ltq orbitrap elite mass spectrometer  (Thermo Fisher)


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    Thermo Fisher ltq orbitrap elite mass spectrometer
    Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a <t>LTQ-Orbitrap-Elite</t> mass spectrometer.
    Ltq Orbitrap Elite Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 324 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq orbitrap elite mass spectrometer/product/Thermo Fisher
    Average 96 stars, based on 324 article reviews
    Price from $9.99 to $1999.99
    ltq orbitrap elite mass spectrometer - by Bioz Stars, 2020-05
    96/100 stars

    Images

    1) Product Images from "Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *"

    Article Title: Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M116.068080

    Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.
    Figure Legend Snippet: Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.

    Techniques Used: Cell Culture, SDS Page, Staining, Labeling, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    2) Product Images from "Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *"

    Article Title: Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M116.068080

    Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.
    Figure Legend Snippet: Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.

    Techniques Used: Cell Culture, SDS Page, Staining, Labeling, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    3) Product Images from "LC-MS/MS Analysis Unravels Deep Oxidation of Manganese Superoxide Dismutase in Kidney Cancer"

    Article Title: LC-MS/MS Analysis Unravels Deep Oxidation of Manganese Superoxide Dismutase in Kidney Cancer

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms18020319

    LC-MS/MS coverage of MNSOD. ( a ) Whole cell lysates from kidney tissues were separated by SDS-PAGE and stained by Coomassie Blue (arrow indicated MNSOD). The gel image is the representative of 4 pairs of tumor and adjacent tissues used for PTMs analysis. A: adjacent; T: tumor; ( b ) CID-based sequence coverage of MNSOD. After Coomassie Blue staining, the 22 kDa protein bands corresponding to MNSOD were cut from the gel and digested, and peptides were analyzed by LC-MS/MS on LTQ-Orbitrap mass spectrometer (MS). The underlined amino acids (bold letters) were identified by Proteome Discoverer 1.4 (MASCOT and SEQUEST), which covered 76.13% sequence of MNSOD. Signal: the signal peptide; α: the α-helices; β: the β-sheets, subscript numbers represent original numbers; solid arrows: metal (Mn 2+ ) binding sites.
    Figure Legend Snippet: LC-MS/MS coverage of MNSOD. ( a ) Whole cell lysates from kidney tissues were separated by SDS-PAGE and stained by Coomassie Blue (arrow indicated MNSOD). The gel image is the representative of 4 pairs of tumor and adjacent tissues used for PTMs analysis. A: adjacent; T: tumor; ( b ) CID-based sequence coverage of MNSOD. After Coomassie Blue staining, the 22 kDa protein bands corresponding to MNSOD were cut from the gel and digested, and peptides were analyzed by LC-MS/MS on LTQ-Orbitrap mass spectrometer (MS). The underlined amino acids (bold letters) were identified by Proteome Discoverer 1.4 (MASCOT and SEQUEST), which covered 76.13% sequence of MNSOD. Signal: the signal peptide; α: the α-helices; β: the β-sheets, subscript numbers represent original numbers; solid arrows: metal (Mn 2+ ) binding sites.

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Staining, Sequencing, Binding Assay

    4) Product Images from "Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm"

    Article Title: Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1619356114

    ( A ) HeLa hCDC14A-YFP and HeLa YFP-inducible stable cell lines were labeled with heavy (Arg 13 C 15 N Lys 13 C 15 N) and light (Arg 12 C 14 N Lys 12 C 14 N) medium, respectively. Phospho-peptides were enriched and then applied on LTQ-Orbitrap for LC-MS/MS analysis. ( B ) Scatter plot of two replicate LC-MS/MS experiments. ( C ) Peptides of B that were hypo-phosphorylated at least twofold were included in this analysis. ( D ) Top five GO protein classifications based on cellular components are shown with P values and protein counts. ( E ) Molecular network based on the hypo-phosphorylated proteins upon hCDC14A overexpression. ( F ) Molecular network based on the hyper-phosphorylated proteins in hCDC14A KO hCDC14B KO cells. Only pSP/pTP sites were considered in this analysis. Protein–protein interactions among the hits were extracted from STRING and BioGrid and then integrated using Cytoscape. The size of the circle represents the number of interactors. IMAC, immobilized metal affinity chromatography.
    Figure Legend Snippet: ( A ) HeLa hCDC14A-YFP and HeLa YFP-inducible stable cell lines were labeled with heavy (Arg 13 C 15 N Lys 13 C 15 N) and light (Arg 12 C 14 N Lys 12 C 14 N) medium, respectively. Phospho-peptides were enriched and then applied on LTQ-Orbitrap for LC-MS/MS analysis. ( B ) Scatter plot of two replicate LC-MS/MS experiments. ( C ) Peptides of B that were hypo-phosphorylated at least twofold were included in this analysis. ( D ) Top five GO protein classifications based on cellular components are shown with P values and protein counts. ( E ) Molecular network based on the hypo-phosphorylated proteins upon hCDC14A overexpression. ( F ) Molecular network based on the hyper-phosphorylated proteins in hCDC14A KO hCDC14B KO cells. Only pSP/pTP sites were considered in this analysis. Protein–protein interactions among the hits were extracted from STRING and BioGrid and then integrated using Cytoscape. The size of the circle represents the number of interactors. IMAC, immobilized metal affinity chromatography.

    Techniques Used: Stable Transfection, Labeling, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Over Expression, Affinity Chromatography

    5) Product Images from "Phosphoproteome and Transcriptome of RA-Responsive and RA-Resistant Breast Cancer Cell Lines"

    Article Title: Phosphoproteome and Transcriptome of RA-Responsive and RA-Resistant Breast Cancer Cell Lines

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0157290

    Workflow for the phosphoproteomics strategy. (A) Phosphoproteome. Nuclear and cytoplasmic extracts were prepared and divided in two: one half was digested with trypsin/Lys-C and the other half with chymotrypsin. A small fraction of the trypsin/Lys-C digests was analyzed directly without further purification. The remaining digests were subjected to phosphopeptide enrichment and MS analysis. (B) RARα phosphorylation. Whole cell extracts were prepared from MCF7 and BT474 cells with and without a 30 min RA treatment. RARα was immunoprecipitated and the eluates were thermolysin-digested. Phosphopeptides were enriched and analyzed by nano-LC-LTQ-Orbitrap MS.
    Figure Legend Snippet: Workflow for the phosphoproteomics strategy. (A) Phosphoproteome. Nuclear and cytoplasmic extracts were prepared and divided in two: one half was digested with trypsin/Lys-C and the other half with chymotrypsin. A small fraction of the trypsin/Lys-C digests was analyzed directly without further purification. The remaining digests were subjected to phosphopeptide enrichment and MS analysis. (B) RARα phosphorylation. Whole cell extracts were prepared from MCF7 and BT474 cells with and without a 30 min RA treatment. RARα was immunoprecipitated and the eluates were thermolysin-digested. Phosphopeptides were enriched and analyzed by nano-LC-LTQ-Orbitrap MS.

    Techniques Used: Purification, Mass Spectrometry, Immunoprecipitation

    6) Product Images from "Host FIH-Mediated Asparaginyl Hydroxylation of Translocated Legionella pneumophila Effectors"

    Article Title: Host FIH-Mediated Asparaginyl Hydroxylation of Translocated Legionella pneumophila Effectors

    Journal: Frontiers in Cellular and Infection Microbiology

    doi: 10.3389/fcimb.2017.00054

    AnkH and AnkB are modified by host asparaginyl hydroxylation . High resolution LCMS analysis 1D-LC-LTQ-Orbitrap-ELITE-MS of AnkH and AnkB protein expressed in HEK293T cells identifies hydroxylated asparagine residues. (A) AnkH: (Top) HCD fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,566.81 Da; (Bottom) HCD fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,582.81 Da; ProteomeDiscover v1.3 analysis of upper MS/MS data set identifies a tryptic peptide (Mascot Ion Score 77.8, Sequest Xcorr 3.94, and deltaCn 0.49) with the sequence LLLTYGADPNATYTR. Analysis of lower MS/MS data set identifies a tryptic peptide (Mascot Ion Score 19.7, Sequest Xcorr 2.33, and deltaCn 0.30) with the sequence LLLTYGADPN(OH)ATYTR. Both peptides were observed with sub-5 ppm mass accuracy and with near complete b-ion (red hash; includes b-, b * -, and b+2H+- ions) and y-ion (blue hash; includes y-. y * -, and y+2H+-) coverage of parent ions. (B) AnkB: (Top) CID fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,274.64 Da; (Bottom) CID fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,290.64 Da; ProteomeDiscover v1.4 analysis of upper MS/MS data set identifies a tryptic peptide (Mascot Ion Score 81.7) with the sequence ELWGNLMVAAR. Analysis of lower MS/MS data set identifies a tryptic peptide (Mascot Ion Score 41.1) with the sequence ELWGN(OH)LMVAAR. Both peptides were observed with
    Figure Legend Snippet: AnkH and AnkB are modified by host asparaginyl hydroxylation . High resolution LCMS analysis 1D-LC-LTQ-Orbitrap-ELITE-MS of AnkH and AnkB protein expressed in HEK293T cells identifies hydroxylated asparagine residues. (A) AnkH: (Top) HCD fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,566.81 Da; (Bottom) HCD fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,582.81 Da; ProteomeDiscover v1.3 analysis of upper MS/MS data set identifies a tryptic peptide (Mascot Ion Score 77.8, Sequest Xcorr 3.94, and deltaCn 0.49) with the sequence LLLTYGADPNATYTR. Analysis of lower MS/MS data set identifies a tryptic peptide (Mascot Ion Score 19.7, Sequest Xcorr 2.33, and deltaCn 0.30) with the sequence LLLTYGADPN(OH)ATYTR. Both peptides were observed with sub-5 ppm mass accuracy and with near complete b-ion (red hash; includes b-, b * -, and b+2H+- ions) and y-ion (blue hash; includes y-. y * -, and y+2H+-) coverage of parent ions. (B) AnkB: (Top) CID fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,274.64 Da; (Bottom) CID fragmentation spectrum for +2 charged ion with a monoisotopic m/z: 1,290.64 Da; ProteomeDiscover v1.4 analysis of upper MS/MS data set identifies a tryptic peptide (Mascot Ion Score 81.7) with the sequence ELWGNLMVAAR. Analysis of lower MS/MS data set identifies a tryptic peptide (Mascot Ion Score 41.1) with the sequence ELWGN(OH)LMVAAR. Both peptides were observed with

    Techniques Used: Modification, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Sequencing

    7) Product Images from "Phosphoproteomic profiling of tumor tissues identifies HSP27 Ser82 phosphorylation as a robust marker of early ischemia"

    Article Title: Phosphoproteomic profiling of tumor tissues identifies HSP27 Ser82 phosphorylation as a robust marker of early ischemia

    Journal: Scientific Reports

    doi: 10.1038/srep13660

    Phosphoproteomic profiling of xenograft tumors during ischemia. A schematic workflow of the strategy used to profile the phoshoproteomic changes resulting from ischemia. Whole xenograft tumors from the breast cancer cell line HCC1395 were harvested from mice and exposed to room temperature for 0, 2, 10 and 30 minutes before snap freezing in liquid nitrogen. After protein extraction and digestion with trypsin, each sample was labeled with different versions of TMT reagents followed by pooling, desalting, and enrichment using TiO 2 beads. The enriched phosphopeptides were then analyzed on LTQ-Orbitrap Elite mass spectrometer without further fractionation. Figure drawn by M.S.Z.
    Figure Legend Snippet: Phosphoproteomic profiling of xenograft tumors during ischemia. A schematic workflow of the strategy used to profile the phoshoproteomic changes resulting from ischemia. Whole xenograft tumors from the breast cancer cell line HCC1395 were harvested from mice and exposed to room temperature for 0, 2, 10 and 30 minutes before snap freezing in liquid nitrogen. After protein extraction and digestion with trypsin, each sample was labeled with different versions of TMT reagents followed by pooling, desalting, and enrichment using TiO 2 beads. The enriched phosphopeptides were then analyzed on LTQ-Orbitrap Elite mass spectrometer without further fractionation. Figure drawn by M.S.Z.

    Techniques Used: Mouse Assay, Protein Extraction, Labeling, Mass Spectrometry, Fractionation

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm
    Article Snippet: .. This resulted in 48 fractions (24 phospho-enriched + 24 phospho-depleted), which were analyzed by LC-MS using a Dionex UltiMate 3000RSLCnano HPLC system (Thermo Scientific) coupled to a LTQ Orbitrap Elite mass spectrometer (Thermo Scientific). .. Peptides were separated on a self-pulled and self-packed analytical emitter C18 column, using gradients of increasing amounts of acetonitrile (phospho-enriched = 90 min, phospho-depleted = 120 min), and measured in the mass spectrometer using a Top15 collision-induced dissociation high–low data-dependent acquisition strategy.

    Mass Spectrometry:

    Article Title: Genetically encoded protein photocrosslinker with a transferable mass spectrometry-identifiable label
    Article Snippet: .. LC–MS/MS analysis of tryptic peptides was performed on an LTQ-Orbitrap-Elite mass spectrometer coupled with an Easy nLC 1,000 system (Thermo Scientific). .. Images of protein gels including coomassie SDS–PAGE gel, fluorescent gel and western blotting membrane were taken on ChemiDoc XRS (Bio-Rad).

    Article Title: Phosphoproteome and Transcriptome of RA-Responsive and RA-Resistant Breast Cancer Cell Lines
    Article Snippet: .. LC-MS/MS analysis Samples were analyzed using an Ultimate 3000 nano-RSLC (Thermo Scientific, San Jose California) coupled in line with an LTQ-Orbitrap ELITE mass spectrometer via a nano-electrospray ionization source (Thermo Scientific, San Jose California). .. Peptides were loaded on a C18 Acclaim PepMap100 trap-column (75 μm ID x 2 cm, 3 μm, 100Å, Thermo Fisher Scientific) for 3.5 minutes at 5 μL/min with 2% ACN, 0.1% formic acid (FA) in H2 O and then separated on a C18 Accucore nano-column (75 μm ID x 50 cm, 2.6 μm, 150Å, Thermo Fisher Scientific) with a linear gradient from 5% to 50% buffer B (A: 0.1% FA in H2 O / B: 80% ACN, 0.08% FA in H2 O).

    Article Title: Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm
    Article Snippet: .. This resulted in 48 fractions (24 phospho-enriched + 24 phospho-depleted), which were analyzed by LC-MS using a Dionex UltiMate 3000RSLCnano HPLC system (Thermo Scientific) coupled to a LTQ Orbitrap Elite mass spectrometer (Thermo Scientific). .. Peptides were separated on a self-pulled and self-packed analytical emitter C18 column, using gradients of increasing amounts of acetonitrile (phospho-enriched = 90 min, phospho-depleted = 120 min), and measured in the mass spectrometer using a Top15 collision-induced dissociation high–low data-dependent acquisition strategy.

    Article Title: LC-MS/MS Analysis Unravels Deep Oxidation of Manganese Superoxide Dismutase in Kidney Cancer
    Article Snippet: .. The MS and MS/MS spectra were acquired by a LTQ-Orbitrap Elite mass spectrometer (Thermo Scientific) in a data-dependent mode, in which MS/MS fragmentation of the 20 most intense peaks were acquired for every full MS scan. .. MS/MS spectra were searched against the human protein database using MASCOT and SEQUEST.

    Article Title: Host FIH-Mediated Asparaginyl Hydroxylation of Translocated Legionella pneumophila Effectors
    Article Snippet: .. The sample was eluted using a linear 2 to 60% acetonitrile gradient using an EASY nano1000 UHPLC and introduced into a LTQ-Orbitrap ELITE mass spectrometer (ThermoElectron, Waltham, MA) for accurate mass measurements using a Nanospray Flex Ion Source (ThermoElectron, Waltham, MA), a stainless steel emitter with a capillary temperature set to 225 C and a spray voltage of 1.6 kV and lock mass enabled (0% lock mass abundance) for the 371.101236 m/z polysiloxane peak as an internal calibrant (Cox et al., ). .. Data dependent tandem mass spectra were collected using HCD and ETD fragmentation using an Nth Order Double Play with ETD Decision Tree method (Swaney et al., ) was created in Xcalibur v2.2 and included a parent mass list for +2 or +3 charge states of tryptic peptides (0, 1, or 2 miss cleavages) based on the protein sequence and putative hydroxylation.

    Article Title: Phosphoproteomic profiling of tumor tissues identifies HSP27 Ser82 phosphorylation as a robust marker of early ischemia
    Article Snippet: .. LC-MS/MS Analysis Enriched phosphopeptides were analyzed on LTQ-Orbitrap Elite mass spectrometer (Thermo Scientific, San Jose, CA, USA) interfaced with Easy-nanoLC II nanoflow liquid chromatography system (Thermo Scientific, Odense, Southern Denmark). .. The peptides from each fraction were reconstituted in 0.1% formic acid and loaded on a pre-column (75 μm × 2 cm) packed in-house with magic C18 AQ (MichromBioresources, Auburn, CA, USA) 5 μ particle and 100 Å pore size at flow rate of 5 μl per minute.

    Article Title: Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *
    Article Snippet: .. For MS analysis, the peptides were resuspended in 0.1% formic acid (FA) and analyzed by a LTQ Orbitrap Elite mass spectrometer (Thermo Scientific) coupled online to an Easy-nLC 1000 in the data-dependent mode. .. Briefly, 2 μl of peptide sample (1 μg/μl) was injected into a 15-cm-long, 75-μm inner diameter capillary analytic column packed with C18 particles of 5-μm diameter.

    Article Title: Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *
    Article Snippet: .. The TMT-labeled peptides were analyzed with a LTQ-Orbitrap-Elite mass spectrometer and 2367 proteins or protein groups, which constitute about 65% of the Synechocystis ). .. Comparing these proteins with a combined list of proteins identified from more than 50 previous studies reveals that 2303 proteins are overlapping and 64 proteins are unique to the current study ( A ) ( ).

    Liquid Chromatography:

    Article Title: Phosphoproteomic profiling of tumor tissues identifies HSP27 Ser82 phosphorylation as a robust marker of early ischemia
    Article Snippet: .. LC-MS/MS Analysis Enriched phosphopeptides were analyzed on LTQ-Orbitrap Elite mass spectrometer (Thermo Scientific, San Jose, CA, USA) interfaced with Easy-nanoLC II nanoflow liquid chromatography system (Thermo Scientific, Odense, Southern Denmark). .. The peptides from each fraction were reconstituted in 0.1% formic acid and loaded on a pre-column (75 μm × 2 cm) packed in-house with magic C18 AQ (MichromBioresources, Auburn, CA, USA) 5 μ particle and 100 Å pore size at flow rate of 5 μl per minute.

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: Human phosphatase CDC14A regulates actin organization through dephosphorylation of epithelial protein lost in neoplasm
    Article Snippet: .. This resulted in 48 fractions (24 phospho-enriched + 24 phospho-depleted), which were analyzed by LC-MS using a Dionex UltiMate 3000RSLCnano HPLC system (Thermo Scientific) coupled to a LTQ Orbitrap Elite mass spectrometer (Thermo Scientific). .. Peptides were separated on a self-pulled and self-packed analytical emitter C18 column, using gradients of increasing amounts of acetonitrile (phospho-enriched = 90 min, phospho-depleted = 120 min), and measured in the mass spectrometer using a Top15 collision-induced dissociation high–low data-dependent acquisition strategy.

    Tandem Mass Spectroscopy:

    Article Title: LC-MS/MS Analysis Unravels Deep Oxidation of Manganese Superoxide Dismutase in Kidney Cancer
    Article Snippet: .. The MS and MS/MS spectra were acquired by a LTQ-Orbitrap Elite mass spectrometer (Thermo Scientific) in a data-dependent mode, in which MS/MS fragmentation of the 20 most intense peaks were acquired for every full MS scan. .. MS/MS spectra were searched against the human protein database using MASCOT and SEQUEST.

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    Thermo Fisher ltq orbitrap elite mass spectrometer
    Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a <t>LTQ-Orbitrap-Elite</t> mass spectrometer.
    Ltq Orbitrap Elite Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 324 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq orbitrap elite mass spectrometer/product/Thermo Fisher
    Average 96 stars, based on 324 article reviews
    Price from $9.99 to $1999.99
    ltq orbitrap elite mass spectrometer - by Bioz Stars, 2020-05
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    Thermo Fisher ltq orbitrap elite mass spectrometry system
    CBP inhibits liver inflammation in mice with intrahepatic cholestasis (A) The effects of CBP on protein levels of NF-κB, IκBα, IKKα, and ICAM-1, detected by western blot. (B) Quantitative analysis of the effects of CBP on NF-κB, IκBα, IKKα, and ICAM-1 proteins, and IL-1 and ICAM-1 mRNA expression. (C) Quantitative analysis of 8, 9-epoxyeicosatrienoic acid by <t>UPLC-LTQ-orbitrap.</t> Data are expressed as the mean ± SD, * p
    Ltq Orbitrap Elite Mass Spectrometry System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq orbitrap elite mass spectrometry system/product/Thermo Fisher
    Average 88 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    ltq orbitrap elite mass spectrometry system - by Bioz Stars, 2020-05
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    92
    Thermo Fisher ltq velos pro orbitrap elite
    FhaA is phosphorylated on Tyr. Precursor ion masses were measured in the <t>Orbitrap</t> Elite mass analyzer, and MS/MS spectra were acquired in the <t>LTQ</t> mass spectrometer. ( A ) Endogenous peptide identified in the phosphopeptide-enriched fraction of total Mtb cell lysate (precursor ion mass accuracy −0.69 ppm). ( B ) Synthetic peptide confirming the fragmentation pattern of the endogenous peptide (mass accuracy 1.04 ppm). ( C ) Nonphosphorylated peptide VPGYAPQGGGYAEPAGR, shown for comparison (mass accuracy 0.61 ppm). ( D ) Sequence annotation of identified fragment ions of the phosphorylated and nonphosphorylated peptides. The mass shift caused by phosphorylation is shown by the different y ion masses observed upstream and the different b ion masses observed downstream of the pTyr residue, as highlighted by arrows in the phosphorylated peptide sequence and shown in bold in the spectra.
    Ltq Velos Pro Orbitrap Elite, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Translating Divergent Environmental Stresses into a Common Proteome Response through the Histidine Kinase 33 (Hik33) in a Model Cyanobacterium *

    doi: 10.1074/mcp.M116.068080

    Figure Lengend Snippet: Rationale and experimental design. A , Confirmation of Δ hik33 growth phenotype under photoautotrophic condition. The deletion of hik33 ), which also contains the photo of the cell culture. B , The WCLs of the WT and Δ hik33 strains of Synechocystis were separated into the membrane (Mem) and the soluble (Sol) fractions. Proteins extracted from either fraction and the WCL were subsequently separated by SDS-PAGE and visualized with Coomassie blue staining. C , Schematic representation of the workflow for the quantitative analysis of the Δ hik33 proteome. Total proteins were extracted from the WCLs of three biological replicates of the WT and Δ hik33 and digested with trypsin. The tryptic peptides were labeled with 6-plex TMT reagents in the order as indicated. The labeled peptides were mixed together with an equal molar ratio, and separated into 15 fractions with RP-HPLC. The peptides in each fraction were quantitatively analyzed by LC-MS/MS using a LTQ-Orbitrap-Elite mass spectrometer.

    Article Snippet: For MS analysis, the peptides were resuspended in 0.1% formic acid (FA) and analyzed by a LTQ Orbitrap Elite mass spectrometer (Thermo Scientific) coupled online to an Easy-nLC 1000 in the data-dependent mode.

    Techniques: Cell Culture, SDS Page, Staining, Labeling, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    CBP inhibits liver inflammation in mice with intrahepatic cholestasis (A) The effects of CBP on protein levels of NF-κB, IκBα, IKKα, and ICAM-1, detected by western blot. (B) Quantitative analysis of the effects of CBP on NF-κB, IκBα, IKKα, and ICAM-1 proteins, and IL-1 and ICAM-1 mRNA expression. (C) Quantitative analysis of 8, 9-epoxyeicosatrienoic acid by UPLC-LTQ-orbitrap. Data are expressed as the mean ± SD, * p

    Journal: Oncotarget

    Article Title: Chicken bile powder protects against α-naphthylisothiocyanate-induced cholestatic liver injury in mice

    doi: 10.18632/oncotarget.21385

    Figure Lengend Snippet: CBP inhibits liver inflammation in mice with intrahepatic cholestasis (A) The effects of CBP on protein levels of NF-κB, IκBα, IKKα, and ICAM-1, detected by western blot. (B) Quantitative analysis of the effects of CBP on NF-κB, IκBα, IKKα, and ICAM-1 proteins, and IL-1 and ICAM-1 mRNA expression. (C) Quantitative analysis of 8, 9-epoxyeicosatrienoic acid by UPLC-LTQ-orbitrap. Data are expressed as the mean ± SD, * p

    Article Snippet: The UPLC system was connected to an LTQ-orbitrap elite mass spectrometry system (Thermo Fisher Scientific; Bremen, Germany) via a heated electrospray ionization (ESI) source in both positive and negative ionization mode.

    Techniques: Mouse Assay, Western Blot, Expressing

    FhaA is phosphorylated on Tyr. Precursor ion masses were measured in the Orbitrap Elite mass analyzer, and MS/MS spectra were acquired in the LTQ mass spectrometer. ( A ) Endogenous peptide identified in the phosphopeptide-enriched fraction of total Mtb cell lysate (precursor ion mass accuracy −0.69 ppm). ( B ) Synthetic peptide confirming the fragmentation pattern of the endogenous peptide (mass accuracy 1.04 ppm). ( C ) Nonphosphorylated peptide VPGYAPQGGGYAEPAGR, shown for comparison (mass accuracy 0.61 ppm). ( D ) Sequence annotation of identified fragment ions of the phosphorylated and nonphosphorylated peptides. The mass shift caused by phosphorylation is shown by the different y ion masses observed upstream and the different b ion masses observed downstream of the pTyr residue, as highlighted by arrows in the phosphorylated peptide sequence and shown in bold in the spectra.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Mycobacterium tuberculosis supports protein tyrosine phosphorylation

    doi: 10.1073/pnas.1323894111

    Figure Lengend Snippet: FhaA is phosphorylated on Tyr. Precursor ion masses were measured in the Orbitrap Elite mass analyzer, and MS/MS spectra were acquired in the LTQ mass spectrometer. ( A ) Endogenous peptide identified in the phosphopeptide-enriched fraction of total Mtb cell lysate (precursor ion mass accuracy −0.69 ppm). ( B ) Synthetic peptide confirming the fragmentation pattern of the endogenous peptide (mass accuracy 1.04 ppm). ( C ) Nonphosphorylated peptide VPGYAPQGGGYAEPAGR, shown for comparison (mass accuracy 0.61 ppm). ( D ) Sequence annotation of identified fragment ions of the phosphorylated and nonphosphorylated peptides. The mass shift caused by phosphorylation is shown by the different y ion masses observed upstream and the different b ion masses observed downstream of the pTyr residue, as highlighted by arrows in the phosphorylated peptide sequence and shown in bold in the spectra.

    Article Snippet: Peptides were analyzed on either an LTQ-Velos Orbitrap or an LTQ-Velos Pro Orbitrap Elite (Thermo Fisher Scientific) mass spectrometer equipped with a nano LC system.

    Techniques: Mass Spectrometry, Sequencing