linear it ltq mass spectrometer  (Thermo Fisher)


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    Structured Review

    Thermo Fisher linear it ltq mass spectrometer
    Linear It Ltq Mass Spectrometer, 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/linear it ltq mass spectrometer/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    linear it ltq mass spectrometer - by Bioz Stars, 2020-05
    86/100 stars

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    Mass Spectrometry:

    Article Title: Systematic comparison of the human saliva and plasma proteomes
    Article Snippet: .. The peptide eluents were monitored using a linear IT mass spectrometer (LTQ, ThermoFisher Scientific) operated in a data-dependent mode. .. Raw LTQ data were converted to peak list files by msn_extract.exe (Thermo Fisher Scientific).

    Article Title: Protein profiling of formalin fixed paraffin embedded tissue: Identification of potential biomarkers for pediatric brainstem glioma
    Article Snippet: .. Differentially labeled peptides from normal and tumor sections were mixed at a 1:1 ratio (4 µL each) and an aliquot (6 µL) was analyzed by LC-MS/MS using an LC-Packing system (DIONEX Ulti-Mate™ Capillary/Nano LC System, Dionex, Sunnyvale, CA) connected to a Linear IT (LTQ) mass spectrometer (Thermo Electron, San Jose, CA). .. Each sample was injected via an autosampler and loaded onto a C18 trap column (300 µm×1 mm, LC Packing) for 6 min at a flow rate of 10 µL/min.

    Article Title: Application of capillary isotachophoresis-based multidimensional separations coupled with electrospray ionization-tandem mass spectrometry for characterization of mouse brain mitochondrial proteome
    Article Snippet: .. The peptide eluants were monitored using a linear IT mass spectrometer (LTQ, ThermoFinnigan, San Jose, CA) operated in a data-dependent mode. .. Full scans were collected from 400 to 1400 m/z and five data-dependent MS/MS scans were collected with dynamic exclusion set to 30 s. A moving stage housing two nano-RPLC columns was employed to provide electrical contacts for applying ESI voltages, and most importantly to position the columns in-line with the ESI inlet at each chromatography separation and data acquisition cycle.

    Labeling:

    Article Title: Protein profiling of formalin fixed paraffin embedded tissue: Identification of potential biomarkers for pediatric brainstem glioma
    Article Snippet: .. Differentially labeled peptides from normal and tumor sections were mixed at a 1:1 ratio (4 µL each) and an aliquot (6 µL) was analyzed by LC-MS/MS using an LC-Packing system (DIONEX Ulti-Mate™ Capillary/Nano LC System, Dionex, Sunnyvale, CA) connected to a Linear IT (LTQ) mass spectrometer (Thermo Electron, San Jose, CA). .. Each sample was injected via an autosampler and loaded onto a C18 trap column (300 µm×1 mm, LC Packing) for 6 min at a flow rate of 10 µL/min.

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    Thermo Fisher ltq ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ltq Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 347 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq ion trap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 347 article reviews
    Price from $9.99 to $1999.99
    ltq ion trap mass spectrometer - by Bioz Stars, 2020-05
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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
    https://www.bioz.com/result/hybrid ltq linear ion trap/product/Thermo Fisher
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    88
    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: 88/100, based on 26 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 88 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    hybrid linear ion trap ft icr mass spectrometer - by Bioz Stars, 2020-05
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    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    Journal: Journal of Clinical Bioinformatics

    Article Title: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools

    doi: 10.1186/2043-9113-1-16

    Figure Lengend Snippet: The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    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 ).

    Techniques: Purification, Mass Spectrometry, Isolation, RNA Binding Assay, Activation Assay

    Phosphosite identification by mass spectrometry. Two phoshosites were identified on human β-catenin using nano-LC coupled to a LTQ/Orbitrap tandem MS with either CID or ETD activation. GST-catenin was phosphorylated by JNK in vitro , and the reaction

    Journal: The FASEB Journal

    Article Title: JNK phosphorylates ?-catenin and regulates adherens junctions

    doi: 10.1096/fj.08-117804

    Figure Lengend Snippet: Phosphosite identification by mass spectrometry. Two phoshosites were identified on human β-catenin using nano-LC coupled to a LTQ/Orbitrap tandem MS with either CID or ETD activation. GST-catenin was phosphorylated by JNK in vitro , and the reaction

    Article Snippet: A lab-made dynamic-flow nanospray ion source was employed to couple the nano-LC system to either a LTQ/ETD (Thermo LTQ XL linear ion trap coupled to an electron-transferring dissociation; Thermo, San Jose, CA, USA) for ETD analysis or a LTQ/Orbitrap (Thermo) for CID analysis.

    Techniques: Mass Spectrometry, Activation Assay, In Vitro

    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