electrospray ionization Search Results


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  • 99
    Thermo Fisher electrospray ionization source
    Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by <t>electrospray</t> ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.
    Electrospray Ionization Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1752 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Agilent technologies esi source
    Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive <t>electrospray</t> mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).
    Esi Source, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 1197 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation esi source
    ( a )–( c ): <t>ESI-IMS-MS</t> Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.
    Esi Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 586 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Abbott Laboratories pcr esi ms
    Assessment of factors influencing performance of <t>PCR/ESI-MS.</t>
    Pcr Esi Ms, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 91/100, based on 182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher nano esi source
    Assessment of factors influencing performance of <t>PCR/ESI-MS.</t>
    Nano Esi Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 486 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation electrospray ionization esi source
    Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive <t>electrospray</t> ionization <t>(ESI+)</t> mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
    Electrospray Ionization Esi Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 360 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher heated electrospray ionization source
    Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive <t>electrospray</t> ionization <t>(ESI+)</t> mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
    Heated Electrospray Ionization Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 224 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Agilent technologies jet stream electrospray ionization source
    Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive <t>electrospray</t> ionization <t>(ESI+)</t> mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
    Jet Stream Electrospray Ionization Source, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 123 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Agilent technologies g1607a ce esi ms sprayer kit
    Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive <t>electrospray</t> ionization <t>(ESI+)</t> mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
    G1607a Ce Esi Ms Sprayer Kit, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 89/100, based on 368 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation electrospray ionization mass spectrometry
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    Electrospray Ionization Mass Spectrometry, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher esi ms
    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by <t>electrospray</t> ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
    Esi Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1415 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation electrospray ionization mass spectrometry esi ms
    <t>Electrospray</t> ionization-tandem mass spectrum of moanachelin gly-D (C14:0).
    Electrospray Ionization Mass Spectrometry Esi Ms, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies electrospray ionization mass spectrometry
    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) <t>Electrospray</t> ionization mass spectrometry analysis of purified recombinant CAM-W.
    Electrospray Ionization Mass Spectrometry, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies electrospray ionization mass spectrometry esi ms
    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) <t>Electrospray</t> ionization mass spectrometry analysis of purified recombinant CAM-W.
    Electrospray Ionization Mass Spectrometry Esi Ms, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 392 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    New Objective Inc electrospray ionization
    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) <t>Electrospray</t> ionization mass spectrometry analysis of purified recombinant CAM-W.
    Electrospray Ionization, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 92/100, based on 282 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher nano lc electrospray ionization source
    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) <t>Electrospray</t> ionization mass spectrometry analysis of purified recombinant CAM-W.
    Nano Lc Electrospray Ionization Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 330 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    ESI 05 is an inhibitor of exchange protein activated by cAMP 2 Epac2 that inhibits cAMP induced Epac2 guanine nucleotide exchange factor GEF activity with an IC value of 0
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    Image Search Results


    Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by electrospray ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.

    Journal: bioRxiv

    Article Title: Covalent Protein Painting Reveals Structural Changes in the Proteome in Alzheimer Disease

    doi: 10.1101/2020.01.31.929117

    Figure Lengend Snippet: Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by electrospray ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.

    Article Snippet: Following chromatographic separation, peptides were transferred into an Orbitrap Lumos mass spectrometer by electrospray ionization (nanoEasy, Thermo Fisher Scientific).

    Techniques: In Vivo, Methylation, Mass Spectrometry, Labeling, Modification, Liquid Chromatography, Tandem Mass Spectroscopy

    Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).

    Journal: Analytical Chemistry

    Article Title: MS2Analyzer: A Software for Small Molecule Substructure Annotations from Accurate Tandem Mass Spectra

    doi: 10.1021/ac502818e

    Figure Lengend Snippet: Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).

    Article Snippet: In order to reduce the impact from different instruments, ionizations, and adducts, only [M + H]+ spectra acquired under positive electrospray ionization from Agilent QTOF 6530 mass spectrometers were used.

    Techniques: Mass Spectrometry

    ( a )–( c ): ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ( a )–( c ): ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry, Mutagenesis

    ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for wild-type β 2 m analyzed at ( a ) pH 6.23, ( b ) pH 4.28, ( c ) pH 3.54, and ( d ) pH 2.60. The number of conformeric species observed for each individual charge state can be seen. Insets at the right hand side of each plot: the summed, full scan m/z spectra of wild-type β 2 m for each data acquisition showing the charge state ions detected.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for wild-type β 2 m analyzed at ( a ) pH 6.23, ( b ) pH 4.28, ( c ) pH 3.54, and ( d ) pH 2.60. The number of conformeric species observed for each individual charge state can be seen. Insets at the right hand side of each plot: the summed, full scan m/z spectra of wild-type β 2 m for each data acquisition showing the charge state ions detected.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry

    ( a ) The summed m/z spectrum from an ESI-IMS-MS data acquisition of cytochrome c analyzed in 50 mM aqueous ammonium acetate solution acidified to pH 3 showing a charge state distribution from +6 to +20 ions consistent with monomeric protein (12,359.4 Da). ( b ) ESI-IMS-MS Driftscope plot showing drift time (x axis) versus m/z (y axis) for the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3. ( c ) ESI-IMS-MS drift time versus intensity graphs for the m/z 1237.0 (+10 ions; upper), m/z 1374.4 (+9 ions; middle), and m/z 1546.0 (+8 ions; lower) signals detected during the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3.

    Journal: Journal of the American Society for Mass Spectrometry

    Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry

    doi: 10.1016/j.jasms.2007.09.017

    Figure Lengend Snippet: ( a ) The summed m/z spectrum from an ESI-IMS-MS data acquisition of cytochrome c analyzed in 50 mM aqueous ammonium acetate solution acidified to pH 3 showing a charge state distribution from +6 to +20 ions consistent with monomeric protein (12,359.4 Da). ( b ) ESI-IMS-MS Driftscope plot showing drift time (x axis) versus m/z (y axis) for the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3. ( c ) ESI-IMS-MS drift time versus intensity graphs for the m/z 1237.0 (+10 ions; upper), m/z 1374.4 (+9 ions; middle), and m/z 1546.0 (+8 ions; lower) signals detected during the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3.

    Article Snippet: ESI-IMS-MS Analyses Samples were infused into the ESI source of a Synapt HDMS, a hybrid quadrupole-IMS-orthogonal acceleration time-of-flight mass spectrometer (oa-TOF) [ ] (Waters UK Ltd, Manchester, UK) using a Harvard syringe pump (model 22; Harvard Apparatus, Holliston, MA) with a flow rate of 10 μL min−1 .

    Techniques: Mass Spectrometry

    Assessment of factors influencing performance of PCR/ESI-MS.

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: Assessment of factors influencing performance of PCR/ESI-MS.

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry

    PCR/ESI-MS and blood culture results by specimen.

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: PCR/ESI-MS and blood culture results by specimen.

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry

    Results of blood cultures (BC) and PCR/ESI-MS in the 105 cases of neutropenic fever. Bloodstream infection (BSI) included both definite and probable BSI based on BC and/or PCR/ESI-MS. MO, microorganism; +, positive result; −, negative result;

    Journal: Journal of Clinical Microbiology

    Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever

    doi: 10.1128/JCM.01066-16

    Figure Lengend Snippet: Results of blood cultures (BC) and PCR/ESI-MS in the 105 cases of neutropenic fever. Bloodstream infection (BSI) included both definite and probable BSI based on BC and/or PCR/ESI-MS. MO, microorganism; +, positive result; −, negative result;

    Article Snippet: Episodes with polymicrobial infection, where PCR/ESI-MS detected only the definite pathogen and not the potential contaminant(s), were categorized as true positive for PCR/ESI-MS compared to BC. summarizes all microorganisms detected by both methods, PCR/ESI-MS only, and BC only.

    Techniques: Polymerase Chain Reaction, Mass Spectrometry, Infection

    Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.

    Journal: Frontiers in Immunology

    Article Title: Alterations of Gut Microbiome and Metabolite Profiling in Mice Infected by Schistosoma japonicum

    doi: 10.3389/fimmu.2020.569727

    Figure Lengend Snippet: Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.

    Article Snippet: Quadrupole-Time-of-Flight Mass Spectrometry Conditions Mass spectrometry data were collected by a SYNAPT G2-Si High-Definition Mass Spectrometer with an electrospray ionization (ESI) source (Waters Ltd., Milford, MA, USA) in both positive and negative ion modes for the serum and the urine samples, whereas only negative ion mode was used for the liver and colon aqueous extracts due to the limited valuable compounds detected in the positive ion mode.

    Techniques: Mouse Assay, Infection

    Three-dimensional score plots of principal component analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.

    Journal: Frontiers in Immunology

    Article Title: Alterations of Gut Microbiome and Metabolite Profiling in Mice Infected by Schistosoma japonicum

    doi: 10.3389/fimmu.2020.569727

    Figure Lengend Snippet: Three-dimensional score plots of principal component analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.

    Article Snippet: Quadrupole-Time-of-Flight Mass Spectrometry Conditions Mass spectrometry data were collected by a SYNAPT G2-Si High-Definition Mass Spectrometer with an electrospray ionization (ESI) source (Waters Ltd., Milford, MA, USA) in both positive and negative ion modes for the serum and the urine samples, whereas only negative ion mode was used for the liver and colon aqueous extracts due to the limited valuable compounds detected in the positive ion mode.

    Techniques: Mouse Assay, Infection

    Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by electrospray ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.

    Journal: Toxins

    Article Title: Anti-Breast Cancer Activity of Latroeggtoxin-V Mined from the Transcriptome of Spider Latrodectus tredecimguttatus Eggs

    doi: 10.3390/toxins10110451

    Figure Lengend Snippet: Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by electrospray ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.

    Article Snippet: The molecular weight of the components in each elution peak was determined by electrospray ionization mass spectrometry (Waters ACQUITY UPLC/Xevo G2 QTOF, Waters, Milford, MA, USA) and thus the peak containing recombinant Latroeggtoxin-V (rLatroeggtoxin-V) was selected and lyophilized.

    Techniques: Purification, High Performance Liquid Chromatography, Molecular Weight, Mass Spectrometry, Labeling

    Electrospray ionization-tandem mass spectrum of moanachelin gly-D (C14:0).

    Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

    Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species

    doi: 10.1007/s00775-013-0995-3

    Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin gly-D (C14:0).

    Article Snippet: The masses of the siderophores and the siderophore fragments were determined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry on a Micromass Q-TOF2 (Waters Corp.).

    Techniques:

    Electrospray ionization-tandem mass spectrum of moanachelin ala-D (C14:0).

    Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

    Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species

    doi: 10.1007/s00775-013-0995-3

    Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin ala-D (C14:0).

    Article Snippet: The masses of the siderophores and the siderophore fragments were determined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry on a Micromass Q-TOF2 (Waters Corp.).

    Techniques:

    Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) Electrospray ionization mass spectrometry analysis of purified recombinant CAM-W.

    Journal: Scientific Reports

    Article Title: Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700

    doi: 10.1038/srep40587

    Figure Lengend Snippet: Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) Electrospray ionization mass spectrometry analysis of purified recombinant CAM-W.

    Article Snippet: The molecular weight of the purified CAM-W was measured using electrospray ionization mass spectrometry (Agilent, USA).

    Techniques: Chick Chorioallantoic Membrane Assay, Produced, Recombinant, Western Blot, SDS Page, Marker, High Performance Liquid Chromatography, Purification, Mass Spectrometry