ltq linear ion trap mass spectrometer Thermo Fisher Search Results


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  • 77
    Thermo Fisher trap quadrupole ltq proteomex 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" />
    Trap Quadrupole Ltq Proteomex Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher linear ion trap ltq orbitrap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Linear Ion Trap Ltq Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 92 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Thermo Fisher linear ion trap ltq velos mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Linear Ion Trap Ltq Velos Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher finningan ltq liner ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Finningan Ltq Liner Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Thermo Fisher esi ion trap
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Esi Ion Trap, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher nanoelectrospray ionization nesi linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Nanoelectrospray Ionization Nesi Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher velos linear ion trap ltq orbitrap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Velos Linear Ion Trap Ltq Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher linear quadrupole ion trap orbitrap
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Linear Quadrupole Ion Trap Orbitrap, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher finnigan ltq velos linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Finnigan Ltq Velos Linear Ion Trap Mass Spectrometer, 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
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    84
    Thermo Fisher linear ion trap mass spectrometer ltq orbitrap discovery
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Linear Ion Trap Mass Spectrometer Ltq Orbitrap Discovery, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1932 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher ion trap lit mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Ion Trap Lit Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher finnigan ltq linear quadrupole ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Finnigan Ltq Linear Quadrupole Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    75
    Thermo Fisher esi ltq xl linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Esi Ltq Xl Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher hybrid linear ion trap orbitrap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Hybrid Linear Ion Trap Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 587 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher nanoelectrospray ionization nesi ltq linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Nanoelectrospray Ionization Nesi Ltq Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 2d linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    2d Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher hybrid linear ion trap fticr
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Hybrid Linear Ion Trap Fticr, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher hybrid linear quadrupole ion trap
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Hybrid Linear Quadrupole Ion Trap, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Fisher Scientific ltq linear ion trap mass spectrometer
    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the <t>LTQ-Orbitrap</t> is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.
    Ltq Linear Ion Trap Mass Spectrometer, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher ion trap orbitrap hybrid mass spectrometer
    Ser 910 and Ser 935 phosphorylation mediate binding of LRRK2 to 14-3-3 ( A ) Endogenous LRRK2 was immunoprecipitated (IP) with anti-LRRK2-(100–500) (S348C) antibody from Swiss 3T3 cells and FLAG–LRRK2 was immunoprecipitated with anti-FLAG–agarose from stable inducible T-REx HEK-293 cells. Immunoprecipitates were subjected to electrophoresis on a 4–12% Novex SDS/polyacrylamide gel and stained with Colloidal Blue. The gel is representative of several experiments. LRRK2 tryptic peptides were subjected to LC-MS/MS on an <t>LTQ-Orbitrap</t> mass spectrometer. M, molecular-mass marker. ( B ) Phospho-peptides identified by LTQ-Orbitrap MS shown in tabular format. Observed mass ( m / z ) and predicted mass (M) are shown, and the site of phosphorylation and peptide sequence are identified. The number of experiments evaluated ( N ) is indicated at the top of the column and the number of times, in total, the phosphorylated peptide was identified is indicated. ( C ) Domain structure of LRRK2 is presented to scale, with amino acid residues indicating domain boundaries indicated. Positions of identified phosphorylation sites are shown. LRR, leucine-rich repeat. ( D ) The indicated phosphorylation sites identified in ( A ) and ( B ) were mutated to an alanine residue and transiently expressed in HEK-293 cells. LRRK2 was immunoprecipitated with anti-FLAG–agarose and equal amounts of each protein were probed with FLAG (total) and the ability to directly bind 14-3-3 was assessed in an overlay assay. 14-3-3 and Hsp90 co-immunoprecipitation (Co-IP) was determined by immunoblotting the immunoprecipitates with the indicated antibodies. Kinase activity was assayed against 30 μM Nictide and specific activity was determined by correcting incorporation of phosphate for protein levels in the immunoprecipitate by quantitative immunoblot using the Odyssey system and is presented as c.p.m./absorbance units (cpm/LICOR AU). The data are the average for duplicate experiments that were repeated four separate times with similar results. ( E ) Streptavidin–agarose was conjugated to a biotinylated di-phosphorylated peptide encompassing Ser 910 (pS910) and Ser 935 (pS935) and incubated in the presence or absence of λ phosphatase in the presence or absence of the EDTA phosphatase inhibitor. The agarose beads were then incubated with HEK-293 cell lysates and interaction of 14-3-3 was assessed after beads were extensively washed and subjected to 14-3-3 immunoblot analysis. ( F ) The indicated forms of FLAG–LRRK2 were expressed in HEK-293 cells by transient transfection. Post-transfection (36 h), these were immunoprecipitated with anti-FLAG antibody and immunoblotted with phospho-specific antibodies against Ser 910 (S357C) and Ser 935 (S814C). Direct binding of immunoprecipitates to 14-3-3 was also assessed by a 14-3-3 overlay assay and co-immunoprecipitation of 14-3-3 and Hsp90 was assessed by immunoblotting with the respective antibodies. Unt., untransfected. ( G ) LRRK2 was immunoprecipitated from tissues of wild-type male C57BL/6 mice and immunoblotted for Ser 910 and Ser 935 phosphorylation and 14-3-3 binding was assessed by overlay assay as in ( F ). ( H ) Multiple sequence alignment of LRRK2 from Homo sapiens (NP_940980), Pan troglodytes (XP_001168494), Mus musculus (NP_080006), Rattus norvegicus (XP_235581), Bos taurus (XP_615760), Canis lupus familiaris (XP_543734) and Gallus gallus (XP_427077). Positions of the phosphorylated residues Ser 910 and Ser 935 are indicated. Identical residues are indicated in grey. ( I ) Sequence comparison of residues surrounding the Ser 910 and Ser 935 phosphorylation sites of human LRRK2.
    Ion Trap Orbitrap Hybrid Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher ltq velos dual pressure linear ion trap mass spectrometer
    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and <t>LTQ</t> <t>Velos</t>
    Ltq Velos Dual Pressure Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Thermo Fisher liner ion trap ltq orbitrap mass spectrometer
    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and <t>LTQ</t> <t>Velos</t>
    Liner Ion Trap Ltq Orbitrap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher linear ion trap orbitrap ft mass spectrometer
    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and <t>LTQ</t> <t>Velos</t>
    Linear Ion Trap Orbitrap Ft Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Thermo Fisher linear quadrupole ion trap lqit mass spectrometer
    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and <t>LTQ</t> <t>Velos</t>
    Linear Quadrupole Ion Trap Lqit Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher scientific ltq linear ion trap mass spectrometer
    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and <t>LTQ</t> <t>Velos</t>
    Scientific Ltq Linear Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tesla Linear Ion Trap Ltq Ion Cyclotron Resonance Ft Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    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

    Journal: PLoS Pathogens

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

    doi: 10.1371/journal.ppat.1002222

    Figure Lengend 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).

    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 .

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

    MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the LTQ-Orbitrap is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Using a Label-free Proteomics Method to Identify Differentially Abundant Proteins in Closely Related Hypo- and Hypervirulent Clinical Mycobacterium tuberculosis Beijing Isolates *

    doi: 10.1074/mcp.M900422-MCP200

    Figure Lengend Snippet: MS/MS profile of ion m / z 601.41. A tandem mass spectrum of a prevalent ion on a particular time point in the LC gradient and ionized on the LTQ-Orbitrap is shown. The peptide fragments randomly on each amide bond, resulting in carboxyl-terminal y ions or amino-terminal b ions. After the fragment masses were submitted to Mascot, the peptide was identified as FGDQVVAVLTR ( inset with detected y and b ions represented) from protein Rv3220c, a probable two-component sensor kinase. * Asterisk represent the parent ion.

    Article Snippet: Mass Spectrometry All experiments were performed on a Dionex Ultimate 3000 nano-LC system (Dionex, Sunnyvale, CA) connected to a linear quadrupole ion trap-Orbitrap (LTQ-Orbitrap) mass spectrometer (Thermo Electron, Bremen, Germany) equipped with a nanoelectrospray ion source.

    Techniques: Mass Spectrometry

    Stem cell therapy-specific subproteome. ( A ): Comparison of stem cell-treated [ES(+)] versus untreated [ES(−)] left ventricular tissue extracts by two-dimensional (2D) electrophoresis. Differentially expressed spots isolated for identification by LTQ-Orbitrap mass spectrometric analysis are circled, and numbered on the ES(+) gel. Inset: Gel-to-gel reproducibility indicated by correlation of scatter plot for average normalized densitometric intensities of matching protein spots from ES(+) versus ES(−) gels. ( B ): Identities of the 61 proteins significantly altered by cell therapy are listed with their symbol (Swiss-Prot gene abbreviation) and spot numbers to locate corresponding 2D gel position(s) in panel ( A ). Mascot score, number of unique identified peptides, % sequence cov. (coverage), predicted M r and p I for each protein (following expected post-translational processing, for example, removal of a mitochondrial signal peptide), and fold change in ES(+) versus ES(−) are indicated. For proteins detected in more than one spot, maximum score and corresponding number of unique peptides are reported. Fold change was calculated as described in experimental procedures, and for proteins detected in both increasing and decreasing spots (*), both values are indicated. Abbreviations: ES, embryonic stem cells; Ox., oxidative; TCA cycle, tricarboxylic acid cycle; SAPK, stress activated protein kinase.

    Journal: Stem cells (Dayton, Ohio)

    Article Title: ATP-Sensitive K+ Channel-Deficient Dilated Cardiomyopathy Proteome Remodeled by Embryonic Stem Cell Therapy

    doi: 10.1002/stem.465

    Figure Lengend Snippet: Stem cell therapy-specific subproteome. ( A ): Comparison of stem cell-treated [ES(+)] versus untreated [ES(−)] left ventricular tissue extracts by two-dimensional (2D) electrophoresis. Differentially expressed spots isolated for identification by LTQ-Orbitrap mass spectrometric analysis are circled, and numbered on the ES(+) gel. Inset: Gel-to-gel reproducibility indicated by correlation of scatter plot for average normalized densitometric intensities of matching protein spots from ES(+) versus ES(−) gels. ( B ): Identities of the 61 proteins significantly altered by cell therapy are listed with their symbol (Swiss-Prot gene abbreviation) and spot numbers to locate corresponding 2D gel position(s) in panel ( A ). Mascot score, number of unique identified peptides, % sequence cov. (coverage), predicted M r and p I for each protein (following expected post-translational processing, for example, removal of a mitochondrial signal peptide), and fold change in ES(+) versus ES(−) are indicated. For proteins detected in more than one spot, maximum score and corresponding number of unique peptides are reported. Fold change was calculated as described in experimental procedures, and for proteins detected in both increasing and decreasing spots (*), both values are indicated. Abbreviations: ES, embryonic stem cells; Ox., oxidative; TCA cycle, tricarboxylic acid cycle; SAPK, stress activated protein kinase.

    Article Snippet: Chromatography was performed using 0.2% formic acid in solvent A (99% water, 1% acetonitrile) and B (80% acetonitrile, 5% isopropanol, 15% water), with peptides eluted over 30 minutes with a 5%–45% solvent B gradient using an Eksigent nanoHPLC system (MDS Sciex, Toronto, Canada) coupled to a linear ion trap quadrupole (LTQ)-Orbitrap mass spectrometer (Thermo Fisher Scientific, Barrington, IL).

    Techniques: Two-Dimensional Gel Electrophoresis, Isolation, Sequencing

    Ser 910 and Ser 935 phosphorylation mediate binding of LRRK2 to 14-3-3 ( A ) Endogenous LRRK2 was immunoprecipitated (IP) with anti-LRRK2-(100–500) (S348C) antibody from Swiss 3T3 cells and FLAG–LRRK2 was immunoprecipitated with anti-FLAG–agarose from stable inducible T-REx HEK-293 cells. Immunoprecipitates were subjected to electrophoresis on a 4–12% Novex SDS/polyacrylamide gel and stained with Colloidal Blue. The gel is representative of several experiments. LRRK2 tryptic peptides were subjected to LC-MS/MS on an LTQ-Orbitrap mass spectrometer. M, molecular-mass marker. ( B ) Phospho-peptides identified by LTQ-Orbitrap MS shown in tabular format. Observed mass ( m / z ) and predicted mass (M) are shown, and the site of phosphorylation and peptide sequence are identified. The number of experiments evaluated ( N ) is indicated at the top of the column and the number of times, in total, the phosphorylated peptide was identified is indicated. ( C ) Domain structure of LRRK2 is presented to scale, with amino acid residues indicating domain boundaries indicated. Positions of identified phosphorylation sites are shown. LRR, leucine-rich repeat. ( D ) The indicated phosphorylation sites identified in ( A ) and ( B ) were mutated to an alanine residue and transiently expressed in HEK-293 cells. LRRK2 was immunoprecipitated with anti-FLAG–agarose and equal amounts of each protein were probed with FLAG (total) and the ability to directly bind 14-3-3 was assessed in an overlay assay. 14-3-3 and Hsp90 co-immunoprecipitation (Co-IP) was determined by immunoblotting the immunoprecipitates with the indicated antibodies. Kinase activity was assayed against 30 μM Nictide and specific activity was determined by correcting incorporation of phosphate for protein levels in the immunoprecipitate by quantitative immunoblot using the Odyssey system and is presented as c.p.m./absorbance units (cpm/LICOR AU). The data are the average for duplicate experiments that were repeated four separate times with similar results. ( E ) Streptavidin–agarose was conjugated to a biotinylated di-phosphorylated peptide encompassing Ser 910 (pS910) and Ser 935 (pS935) and incubated in the presence or absence of λ phosphatase in the presence or absence of the EDTA phosphatase inhibitor. The agarose beads were then incubated with HEK-293 cell lysates and interaction of 14-3-3 was assessed after beads were extensively washed and subjected to 14-3-3 immunoblot analysis. ( F ) The indicated forms of FLAG–LRRK2 were expressed in HEK-293 cells by transient transfection. Post-transfection (36 h), these were immunoprecipitated with anti-FLAG antibody and immunoblotted with phospho-specific antibodies against Ser 910 (S357C) and Ser 935 (S814C). Direct binding of immunoprecipitates to 14-3-3 was also assessed by a 14-3-3 overlay assay and co-immunoprecipitation of 14-3-3 and Hsp90 was assessed by immunoblotting with the respective antibodies. Unt., untransfected. ( G ) LRRK2 was immunoprecipitated from tissues of wild-type male C57BL/6 mice and immunoblotted for Ser 910 and Ser 935 phosphorylation and 14-3-3 binding was assessed by overlay assay as in ( F ). ( H ) Multiple sequence alignment of LRRK2 from Homo sapiens (NP_940980), Pan troglodytes (XP_001168494), Mus musculus (NP_080006), Rattus norvegicus (XP_235581), Bos taurus (XP_615760), Canis lupus familiaris (XP_543734) and Gallus gallus (XP_427077). Positions of the phosphorylated residues Ser 910 and Ser 935 are indicated. Identical residues are indicated in grey. ( I ) Sequence comparison of residues surrounding the Ser 910 and Ser 935 phosphorylation sites of human LRRK2.

    Journal: Biochemical Journal

    Article Title: 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

    doi: 10.1042/BJ20100483

    Figure Lengend Snippet: Ser 910 and Ser 935 phosphorylation mediate binding of LRRK2 to 14-3-3 ( A ) Endogenous LRRK2 was immunoprecipitated (IP) with anti-LRRK2-(100–500) (S348C) antibody from Swiss 3T3 cells and FLAG–LRRK2 was immunoprecipitated with anti-FLAG–agarose from stable inducible T-REx HEK-293 cells. Immunoprecipitates were subjected to electrophoresis on a 4–12% Novex SDS/polyacrylamide gel and stained with Colloidal Blue. The gel is representative of several experiments. LRRK2 tryptic peptides were subjected to LC-MS/MS on an LTQ-Orbitrap mass spectrometer. M, molecular-mass marker. ( B ) Phospho-peptides identified by LTQ-Orbitrap MS shown in tabular format. Observed mass ( m / z ) and predicted mass (M) are shown, and the site of phosphorylation and peptide sequence are identified. The number of experiments evaluated ( N ) is indicated at the top of the column and the number of times, in total, the phosphorylated peptide was identified is indicated. ( C ) Domain structure of LRRK2 is presented to scale, with amino acid residues indicating domain boundaries indicated. Positions of identified phosphorylation sites are shown. LRR, leucine-rich repeat. ( D ) The indicated phosphorylation sites identified in ( A ) and ( B ) were mutated to an alanine residue and transiently expressed in HEK-293 cells. LRRK2 was immunoprecipitated with anti-FLAG–agarose and equal amounts of each protein were probed with FLAG (total) and the ability to directly bind 14-3-3 was assessed in an overlay assay. 14-3-3 and Hsp90 co-immunoprecipitation (Co-IP) was determined by immunoblotting the immunoprecipitates with the indicated antibodies. Kinase activity was assayed against 30 μM Nictide and specific activity was determined by correcting incorporation of phosphate for protein levels in the immunoprecipitate by quantitative immunoblot using the Odyssey system and is presented as c.p.m./absorbance units (cpm/LICOR AU). The data are the average for duplicate experiments that were repeated four separate times with similar results. ( E ) Streptavidin–agarose was conjugated to a biotinylated di-phosphorylated peptide encompassing Ser 910 (pS910) and Ser 935 (pS935) and incubated in the presence or absence of λ phosphatase in the presence or absence of the EDTA phosphatase inhibitor. The agarose beads were then incubated with HEK-293 cell lysates and interaction of 14-3-3 was assessed after beads were extensively washed and subjected to 14-3-3 immunoblot analysis. ( F ) The indicated forms of FLAG–LRRK2 were expressed in HEK-293 cells by transient transfection. Post-transfection (36 h), these were immunoprecipitated with anti-FLAG antibody and immunoblotted with phospho-specific antibodies against Ser 910 (S357C) and Ser 935 (S814C). Direct binding of immunoprecipitates to 14-3-3 was also assessed by a 14-3-3 overlay assay and co-immunoprecipitation of 14-3-3 and Hsp90 was assessed by immunoblotting with the respective antibodies. Unt., untransfected. ( G ) LRRK2 was immunoprecipitated from tissues of wild-type male C57BL/6 mice and immunoblotted for Ser 910 and Ser 935 phosphorylation and 14-3-3 binding was assessed by overlay assay as in ( F ). ( H ) Multiple sequence alignment of LRRK2 from Homo sapiens (NP_940980), Pan troglodytes (XP_001168494), Mus musculus (NP_080006), Rattus norvegicus (XP_235581), Bos taurus (XP_615760), Canis lupus familiaris (XP_543734) and Gallus gallus (XP_427077). Positions of the phosphorylated residues Ser 910 and Ser 935 are indicated. Identical residues are indicated in grey. ( I ) Sequence comparison of residues surrounding the Ser 910 and Ser 935 phosphorylation sites of human LRRK2.

    Article Snippet: The HPLC system was coupled to a linear ion-trap–orbitrap hybrid mass spectrometer (LTQ-Orbitrap XL, Thermo Fisher Scientific) via a nanoelectrospray ion source (Proxeon Biosystems) fitted with a 5 cm Picotip FS360-20-10 emitter.

    Techniques: Binding Assay, Immunoprecipitation, Electrophoresis, Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Marker, Sequencing, Overlay Assay, Co-Immunoprecipitation Assay, Activity Assay, Incubation, Transfection, Mouse Assay

    Quantitative MS identifies 14-3-3 as an LRRK2 interactor HEK-293 cells stably expressing GFP, wild-type full-length GFP–LRRK2 or full-length GFP–LRRK2(G2019S) mutant were cultured for multiple passages in either R6K4 SILAC medium (GFP–LRRK2) or R10K8 SILAC medium [GFP–LRRK2(G2019S)] or normal R0K0 SILAC medium (GFP). Cells were lysed and equal amounts of lysates from GFP and GFP–LRRK2 ( A ) or GFP and GFP–LRRK2(G2019S) ( B ) were mixed. Immunoprecipitations were undertaken employing an anti-GFP antibody and electrophoresed on an SDS/polyacrylamide gel, which was stained with Colloidal Blue ( A ). Migration of the LRRK2 band is indicated with an arrowhead and the GFP band is indicated with an arrow. Molecular-mass markers (kDa) are indicated on the left-hand side of the gels. The entire lane from each gel was excised, digested with trypsin and processed for MS. Each sample was analysed with Orbitrap MS and quantified using MaxQuant (version 13.13.10) [ 34 ] and a summary of results are presented in the Tables on the right-hand side. The number of peptides and percentage of sequence coverage corresponding to the indicated protein which were quantified are shown along with the ratios of enrichment for labelled compared with unlabelled peptides (Ratio H/L) for each comparison of GFP with wild-type LRRK2 ( A ) and GFP with LRRK2(G2019S) ( B ). The posterior error probability (PEP) is shown, which measures the accuracy of MaxQuant quantification where the closer to zero, the higher the probability of specific interaction [ 34 ].

    Journal: Biochemical Journal

    Article Title: 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

    doi: 10.1042/BJ20100483

    Figure Lengend Snippet: Quantitative MS identifies 14-3-3 as an LRRK2 interactor HEK-293 cells stably expressing GFP, wild-type full-length GFP–LRRK2 or full-length GFP–LRRK2(G2019S) mutant were cultured for multiple passages in either R6K4 SILAC medium (GFP–LRRK2) or R10K8 SILAC medium [GFP–LRRK2(G2019S)] or normal R0K0 SILAC medium (GFP). Cells were lysed and equal amounts of lysates from GFP and GFP–LRRK2 ( A ) or GFP and GFP–LRRK2(G2019S) ( B ) were mixed. Immunoprecipitations were undertaken employing an anti-GFP antibody and electrophoresed on an SDS/polyacrylamide gel, which was stained with Colloidal Blue ( A ). Migration of the LRRK2 band is indicated with an arrowhead and the GFP band is indicated with an arrow. Molecular-mass markers (kDa) are indicated on the left-hand side of the gels. The entire lane from each gel was excised, digested with trypsin and processed for MS. Each sample was analysed with Orbitrap MS and quantified using MaxQuant (version 13.13.10) [ 34 ] and a summary of results are presented in the Tables on the right-hand side. The number of peptides and percentage of sequence coverage corresponding to the indicated protein which were quantified are shown along with the ratios of enrichment for labelled compared with unlabelled peptides (Ratio H/L) for each comparison of GFP with wild-type LRRK2 ( A ) and GFP with LRRK2(G2019S) ( B ). The posterior error probability (PEP) is shown, which measures the accuracy of MaxQuant quantification where the closer to zero, the higher the probability of specific interaction [ 34 ].

    Article Snippet: The HPLC system was coupled to a linear ion-trap–orbitrap hybrid mass spectrometer (LTQ-Orbitrap XL, Thermo Fisher Scientific) via a nanoelectrospray ion source (Proxeon Biosystems) fitted with a 5 cm Picotip FS360-20-10 emitter.

    Techniques: Mass Spectrometry, Stable Transfection, Expressing, Mutagenesis, Cell Culture, Staining, Migration, Sequencing

    LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and LTQ Velos

    Journal: Journal of proteomics

    Article Title: Confident identification of 3-nitrotyrosine modifications in mass spectral data across multiple mass spectrometry platforms

    doi: 10.1016/j.jprot.2011.04.007

    Figure Lengend Snippet: LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and LTQ Velos

    Article Snippet: Chromatographic separation of peptides was carried out using an Eksigent nanoLC-ultra 2D plus HPLC system directly connected to the LTQ Velos dual-pressure linear ion trap mass spectrometer (Thermo Scientific, San Jose, CA).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    LC-MS/MS properties of the 3NT peptides identified by the QSTAR Elite and LTQ Velos

    Journal: Journal of proteomics

    Article Title: Confident identification of 3-nitrotyrosine modifications in mass spectral data across multiple mass spectrometry platforms

    doi: 10.1016/j.jprot.2011.04.007

    Figure Lengend Snippet: LC-MS/MS properties of the 3NT peptides identified by the QSTAR Elite and LTQ Velos

    Article Snippet: Chromatographic separation of peptides was carried out using an Eksigent nanoLC-ultra 2D plus HPLC system directly connected to the LTQ Velos dual-pressure linear ion trap mass spectrometer (Thermo Scientific, San Jose, CA).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    Overlap of validated 3NT peptides identified by the QSTAR Elite and LTQ Velos

    Journal: Journal of proteomics

    Article Title: Confident identification of 3-nitrotyrosine modifications in mass spectral data across multiple mass spectrometry platforms

    doi: 10.1016/j.jprot.2011.04.007

    Figure Lengend Snippet: Overlap of validated 3NT peptides identified by the QSTAR Elite and LTQ Velos

    Article Snippet: Chromatographic separation of peptides was carried out using an Eksigent nanoLC-ultra 2D plus HPLC system directly connected to the LTQ Velos dual-pressure linear ion trap mass spectrometer (Thermo Scientific, San Jose, CA).

    Techniques: