orbitrap fusion lumos instrument  (Thermo Fisher)


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    Structured Review

    Thermo Fisher orbitrap fusion lumos instrument
    Orbitrap Fusion Lumos Instrument, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/orbitrap fusion lumos instrument/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion lumos instrument - by Bioz Stars, 2020-02
    99/100 stars

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    Injection:

    Article Title: Characterization of Aspergillus fumigatus Extracellular Vesicles and Their Effects on Macrophages and Neutrophils Functions
    Article Snippet: An Easy-nLC 1200 system (Thermo Fisher Scientific Corp., Waltham, MA, United States) was coupled to an Orbitrap Fusion Lumos instrument equipped with a nanospray source (Thermo Fisher Scientific Corp., Waltham, MA, United States). .. Samples (3 μL) were injected onto a trapping column (Acclaim PepMap 0.075 mm, 2 cm, C18, 3 μm, 100 A; Thermo) in line with a Nano-LC column (Acclaim PepMap RSLC (0.075 mm, 15 cm, C18, 2 μm, 100 A; Thermo).

    Flow Cytometry:

    Article Title: Characterization of Aspergillus fumigatus Extracellular Vesicles and Their Effects on Macrophages and Neutrophils Functions
    Article Snippet: An Easy-nLC 1200 system (Thermo Fisher Scientific Corp., Waltham, MA, United States) was coupled to an Orbitrap Fusion Lumos instrument equipped with a nanospray source (Thermo Fisher Scientific Corp., Waltham, MA, United States). .. Nano-LC solvents were water with 0.1% formic acid (A) and acetonitrile: water (80:20) with 0.1% formic acid (B) and the flow rate was 300 nL/min.

    Mass Spectrometry:

    Article Title: Characterization of Aspergillus fumigatus Extracellular Vesicles and Their Effects on Macrophages and Neutrophils Functions
    Article Snippet: Paragraph title: Proteomic Analysis by Liquid Chromatography-Tandem Mass Spectrometry ... An Easy-nLC 1200 system (Thermo Fisher Scientific Corp., Waltham, MA, United States) was coupled to an Orbitrap Fusion Lumos instrument equipped with a nanospray source (Thermo Fisher Scientific Corp., Waltham, MA, United States).

    Chromatography:

    Article Title: Characterization of Aspergillus fumigatus Extracellular Vesicles and Their Effects on Macrophages and Neutrophils Functions
    Article Snippet: Paragraph title: Proteomic Analysis by Liquid Chromatography-Tandem Mass Spectrometry ... An Easy-nLC 1200 system (Thermo Fisher Scientific Corp., Waltham, MA, United States) was coupled to an Orbitrap Fusion Lumos instrument equipped with a nanospray source (Thermo Fisher Scientific Corp., Waltham, MA, United States).

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    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: 90/100, based on 61 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 90 stars, based on 61 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion lumos mass spectrometer - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    75
    Thermo Fisher instrument orbitrap fusion lumos
    MS/MS spectra of sequences generated on <t>Orbitrap</t> Fusion <t>Lumos</t> under ETD mode.
    Instrument Orbitrap Fusion Lumos, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 75/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/instrument orbitrap fusion lumos/product/Thermo Fisher
    Average 75 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    instrument orbitrap fusion lumos - by Bioz Stars, 2020-02
    75/100 stars
      Buy from Supplier

    Image Search Results


    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

    MS/MS spectra of sequences generated on Orbitrap Fusion Lumos under ETD mode.

    Journal: EuPA Open Proteomics

    Article Title: Quick and clean: Cracking sentences encoded in E. coli by LC–MS/MS, de novo sequencing, and dictionary search

    doi: 10.1016/j.euprot.2019.07.010

    Figure Lengend Snippet: MS/MS spectra of sequences generated on Orbitrap Fusion Lumos under ETD mode.

    Article Snippet: At the same time, we decided to analyze the sample on a different instrument – Orbitrap Fusion Lumos (Thermo Fisher) – to take advantage of multiple fragmentation modes (CID, HCD, ETD and EThcD) since we had plenty of sample left.

    Techniques: Mass Spectrometry, Generated

    MS/MS spectra of sequences generated on Orbitrap Fusion Lumos under CID mode and on Q Exactive HF-X under HCD mode.

    Journal: EuPA Open Proteomics

    Article Title: Quick and clean: Cracking sentences encoded in E. coli by LC–MS/MS, de novo sequencing, and dictionary search

    doi: 10.1016/j.euprot.2019.07.010

    Figure Lengend Snippet: MS/MS spectra of sequences generated on Orbitrap Fusion Lumos under CID mode and on Q Exactive HF-X under HCD mode.

    Article Snippet: At the same time, we decided to analyze the sample on a different instrument – Orbitrap Fusion Lumos (Thermo Fisher) – to take advantage of multiple fragmentation modes (CID, HCD, ETD and EThcD) since we had plenty of sample left.

    Techniques: Mass Spectrometry, Generated

    Experimental design for comparing the ability of a label-free (LFQ) and a tandem mass tag (TMT) dependent method to quantify changes among the less abundant proteins in a proteome. Yeast lysate was spiked into human lysate to 10% of total protein concentration (1× group), 5% (2× group), and 3.3% (3× group) for a total of 11 samples so that the ratio between the first group and second was a 2-fold change, and between the first and third group was a 3-fold change. Samples for TMT were labeled with unique isobaric tags per sample, mixed, and fractionated by basic pH reversed phase HPLC (RP-HPLC). Eleven samples from LFQ and 11 fractions of the TMT set were analyzed on the same Orbitrap Fusion Lumos mass spectrometer with online RP-nHPLC separation with 3 h gradients. Data from label-free samples were processed through MaxQuant using the Andromeda search engine (including match-between-runs and the MaxLFQ algorithm). Data from the TMT fractions were processed using the SEQUEST search engine to identify peptides, and reporter ion abundances were extracted directly from associated SPS-MS3 spectra.

    Journal: Journal of proteome research

    Article Title: Proteome-Wide Evaluation of Two Common Protein Quantification Methods

    doi: 10.1021/acs.jproteome.8b00016

    Figure Lengend Snippet: Experimental design for comparing the ability of a label-free (LFQ) and a tandem mass tag (TMT) dependent method to quantify changes among the less abundant proteins in a proteome. Yeast lysate was spiked into human lysate to 10% of total protein concentration (1× group), 5% (2× group), and 3.3% (3× group) for a total of 11 samples so that the ratio between the first group and second was a 2-fold change, and between the first and third group was a 3-fold change. Samples for TMT were labeled with unique isobaric tags per sample, mixed, and fractionated by basic pH reversed phase HPLC (RP-HPLC). Eleven samples from LFQ and 11 fractions of the TMT set were analyzed on the same Orbitrap Fusion Lumos mass spectrometer with online RP-nHPLC separation with 3 h gradients. Data from label-free samples were processed through MaxQuant using the Andromeda search engine (including match-between-runs and the MaxLFQ algorithm). Data from the TMT fractions were processed using the SEQUEST search engine to identify peptides, and reporter ion abundances were extracted directly from associated SPS-MS3 spectra.

    Article Snippet: Eleven, 3-h gradients were collected using an Orbitrap Fusion Lumos instrument coupled to a Proxeon EASY-nLC 1200 liquid chromatography (LC) pump (Thermo Fisher Scientific).

    Techniques: Protein Concentration, Labeling, High Performance Liquid Chromatography, Mass Spectrometry