liquid chromatography electrospray ionization tandem mass spectrometry  (SCIEX)

 
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    Structured Review

    SCIEX liquid chromatography electrospray ionization tandem mass spectrometry
    Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry, supplied by SCIEX, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Chromatography:

    Article Title: Optically-controlled bacterial metabolite for cancer therapy
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS)/MS analysis was conducted with an AB SCIEX nanoLC-MS/MS (Triple TOF 5600 plus) system. ..

    Article Title: Direct profiling of the phospholipid composition of adult Caenorhabditis elegans using whole-body imaging mass spectrometry
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) Phospholipids of the harvested wild-type and fat-1 mutants were extracted with Folch method [ ], and they were analyzed using LC-ESI-MS/MS with a 4000Q-TRAP triple quadrupole linear ion trap mass spectrometer (AB SCIEX, Framingham, MA, USA) equipped with an ACQUITY ultra-performance liquid chromatography system (Waters, Milford, MA, USA). .. An ACQUITY UPLC BEH C18 column (2.1 × 50 mm, i.d., 1.7 mm particles; Waters) was connected to a guard column (2.1 × 5 mm; Waters), and the temperature of column oven was maintained at 40 °C [ ].

    Article Title: Comparative Proteomic Analysis of Cultured Suspension Cells of the Halophyte Halogeton glomeratus by iTRAQ Provides Insights into Response Mechanisms to Salt Stress
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysis of fractionated samples was performed using a TripleTOF 5600 System (AB SCIEX, Concord, ON, Canada), as described previously, at Beijing Genomics Institute (BGI, Shenzhen, China; Yang et al., ). ..

    Mass Spectrometry:

    Article Title: Optically-controlled bacterial metabolite for cancer therapy
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS)/MS analysis was conducted with an AB SCIEX nanoLC-MS/MS (Triple TOF 5600 plus) system. ..

    Article Title: Enhancement of Non-photochemical Quenching as an Adaptive Strategy under Phosphorus Deprivation in the Dinoflagellate Karlodinium veneficum
    Article Snippet: .. Liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) analysis was then performed based on a TripleTOF 5600 System (AB SCIEX, Concord, ON, USA), followed by protein identification through Mascot search engine (Matrix Science, London, UK; version 2.3.02) against the above-mentioned DinoSL-based K. veneficum cDNA database. ..

    Article Title: Direct profiling of the phospholipid composition of adult Caenorhabditis elegans using whole-body imaging mass spectrometry
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) Phospholipids of the harvested wild-type and fat-1 mutants were extracted with Folch method [ ], and they were analyzed using LC-ESI-MS/MS with a 4000Q-TRAP triple quadrupole linear ion trap mass spectrometer (AB SCIEX, Framingham, MA, USA) equipped with an ACQUITY ultra-performance liquid chromatography system (Waters, Milford, MA, USA). .. An ACQUITY UPLC BEH C18 column (2.1 × 50 mm, i.d., 1.7 mm particles; Waters) was connected to a guard column (2.1 × 5 mm; Waters), and the temperature of column oven was maintained at 40 °C [ ].

    Article Title: Comparative Proteomic Analysis of Cultured Suspension Cells of the Halophyte Halogeton glomeratus by iTRAQ Provides Insights into Response Mechanisms to Salt Stress
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysis of fractionated samples was performed using a TripleTOF 5600 System (AB SCIEX, Concord, ON, Canada), as described previously, at Beijing Genomics Institute (BGI, Shenzhen, China; Yang et al., ). ..

    Liquid Chromatography:

    Article Title: Enhancement of Non-photochemical Quenching as an Adaptive Strategy under Phosphorus Deprivation in the Dinoflagellate Karlodinium veneficum
    Article Snippet: .. Liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) analysis was then performed based on a TripleTOF 5600 System (AB SCIEX, Concord, ON, USA), followed by protein identification through Mascot search engine (Matrix Science, London, UK; version 2.3.02) against the above-mentioned DinoSL-based K. veneficum cDNA database. ..

    Article Title: Direct profiling of the phospholipid composition of adult Caenorhabditis elegans using whole-body imaging mass spectrometry
    Article Snippet: .. Liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) Phospholipids of the harvested wild-type and fat-1 mutants were extracted with Folch method [ ], and they were analyzed using LC-ESI-MS/MS with a 4000Q-TRAP triple quadrupole linear ion trap mass spectrometer (AB SCIEX, Framingham, MA, USA) equipped with an ACQUITY ultra-performance liquid chromatography system (Waters, Milford, MA, USA). .. An ACQUITY UPLC BEH C18 column (2.1 × 50 mm, i.d., 1.7 mm particles; Waters) was connected to a guard column (2.1 × 5 mm; Waters), and the temperature of column oven was maintained at 40 °C [ ].

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    SCIEX lc esi ms ms approach
    IL-13 driven lesion development in mouse skin profoundly affects stratum corneum lipids. Changes in relative level of short- and long-chain molecular species in NS <t>ceramides</t> with C18 sphingosine ( A ), sphingomyelins ( B ), and lysophosphatidylcholines ( C ) in stratum corneum from nonlesional and lesional skin of IL-13 Tg mice and their littermate controls. IL-13 Tg mice spontaneously develop skin lesions. Tape strips were collected from both lesional and nonlesional areas of mouse skin. Each lipid molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry <t>(LC-ESI-MS/MS)</t> and normalized by sample total protein content, and data were expressed as relative percentage within each lipid subclass. Data are presented as box-and-whisker plot, with whiskers showing minimum and maximum values. * P
    Lc Esi Ms Ms Approach, supplied by SCIEX, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SCIEX protein esi
    Whole protein <t>ESI-MS</t> and LC-MS/MS characterization of <t>HMGB1</t> isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.
    Protein Esi, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SCIEX selective reaction monitoring mode hplc electrospray ionization esi tandem mass spectrometry
    Nuclear localization of lipin1 is promoted by pharmacological inhibition of phospholipase D. (A) HEK 293 cells expressing wild-type lipin1β and the 4A and 9A polybasic motif mutants were treated with 1.5 μM of the dual PLD1/PLD2 inhibitor FIPI or 50 μM of the PLD2 selective inhibitor CAY10593 for 4h. Subcellular localization of lipin1β (green) was visualized by indirect immunofluorescence and compared with the nuclear marker DAPI (blue). (B) Total PA levels in cells incubated with vehicle or the indicated PLD inhibitors at the concentrations used for the experiment shown in panel A and total PA levels (the sum of 16 abundant PA species) quantitated by <t>HPLC</t> <t>ESI</t> MS/MS. (C) Percent of total number of transfected cells, which lipin1β was localized in cytoplasm, nucleus, or both cytoplasm and nucleus (mean ± SD of at least 100 cells counted in 10 distinct fields).
    Selective Reaction Monitoring Mode Hplc Electrospray Ionization Esi Tandem Mass Spectrometry, supplied by SCIEX, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    SCIEX lc nano esi ms analysis
    Extracted ion chromatograms of a cross-linked peptide obtained from DSG-modified (left) and DSS-modified (right) HSA samples analysed by <t>HPLC/nano-ESI/MS/MS</t>
    Lc Nano Esi Ms Analysis, supplied by SCIEX, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    IL-13 driven lesion development in mouse skin profoundly affects stratum corneum lipids. Changes in relative level of short- and long-chain molecular species in NS ceramides with C18 sphingosine ( A ), sphingomyelins ( B ), and lysophosphatidylcholines ( C ) in stratum corneum from nonlesional and lesional skin of IL-13 Tg mice and their littermate controls. IL-13 Tg mice spontaneously develop skin lesions. Tape strips were collected from both lesional and nonlesional areas of mouse skin. Each lipid molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total protein content, and data were expressed as relative percentage within each lipid subclass. Data are presented as box-and-whisker plot, with whiskers showing minimum and maximum values. * P

    Journal: JCI Insight

    Article Title: Lipid abnormalities in atopic skin are driven by type 2 cytokines

    doi: 10.1172/jci.insight.98006

    Figure Lengend Snippet: IL-13 driven lesion development in mouse skin profoundly affects stratum corneum lipids. Changes in relative level of short- and long-chain molecular species in NS ceramides with C18 sphingosine ( A ), sphingomyelins ( B ), and lysophosphatidylcholines ( C ) in stratum corneum from nonlesional and lesional skin of IL-13 Tg mice and their littermate controls. IL-13 Tg mice spontaneously develop skin lesions. Tape strips were collected from both lesional and nonlesional areas of mouse skin. Each lipid molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total protein content, and data were expressed as relative percentage within each lipid subclass. Data are presented as box-and-whisker plot, with whiskers showing minimum and maximum values. * P

    Article Snippet: Ceramides, LPC, and SM were identified and quantified using the targeted LC-ESI-MS/MS approach on a Sciex 6500QTRAP mass spectrometer coupled with a Shimadzu Nexera X2 UHPLC system.

    Techniques: Mouse Assay, Liquid Chromatography, Mass Spectrometry, Whisker Assay

    The effect of differentiation and type 2 cytokines on keratinocyte lipids. ( A ) The effect of Ca 2+ -induced differentiation in vitro on relative proportion of selected ceramides in keratinocytes. Each ceramide molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total lipid phosphorus content, and data were expressed as relative percentage within each lipid subclass. Each individual data point was expressed relative to an average of nondifferentiated control. Note the decrease in relative content of short-chain ceramides and the increase in long-chain ceramides. STAT6 controls the effect of IL-4/IL-13 on NS ceramides with C18 sphingosine ( B ) and sphingomyelins ( C ) in differentiated keratinocytes. No differences in lysophosphatidylcholines (LPC) are observed in the keratinocyte model ( D ). Keratinocytes were differentiated in the absence or presence of IL-4/IL-13. Keratinocytes were treated with STAT6 siRNA during a 5-day differentiation period. Lipids were quantified by LC-ESI-MS/MS and normalized by total lipid phosphorus content ( n = 3). One from 2 typical experiments is shown; each treatment condition done in triplicates. Two-tailed Student’s t test was used for statistical analysis.

    Journal: JCI Insight

    Article Title: Lipid abnormalities in atopic skin are driven by type 2 cytokines

    doi: 10.1172/jci.insight.98006

    Figure Lengend Snippet: The effect of differentiation and type 2 cytokines on keratinocyte lipids. ( A ) The effect of Ca 2+ -induced differentiation in vitro on relative proportion of selected ceramides in keratinocytes. Each ceramide molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total lipid phosphorus content, and data were expressed as relative percentage within each lipid subclass. Each individual data point was expressed relative to an average of nondifferentiated control. Note the decrease in relative content of short-chain ceramides and the increase in long-chain ceramides. STAT6 controls the effect of IL-4/IL-13 on NS ceramides with C18 sphingosine ( B ) and sphingomyelins ( C ) in differentiated keratinocytes. No differences in lysophosphatidylcholines (LPC) are observed in the keratinocyte model ( D ). Keratinocytes were differentiated in the absence or presence of IL-4/IL-13. Keratinocytes were treated with STAT6 siRNA during a 5-day differentiation period. Lipids were quantified by LC-ESI-MS/MS and normalized by total lipid phosphorus content ( n = 3). One from 2 typical experiments is shown; each treatment condition done in triplicates. Two-tailed Student’s t test was used for statistical analysis.

    Article Snippet: Ceramides, LPC, and SM were identified and quantified using the targeted LC-ESI-MS/MS approach on a Sciex 6500QTRAP mass spectrometer coupled with a Shimadzu Nexera X2 UHPLC system.

    Techniques: In Vitro, Liquid Chromatography, Mass Spectrometry, Two Tailed Test

    The effect of skin atopy on stratum corneum lipids. Changes in relative level of short- and long-chain molecular species in ceramides ( A ), sphingomyelins ( B ) and lysophosphatidylcholines ( C ) in stratum corneum of atopic dermatitis (AD) patients as compared with skin of normal control subjects. Each lipid molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total protein content, and data were expressed as relative percentage within each lipid subclass. Data are presented as box-and-whisker plot, with whiskers showing minimum and maximum values. *, + P

    Journal: JCI Insight

    Article Title: Lipid abnormalities in atopic skin are driven by type 2 cytokines

    doi: 10.1172/jci.insight.98006

    Figure Lengend Snippet: The effect of skin atopy on stratum corneum lipids. Changes in relative level of short- and long-chain molecular species in ceramides ( A ), sphingomyelins ( B ) and lysophosphatidylcholines ( C ) in stratum corneum of atopic dermatitis (AD) patients as compared with skin of normal control subjects. Each lipid molecular species was quantified by targeted liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) and normalized by sample total protein content, and data were expressed as relative percentage within each lipid subclass. Data are presented as box-and-whisker plot, with whiskers showing minimum and maximum values. *, + P

    Article Snippet: Ceramides, LPC, and SM were identified and quantified using the targeted LC-ESI-MS/MS approach on a Sciex 6500QTRAP mass spectrometer coupled with a Shimadzu Nexera X2 UHPLC system.

    Techniques: Liquid Chromatography, Mass Spectrometry, Whisker Assay

    Whole protein ESI-MS and LC-MS/MS characterization of HMGB1 isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.

    Journal: The Journal of Biological Chemistry

    Article Title: High Mobility Group Box-1 (HMGB1) Participates in the Pathogenesis of Alcoholic Liver Disease (ALD) *

    doi: 10.1074/jbc.M114.552141

    Figure Lengend Snippet: Whole protein ESI-MS and LC-MS/MS characterization of HMGB1 isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.

    Article Snippet: Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 was performed as described previously by whole protein ESI or tandem mass spectrometry (MS/MS) ( ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc., Framingham, MA).

    Techniques: Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Isolation, Sequencing, Labeling

    Identification of HMGB1 PTMs in serum and liver from control and ethanol-fed mice. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from either serum ( A ) or liver ( B ) from control mice are shown. Peptide MS of HMGB1 derived from control mouse serum or liver was performed following enzymatic digestion with either Glu-C to confirm acetyl status ( C ) or trypsin to confirm redox status ( D ). Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from either serum ( E ) or liver ( F ) from ethanol-fed mice are shown. Peptide MS of HMGB1 derived from serum or liver from ethanol-fed mice was performed following enzymatic digestion with endopeptidase Glu-C to confirm the lack of acetyl modifications on the 24,587 and 24,585-Da isoforms ( G ) and the presence of acetyl modifications on the 25,467-, 25,469-, and 25,549-Da isoforms ( H ). Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Acetyl modifications were confirmed on lysine residues (shown as K(Ac) ) after LC-MS/MS analysis for peptides spanning NLS1 (amino acids 27–39) ( I ) and NLS2 (amino acids 180–188 (179–187 minus methionine)) ( J ) in HMGB1 derived from mice fed ethanol. Phosphorylation modifications were confirmed on serine 35 (shown as pS 35 ) after LC-MS/MS analysis of NLS1 ( K ) in HMGB1 derived from mice fed ethanol. The one-letter amino acid code is given for each peptide sequence, and b and y ions are highlighted with molecular weights where appropriate. Data are representative of at least six individual mice per group.

    Journal: The Journal of Biological Chemistry

    Article Title: High Mobility Group Box-1 (HMGB1) Participates in the Pathogenesis of Alcoholic Liver Disease (ALD) *

    doi: 10.1074/jbc.M114.552141

    Figure Lengend Snippet: Identification of HMGB1 PTMs in serum and liver from control and ethanol-fed mice. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from either serum ( A ) or liver ( B ) from control mice are shown. Peptide MS of HMGB1 derived from control mouse serum or liver was performed following enzymatic digestion with either Glu-C to confirm acetyl status ( C ) or trypsin to confirm redox status ( D ). Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from either serum ( E ) or liver ( F ) from ethanol-fed mice are shown. Peptide MS of HMGB1 derived from serum or liver from ethanol-fed mice was performed following enzymatic digestion with endopeptidase Glu-C to confirm the lack of acetyl modifications on the 24,587 and 24,585-Da isoforms ( G ) and the presence of acetyl modifications on the 25,467-, 25,469-, and 25,549-Da isoforms ( H ). Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Acetyl modifications were confirmed on lysine residues (shown as K(Ac) ) after LC-MS/MS analysis for peptides spanning NLS1 (amino acids 27–39) ( I ) and NLS2 (amino acids 180–188 (179–187 minus methionine)) ( J ) in HMGB1 derived from mice fed ethanol. Phosphorylation modifications were confirmed on serine 35 (shown as pS 35 ) after LC-MS/MS analysis of NLS1 ( K ) in HMGB1 derived from mice fed ethanol. The one-letter amino acid code is given for each peptide sequence, and b and y ions are highlighted with molecular weights where appropriate. Data are representative of at least six individual mice per group.

    Article Snippet: Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 was performed as described previously by whole protein ESI or tandem mass spectrometry (MS/MS) ( ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc., Framingham, MA).

    Techniques: Mouse Assay, Mass Spectrometry, Isolation, Derivative Assay, Liquid Chromatography with Mass Spectroscopy, Sequencing

    Nuclear localization of lipin1 is promoted by pharmacological inhibition of phospholipase D. (A) HEK 293 cells expressing wild-type lipin1β and the 4A and 9A polybasic motif mutants were treated with 1.5 μM of the dual PLD1/PLD2 inhibitor FIPI or 50 μM of the PLD2 selective inhibitor CAY10593 for 4h. Subcellular localization of lipin1β (green) was visualized by indirect immunofluorescence and compared with the nuclear marker DAPI (blue). (B) Total PA levels in cells incubated with vehicle or the indicated PLD inhibitors at the concentrations used for the experiment shown in panel A and total PA levels (the sum of 16 abundant PA species) quantitated by HPLC ESI MS/MS. (C) Percent of total number of transfected cells, which lipin1β was localized in cytoplasm, nucleus, or both cytoplasm and nucleus (mean ± SD of at least 100 cells counted in 10 distinct fields).

    Journal: Molecular Biology of the Cell

    Article Title: A Phosphatidic Acid Binding/Nuclear Localization Motif Determines Lipin1 Function in Lipid Metabolism and Adipogenesis

    doi: 10.1091/mbc.E10-01-0073

    Figure Lengend Snippet: Nuclear localization of lipin1 is promoted by pharmacological inhibition of phospholipase D. (A) HEK 293 cells expressing wild-type lipin1β and the 4A and 9A polybasic motif mutants were treated with 1.5 μM of the dual PLD1/PLD2 inhibitor FIPI or 50 μM of the PLD2 selective inhibitor CAY10593 for 4h. Subcellular localization of lipin1β (green) was visualized by indirect immunofluorescence and compared with the nuclear marker DAPI (blue). (B) Total PA levels in cells incubated with vehicle or the indicated PLD inhibitors at the concentrations used for the experiment shown in panel A and total PA levels (the sum of 16 abundant PA species) quantitated by HPLC ESI MS/MS. (C) Percent of total number of transfected cells, which lipin1β was localized in cytoplasm, nucleus, or both cytoplasm and nucleus (mean ± SD of at least 100 cells counted in 10 distinct fields).

    Article Snippet: Molecular species of TG, DG, PA, and phosphatidylcholine (PC) were quantitated by selective reaction monitoring mode HPLC- electrospray ionization (ESI) tandem mass spectrometry using an AB Sciex (Foster City, CA) 4000 Q-Trap hybrid linear ion trap triple-quadrupole mass spectrometer equipped with a Turbo V electrospray ion source.

    Techniques: Inhibition, Expressing, Immunofluorescence, Marker, Incubation, High Performance Liquid Chromatography, Mass Spectrometry, Transfection

    The polybasic motif plays an important role in complementation of the adipogenesis defect of fld/fld mouse embryo fibroblasts by lipin1β. (A) Oil red-O staining (red) of differentiated wt and fld/fld mouse embryo fibroblasts expressing wild-type lipin1β, the indicated lipin1β mutants, or a GFP control using lentivirus vectors at day 6 postinduction of differentiation. (B) Expression of lipin 1 variants was quantitated by Western blotting. (C) Adipogenic differentiation was quantitated by counting the number of oil red-O–stained colonies per field. (D) Adipogenic differentiation was quantitated by measuring total TG levels (the sum of 36 abundant TG species) using HPLC ESI MS/MS. Data shown are means ± SD of three or more independent determinations. Statistically significant differences between cells expressing wt lipin 1 and the indicated lipin 1 mutants are indicated by asterisks. Note that TG accumulation or the number of differentiated colonies was not significantly different (N.S.) between cells expressing GFP or Lipin1 D712E.

    Journal: Molecular Biology of the Cell

    Article Title: A Phosphatidic Acid Binding/Nuclear Localization Motif Determines Lipin1 Function in Lipid Metabolism and Adipogenesis

    doi: 10.1091/mbc.E10-01-0073

    Figure Lengend Snippet: The polybasic motif plays an important role in complementation of the adipogenesis defect of fld/fld mouse embryo fibroblasts by lipin1β. (A) Oil red-O staining (red) of differentiated wt and fld/fld mouse embryo fibroblasts expressing wild-type lipin1β, the indicated lipin1β mutants, or a GFP control using lentivirus vectors at day 6 postinduction of differentiation. (B) Expression of lipin 1 variants was quantitated by Western blotting. (C) Adipogenic differentiation was quantitated by counting the number of oil red-O–stained colonies per field. (D) Adipogenic differentiation was quantitated by measuring total TG levels (the sum of 36 abundant TG species) using HPLC ESI MS/MS. Data shown are means ± SD of three or more independent determinations. Statistically significant differences between cells expressing wt lipin 1 and the indicated lipin 1 mutants are indicated by asterisks. Note that TG accumulation or the number of differentiated colonies was not significantly different (N.S.) between cells expressing GFP or Lipin1 D712E.

    Article Snippet: Molecular species of TG, DG, PA, and phosphatidylcholine (PC) were quantitated by selective reaction monitoring mode HPLC- electrospray ionization (ESI) tandem mass spectrometry using an AB Sciex (Foster City, CA) 4000 Q-Trap hybrid linear ion trap triple-quadrupole mass spectrometer equipped with a Turbo V electrospray ion source.

    Techniques: Staining, Expressing, Western Blot, High Performance Liquid Chromatography, Mass Spectrometry

    Effects of overexpression of lipin1β wt and mutants on diacylglycerol (DG), phosphatidylcholine (PC), and phosphatidic acid (PA) levels. (A) HA-tagged wt lipin1β and the indicated mutants were overexpressed in HepG2 cells and detected by Western blotting. (B) HepG2 cells expressing wt lipin1β and the indicated mutants were radiolabeled with [ 3 H]palmitic acid for 24 h. DG levels were determined after separation by TLC, and quantitation by scintillation counting. (C–E) Levels of 16 abundant molecular species of PA, DG, and PC were determined in HepG2 cells overexpressing lipin1β wt, and mutants incubated with 1 μM palmitic acid were measured by HPLC ESI MS/MS. Data are means ± SD of at least three independent determinations.

    Journal: Molecular Biology of the Cell

    Article Title: A Phosphatidic Acid Binding/Nuclear Localization Motif Determines Lipin1 Function in Lipid Metabolism and Adipogenesis

    doi: 10.1091/mbc.E10-01-0073

    Figure Lengend Snippet: Effects of overexpression of lipin1β wt and mutants on diacylglycerol (DG), phosphatidylcholine (PC), and phosphatidic acid (PA) levels. (A) HA-tagged wt lipin1β and the indicated mutants were overexpressed in HepG2 cells and detected by Western blotting. (B) HepG2 cells expressing wt lipin1β and the indicated mutants were radiolabeled with [ 3 H]palmitic acid for 24 h. DG levels were determined after separation by TLC, and quantitation by scintillation counting. (C–E) Levels of 16 abundant molecular species of PA, DG, and PC were determined in HepG2 cells overexpressing lipin1β wt, and mutants incubated with 1 μM palmitic acid were measured by HPLC ESI MS/MS. Data are means ± SD of at least three independent determinations.

    Article Snippet: Molecular species of TG, DG, PA, and phosphatidylcholine (PC) were quantitated by selective reaction monitoring mode HPLC- electrospray ionization (ESI) tandem mass spectrometry using an AB Sciex (Foster City, CA) 4000 Q-Trap hybrid linear ion trap triple-quadrupole mass spectrometer equipped with a Turbo V electrospray ion source.

    Techniques: Over Expression, Western Blot, Expressing, Thin Layer Chromatography, Quantitation Assay, Incubation, High Performance Liquid Chromatography, Mass Spectrometry

    Extracted ion chromatograms of a cross-linked peptide obtained from DSG-modified (left) and DSS-modified (right) HSA samples analysed by HPLC/nano-ESI/MS/MS

    Journal:

    Article Title: Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry

    doi: 10.1042/BJ20041624

    Figure Lengend Snippet: Extracted ion chromatograms of a cross-linked peptide obtained from DSG-modified (left) and DSS-modified (right) HSA samples analysed by HPLC/nano-ESI/MS/MS

    Article Snippet: LC/nano-ESI MS analysis was performed on a QSTAR pulsar Qq-TOF mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, Canada), or an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow LC system.

    Techniques: Modification, High Performance Liquid Chromatography, Mass Spectrometry

    Nano-ESI-QqTOF reconstructed mass spectra of tryptic digests from unmodified (a), and BS 3 -modified control (b), OA-bound (c), AA-bound (d) and DHA-bound (e) HSA

    Journal:

    Article Title: Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry

    doi: 10.1042/BJ20041624

    Figure Lengend Snippet: Nano-ESI-QqTOF reconstructed mass spectra of tryptic digests from unmodified (a), and BS 3 -modified control (b), OA-bound (c), AA-bound (d) and DHA-bound (e) HSA

    Article Snippet: LC/nano-ESI MS analysis was performed on a QSTAR pulsar Qq-TOF mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, Canada), or an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow LC system.

    Techniques: Modification

    Nano-ESI-QqTOF reconstructed mass spectra of BS 3 -modified HSA samples

    Journal:

    Article Title: Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry

    doi: 10.1042/BJ20041624

    Figure Lengend Snippet: Nano-ESI-QqTOF reconstructed mass spectra of BS 3 -modified HSA samples

    Article Snippet: LC/nano-ESI MS analysis was performed on a QSTAR pulsar Qq-TOF mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, Canada), or an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow LC system.

    Techniques: Modification

    Nano-ESI-QqTOF-MS/MS analysis of the cross-linked peptide with mass of 3552.8 Da depicted in

    Journal:

    Article Title: Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry

    doi: 10.1042/BJ20041624

    Figure Lengend Snippet: Nano-ESI-QqTOF-MS/MS analysis of the cross-linked peptide with mass of 3552.8 Da depicted in

    Article Snippet: LC/nano-ESI MS analysis was performed on a QSTAR pulsar Qq-TOF mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, Canada), or an Agilent ion trap mass spectrometer (XCT) equipped with an Agilent 1100 nanoflow LC system.

    Techniques: Mass Spectrometry