orbitrap fusion instrument  (Thermo Fisher)


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  • 90

    Structured Review

    Thermo Fisher orbitrap fusion instrument
    Tandem MS (EThcD) of an AGP middle-down glycopeptide on an <t>Orbitrap</t> Fusion instrument (precursor m/z : 1302.4178, [M+7H] 7+ ). ETD reaction time was 8.75 msec and HCD normalized collision energy was set at 20 for this scan. C* = Carbamidomethyl Cysteine.
    Orbitrap Fusion Instrument, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/orbitrap fusion instrument/product/Thermo Fisher
    Average 90 stars, based on 32 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion instrument - by Bioz Stars, 2020-07
    90/100 stars

    Images

    1) Product Images from "Comparison of collisional and electron-based dissociation modes for middle-down analysis of multiply glycosylated peptides"

    Article Title: Comparison of collisional and electron-based dissociation modes for middle-down analysis of multiply glycosylated peptides

    Journal: Journal of the American Society for Mass Spectrometry

    doi: 10.1007/s13361-018-1909-y

    Tandem MS (EThcD) of an AGP middle-down glycopeptide on an Orbitrap Fusion instrument (precursor m/z : 1302.4178, [M+7H] 7+ ). ETD reaction time was 8.75 msec and HCD normalized collision energy was set at 20 for this scan. C* = Carbamidomethyl Cysteine.
    Figure Legend Snippet: Tandem MS (EThcD) of an AGP middle-down glycopeptide on an Orbitrap Fusion instrument (precursor m/z : 1302.4178, [M+7H] 7+ ). ETD reaction time was 8.75 msec and HCD normalized collision energy was set at 20 for this scan. C* = Carbamidomethyl Cysteine.

    Techniques Used: Mass Spectrometry

    Related Articles

    Activation Assay:

    Article Title: Comparison of collisional and electron-based dissociation modes for middle-down analysis of multiply glycosylated peptides
    Article Snippet: .. HCD and EThcD (Higher-energy Collisional Dissociation and Electron Transfer Dissociation supplemental collisional activation) ( – ) experiments were performed on ZIC-HILIC-enriched and unfractionated bottom-up and middle-down glycopeptide samples by LC-MS using an EASY-nLC chromatograph with an EASY-Spray C18 LC column on a Thermo Orbitrap Fusion™ instrument. .. The instrument was set to perform HCD-triggered EThcD, which allowed EThcD to be performed only on precursor ions that generated saccharide oxonium ions.

    Mass Spectrometry:

    Article Title: Mechanism of pharmacochaperoning in a mammalian KATP channel revealed by cryo-EM
    Article Snippet: .. Data-dependent tandem mass spectrometry analysis was performed using an Orbitrap Fusion instrument fitted with an EasySpray source (Thermo Fisher Scientific). .. Survey scans (m/z = 400–1500) and data-dependent MS2 scans were performed in the Orbitrap mass analyzer at a resolution = 120,000, and 30,000, respectively, following higher energy collision dissociation (HCD) using a collision energy of 35 following quadrupole isolation at a 1.6 m/z isolation width.

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: Comparison of collisional and electron-based dissociation modes for middle-down analysis of multiply glycosylated peptides
    Article Snippet: .. HCD and EThcD (Higher-energy Collisional Dissociation and Electron Transfer Dissociation supplemental collisional activation) ( – ) experiments were performed on ZIC-HILIC-enriched and unfractionated bottom-up and middle-down glycopeptide samples by LC-MS using an EASY-nLC chromatograph with an EASY-Spray C18 LC column on a Thermo Orbitrap Fusion™ instrument. .. The instrument was set to perform HCD-triggered EThcD, which allowed EThcD to be performed only on precursor ions that generated saccharide oxonium ions.

    Tandem Mass Spectroscopy:

    Article Title: Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions
    Article Snippet: .. MS/MS experiments were performed on-line on an Orbitrap Fusion instrument (Thermo) performing a full scan acquisition (in the Orbitrap), followed by a MS/MS scan of the top five most intense ions of each full scan (in the Ion Trap) using helium as collision gas (low-energy CID). ..

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    Thermo Fisher orbitrap fusion tribrid mass spectrometer
    Proteomic analysis of tryptic peptides from (a) expressed archetype and splice variants of human OGDH E1 and (b) OGDH E1 separated from rat brain and heart mitochondria. Results are shown as PSM for the indicated peptide or the mean of peptides a and b expressed as percentages of the total E1 protein PSM and are means ± S.E.M. for three or four observations. Values of total E1 protein PSM were archetype 3571 ± 552 ( n = 4), LS1 3719 ± 552 ( n = 3), Insert 3782 ± 1961 ( n = 3), LS1/Insert 3407 ± 156 ( n = 3), rat brain OGDH E1 620 ± 126 ( n = 4) and rat heart OGDH E1 1086 ± 126 ( n = 4). All observations were obtained using an <t>Orbitrap</t> Fusion <t>Tribrid</t> mass spectrometer. The number of PSM is a measure of the amount of a peptide.
    Orbitrap Fusion Tribrid Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 654 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/orbitrap fusion tribrid mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 654 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion tribrid mass spectrometer - by Bioz Stars, 2020-07
    99/100 stars
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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 265 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 265 article reviews
    Price from $9.99 to $1999.99
    orbitrap fusion lumos mass spectrometer - by Bioz Stars, 2020-07
    99/100 stars
      Buy from Supplier

    Image Search Results


    Proteomic analysis of tryptic peptides from (a) expressed archetype and splice variants of human OGDH E1 and (b) OGDH E1 separated from rat brain and heart mitochondria. Results are shown as PSM for the indicated peptide or the mean of peptides a and b expressed as percentages of the total E1 protein PSM and are means ± S.E.M. for three or four observations. Values of total E1 protein PSM were archetype 3571 ± 552 ( n = 4), LS1 3719 ± 552 ( n = 3), Insert 3782 ± 1961 ( n = 3), LS1/Insert 3407 ± 156 ( n = 3), rat brain OGDH E1 620 ± 126 ( n = 4) and rat heart OGDH E1 1086 ± 126 ( n = 4). All observations were obtained using an Orbitrap Fusion Tribrid mass spectrometer. The number of PSM is a measure of the amount of a peptide.

    Journal: The Biochemical journal

    Article Title: Calcium-insensitive splice variants of mammalian E1 subunit of 2-oxoglutarate dehydrogenase complex with tissue-specific patterns of expression

    doi: 10.1042/BCJ20160135

    Figure Lengend Snippet: Proteomic analysis of tryptic peptides from (a) expressed archetype and splice variants of human OGDH E1 and (b) OGDH E1 separated from rat brain and heart mitochondria. Results are shown as PSM for the indicated peptide or the mean of peptides a and b expressed as percentages of the total E1 protein PSM and are means ± S.E.M. for three or four observations. Values of total E1 protein PSM were archetype 3571 ± 552 ( n = 4), LS1 3719 ± 552 ( n = 3), Insert 3782 ± 1961 ( n = 3), LS1/Insert 3407 ± 156 ( n = 3), rat brain OGDH E1 620 ± 126 ( n = 4) and rat heart OGDH E1 1086 ± 126 ( n = 4). All observations were obtained using an Orbitrap Fusion Tribrid mass spectrometer. The number of PSM is a measure of the amount of a peptide.

    Article Snippet: The number of peptide spectral matches (PSM) can be used as a measure of the amount of a particular peptide [ – ]. shows the values of PSM for the various relevant peptides with mass/charge ratios in the range 300–2000 which were detected in studies using the Orbitrap Fusion Tribrid mass spectrometer on samples of expressed human archetype and the three splice variants.

    Techniques: Mass Spectrometry

    Metabolic Labeling and Workflow. ( A ) Glucose, acetate, fatty acids, and amino acids produce acetyl-CoA for use in acetylating cytoplasmic and nuclear proteins. The thicker arrows indicate that glucose contributes more to the production of acetyl-coA that subsequently acetylates proteins, compared to acetate. ( B ) The workflow consisted of growing HeLa cells in heavy-labeled media, collecting samples at eight time points, lysing the cells, digesting the proteins, enriching for acetylated peptides, and analyzing the peptides by mass spectrometry. The Orbitrap image is adapted from Thermo Fisher Scientific 56 . The cartoon cell matter and lab equipment were slightly modified from Servier Medical Art 57 .

    Journal: Scientific Reports

    Article Title: Proteome-wide acetylation dynamics in human cells

    doi: 10.1038/s41598-017-09918-3

    Figure Lengend Snippet: Metabolic Labeling and Workflow. ( A ) Glucose, acetate, fatty acids, and amino acids produce acetyl-CoA for use in acetylating cytoplasmic and nuclear proteins. The thicker arrows indicate that glucose contributes more to the production of acetyl-coA that subsequently acetylates proteins, compared to acetate. ( B ) The workflow consisted of growing HeLa cells in heavy-labeled media, collecting samples at eight time points, lysing the cells, digesting the proteins, enriching for acetylated peptides, and analyzing the peptides by mass spectrometry. The Orbitrap image is adapted from Thermo Fisher Scientific 56 . The cartoon cell matter and lab equipment were slightly modified from Servier Medical Art 57 .

    Article Snippet: Acetylated peptides were then enriched using anti-acetyl-lysine antibodies and run on nano liquid chromatography coupled online with tandem mass spectrometry (nanoLC-MS/MS) on an Orbitrap Fusion mass spectrometer (Thermo Fisher Scientific), which allows for detection of isotope incorporation into acetylated proteins.

    Techniques: Labeling, Mass Spectrometry, Modification

    Experiment workflow. A) Control and AD human postmortem frontal cortex brain tissues (n=5 each group) were homogenized in 8M urea lysis buffer. For both global and ubiquitylome analysis, brain protein extracts from each sample was first denatured, alkylated and proteolytically digested followed by peptide desalting as described in methods. For global proteome analysis, peptides were analyzed by LC-MS/MS on Orbitrap Fusion Tribrid mass spectrometer. For brain ubiquitylome analysis, peptides were subjected to di-Gly affinity enrichment as described in methods followed by LC-MS/MS analysis in replicate on an Orbitrap Fusion Tribrid mass spectrometer. Protein abundance was calculated by peptide ion-intensity measurements across LC-MS runs using the label free quantification (LFQ) algorithm in MaxQuant.

    Journal: Proteomics

    Article Title: Quantitative Analysis of the Brain Ubiquitylome in Alzheimer’s Disease

    doi: 10.1002/pmic.201800108

    Figure Lengend Snippet: Experiment workflow. A) Control and AD human postmortem frontal cortex brain tissues (n=5 each group) were homogenized in 8M urea lysis buffer. For both global and ubiquitylome analysis, brain protein extracts from each sample was first denatured, alkylated and proteolytically digested followed by peptide desalting as described in methods. For global proteome analysis, peptides were analyzed by LC-MS/MS on Orbitrap Fusion Tribrid mass spectrometer. For brain ubiquitylome analysis, peptides were subjected to di-Gly affinity enrichment as described in methods followed by LC-MS/MS analysis in replicate on an Orbitrap Fusion Tribrid mass spectrometer. Protein abundance was calculated by peptide ion-intensity measurements across LC-MS runs using the label free quantification (LFQ) algorithm in MaxQuant.

    Article Snippet: Peptides were analyzed on an Orbitrap Fusion Tribrid Mass Spectrometer (ThermoFisher Scientific).

    Techniques: Lysis, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    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