lc ms analysis  (Thermo Fisher)


Bioz Verified Symbol Thermo Fisher is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Thermo Fisher lc ms analysis
    Lc Ms Analysis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc ms analysis/product/Thermo Fisher
    Average 94 stars, based on 101 article reviews
    Price from $9.99 to $1999.99
    lc ms analysis - by Bioz Stars, 2020-09
    94/100 stars

    Images

    Related Articles

    Chromatography:

    Article Title: Molecular Cloning and Functional Characterization of a Novel (Iso)flavone 4′,7-O-diglucoside Glucosyltransferase from Pueraria lobata
    Article Snippet: .. Liquid chromatography–mass spectrometry analysis was performed on an Accela LC system coupled with TSQ Quantum Access Max mass spectrometer (Thermo Scientific, USA). .. The column and analysis method were same with the HPLC analyses as described above.

    Article Title: Fumarate Hydratase Loss Causes Combined Respiratory Chain Defects
    Article Snippet: .. Liquid Chromatography-Mass Spectrometry Analysis The peptide fractions were analyzed on a Dionex Ultimate 3000 UHPLC system coupled with Q-Exactive mass spectrometer (Thermo Scientific). .. The RP fractions were reconstituted in 40 μL loading solution (2% acetonitrile and 0.1% formic acid), and a 4-μL volume was loaded on the Acclaim PepMap 100, 100 μm × 2 cm C18, 5 μm, 100 Ȧ trapping column with the ulPickUp Injection mode using the loading pump at a 4 μL/min flow rate for 10 min. For the peptide separation, the Acclaim PepMap RSLC, 75 μm × 50 cm, nanoViper, C18, 3 μm, 100 Ȧ column retrofitted to an easy source was used for multi-step gradient elution.

    Flow Cytometry:

    Article Title: ProTargetMiner as a proteome signature library of anticancer molecules for functional discovery
    Article Snippet: .. LC-MS analysis Samples were loaded with buffer A (0.1% FA in water) onto a 50 cm EASY-Spray column (75 µm internal diameter, packed with PepMap C18, 2 µm beads, 100 Å pore size; Cat#ES803) connected to the EASY-nLC 1000 (Thermo; Cat#LC120) and eluted with a buffer B (98% ACN, 0.1% FA, 2% H2 O) gradient from 2 to 35% of at a flow rate of 250 nL min−1 . .. Mass spectra were acquired with an Orbitrap Q Exactive Plus mass spectrometer (Thermo; Cat# IQLAAEGAAPFALGMBDK) in the data-dependent mode with MS1 scan at 70,000 resolution, and MS2 at 35,000, in the m/z range from 375 to 1400.

    Chloramphenicol Acetyltransferase Assay:

    Article Title: ProTargetMiner as a proteome signature library of anticancer molecules for functional discovery
    Article Snippet: .. LC-MS analysis Samples were loaded with buffer A (0.1% FA in water) onto a 50 cm EASY-Spray column (75 µm internal diameter, packed with PepMap C18, 2 µm beads, 100 Å pore size; CatES803) connected to the EASY-nLC 1000 (Thermo; Cat#LC120) and eluted with a buffer B (98% ACN, 0.1% FA, 2% H2 O) gradient from 2 to 35% of at a flow rate of 250 nL min−1 . .. Mass spectra were acquired with an Orbitrap Q Exactive Plus mass spectrometer (Thermo; Cat# IQLAAEGAAPFALGMBDK) in the data-dependent mode with MS1 scan at 70,000 resolution, and MS2 at 35,000, in the m/z range from 375 to 1400.

    Mass Spectrometry:

    Article Title: HLA-F Allele-Specific Peptide Restriction Represents an Exceptional Proteomic Footprint
    Article Snippet: .. The LC/MS analysis was performed using a Dionex Ultimate 3000 high-performance LC system and a LTQ Orbitrap Lumos Mass Spectrometer (Thermo Fisher Scientific) in data-dependent acquisition (DDA) mode. ..

    Article Title: Molecular Cloning and Functional Characterization of a Novel (Iso)flavone 4′,7-O-diglucoside Glucosyltransferase from Pueraria lobata
    Article Snippet: .. Liquid chromatography–mass spectrometry analysis was performed on an Accela LC system coupled with TSQ Quantum Access Max mass spectrometer (Thermo Scientific, USA). .. The column and analysis method were same with the HPLC analyses as described above.

    Article Title: Fumarate Hydratase Loss Causes Combined Respiratory Chain Defects
    Article Snippet: .. Liquid Chromatography-Mass Spectrometry Analysis The peptide fractions were analyzed on a Dionex Ultimate 3000 UHPLC system coupled with Q-Exactive mass spectrometer (Thermo Scientific). .. The RP fractions were reconstituted in 40 μL loading solution (2% acetonitrile and 0.1% formic acid), and a 4-μL volume was loaded on the Acclaim PepMap 100, 100 μm × 2 cm C18, 5 μm, 100 Ȧ trapping column with the ulPickUp Injection mode using the loading pump at a 4 μL/min flow rate for 10 min. For the peptide separation, the Acclaim PepMap RSLC, 75 μm × 50 cm, nanoViper, C18, 3 μm, 100 Ȧ column retrofitted to an easy source was used for multi-step gradient elution.

    Article Title: Bright ligand-activatable fluorescent protein for high-quality multicolor live-cell super-resolution microscopy
    Article Snippet: .. For LC/MS analysis, the LC system was interfaced to a Thermo Finnigan LTQ XL linear ion trap mass spectrometer (Thermo Scientific Inc.) via Ion Max electrospray ionization (ESI) source. ..

    Article Title: Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter
    Article Snippet: .. One microgram of peptides of each sample were subjected to LC-MS analysis using a dual pressure LTQ-Orbitrap Elite mass spectrometer connected to an electrospray ion source (both Thermo Fisher Scientific). .. Peptide separation was carried out using an EASY nLC-1000 system (Thermo Fisher Scientific) equipped with a RP-HPLC column (75 μm × 30 cm) packed in-house with C18 resin (ReproSil-Pur C18–AQ, 1.9 μm resin; Dr Maisch GmbH, Ammerbuch-Entringen, Germany) using a linear gradient from 95% solvent A (0.15% formic acid, 2% acetonitrile) and 5% solvent B (98% acetonitrile, 0.15% formic acid) to 28% solvent B over 75 min at a flow rate of 0.2 μl/min.

    Article Title: Novel Hemizygous IL2RG p.(Pro58Ser) Mutation Impairs IL-2 Receptor Complex Expression on Lymphocytes Causing X-Linked Combined Immunodeficiency
    Article Snippet: .. LC-MS analysis was done with a Q Exactive ESI-quadrupole-orbitrap mass spectrometer coupled to an EASY-nLC 1000 nanoflow LC (Thermo Fisher Scientific) using the Xcalibur version 3.1.66.10 (Thermo Fisher Scientific). .. Database Analysis SEQUEST search algorithm in Proteome Discoverer software (Thermo Fisher Scientific) was used for peak extraction and protein identification with the human reference proteome of UniProtKB database ( www.uniprot.org , Uniprot human 10_2016, with 20,118 sequences).

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: HLA-F Allele-Specific Peptide Restriction Represents an Exceptional Proteomic Footprint
    Article Snippet: .. The LC/MS analysis was performed using a Dionex Ultimate 3000 high-performance LC system and a LTQ Orbitrap Lumos Mass Spectrometer (Thermo Fisher Scientific) in data-dependent acquisition (DDA) mode. ..

    Article Title: Profiling the effect of nafcillin on HA-MRSA D592 using bacteriological and physiological media
    Article Snippet: .. For LC/MS analysis, samples were subjected to chromatographic separation using an UltiMate 3000 UHPLC system (Thermo Scientific). .. Chromatographic separations were achieved using a 50 mm × 2.1 mm Kinetex 2.6 micron polar-C18 column (Phenomenex) held at a fixed temperature of 30 °C within an actively heated column compartment.

    Article Title: ProTargetMiner as a proteome signature library of anticancer molecules for functional discovery
    Article Snippet: .. LC-MS analysis Samples were loaded with buffer A (0.1% FA in water) onto a 50 cm EASY-Spray column (75 µm internal diameter, packed with PepMap C18, 2 µm beads, 100 Å pore size; Cat#ES803) connected to the EASY-nLC 1000 (Thermo; Cat#LC120) and eluted with a buffer B (98% ACN, 0.1% FA, 2% H2 O) gradient from 2 to 35% of at a flow rate of 250 nL min−1 . .. Mass spectra were acquired with an Orbitrap Q Exactive Plus mass spectrometer (Thermo; Cat# IQLAAEGAAPFALGMBDK) in the data-dependent mode with MS1 scan at 70,000 resolution, and MS2 at 35,000, in the m/z range from 375 to 1400.

    Article Title: Bright ligand-activatable fluorescent protein for high-quality multicolor live-cell super-resolution microscopy
    Article Snippet: .. For LC/MS analysis, the LC system was interfaced to a Thermo Finnigan LTQ XL linear ion trap mass spectrometer (Thermo Scientific Inc.) via Ion Max electrospray ionization (ESI) source. ..

    Article Title: Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter
    Article Snippet: .. One microgram of peptides of each sample were subjected to LC-MS analysis using a dual pressure LTQ-Orbitrap Elite mass spectrometer connected to an electrospray ion source (both Thermo Fisher Scientific). .. Peptide separation was carried out using an EASY nLC-1000 system (Thermo Fisher Scientific) equipped with a RP-HPLC column (75 μm × 30 cm) packed in-house with C18 resin (ReproSil-Pur C18–AQ, 1.9 μm resin; Dr Maisch GmbH, Ammerbuch-Entringen, Germany) using a linear gradient from 95% solvent A (0.15% formic acid, 2% acetonitrile) and 5% solvent B (98% acetonitrile, 0.15% formic acid) to 28% solvent B over 75 min at a flow rate of 0.2 μl/min.

    Article Title: Novel Hemizygous IL2RG p.(Pro58Ser) Mutation Impairs IL-2 Receptor Complex Expression on Lymphocytes Causing X-Linked Combined Immunodeficiency
    Article Snippet: .. LC-MS analysis was done with a Q Exactive ESI-quadrupole-orbitrap mass spectrometer coupled to an EASY-nLC 1000 nanoflow LC (Thermo Fisher Scientific) using the Xcalibur version 3.1.66.10 (Thermo Fisher Scientific). .. Database Analysis SEQUEST search algorithm in Proteome Discoverer software (Thermo Fisher Scientific) was used for peak extraction and protein identification with the human reference proteome of UniProtKB database ( www.uniprot.org , Uniprot human 10_2016, with 20,118 sequences).

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Thermo Fisher lc ms ms analysis all peptide
    GPS leads to the identification of ADP-ribosylated ARTDs/PARPs other than ARTD1/PARP1. (A) A comparison using Venn diagrams for ADPr peptides found in two replicates for full scan (400–1500 m / z ) and combined 4× GPS scans (GPS-1, 400–605; GPS-2, 595–805; GPS-3, 795–1005; GPS-4, 995–1200 m / z ). (B) A comparison of ADPr peptides found in control and IFN-γ-treated THP-1 cells for the full scan and combined 4× GPS scans. (C) Sequence motif <t>analysis</t> for ADPr acceptor amino acids (N, number of ADPr peptides used for the analysis). (D) A plot of the number of ADP-ribosylation sites per protein. (E) Comparison of ADPr <t>peptide</t> abundances between control and IFN-γ in each replicate; regression lines, 95% confidence interval, and standard error of estimate (SEE) are provided (red dots are outliers). (F) <t>MS/MS</t> spectra of an ARTD8/PARP14 ADPr peptide using PRM acquisitions. Black peaks were manually annotated. *, ADPr site. (G) A comparison of the number of proteins identified in the Af1521 elution (ADPr proteins) and input samples (backbone proteins) per replicate. (H) A comparison of the relative changes to ADPr peptides versus their backbone proteins in response to IFN-γ (IFN-γ/control).
    Lc Ms Ms Analysis All Peptide, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc ms ms analysis all peptide/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lc ms ms analysis all peptide - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

    88
    Thermo Fisher lc ms analysis lc ms
    Chromatographic profile of the Impatiens glandulifera Royle methanolic extract of the roots measured as total ion current (TIC) by <t>LC-MS</t> (APCI). MS spectrum of THNG is shown on the Figure 3 .
    Lc Ms Analysis Lc Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc ms analysis lc ms/product/Thermo Fisher
    Average 88 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    lc ms analysis lc ms - by Bioz Stars, 2020-09
    88/100 stars
      Buy from Supplier

    90
    Thermo Fisher enriched proteins lc ms analysis
    Heatmap visualization of quantitative values of the 182 <t>proteins</t> <t>enriched</t> at the protein level . Left: heatmap of the 182 proteins identified and quantified over all six HNE exposure groups; Right: Zoomed-in region of the heatmap focusing on the most abundantly detected and identified putative HNE protein adducts. After affinity capture, samples were trypsin-digested and analyzed using <t>LC-MS.</t> Protein quantification was based on the peak intensity of the 3 most intense peptides. A total of 182 proteins were quantified. From top to bottom the 182 identified proteins are listed and each row represents a protein and its corresponding abundance. From left to right, HNE concentrations that were used for the in vitro exposure experiments of the mitochondrial protein samples. The color in each cell represents protein abundance obtained from the “Hi3” peptide intensity approach: red is more abundant and dark green is less abundant. Black indicates missing values.
    Enriched Proteins Lc Ms Analysis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/enriched proteins lc ms analysis/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    enriched proteins lc ms analysis - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    Image Search Results


    GPS leads to the identification of ADP-ribosylated ARTDs/PARPs other than ARTD1/PARP1. (A) A comparison using Venn diagrams for ADPr peptides found in two replicates for full scan (400–1500 m / z ) and combined 4× GPS scans (GPS-1, 400–605; GPS-2, 595–805; GPS-3, 795–1005; GPS-4, 995–1200 m / z ). (B) A comparison of ADPr peptides found in control and IFN-γ-treated THP-1 cells for the full scan and combined 4× GPS scans. (C) Sequence motif analysis for ADPr acceptor amino acids (N, number of ADPr peptides used for the analysis). (D) A plot of the number of ADP-ribosylation sites per protein. (E) Comparison of ADPr peptide abundances between control and IFN-γ in each replicate; regression lines, 95% confidence interval, and standard error of estimate (SEE) are provided (red dots are outliers). (F) MS/MS spectra of an ARTD8/PARP14 ADPr peptide using PRM acquisitions. Black peaks were manually annotated. *, ADPr site. (G) A comparison of the number of proteins identified in the Af1521 elution (ADPr proteins) and input samples (backbone proteins) per replicate. (H) A comparison of the relative changes to ADPr peptides versus their backbone proteins in response to IFN-γ (IFN-γ/control).

    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: GPS leads to the identification of ADP-ribosylated ARTDs/PARPs other than ARTD1/PARP1. (A) A comparison using Venn diagrams for ADPr peptides found in two replicates for full scan (400–1500 m / z ) and combined 4× GPS scans (GPS-1, 400–605; GPS-2, 595–805; GPS-3, 795–1005; GPS-4, 995–1200 m / z ). (B) A comparison of ADPr peptides found in control and IFN-γ-treated THP-1 cells for the full scan and combined 4× GPS scans. (C) Sequence motif analysis for ADPr acceptor amino acids (N, number of ADPr peptides used for the analysis). (D) A plot of the number of ADP-ribosylation sites per protein. (E) Comparison of ADPr peptide abundances between control and IFN-γ in each replicate; regression lines, 95% confidence interval, and standard error of estimate (SEE) are provided (red dots are outliers). (F) MS/MS spectra of an ARTD8/PARP14 ADPr peptide using PRM acquisitions. Black peaks were manually annotated. *, ADPr site. (G) A comparison of the number of proteins identified in the Af1521 elution (ADPr proteins) and input samples (backbone proteins) per replicate. (H) A comparison of the relative changes to ADPr peptides versus their backbone proteins in response to IFN-γ (IFN-γ/control).

    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: Sequencing, Mass Spectrometry

    Data processing of product ion triggered MS/MS spectra. (A) A schematic of SEQUEST-HT searches of triggered EThcD and HCD spectra using the second Af1521 replicate of IFN-γ-treated THP-1 cells. (B) Number of peptide-spectrum matches (PSMs) of assigned ADPr and unmodified peptides from the triggered spectra. (C–E) Distribution of isolation interference for product ion triggered or DDA PSMs. (F) Number of ADPr peptides with high confidence detected by either EThcD or HCD. (G) Venn diagrams comparing ADPr peptide identifications between EThcD and HCD for all ADPr peptides, and those with > 95% ADPr acceptor site probability.

    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: Data processing of product ion triggered MS/MS spectra. (A) A schematic of SEQUEST-HT searches of triggered EThcD and HCD spectra using the second Af1521 replicate of IFN-γ-treated THP-1 cells. (B) Number of peptide-spectrum matches (PSMs) of assigned ADPr and unmodified peptides from the triggered spectra. (C–E) Distribution of isolation interference for product ion triggered or DDA PSMs. (F) Number of ADPr peptides with high confidence detected by either EThcD or HCD. (G) Venn diagrams comparing ADPr peptide identifications between EThcD and HCD for all ADPr peptides, and those with > 95% ADPr acceptor site probability.

    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: Mass Spectrometry, Isolation

    Chromatographic profile of the Impatiens glandulifera Royle methanolic extract of the roots measured as total ion current (TIC) by LC-MS (APCI). MS spectrum of THNG is shown on the Figure 3 .

    Journal: Molecules

    Article Title: Separation and Identification of 1,2,4-Trihydroxynaphthalene-1-O-glucoside in Impatiens glandulifera Royle

    doi: 10.3390/molecules18078429

    Figure Lengend Snippet: Chromatographic profile of the Impatiens glandulifera Royle methanolic extract of the roots measured as total ion current (TIC) by LC-MS (APCI). MS spectrum of THNG is shown on the Figure 3 .

    Article Snippet: LC-MS Analysis LC-MS was performed using LCQ Accela Fleet (Thermo Fisher Scientific, San Jose, CA, USA) with atmospheric pressure chemical (APCI) and a photodiode array detector.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    Strategy of SUMO1 modified sites immunoaffinity purification. (A) Representation of the C-terminal sequence comparison of SUMO1 WT , SUMO1 ΔGG and SUMO1 T95R after trypsin digestion. (B) Immunoblot analysis confirmed the expressions of SUMO1-conjugated proteins in SUMO1 WT and SUMO1 T95R . HEK293T cells were stably transfected with indicated plasmids and SUMO1 ΔGG was chosen as the negative control. Ponceau-S staining was shown as loading control. (C) Schematic overview of His 10 -SUMO1 T95R -modified peptides identification. Stably expressing cell samples transfected with indicated plasmids were subjected to the first concentration of SUMOylated proteins and trypsin digestion, followed by peptide IP to enrich SUMO1-conjugated peptides. diGly featured peptides were subsequently exposed for LC-MS/MS identification. (D) Validation of expression patterns and level of conjugation by immunoblot analysis. His 10 -SUMO1 WT , His 10 -SUMO1 ΔGG , SUMO1 T95R and SUMO1 T95K stable cells were lysed and subjected to Ni-NTA pulldown assay. The presence of ubiquitin and ubiquitin-like modifier patterns were confirmed with indicated antibodies. (E) Detection of SUMOylation patterns after transfection of SENP family members. SUMOylated proteins from His 10 -SUMO1 T95R stably expressed cells with EV and Flag-tagged SENP family members transfected were pulled down and analyzed by immunoblot using anti-SUMO1, anti-Flag or anti-Actin antibodies. Ponceau-S staining was shown as loading control. (F) Schematic workflow of the deduction strategy for constructing SUMO1-modified proteome. Venn plot indicated the number of overlapped diGly sites detected in His 10 -SUMO1 ΔGG , SUMO1 T95R and SUMO1 T95K stable cells.

    Journal: bioRxiv

    Article Title: Global Screening of Sentrin-Specific Protease Family Substrates in SUMOylation

    doi: 10.1101/2020.02.25.964072

    Figure Lengend Snippet: Strategy of SUMO1 modified sites immunoaffinity purification. (A) Representation of the C-terminal sequence comparison of SUMO1 WT , SUMO1 ΔGG and SUMO1 T95R after trypsin digestion. (B) Immunoblot analysis confirmed the expressions of SUMO1-conjugated proteins in SUMO1 WT and SUMO1 T95R . HEK293T cells were stably transfected with indicated plasmids and SUMO1 ΔGG was chosen as the negative control. Ponceau-S staining was shown as loading control. (C) Schematic overview of His 10 -SUMO1 T95R -modified peptides identification. Stably expressing cell samples transfected with indicated plasmids were subjected to the first concentration of SUMOylated proteins and trypsin digestion, followed by peptide IP to enrich SUMO1-conjugated peptides. diGly featured peptides were subsequently exposed for LC-MS/MS identification. (D) Validation of expression patterns and level of conjugation by immunoblot analysis. His 10 -SUMO1 WT , His 10 -SUMO1 ΔGG , SUMO1 T95R and SUMO1 T95K stable cells were lysed and subjected to Ni-NTA pulldown assay. The presence of ubiquitin and ubiquitin-like modifier patterns were confirmed with indicated antibodies. (E) Detection of SUMOylation patterns after transfection of SENP family members. SUMOylated proteins from His 10 -SUMO1 T95R stably expressed cells with EV and Flag-tagged SENP family members transfected were pulled down and analyzed by immunoblot using anti-SUMO1, anti-Flag or anti-Actin antibodies. Ponceau-S staining was shown as loading control. (F) Schematic workflow of the deduction strategy for constructing SUMO1-modified proteome. Venn plot indicated the number of overlapped diGly sites detected in His 10 -SUMO1 ΔGG , SUMO1 T95R and SUMO1 T95K stable cells.

    Article Snippet: MS Analysis LC-MS/MS analyses were performed on an Easy-nLC 1000 liquid-chromatography system (Thermo Fisher Scientific) coupled with a Q-Exactive HF through a nano-electrospray ion source (Thermo Fisher Scientific).

    Techniques: Modification, Immunoaffinity Purification, Sequencing, Stable Transfection, Transfection, Negative Control, Staining, Expressing, Concentration Assay, Liquid Chromatography with Mass Spectroscopy, Conjugation Assay

    SENP3 promotes antiviral immunity during poly (I:C) stimulation in HEK293 cells. (A) Schematic representations of SENP3 interactome identification during poly (I:C) stimulation in HEK293 cells. EV and Flag-tagged SENP3 were transfected into HEK293 cells and poly (I:C) stimulation was performed 6hr before cell collection. The lysates were subjected to immunoprecipitation and then in gel digestion for LC-MS/MS. Three biological replicates were performed for data analysis. (B) The interaction network of SENP3 in HEK293 cells, with or without poly (I:C) treatment. (C) Increased association of SENP3 interacted inflammatory proteins under poly (I:C) stimulation and the expression profiles were represented. (D) The GO/pathway enrichment analysis of SENP3 interactome under poly (I:C) stimulation. (E) Potential mechanism of SENP3 in regulating RNA-virus induced immune signaling pathway.

    Journal: bioRxiv

    Article Title: Global Screening of Sentrin-Specific Protease Family Substrates in SUMOylation

    doi: 10.1101/2020.02.25.964072

    Figure Lengend Snippet: SENP3 promotes antiviral immunity during poly (I:C) stimulation in HEK293 cells. (A) Schematic representations of SENP3 interactome identification during poly (I:C) stimulation in HEK293 cells. EV and Flag-tagged SENP3 were transfected into HEK293 cells and poly (I:C) stimulation was performed 6hr before cell collection. The lysates were subjected to immunoprecipitation and then in gel digestion for LC-MS/MS. Three biological replicates were performed for data analysis. (B) The interaction network of SENP3 in HEK293 cells, with or without poly (I:C) treatment. (C) Increased association of SENP3 interacted inflammatory proteins under poly (I:C) stimulation and the expression profiles were represented. (D) The GO/pathway enrichment analysis of SENP3 interactome under poly (I:C) stimulation. (E) Potential mechanism of SENP3 in regulating RNA-virus induced immune signaling pathway.

    Article Snippet: MS Analysis LC-MS/MS analyses were performed on an Easy-nLC 1000 liquid-chromatography system (Thermo Fisher Scientific) coupled with a Q-Exactive HF through a nano-electrospray ion source (Thermo Fisher Scientific).

    Techniques: Transfection, Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Expressing

    Heatmap visualization of quantitative values of the 182 proteins enriched at the protein level . Left: heatmap of the 182 proteins identified and quantified over all six HNE exposure groups; Right: Zoomed-in region of the heatmap focusing on the most abundantly detected and identified putative HNE protein adducts. After affinity capture, samples were trypsin-digested and analyzed using LC-MS. Protein quantification was based on the peak intensity of the 3 most intense peptides. A total of 182 proteins were quantified. From top to bottom the 182 identified proteins are listed and each row represents a protein and its corresponding abundance. From left to right, HNE concentrations that were used for the in vitro exposure experiments of the mitochondrial protein samples. The color in each cell represents protein abundance obtained from the “Hi3” peptide intensity approach: red is more abundant and dark green is less abundant. Black indicates missing values.

    Journal: Frontiers in Chemistry

    Article Title: Label-Free Proteomics Assisted by Affinity Enrichment for Elucidating the Chemical Reactivity of the Liver Mitochondrial Proteome toward Adduction by the Lipid Electrophile 4-hydroxy-2-nonenal (HNE)

    doi: 10.3389/fchem.2016.00002

    Figure Lengend Snippet: Heatmap visualization of quantitative values of the 182 proteins enriched at the protein level . Left: heatmap of the 182 proteins identified and quantified over all six HNE exposure groups; Right: Zoomed-in region of the heatmap focusing on the most abundantly detected and identified putative HNE protein adducts. After affinity capture, samples were trypsin-digested and analyzed using LC-MS. Protein quantification was based on the peak intensity of the 3 most intense peptides. A total of 182 proteins were quantified. From top to bottom the 182 identified proteins are listed and each row represents a protein and its corresponding abundance. From left to right, HNE concentrations that were used for the in vitro exposure experiments of the mitochondrial protein samples. The color in each cell represents protein abundance obtained from the “Hi3” peptide intensity approach: red is more abundant and dark green is less abundant. Black indicates missing values.

    Article Snippet: LC-MS-based quantitative analysis of enriched proteins LC-MS analysis of the peptide samples from protein level or peptide level enrichment was performed using a hybrid linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer (LTQ-FT Ultra, Thermo Fisher) coupled to a NanoAcquity UPLC (Waters, MA) equipped with a BEH C18 column (100 μm × 15 cm) (Waters Corp.).

    Techniques: Liquid Chromatography with Mass Spectroscopy, In Vitro