ltq linear ion trap mass spectrometer  (Thermo Fisher)


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    Name:
    LTQ XL Linear Ion Trap Mass Spectrometer
    Description:
    Obtain more structural information for proteomics and metabolism applications The Thermo Scientific LTQ XL ion trap mass spectrometer offers multiple dissociation techniques PQD ETD and CID for routine structural elucidation PQD is a proprietary technique that eliminates low mass cut off concerns The result is more extensive coverage for predicted and unpredicted metabolites and the ability to perform peptide quantification using isobaric labels
    Catalog Number:
    iqlaaegaavfaczmaik
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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 ltq linear ion trap mass spectrometer
    Quantification of calcium-dependent regulation of phosphorylation sites of Toxoplasma invasion motor complex components. A ) Work flow to identify individual phosphorylation sites and quantitatively assess their responsiveness to calcium signals using a SILAC-based proteomics approach. A 1∶1 mixture of Triton X-100 lysates from “Heavy” (H; Arg4/Lys8)-labeled ethanol-stimulated tachyzoites or phosphopeptide sample of H/L-labeled Toxoplasma invasion motor complexes was prepared and analysed by LC-MS/MS on an LTQ-Orbitrap instrument. Mascot and MaxQuant search engines facilitated subsequent manual identification, phosphosite localization and quantification of proteins or peptides as detailed in materials and mathods. B ) Sypro Ruby-stained SDS-PAGE separation of the relative amounts of light (lane 1) or heavy (lane 2) Triton X-100 whole protein extracts are shown. Intact tachyzoite invasion motor complexes comprising the five major components MyoA, GAP50, GAP45 and MLC1 were precipitated from a 1∶1 H/L mixture by GAP45-specific immuno-affinity chromatography (lane 3). " width='250' height="auto" />
    Obtain more structural information for proteomics and metabolism applications The Thermo Scientific LTQ XL ion trap mass spectrometer offers multiple dissociation techniques PQD ETD and CID for routine structural elucidation PQD is a proprietary technique that eliminates low mass cut off concerns The result is more extensive coverage for predicted and unpredicted metabolites and the ability to perform peptide quantification using isobaric labels
    https://www.bioz.com/result/ltq linear ion trap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 699 article reviews
    Price from $9.99 to $1999.99
    ltq linear ion trap mass spectrometer - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Quantitative in vivo Analyses Reveal Calcium-dependent Phosphorylation Sites and Identifies a Novel Component of the Toxoplasma Invasion Motor Complex"

    Article Title: Quantitative in vivo Analyses Reveal Calcium-dependent Phosphorylation Sites and Identifies a Novel Component of the Toxoplasma Invasion Motor Complex

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1002222

    Quantification of calcium-dependent regulation of phosphorylation sites of Toxoplasma invasion motor complex components. A ) Work flow to identify individual phosphorylation sites and quantitatively assess their responsiveness to calcium signals using a SILAC-based proteomics approach. A 1∶1 mixture of Triton X-100 lysates from “Heavy” (H; Arg4/Lys8)-labeled ethanol-stimulated tachyzoites or
    Figure Legend Snippet: Quantification of calcium-dependent regulation of phosphorylation sites of Toxoplasma invasion motor complex components. A ) Work flow to identify individual phosphorylation sites and quantitatively assess their responsiveness to calcium signals using a SILAC-based proteomics approach. A 1∶1 mixture of Triton X-100 lysates from “Heavy” (H; Arg4/Lys8)-labeled ethanol-stimulated tachyzoites or "Light" (L; Arg0/Lys0)-labeled non-stimulated parasites was generated, and a TiO 2 -enriched phosphopeptide sample of H/L-labeled Toxoplasma invasion motor complexes was prepared and analysed by LC-MS/MS on an LTQ-Orbitrap instrument. Mascot and MaxQuant search engines facilitated subsequent manual identification, phosphosite localization and quantification of proteins or peptides as detailed in materials and mathods. B ) Sypro Ruby-stained SDS-PAGE separation of the relative amounts of light (lane 1) or heavy (lane 2) Triton X-100 whole protein extracts are shown. Intact tachyzoite invasion motor complexes comprising the five major components MyoA, GAP50, GAP45 and MLC1 were precipitated from a 1∶1 H/L mixture by GAP45-specific immuno-affinity chromatography (lane 3).

    Techniques Used: Flow Cytometry, Labeling, Generated, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Staining, SDS Page, Affinity Chromatography

    2) Product Images from "Accurate Label-Free Protein Quantitation with High- and Low-Resolution Mass Spectrometers"

    Article Title: Accurate Label-Free Protein Quantitation with High- and Low-Resolution Mass Spectrometers

    Journal: Journal of proteome research

    doi: 10.1021/pr401017h

    Comparison of label-free quantitation of UPS2 proteins to known mole fraction. UPS2 human protein standards were spiked into an E. coli extract. Identical samples were run on Orbitrap, Velos, and LTQ mass spectrometers. Points from dilutions at 10 −4
    Figure Legend Snippet: Comparison of label-free quantitation of UPS2 proteins to known mole fraction. UPS2 human protein standards were spiked into an E. coli extract. Identical samples were run on Orbitrap, Velos, and LTQ mass spectrometers. Points from dilutions at 10 −4

    Techniques Used: Quantitation Assay

    3) Product Images from "Effects of a Single Dose of Oral Iron on Hepcidin Concentrations in Human Urine and Serum Analyzed by a Robust LC-MS/MS Method"

    Article Title: Effects of a Single Dose of Oral Iron on Hepcidin Concentrations in Human Urine and Serum Analyzed by a Robust LC-MS/MS Method

    Journal: Clinica chimica acta; international journal of clinical chemistry

    doi: 10.1016/j.cca.2011.08.014

    Representative standard curves of the Hepcidin-25H calibration. (A) A linear response of Hepcidin-25H quantitation between 0.5 to 6 picomoles was demonstrated in TSQ Quantum Ultra, (B) The linear response of the Hepcidin-25H quantification between 100 to 500 femtomoles was demonstrated in LTQ-XL linear ion trap instrument.
    Figure Legend Snippet: Representative standard curves of the Hepcidin-25H calibration. (A) A linear response of Hepcidin-25H quantitation between 0.5 to 6 picomoles was demonstrated in TSQ Quantum Ultra, (B) The linear response of the Hepcidin-25H quantification between 100 to 500 femtomoles was demonstrated in LTQ-XL linear ion trap instrument.

    Techniques Used: Quantitation Assay

    Related Articles

    Activation Assay:

    Article Title: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools
    Article Snippet: .. In fact, multistage activation resulted in more information for the suite of phosphopeptides studied (Table ) (see an example of the spectrum of an identified phosphorylated peptide when using SIMAC coupled to MSA in the LTQ ion Trap mass spectrometer and Mascot, Figure ). ..

    Mass Spectrometry:

    Article Title: Vaccination Targeting a Surface Sialidase of P. acnes: Implication for New Treatment of Acne Vulgaris
    Article Snippet: .. A reversed-phase LC directly coupled to a LTQ ion trap mass spectrometer (Thermo Electron, Waltham, MA) was run using a linear gradient elution from buffer A (H2 O plus 0.1% formic acid) to 50% buffer A plus 50% buffer B (acetonitrile plus 0.1% formic acid) in 100 min. ..

    Article Title: Quantitative in vivo Analyses Reveal Calcium-dependent Phosphorylation Sites and Identifies a Novel Component of the Toxoplasma Invasion Motor Complex
    Article Snippet: .. Individual TiO2 -bound phosphopeptide fractions were analyzed by multi-dimensional LC-MS/MS on an LTQ linear ion trap mass spectrometer (Thermo Scientific), according to published protocols . ..

    Article Title: High Throughput Characterization of Combinatorial Histone Codes *
    Article Snippet: .. Several other buffer systems for the B mobile phase were tried during method development as noted under “Results.” The column eluent was introduced into an LTQ-ETD ion trap mass spectrometer (Thermo Scientific, Waltham, MA) or an LTQ-Orbitrap XL (Thermo Scientific) (data in only) by nanoelectrospray ionization. .. Every cycle a full mass spectrum was acquired from 300 to 2000 m/z followed by narrower mass range full mass spectrum to select a given charge state of the histone for data-dependent selection.

    Article Title: Systematic metabolic profiling and bioactivity assays for bioconversion of Aceraceae family
    Article Snippet: .. UHPLC-LTQ-XL-IT-MS/MS analysis The Thermo Fischer Scientific LTQ XL linear ion trap mass spectrometry system used in the present study consisted of an electrospray interface (Thermo Fischer Scientific, San José, CA, USA) coupled with a DIONEX UltiMate 3000 RS Pump, RS Autosampler, RS Column Compartment, and RS Diode Array Detector (Dionex Corporation, Sunnyvale, CA, USA). .. The samples were separated on a Thermo Scientific Syncronis C18 UHPLC column with 1.7 μm particle size.

    Article Title: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools
    Article Snippet: .. In fact, multistage activation resulted in more information for the suite of phosphopeptides studied (Table ) (see an example of the spectrum of an identified phosphorylated peptide when using SIMAC coupled to MSA in the LTQ ion Trap mass spectrometer and Mascot, Figure ). ..

    Article Title: Ultrahigh Pressure Processing Produces Alterations in the Metabolite Profiles of Panax ginseng
    Article Snippet: .. UHPLC-LTQ-IT-MS/MS Analysis The Thermo Fisher Scientific LTQ XL ion trap mass spectrometer consisted of an electrospray interface (Thermo Fisher Scientific, San Jose, CA, USA) coupled with a DIONEX UltiMate 3000 RS Pump, RS autosampler, RS column compartment, and RS diode array detector (Dionex Corporation, Sunnyvale, CA, USA). .. Each 10 μL sample was injected into and separated on a Thermo Scientific Syncronis C18 UHPLC column (100 mm × 2.1 mm i.d.

    Article Title: Increased expression of the high-mannose M6N2 and NeuAc3H3N3M3N2F tri-antennary N-glycans in cholangiocarcinoma
    Article Snippet: .. Briefly, permethylated glycans were dissolved in 1 mM NaOH in 50% methanol and infused directly into a linear ion trap mass spectrometer (LTQ Orbitrap Discovery; Thermo Fisher Scientific, Inc., Waltham, MA, USA) using a Thermo Fisher Scientific™ nanospray ion source (Thermo Fisher Scientific, Inc.). .. MS analysis was performed in a positive ion mode and MS/MS spectra (at 28% collision energy) were obtained using the total ion mapping function of the Xcalibur software (version 2; Thermo Fisher Scientific, Inc.).

    Article Title: Label-free and isobaric tandem mass tag (TMT) multiplexed quantitative proteomic data of two contrasting rice cultivars exposed to drought stress and recovery
    Article Snippet: .. The resulting peptides were analysed by nanoflow LC-MS/MS (nanoLC-MS/MS) using a LTQ-XL ion-trap mass spectrometer (Thermo, CA, USA). ..

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    Thermo Fisher ion trap orbitrap fourier transform mass spectrometer
    <t>Orbitrap-FT</t> data for the peptide HGGIDLGFNMPSFGGK at m / z 817. 39. A , The MS spectrum for the doubly charged peptide at 817.39. B , The fragmentation spectrum (MS/MS) with the fragment ions annotated.
    Ion Trap Orbitrap Fourier Transform Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
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    85
    Thermo Fisher hybrid ltq linear ion trap
    Peptide identifications from liver and brain tissue. The number (y-axis) of phosphorylated and unmodified proteins identified from brain and liver on a <t>LTQ-Orbitrap</t> mass spectrometer following the phosphopeptide enrichment using IMAC.
    Hybrid Ltq Linear Ion Trap, 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
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    89
    Thermo Fisher hybrid linear ion trap ft icr mass spectrometer
    Mass spectrometry characterization of rhamnosylated EF-P. (A) A mass spectrum of His6–EF-P protein, recorded on a <t>7T</t> <t>FT-ICR</t> instrument, from which protein molecular masses were calculated. (B) Lys-C-digested peptide fragmented by ETD maps the additional mass of 146.057 Da on Arg32. The precursor ion, m / z 349.865, is indicated by a dashed line. (C) A proposed fragmentation pattern based on ETD-HCD MS 3 data from the c3 + ion. The neutral losses are colored uniquely to associate the fragment ion with the hypothetical structure. The asterisk indicates a background ion. The precursor ion, m / z 464.246, is indicated by a dashed line.
    Hybrid Linear Ion Trap Ft Icr Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hybrid linear ion trap ft icr mass spectrometer/product/Thermo Fisher
    Average 89 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Orbitrap-FT data for the peptide HGGIDLGFNMPSFGGK at m / z 817. 39. A , The MS spectrum for the doubly charged peptide at 817.39. B , The fragmentation spectrum (MS/MS) with the fragment ions annotated.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Proteomic Profiling of the Planarian Schmidtea mediterranea and Its Mucous Reveals Similarities with Human Secretions and Those Predicted for Parasitic Flatworms *

    doi: 10.1074/mcp.M112.019026

    Figure Lengend Snippet: Orbitrap-FT data for the peptide HGGIDLGFNMPSFGGK at m / z 817. 39. A , The MS spectrum for the doubly charged peptide at 817.39. B , The fragmentation spectrum (MS/MS) with the fragment ions annotated.

    Article Snippet: Eluted peptides from both column setups were electrosprayed directly into a linear ion trap-Orbitrap Fourier transform mass spectrometer (LTQ-Orbitrap Classic; Thermo Fisher Scientific, Bremen, Germany) using a nanoelectrospray ion source (Proxeon Biosystems A/S, Odense, Denmark).

    Techniques: Mass Spectrometry

    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

    Peptide identifications from liver and brain tissue. The number (y-axis) of phosphorylated and unmodified proteins identified from brain and liver on a LTQ-Orbitrap mass spectrometer following the phosphopeptide enrichment using IMAC.

    Journal: PLoS ONE

    Article Title: Differential Proteomic Analysis of Mammalian Tissues Using SILAM

    doi: 10.1371/journal.pone.0016039

    Figure Lengend Snippet: Peptide identifications from liver and brain tissue. The number (y-axis) of phosphorylated and unmodified proteins identified from brain and liver on a LTQ-Orbitrap mass spectrometer following the phosphopeptide enrichment using IMAC.

    Article Snippet: As peptides were eluted from the microcapillary column they were electrosprayed directly into a hybrid LTQ linear ion trap and Orbitrap (ThermoFisher, San Jose, CA) with the application of a distal 2.4 kV spray voltage.

    Techniques: Mass Spectrometry

    Mass spectrometry characterization of rhamnosylated EF-P. (A) A mass spectrum of His6–EF-P protein, recorded on a 7T FT-ICR instrument, from which protein molecular masses were calculated. (B) Lys-C-digested peptide fragmented by ETD maps the additional mass of 146.057 Da on Arg32. The precursor ion, m / z 349.865, is indicated by a dashed line. (C) A proposed fragmentation pattern based on ETD-HCD MS 3 data from the c3 + ion. The neutral losses are colored uniquely to associate the fragment ion with the hypothetical structure. The asterisk indicates a background ion. The precursor ion, m / z 464.246, is indicated by a dashed line.

    Journal: mBio

    Article Title: Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa

    doi: 10.1128/mBio.00823-15

    Figure Lengend Snippet: Mass spectrometry characterization of rhamnosylated EF-P. (A) A mass spectrum of His6–EF-P protein, recorded on a 7T FT-ICR instrument, from which protein molecular masses were calculated. (B) Lys-C-digested peptide fragmented by ETD maps the additional mass of 146.057 Da on Arg32. The precursor ion, m / z 349.865, is indicated by a dashed line. (C) A proposed fragmentation pattern based on ETD-HCD MS 3 data from the c3 + ion. The neutral losses are colored uniquely to associate the fragment ion with the hypothetical structure. The asterisk indicates a background ion. The precursor ion, m / z 464.246, is indicated by a dashed line.

    Article Snippet: All samples were analyzed using a hybrid linear ion-trap/FT-ICR mass spectrometer (7T, LTQ FT Ultra; Thermo Scientific) operated with a standard (up to m /z 2,000) or extended (up to m /z 4,000) mass range.

    Techniques: Mass Spectrometry