrometer (8 citations) Thermo Orbitrap Fusion Lumos Tribrid Mass Spectrometer (4 citations) OrbiTrap Fusion LUMOS Tribrid Mass Spectrometer (LC–MS) (3 citations) Nano Orbitrap Fusion Lumos Tribrid Mass Spectrometer system (2 citations)

4 protocols using lumos tribrid mass spectrometer

1

Whole Proteome Analysis by LC-MS/MS

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Peptides fractions for whole proteome analysis or phosphorylation analysis were reconstituted in 0.1% FA and submitted to Orbitrap Fusion Lumos Tribrid Mass Spectrometer connected with an Easy-nLC-1200 high-pressure liquid chromatography system (Thermo Fisher Scientific, Waltham, MA, USA). Each sample was loaded on a 15 cm C18 column (HS-Anal-C-5U-15CM, Beijing Happy Science Scientific, Beijing, China) of 5 μm mean particle size and 120 A pore diameter. Peptides were separated with a 80 min gradient at the flow rate of 300 nL/ min. For mobile phase, Buffer A is 0.1% FA, Buffer B is 0.1% FA/90% acetonitrile. MS1 spectra were collected with Orbitrap detector using these parameters: resolution of 120,000, scan range of 350-1800 (m/z), AGC target value of 4 × 105, 50 ms maximum injection time (MIT), including charge states 2–6. MS2 spectra were collected in data-dependent mode, in which top 12 precursors were scanned, and the following parameters included: quadrupole isolation mode, 38% high energy collision dissociation (HCD) energy, auto scan range mode, 50,000 orbitrap resolution, 1 × 105 AGC target value.
Luo A., Hao R., Zhou X., Jia Y, & Tang H. (2022). Integrative Proteomic and Phosphoproteomic Analyses of Hypoxia-Treated Pulmonary Artery Smooth Muscle Cells. Proteomes, 10(3), 23.
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2

Nanoflow LC-MS/MS Proteomics Analysis

Cited 1 time
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Online nanoLC-MS/MS analysis was performed using an Ultimate 3000 RSLC Nano-UPHLC system (Thermo Scientific, USA) coupled to a nanospray Orbitrap Fusion™ Lumos™ Tribrid™ Mass Spectrometer. LC-MS/MS parameters have been previously described.13 (link),14 (link)
Di Tommaso S., Dourthe C., Dupuy J.W., Dugot-Senant N., Cappellen D., Cazier H., Paradis V., Blanc J.F., Le Bail B., Balabaud C., Bioulac-Sage P., Saltel F, & Raymond A.A. (2023). Spatial characterisation of β-catenin-mutated hepatocellular adenoma subtypes by proteomic profiling of the tumour rim. JHEP Reports, 6(2), 100913.
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3

Intact Protein Tetramers Mass Spectrometry

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Intact tetramers were diluted to 0.03 mg/mL in Solvent A (97.5% water, 2.5% ACN and 0.1% formic acid). The chromatography was performed using an Ultimate 3000 ultra-high performance liquid chromatograph (ThermoFisher Scientific, San Jose, CA) interfaced to a orbitrap Fusion Lumos Tribrid mass spectrometer (ThermoFisher Scientific). Five µL (~4.4 pmol) was injected, concentrated and desalted on a PepSwift Monolith trap (200 µm × 5 mm) for 5 min at 99% Solvent A before separation on a ProSwift RP-4H column (100 µm × 25 cm) (ThermoFisher Scientific) with a gradient of 30% to 50% solvent B (75% ACN, 25% water, 0.1% formic acid) over 15 min. Precursor and fragment ion masses were acquired with a resolution of 120,000 at m/z 200 using “intact protein mode” with 1mtorr ion routing multipole pressure. Data dependent MS/MS was carried in top-N mode (N=2) with a precursor list of m/z values calculated for each tetramer. Isolated parents ions were fragmented using electron transfer dissociation supplemented with collisionally induced dissociation (ETciD) with a 3 msec ETD reaction time and supplemental activation at 10% normalized CID and averaging 20 microscans.
Lee A.E., Geis-Asteggiante L., Dixon E.K., Miller M., Wang Y., Fushman D, & Fenselau C. (2016). Preparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers. Journal of mass spectrometry : JMS, 51(8), 629-637.
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4

Comprehensive LC-MS/MS Analysis of Peptide Fractions

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Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Germany) connected to an Ultimate 3000 RSLCnano system (Dionex, Thermo Fisher Scientific, Germany), which were operated under Tune 3.4, SII for Xcalibur 1.6 and Xcalibur 4.4. Fractions from peptide SEC were resuspended in 1.6% ACN 0.1% formic acid and loaded onto an EASY-Spray column of 50 cm length (Thermo Scientific) running at 300 nl/min. Gradient elution was performed using mobile phase A of 0.1% formic acid in water and mobile phase B of 80% acetonitrile, 0.1% formic. For each SEC fraction, we used an optimized elution gradient (from 2-18% mobile phase B to 37.5-46.5% over 90 min, followed by a linear increase to 45-55 and 95% over 2.5 min each). Each fraction was analyzed in duplicates. The settings of the mass spectrometer were as follows: Data-dependent mode with 2.5s-Top-speed setting; MS1 scan in the Orbitrap at 120,000 resolution over 400 to 1500 m/z with 250% normalized automatic gain control (AGC) target; MS2 scan trigger only on precursors with z = 3-7+, AGC target set to "standard", maximum injection time set to "dynamic"; fragmentation by HCD employing a decision tree logic with (35) optimized collision energies; MS2 scan in the Orbitrap at a resolution of 60,000; dynamic exclusion was enabled upon a single observation for 60 s.
Each LC-MS acquisition took 120 min.
Graziadei A., Schildhauer F., Spahn C., Kraushar M.L., & Rappsilber J. (2022). SARS-CoV-2 Nsp1 N-terminal and linker regions as a platform for host translational shutoff.
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