orbitrap fusion lumos tribrid mass spectrometer lc ms  (Thermo Fisher)


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    Orbitrap Fusion Lumos Tribrid Mass Spectrometer
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    Excel at the most challenging of applications including low level PTM analysis multiplexed relative quantitation using isobaric tags intact protein characterization as well as MSn analysis of small molecules with the new Thermo Scientific Orbitrap Fusion Lumos Tribrid Mass Spectrometer This system incorporates the brightest ion source a segmented quadrupole mass filter with improved selectivity and ion transmission Advanced Vacuum Technology for improved ion transmission to the Thermo Scientific Orbitrap mass analyzer and ETD HD a higher capacity ETD fragmentation Latest innovations include the Advanced Peak Determination APD algorithm for improved data dependent experiments and two new hardware options UVPD a new fragmentation technique achieved with a 213 nm UV laser and 1M which provides 1 000 000 FWHM ultra high resolution for improved structural elucidation and quantitation of isobaric compounds
    Catalog Number:
    iqlaaegaapfadbmbhq
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    Applications:
    Industrial & Applied Science|Industrial Mass Spectrometry
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    Instruments and Equipment
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    Structured Review

    Thermo Fisher orbitrap fusion lumos tribrid mass spectrometer lc ms
    Excel at the most challenging of applications including low level PTM analysis multiplexed relative quantitation using isobaric tags intact protein characterization as well as MSn analysis of small molecules with the new Thermo Scientific Orbitrap Fusion Lumos Tribrid Mass Spectrometer This system incorporates the brightest ion source a segmented quadrupole mass filter with improved selectivity and ion transmission Advanced Vacuum Technology for improved ion transmission to the Thermo Scientific Orbitrap mass analyzer and ETD HD a higher capacity ETD fragmentation Latest innovations include the Advanced Peak Determination APD algorithm for improved data dependent experiments and two new hardware options UVPD a new fragmentation technique achieved with a 213 nm UV laser and 1M which provides 1 000 000 FWHM ultra high resolution for improved structural elucidation and quantitation of isobaric compounds
    https://www.bioz.com/result/orbitrap fusion lumos tribrid mass spectrometer lc ms/product/Thermo Fisher
    Average 99 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion lumos tribrid mass spectrometer lc ms - by Bioz Stars, 2020-09
    99/100 stars

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    protein mass spectrometry

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    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Growth factor receptor signaling inhibition prevents SARS-CoV-2 replication
    Article Snippet: .. Liquid chromatography mass spectrometry All mass spectrometry data was acquired in centroid mode on an Orbitrap Fusion Lumos mass spectrometer hyphenated to an easy-nLC 1200 nano HPLC system using a nanoFlex ion source (ThermoFisher Scientific) applying a spray voltage of 2.6 kV with the transfer tube heated to 300°C and a funnel RF of 30%. .. Internal mass calibration was enabled (lock mass 445.12003 m/z).

    Article Title: A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
    Article Snippet: .. LC–MS/MS Analysis All peptide samples were analyzed on an Orbitrap Fusion Lumos mass spectrometer fronted with an EASY-Spray Source, coupled to an Easy-nLC1000 HPLC pump (Thermo Fisher Scientific). .. The peptides were subjected to a dual column setup: an Acclaim PepMap RSLC C18 trap column, 75 μm × 20 mm (Thermo Fisher Scientific, Cat# 164261); and an EASY-Spray LC Column, 75 μm × 250 mm (Thermo Fisher Scientific, Cat# ES802).

    Article Title: Early urine proteome changes in the Walker-256 tail-vein injection rat model
    Article Snippet: .. PRM samples were analyzed by the EASY-nLC 1200 HPLC system (Thermo Fisher Scientific, Waltham, MA) coupled to the Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Waltham, MA). ..

    other:

    Article Title: Quantitative Method for Assessing the Role of Lysine Arginine Post-Translational Modifications in Nonalcoholic Steatohepatitis
    Article Snippet: For DDA-MS methods used for the Orbitrap Fusion Lumos, see Supplementary Methods.

    Liquid Chromatography:

    Article Title: Growth factor receptor signaling inhibition prevents SARS-CoV-2 replication
    Article Snippet: .. Liquid chromatography mass spectrometry All mass spectrometry data was acquired in centroid mode on an Orbitrap Fusion Lumos mass spectrometer hyphenated to an easy-nLC 1200 nano HPLC system using a nanoFlex ion source (ThermoFisher Scientific) applying a spray voltage of 2.6 kV with the transfer tube heated to 300°C and a funnel RF of 30%. .. Internal mass calibration was enabled (lock mass 445.12003 m/z).

    Mass Spectrometry:

    Article Title: Early urine proteome changes in the Walker-256 tail-vein injection rat model
    Article Snippet: .. Peptides were analyzed with an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Waltham, MA). .. MS data were acquired in high-sensitivity mode using the following parameters: data-dependent MS/MS scans per full scan with top-speed mode (3 s), MS scans at a resolution of 120,000 and MS/MS scans at a resolution of 30,000 in the Orbitrap, 30% HCD collision energy, charge-state screening (+2 to +7), dynamic exclusion (exclusion duration 30 s), and a maximum injection time of 45 ms .

    Article Title: Quantitative Method for Assessing the Role of Lysine Arginine Post-Translational Modifications in Nonalcoholic Steatohepatitis
    Article Snippet: .. Orbitrap Fusion Lumos MS AcquisitionFor DIA-MS analysis, a Orbitrap LUMOS Fusion mass spectrometer (Thermo Scientific) was equipped with an EasySpray ion source and connected to Ultimate 3000 nano LC system (Thermo Scientific). .. Peptides were loaded onto a PepMap RSLC C18 column (2 μm, 100 Å, 150 μm i.d. x 15 cm, Thermo) using a flow rate of 1.4 μL/min for 7 min at 1% B (mobile phase A was 0.1% formic acid in water and mobile phase B was 0.1 % formic acid in acetonitrile) after which point they were separated with a linear gradient of 5-20%B for 45 minutes, 20-35%B for 15 min, 35-85%B for 3 min, holding at 85%B for 5 minutes and re-equilibrating at 1%B for 5 minutes.

    Article Title: Increased N,N-Dimethyl Leucine Isobaric Tag Multiplexing by a Combined Precursor Isotopic Labeling and Isobaric Tagging Approach
    Article Snippet: .. Samples were analyzed by nanoLC-MS/MS using a Dionex UltiMate 3000 UPLC system coupled to a Thermo Scientific Orbitrap Fusion Lumos mass spectrometer. .. Labeled peptide samples were dried in vacuo and dissolved in 3% ACN, 0.1% formic acid in water.

    Article Title: Growth factor receptor signaling inhibition prevents SARS-CoV-2 replication
    Article Snippet: .. Liquid chromatography mass spectrometry All mass spectrometry data was acquired in centroid mode on an Orbitrap Fusion Lumos mass spectrometer hyphenated to an easy-nLC 1200 nano HPLC system using a nanoFlex ion source (ThermoFisher Scientific) applying a spray voltage of 2.6 kV with the transfer tube heated to 300°C and a funnel RF of 30%. .. Internal mass calibration was enabled (lock mass 445.12003 m/z).

    Article Title: Targeted MultiNotch MS3 Approach for Relative Quantification of N-Glycans Using Multiplexed Carbonyl-Reactive Isobaric Tags
    Article Snippet: .. An Orbitrap Fusion Lumos Tribrid quadrupole-ion trap-Orbitrap mass spectrometer with NanoSpray Flex ion source (Thermo Scientific, Bremen, Germany) was used for data acquisition. ..

    Article Title: A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
    Article Snippet: .. LC–MS/MS Analysis All peptide samples were analyzed on an Orbitrap Fusion Lumos mass spectrometer fronted with an EASY-Spray Source, coupled to an Easy-nLC1000 HPLC pump (Thermo Fisher Scientific). .. The peptides were subjected to a dual column setup: an Acclaim PepMap RSLC C18 trap column, 75 μm × 20 mm (Thermo Fisher Scientific, Cat# 164261); and an EASY-Spray LC Column, 75 μm × 250 mm (Thermo Fisher Scientific, Cat# ES802).

    Article Title: Early urine proteome changes in the Walker-256 tail-vein injection rat model
    Article Snippet: .. PRM samples were analyzed by the EASY-nLC 1200 HPLC system (Thermo Fisher Scientific, Waltham, MA) coupled to the Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Waltham, MA). ..

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  • 99
    Thermo Fisher orbitrap fusion lumos mass spectrometer
    Gas phase segmentation (GPS) improves ADPr peptide detection. (A) A screenshot of the ADP-ribose product ion triggered EThcD and HCD data acquisition method on the <t>Orbitrap</t> Fusion <t>Lumos.</t> (B) Area under the curve (AUC) of the four ADPr fragment ions (136.06, 250.09, 348.07, and 428.04 m / z ) dissociated from an ARTD8/PARP14-MARylated STAT1 peptide using HCD. (C) Pilot Af1521 enrichment study to determine the optimal collision energy for ADP-ribose product ion screening and ADPr peptide identification. Only high confidence (HCD and EThcD combined peptides) were used in this plot (more details in Figure 3 ). (D) A schematic showing the principle of GPS using multiple injections. (E) The extracted ion chromatograms of the ADPr fragment peak (348.07 m / z ) in each full scan and GPS injection. (F,G) Precursor ion m / z and retention time of triggered EThcD spectra in full scan and combined GPS scans.
    Orbitrap Fusion Lumos Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 309 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/orbitrap fusion lumos mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 309 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion lumos mass spectrometer - by Bioz Stars, 2020-09
    99/100 stars
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    Gas phase segmentation (GPS) improves ADPr peptide detection. (A) A screenshot of the ADP-ribose product ion triggered EThcD and HCD data acquisition method on the Orbitrap Fusion Lumos. (B) Area under the curve (AUC) of the four ADPr fragment ions (136.06, 250.09, 348.07, and 428.04 m / z ) dissociated from an ARTD8/PARP14-MARylated STAT1 peptide using HCD. (C) Pilot Af1521 enrichment study to determine the optimal collision energy for ADP-ribose product ion screening and ADPr peptide identification. Only high confidence (HCD and EThcD combined peptides) were used in this plot (more details in Figure 3 ). (D) A schematic showing the principle of GPS using multiple injections. (E) The extracted ion chromatograms of the ADPr fragment peak (348.07 m / z ) in each full scan and GPS injection. (F,G) Precursor ion m / z and retention time of triggered EThcD spectra in full scan and combined GPS scans.

    Journal: Journal of Proteome Research

    Article Title: A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation

    doi: 10.1021/acs.jproteome.8b00895

    Figure Lengend Snippet: Gas phase segmentation (GPS) improves ADPr peptide detection. (A) A screenshot of the ADP-ribose product ion triggered EThcD and HCD data acquisition method on the Orbitrap Fusion Lumos. (B) Area under the curve (AUC) of the four ADPr fragment ions (136.06, 250.09, 348.07, and 428.04 m / z ) dissociated from an ARTD8/PARP14-MARylated STAT1 peptide using HCD. (C) Pilot Af1521 enrichment study to determine the optimal collision energy for ADP-ribose product ion screening and ADPr peptide identification. Only high confidence (HCD and EThcD combined peptides) were used in this plot (more details in Figure 3 ). (D) A schematic showing the principle of GPS using multiple injections. (E) The extracted ion chromatograms of the ADPr fragment peak (348.07 m / z ) in each full scan and GPS injection. (F,G) Precursor ion m / z and retention time of triggered EThcD spectra in full scan and combined GPS scans.

    Article Snippet: LC–MS/MS Analysis All peptide samples were analyzed on an Orbitrap Fusion Lumos mass spectrometer fronted with an EASY-Spray Source, coupled to an Easy-nLC1000 HPLC pump (Thermo Fisher Scientific).

    Techniques: Injection

    DiLeu cPILOT experimental workflow. Protein digest samples undergo stable isotope dimethyl labeling of peptide N-termini with either light [–(CH 3 ) 2 ] or heavy [–( 13 C 2 H 3 ) 2 ] dimethyl groups at low pH followed by labeling of lysine residues with 12-plex DiLeu isobaric tags at high pH. Pooled samples are analyzed by LC-MS/MS on the Orbitrap Fusion Lumos using CID MS 2 acquisition of peak pairs for peptide sequence identification and HCD SPS-MS 3 acquisition for accurate 24-plex quantification via DiLeu reporter ions.

    Journal: Analytical chemistry

    Article Title: Increased N,N-Dimethyl Leucine Isobaric Tag Multiplexing by a Combined Precursor Isotopic Labeling and Isobaric Tagging Approach

    doi: 10.1021/acs.analchem.8b01301

    Figure Lengend Snippet: DiLeu cPILOT experimental workflow. Protein digest samples undergo stable isotope dimethyl labeling of peptide N-termini with either light [–(CH 3 ) 2 ] or heavy [–( 13 C 2 H 3 ) 2 ] dimethyl groups at low pH followed by labeling of lysine residues with 12-plex DiLeu isobaric tags at high pH. Pooled samples are analyzed by LC-MS/MS on the Orbitrap Fusion Lumos using CID MS 2 acquisition of peak pairs for peptide sequence identification and HCD SPS-MS 3 acquisition for accurate 24-plex quantification via DiLeu reporter ions.

    Article Snippet: Samples were analyzed by nanoLC-MS/MS using a Dionex UltiMate 3000 UPLC system coupled to a Thermo Scientific Orbitrap Fusion Lumos mass spectrometer.

    Techniques: Labeling, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Sequencing

    Cluster analysis of validated seven differential proteins by different mass spectrometers. Cluster analysis of differential proteins by Triple TOF 5600 ( a ) and by Orbitrap Fusion Lumos ( b ).

    Journal: Scientific Reports

    Article Title: Early urine proteome changes in the Walker-256 tail-vein injection rat model

    doi: 10.1038/s41598-019-50301-1

    Figure Lengend Snippet: Cluster analysis of validated seven differential proteins by different mass spectrometers. Cluster analysis of differential proteins by Triple TOF 5600 ( a ) and by Orbitrap Fusion Lumos ( b ).

    Article Snippet: PRM samples were analyzed by the EASY-nLC 1200 HPLC system (Thermo Fisher Scientific, Waltham, MA) coupled to the Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Waltham, MA).

    Techniques:

    Phospho proteomic profiling of SARS-CoV-2 infected cells. ( A ) Experimental scheme. Caco-2 cells were infected with SARS-CoV-2 for one hour, washed and incubated for additional 24 hours. Proteins were extracted and prepared for bottom-up proteomics. All ten conditions were multiplexed using TMT10 reagents. 250 μg of pooled samples were used for whole cell proteomics (24 Fractions) and the remainder (~1 mg) enriched for phosphopeptides by Fe-NTA. Phosphopeptides were fractionated into 8 fractions and concatenated into 4 fractions. All samples were measured on an Orbitrap Fusion Lumos. ( B ) Volcano plot showing fold changes of infected versus mock cells for all 15,392 quantified phosphopeptides. P values were calculated using an unpaired, two-sided student’s t-test with equal variance assumed and adjusted using the Benjamini Hochberg FDR method (N = 5). Orange or blue points indicate significantly increased or decreased phosphopeptides, respectively. ( C ) Volcano plot showing differences between SARS-CoV-2 and mock infected cells in total protein levels for all 7,150 quantified proteins. P values were calculated using an unpaired, two-sided student’s t-test with equal variance assumed and adjusted using the Benjamini Hochberg FDR method (N = 5). Orange or blue points indicate significantly increased or decreased phosphopeptides, respectively. ( D ) Distribution of phosphorylation sites identified across modified amino acids. See also Figure S1 and Tables S1 and S2. ( E – K ) Domain structures of SARS-CoV-2 proteins predicted by InterPro. Identified phosphorylation sites are indicated.. Protein 3a ( E ), Membrane Protein M ( F ), Non-structural protein 6 ( G ), Protein 9b ( H ), Replicase Polyprotein 1b ( I ) and Nucleoprotein N ( J ). ( K ) X-ray structure of the RNA binding domain (PDB: 6vyo, residues 47-173) with identified phosphorylation sites marked in red.

    Journal: bioRxiv

    Article Title: Growth factor receptor signaling inhibition prevents SARS-CoV-2 replication

    doi: 10.1101/2020.05.14.095661

    Figure Lengend Snippet: Phospho proteomic profiling of SARS-CoV-2 infected cells. ( A ) Experimental scheme. Caco-2 cells were infected with SARS-CoV-2 for one hour, washed and incubated for additional 24 hours. Proteins were extracted and prepared for bottom-up proteomics. All ten conditions were multiplexed using TMT10 reagents. 250 μg of pooled samples were used for whole cell proteomics (24 Fractions) and the remainder (~1 mg) enriched for phosphopeptides by Fe-NTA. Phosphopeptides were fractionated into 8 fractions and concatenated into 4 fractions. All samples were measured on an Orbitrap Fusion Lumos. ( B ) Volcano plot showing fold changes of infected versus mock cells for all 15,392 quantified phosphopeptides. P values were calculated using an unpaired, two-sided student’s t-test with equal variance assumed and adjusted using the Benjamini Hochberg FDR method (N = 5). Orange or blue points indicate significantly increased or decreased phosphopeptides, respectively. ( C ) Volcano plot showing differences between SARS-CoV-2 and mock infected cells in total protein levels for all 7,150 quantified proteins. P values were calculated using an unpaired, two-sided student’s t-test with equal variance assumed and adjusted using the Benjamini Hochberg FDR method (N = 5). Orange or blue points indicate significantly increased or decreased phosphopeptides, respectively. ( D ) Distribution of phosphorylation sites identified across modified amino acids. See also Figure S1 and Tables S1 and S2. ( E – K ) Domain structures of SARS-CoV-2 proteins predicted by InterPro. Identified phosphorylation sites are indicated.. Protein 3a ( E ), Membrane Protein M ( F ), Non-structural protein 6 ( G ), Protein 9b ( H ), Replicase Polyprotein 1b ( I ) and Nucleoprotein N ( J ). ( K ) X-ray structure of the RNA binding domain (PDB: 6vyo, residues 47-173) with identified phosphorylation sites marked in red.

    Article Snippet: Liquid chromatography mass spectrometry All mass spectrometry data was acquired in centroid mode on an Orbitrap Fusion Lumos mass spectrometer hyphenated to an easy-nLC 1200 nano HPLC system using a nanoFlex ion source (ThermoFisher Scientific) applying a spray voltage of 2.6 kV with the transfer tube heated to 300°C and a funnel RF of 30%.

    Techniques: Infection, Incubation, Modification, RNA Binding Assay