hybrid thermo ltq orbitrapxl  (Thermo Fisher)


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    Thermo Fisher hybrid thermo ltq orbitrapxl
    Hybrid Thermo Ltq Orbitrapxl, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hybrid thermo ltq orbitrapxl/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hybrid thermo ltq orbitrapxl - by Bioz Stars, 2020-07
    86/100 stars

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    Mass Spectrometry:

    Article Title: Mechanism of Ca2+-triggered ESCRT assembly and regulation of cell membrane repair
    Article Snippet: .. LC-MS/MS All analyses were carried out on a hybrid Thermo LTQ-OrbitrapXL (San Jose, CA) mass spectrometer coupled online to an Eksigent nano-LC system (AB Sciex, Framingham, MA). .. Each sample was injected via an autosampler and loaded onto a Symmetry C18 trap column (5μm, 300 μm i.d.

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    Thermo Fisher maldi linear ion trap orbitrap hybrid mass spectrometer
    Accumulation of lipid droplets and spatial distribution of different triacylglycerol (TAG) molecular species within transgenic leaf tissue. (a) 3D reconstructed z-stacks of confocal images from wild-type (left) and transgenic (right) leaf tissue. Neutral lipids including TAG, stained with BODIPY, appear as green droplets within the leaf mesophyll cells that contain visible chloroplasts (red autofluorescence). Note that non-TAG features also fluorescing green include the vascular bundle and leaf epidermis. (b) Bright-field microscopy images of wild-type (upper) and transgenic (lower) leaf cross-sections subsequently used for <t>MALDI-Orbitrap</t> imaging. Scale bars correspond to 1000 microns. (c) Ratio of TAG total ion counts (TIC; all TAG molecular species summed at each analysed position) to PC-TIC as detected by MALDI-Orbitrap imaging in wild-type (upper) and transgenic (lower) leaf cross-sections. (d) Spatial distribution of selected dominant TAG and PC species across a transgenic leaf cross-section as observed by MALDI-Orbitrap.
    Maldi Linear Ion Trap Orbitrap Hybrid Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/maldi linear ion trap orbitrap hybrid mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 34 article reviews
    Price from $9.99 to $1999.99
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    85
    Thermo Fisher esi ltq orbitrap hybrid mass spectrometer
    <t>ESI</t> <t>LTQ</t> <t>OrbiTrap</t> mass spectrum of digested sPNAG, acquired in positive mode. Purified sPNAG was digested with Dispersin B in water and analyzed by mass spectrometry after dialysis. For simplicity, only the most prominent peaks are labeled with their m/z and z values (where z is the charge). For each labeled peak, molecular composition was schematically illustrated by red and green circles representing acetylated and non-acetylated saccharide units, respectively (e.g., two red and three green circles corresponds to a pentamer with two N-acetylglucosamine and three glucosamine residues). For all identified molecules, the ion-pairs corresponding to the singly-charged protonated ions and their dehydration products were detected (e.g., 383.17 and 365.16). As shown in the figure, all prominent peaks correspond to a partially de-acetylated N-acetylglucosamine oligomer or the monomers. Almost all unlabeled peaks correspond to one member of some dehydrated-nondehydrated ion pairs, doubly charged versions of some of the expected molecules, or some adducts. A complete list of m/z values for all potential mono- and oligosaccharides species that could be generated from an incomplete digestion of a PNAG sample with all possible acetylation patterns is also given in Table S1 , as a reference.
    Esi Ltq Orbitrap Hybrid Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
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    85
    Thermo Fisher ltq orbitrap hybrid instrument
    Quantitative analysis of the rapamycin-sensitive phosphoproteome by SILAC. (A) Schematic overview of the experimental approach for the identification of TORC1 regulated phosphorylation sites in S. cerevisiae . Two yeast cultures (strain YPJ2) were metabolically labeled with 12 C 6 - 14 N 2 -lysine/ 12 C 6 -arginine (light) or 13 C 6 - 15 N 2 -lysine/ 13 C 6 -arginine (heavy). The heavy culture was treated for 15 min with rapamycin. Extracts were mixed in a 1:1 ratio and separated by preparative SDS-PAGE. The gel was horizontally sliced into 16 sections and in-gel–digested, and phosphopeptides were IMAC-enriched and analyzed in an <t>LTQ-Orbitrap.</t> (B) Merged data from the four experiments revealed 972 phosphoproteins, corresponding to 2487 unique phosphopeptides and 2607 unique phosphosites. (C) Analysis by Motif-X of all regulated phosphopeptides.
    Ltq Orbitrap Hybrid Instrument, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq orbitrap hybrid instrument/product/Thermo Fisher
    Average 85 stars, based on 1 article reviews
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    Accumulation of lipid droplets and spatial distribution of different triacylglycerol (TAG) molecular species within transgenic leaf tissue. (a) 3D reconstructed z-stacks of confocal images from wild-type (left) and transgenic (right) leaf tissue. Neutral lipids including TAG, stained with BODIPY, appear as green droplets within the leaf mesophyll cells that contain visible chloroplasts (red autofluorescence). Note that non-TAG features also fluorescing green include the vascular bundle and leaf epidermis. (b) Bright-field microscopy images of wild-type (upper) and transgenic (lower) leaf cross-sections subsequently used for MALDI-Orbitrap imaging. Scale bars correspond to 1000 microns. (c) Ratio of TAG total ion counts (TIC; all TAG molecular species summed at each analysed position) to PC-TIC as detected by MALDI-Orbitrap imaging in wild-type (upper) and transgenic (lower) leaf cross-sections. (d) Spatial distribution of selected dominant TAG and PC species across a transgenic leaf cross-section as observed by MALDI-Orbitrap.

    Journal: Plant Biotechnology Journal

    Article Title: Metabolic engineering of biomass for high energy density: oilseed-like triacylglycerol yields from plant leaves

    doi: 10.1111/pbi.12131

    Figure Lengend Snippet: Accumulation of lipid droplets and spatial distribution of different triacylglycerol (TAG) molecular species within transgenic leaf tissue. (a) 3D reconstructed z-stacks of confocal images from wild-type (left) and transgenic (right) leaf tissue. Neutral lipids including TAG, stained with BODIPY, appear as green droplets within the leaf mesophyll cells that contain visible chloroplasts (red autofluorescence). Note that non-TAG features also fluorescing green include the vascular bundle and leaf epidermis. (b) Bright-field microscopy images of wild-type (upper) and transgenic (lower) leaf cross-sections subsequently used for MALDI-Orbitrap imaging. Scale bars correspond to 1000 microns. (c) Ratio of TAG total ion counts (TIC; all TAG molecular species summed at each analysed position) to PC-TIC as detected by MALDI-Orbitrap imaging in wild-type (upper) and transgenic (lower) leaf cross-sections. (d) Spatial distribution of selected dominant TAG and PC species across a transgenic leaf cross-section as observed by MALDI-Orbitrap.

    Article Snippet: Sections were scanned at 25 micron step-size in a MALDI linear ion-trap-Orbitrap hybrid mass spectrometer (MALDI LTQ Orbitrap-XL; Thermo Fisher Scientific, Bremen, Germany).

    Techniques: Transgenic Assay, Staining, Microscopy, Imaging

    Schematic outline of proteomic analysis methodology. Sample processing, followed by strong cation exchange (SCX) and reverse-phase chromatography coupled online to an LTQ-Orbitrap mass spectrometer, and subsequent data analysis is outlined. CM, conditioned media; LC-MS/MS, liquid chromatography tandem mass spectrometry.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title:

    doi: 10.1074/mcp.M111.008599

    Figure Lengend Snippet: Schematic outline of proteomic analysis methodology. Sample processing, followed by strong cation exchange (SCX) and reverse-phase chromatography coupled online to an LTQ-Orbitrap mass spectrometer, and subsequent data analysis is outlined. CM, conditioned media; LC-MS/MS, liquid chromatography tandem mass spectrometry.

    Article Snippet: The trap and analytical columns were operated on the EASY-nLC system (Proxeon Biosystems, Odense, Denmark), and this liquid chromatography setup was coupled online to an LTQ-Orbitrap XL hybrid mass spectrometer (Thermo Fisher Scientific, San Jose, California) using a nano-electrospray ionization (ESI) source (Proxeon Biosystems, Odense, Denmark).

    Techniques: Reversed-phase Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Liquid Chromatography

    ESI LTQ OrbiTrap mass spectrum of digested sPNAG, acquired in positive mode. Purified sPNAG was digested with Dispersin B in water and analyzed by mass spectrometry after dialysis. For simplicity, only the most prominent peaks are labeled with their m/z and z values (where z is the charge). For each labeled peak, molecular composition was schematically illustrated by red and green circles representing acetylated and non-acetylated saccharide units, respectively (e.g., two red and three green circles corresponds to a pentamer with two N-acetylglucosamine and three glucosamine residues). For all identified molecules, the ion-pairs corresponding to the singly-charged protonated ions and their dehydration products were detected (e.g., 383.17 and 365.16). As shown in the figure, all prominent peaks correspond to a partially de-acetylated N-acetylglucosamine oligomer or the monomers. Almost all unlabeled peaks correspond to one member of some dehydrated-nondehydrated ion pairs, doubly charged versions of some of the expected molecules, or some adducts. A complete list of m/z values for all potential mono- and oligosaccharides species that could be generated from an incomplete digestion of a PNAG sample with all possible acetylation patterns is also given in Table S1 , as a reference.

    Journal: PLoS Pathogens

    Article Title: Genetic Dissection of an Exogenously Induced Biofilm in Laboratory and Clinical Isolates of E. coli

    doi: 10.1371/journal.ppat.1000432

    Figure Lengend Snippet: ESI LTQ OrbiTrap mass spectrum of digested sPNAG, acquired in positive mode. Purified sPNAG was digested with Dispersin B in water and analyzed by mass spectrometry after dialysis. For simplicity, only the most prominent peaks are labeled with their m/z and z values (where z is the charge). For each labeled peak, molecular composition was schematically illustrated by red and green circles representing acetylated and non-acetylated saccharide units, respectively (e.g., two red and three green circles corresponds to a pentamer with two N-acetylglucosamine and three glucosamine residues). For all identified molecules, the ion-pairs corresponding to the singly-charged protonated ions and their dehydration products were detected (e.g., 383.17 and 365.16). As shown in the figure, all prominent peaks correspond to a partially de-acetylated N-acetylglucosamine oligomer or the monomers. Almost all unlabeled peaks correspond to one member of some dehydrated-nondehydrated ion pairs, doubly charged versions of some of the expected molecules, or some adducts. A complete list of m/z values for all potential mono- and oligosaccharides species that could be generated from an incomplete digestion of a PNAG sample with all possible acetylation patterns is also given in Table S1 , as a reference.

    Article Snippet: Finally, the sample was analyzed by an ESI-LTQ Orbitrap Hybrid mass spectrometer from Thermo Fisher Scientific.

    Techniques: Purification, Mass Spectrometry, Labeling, Generated

    Quantitative analysis of the rapamycin-sensitive phosphoproteome by SILAC. (A) Schematic overview of the experimental approach for the identification of TORC1 regulated phosphorylation sites in S. cerevisiae . Two yeast cultures (strain YPJ2) were metabolically labeled with 12 C 6 - 14 N 2 -lysine/ 12 C 6 -arginine (light) or 13 C 6 - 15 N 2 -lysine/ 13 C 6 -arginine (heavy). The heavy culture was treated for 15 min with rapamycin. Extracts were mixed in a 1:1 ratio and separated by preparative SDS-PAGE. The gel was horizontally sliced into 16 sections and in-gel–digested, and phosphopeptides were IMAC-enriched and analyzed in an LTQ-Orbitrap. (B) Merged data from the four experiments revealed 972 phosphoproteins, corresponding to 2487 unique phosphopeptides and 2607 unique phosphosites. (C) Analysis by Motif-X of all regulated phosphopeptides.

    Journal: Molecular Biology of the Cell

    Article Title: The Rapamycin-sensitive Phosphoproteome Reveals That TOR Controls Protein Kinase A Toward Some But Not All Substrates

    doi: 10.1091/mbc.E10-03-0182

    Figure Lengend Snippet: Quantitative analysis of the rapamycin-sensitive phosphoproteome by SILAC. (A) Schematic overview of the experimental approach for the identification of TORC1 regulated phosphorylation sites in S. cerevisiae . Two yeast cultures (strain YPJ2) were metabolically labeled with 12 C 6 - 14 N 2 -lysine/ 12 C 6 -arginine (light) or 13 C 6 - 15 N 2 -lysine/ 13 C 6 -arginine (heavy). The heavy culture was treated for 15 min with rapamycin. Extracts were mixed in a 1:1 ratio and separated by preparative SDS-PAGE. The gel was horizontally sliced into 16 sections and in-gel–digested, and phosphopeptides were IMAC-enriched and analyzed in an LTQ-Orbitrap. (B) Merged data from the four experiments revealed 972 phosphoproteins, corresponding to 2487 unique phosphopeptides and 2607 unique phosphosites. (C) Analysis by Motif-X of all regulated phosphopeptides.

    Article Snippet: Phosphoproteome Analysis: LC-MS/MS Analysis LC-MS/MS analysis was performed on an LTQ-Orbitrap hybrid instrument (Thermo Scientific).

    Techniques: Metabolic Labelling, Labeling, SDS Page