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  • 97
    Agilent technologies lc esi ms
    Lc Esi Ms, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 97/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc esi ms/product/Agilent technologies
    Average 97 stars, based on 175 article reviews
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    lc esi ms - by Bioz Stars, 2020-04
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    96
    Bruker Corporation lc esi ms
    Milk protein profiling by <t>LC-ESI-MS</t> of a Bactrian camel milk from the Shymkent region. Eleven major milk protein fractions were identified from RP-HPLC profile ( 3.A ) in the following order: glycosylated κ-CN A and B (I), non-glycosylated κ-CN A and B (II), WAP (III), shorter (∆ex16 and 13′) + short (∆ex16) isoforms of α s1 -CN A and C (IV and V), α-LAC + α s1 -CN A and C + (VI), α s2 -CN* (VII), PGRP + α s2 -CN* (VIII), LPO/CSA (IX), β-CN A and B (X) and γ 2 -CN A and B (XI). Multicharged-ions spectrum from compounds contained in fraction III ( 3.B ). After deconvolution ( 3.C ) the spectrum shows the presence of cognate camel WAP A-0P (12,546 Da) and <t>1P</t> (12,644 Da) indicated in black, and molecular masses corresponding to a new WAP variant (named B) without (12,596 Da) and with (12,676 Da) one phosphate group, indicated in red. *Splicing variants of αs2-CN with different phosphorylation levels (Ryskaliyeva et al., submitted)
    Lc Esi Ms, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 96/100, based on 160 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc esi ms/product/Bruker Corporation
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    92
    Shimadzu Corporation lc esi ms
    Milk protein profiling by <t>LC-ESI-MS</t> of a Bactrian camel milk from the Shymkent region. Eleven major milk protein fractions were identified from RP-HPLC profile ( 3.A ) in the following order: glycosylated κ-CN A and B (I), non-glycosylated κ-CN A and B (II), WAP (III), shorter (∆ex16 and 13′) + short (∆ex16) isoforms of α s1 -CN A and C (IV and V), α-LAC + α s1 -CN A and C + (VI), α s2 -CN* (VII), PGRP + α s2 -CN* (VIII), LPO/CSA (IX), β-CN A and B (X) and γ 2 -CN A and B (XI). Multicharged-ions spectrum from compounds contained in fraction III ( 3.B ). After deconvolution ( 3.C ) the spectrum shows the presence of cognate camel WAP A-0P (12,546 Da) and <t>1P</t> (12,644 Da) indicated in black, and molecular masses corresponding to a new WAP variant (named B) without (12,596 Da) and with (12,676 Da) one phosphate group, indicated in red. *Splicing variants of αs2-CN with different phosphorylation levels (Ryskaliyeva et al., submitted)
    Lc Esi Ms, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc esi ms/product/Shimadzu Corporation
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    lc esi ms - by Bioz Stars, 2020-04
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    94
    Thermo Fisher lc esi ms
    <t>LC-ESI-MS</t> analysis of fungal <t>VBL.</t> The mass spectrum of the fungal extract showed a (M+H + ) peak at a molecular mass of 811.51, which was identical to that observed in the mass spectrum of the VBL standard.
    Lc Esi Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 339 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Waters Corporation lc esi ms
    Stereoisomers of <t>12-HETE.</t> ( a ) Chromatogram of 12(R)-HETE and 12(S)-HETE standards separated on a chiral column and detected by UV detection. ( b ) Chromatogram of 15-, 11-, 12- and 5-HETE separated on a reverse phase C 18 column and detected by <t>ESI-MS.</t> Note : The LC-ESI-MS technique used in this study cannot differentiate the 12-HETE stereoisomers. Chromatograms of ( c ) 12(S)-HETE and ( d ) 12(R)-HETE in PC-3 cells treated with exogenous 2-AG (1 μM). 12-HETE mixtures were first separated on an HPLC chiral column as in ( a ) and subsequently analyzed by LC-ESI-MS.
    Lc Esi Ms, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 91/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    honeywell international lc esi ms
    Structures of the identified compounds by <t>LC-ESI-MS</t> analysis in the avocado seeds extracts and the tested <t>HSCCC</t> fractions.
    Lc Esi Ms, supplied by honeywell international, used in various techniques. Bioz Stars score: 86/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    SCIEX lc esi ms
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms, supplied by SCIEX, used in various techniques. Bioz Stars score: 96/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    lc esi ms - by Bioz Stars, 2020-04
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    86
    NextGen Sciences lc esi ms ms
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Ms, supplied by NextGen Sciences, used in various techniques. Bioz Stars score: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    lc esi ms ms - by Bioz Stars, 2020-04
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    92
    Millipore lc esi ms analyses
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Analyses, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bruker Corporation micro lc esi ms
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Micro Lc Esi Ms, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/micro lc esi ms/product/Bruker Corporation
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    95
    Agilent technologies lc esi ms system
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 95/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher lc esi ms system
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Agilent technologies lc esi ms qtof
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Qtof, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    SCIEX lc esi ms ms machine
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Ms Machine, supplied by SCIEX, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    SCIEX lc esi ms ms system
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Ms System, supplied by SCIEX, used in various techniques. Bioz Stars score: 93/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies lc esi ms ms apparatus
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
    Lc Esi Ms Ms Apparatus, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Agilent technologies lc esi ms ms analysis
    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by <t>MRM</t> analysis using <t>LC-ESI</t> MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.
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    KLA induces time-dependent increases in <t>ceramide</t> and dihydroceramide. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC <t>ESI-MS/MS.</t> A , amounts of the major chain length subspecies of DHCer. Data represent the means ( n = 9). B , amounts of total DHCer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001. C , amounts of the major chain length subspecies of Cer. Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (9 pmol/μg DNA); C18 (0.4 pmol/μg DNA); C20 (0.2 pmol/μg DNA); C22 (1.9 pmol/μg DNA); C24:1 (5.4 pmol/μg DNA); C24 (5.5 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); and C26 (0.1 pmol/μg DNA). Data represent the means ± S.E. ( n = 9). D , amounts of total Cer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001.
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    KLA induces time-dependent increases in <t>ceramide</t> and dihydroceramide. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC <t>ESI-MS/MS.</t> A , amounts of the major chain length subspecies of DHCer. Data represent the means ( n = 9). B , amounts of total DHCer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001. C , amounts of the major chain length subspecies of Cer. Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (9 pmol/μg DNA); C18 (0.4 pmol/μg DNA); C20 (0.2 pmol/μg DNA); C22 (1.9 pmol/μg DNA); C24:1 (5.4 pmol/μg DNA); C24 (5.5 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); and C26 (0.1 pmol/μg DNA). Data represent the means ± S.E. ( n = 9). D , amounts of total Cer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001.
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    Image Search Results


    Milk protein profiling by LC-ESI-MS of a Bactrian camel milk from the Shymkent region. Eleven major milk protein fractions were identified from RP-HPLC profile ( 3.A ) in the following order: glycosylated κ-CN A and B (I), non-glycosylated κ-CN A and B (II), WAP (III), shorter (∆ex16 and 13′) + short (∆ex16) isoforms of α s1 -CN A and C (IV and V), α-LAC + α s1 -CN A and C + (VI), α s2 -CN* (VII), PGRP + α s2 -CN* (VIII), LPO/CSA (IX), β-CN A and B (X) and γ 2 -CN A and B (XI). Multicharged-ions spectrum from compounds contained in fraction III ( 3.B ). After deconvolution ( 3.C ) the spectrum shows the presence of cognate camel WAP A-0P (12,546 Da) and 1P (12,644 Da) indicated in black, and molecular masses corresponding to a new WAP variant (named B) without (12,596 Da) and with (12,676 Da) one phosphate group, indicated in red. *Splicing variants of αs2-CN with different phosphorylation levels (Ryskaliyeva et al., submitted)

    Journal: BMC Genetics

    Article Title: The main WAP isoform usually found in camel milk arises from the usage of an improbable intron cryptic splice site in the precursor to mRNA in which a GC-AG intron occurs

    doi: 10.1186/s12863-018-0704-x

    Figure Lengend Snippet: Milk protein profiling by LC-ESI-MS of a Bactrian camel milk from the Shymkent region. Eleven major milk protein fractions were identified from RP-HPLC profile ( 3.A ) in the following order: glycosylated κ-CN A and B (I), non-glycosylated κ-CN A and B (II), WAP (III), shorter (∆ex16 and 13′) + short (∆ex16) isoforms of α s1 -CN A and C (IV and V), α-LAC + α s1 -CN A and C + (VI), α s2 -CN* (VII), PGRP + α s2 -CN* (VIII), LPO/CSA (IX), β-CN A and B (X) and γ 2 -CN A and B (XI). Multicharged-ions spectrum from compounds contained in fraction III ( 3.B ). After deconvolution ( 3.C ) the spectrum shows the presence of cognate camel WAP A-0P (12,546 Da) and 1P (12,644 Da) indicated in black, and molecular masses corresponding to a new WAP variant (named B) without (12,596 Da) and with (12,676 Da) one phosphate group, indicated in red. *Splicing variants of αs2-CN with different phosphorylation levels (Ryskaliyeva et al., submitted)

    Article Snippet: This single base substitution corresponds to a V/M amino acid substitution in position 12 of the mature protein, in agreement with the mass difference of 32 Da (V12 M, 99 Da = > 131 Da), found between WAP variants detected in LC-ESI-MS. We propose to name the camel WAP (V12) described by Beg et al. [ ] as variant A and the newly identified variant (M12) as variant B. Consequently, molecular masses observed by LC-ESI-MS (12,596 Da, 12,676 Da) precisely correspond to unphosphorylated and phosphorylated (1P) isoforms of WAP variant B, respectively.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography, Variant Assay

    LC-ESI-MS analysis of fungal VBL. The mass spectrum of the fungal extract showed a (M+H + ) peak at a molecular mass of 811.51, which was identical to that observed in the mass spectrum of the VBL standard.

    Journal: PLoS ONE

    Article Title: An Endophytic Fungus, Talaromyces radicus, Isolated from Catharanthus roseus, Produces Vincristine and Vinblastine, Which Induce Apoptotic Cell Death

    doi: 10.1371/journal.pone.0144476

    Figure Lengend Snippet: LC-ESI-MS analysis of fungal VBL. The mass spectrum of the fungal extract showed a (M+H + ) peak at a molecular mass of 811.51, which was identical to that observed in the mass spectrum of the VBL standard.

    Article Snippet: The molecular masses of fungal VCR and VBL were determined by subjecting the crude fungal extracts to LC-ESI-MS (M/S applied Thermo LCQ Deca XP Max ESI-MS analyzer) along with VCR and VBL standards as the reference compounds.

    Techniques: Mass Spectrometry

    LC-ESI-MS analysis. of fungal VCR. The mass spectrum of the fungal extract showed a (M+H + ) peak at a molecular mass of 825.46, which was identical to that observed in the mass spectrum of the VCR standard.

    Journal: PLoS ONE

    Article Title: An Endophytic Fungus, Talaromyces radicus, Isolated from Catharanthus roseus, Produces Vincristine and Vinblastine, Which Induce Apoptotic Cell Death

    doi: 10.1371/journal.pone.0144476

    Figure Lengend Snippet: LC-ESI-MS analysis. of fungal VCR. The mass spectrum of the fungal extract showed a (M+H + ) peak at a molecular mass of 825.46, which was identical to that observed in the mass spectrum of the VCR standard.

    Article Snippet: The molecular masses of fungal VCR and VBL were determined by subjecting the crude fungal extracts to LC-ESI-MS (M/S applied Thermo LCQ Deca XP Max ESI-MS analyzer) along with VCR and VBL standards as the reference compounds.

    Techniques: Mass Spectrometry

    Hsc70 is a novel neuronal interaction partner of NF-κB. A. Porcine brain extracts were immunoprecipitated with anti NF-κB p65 antibody or isotype control on protein G sepharose in presence of cross-linker. The IP were separated in a 1D SDS gel. Each lane (p65 precipitate and control) were cut into 36 slices and prepared for MS by trypsin digestion. All 36 slices were analyzed by MS. Seven samples in range of 95 to 60 and 27 to 24 kDa were additionally analyzed by LC-ESI-MS/MS. The hits identified by MS included the heat shock cognate Hsc70 as a potential interaction partner of NF-κB p65. B. HEK293 co-transfected with p65-flag and Hsc70-myc or IκBε-myc were lysed followed by co-immunoprecipitation in presence of cross-linker using αmyc (IP) antibody with subsequent WB analysis. A clear interaction band (WB: αFlag) was detectable if myc-tagged IκBε and flag-tagged NF-κB p65 were co-transfected. Similarly, co-transfection of p65-flag and Hsc70-myc resulted in a clear interaction band (WB: αFlag), whereas no band was observed in negative controls (no p65-flag, or no IκBε-myc or Hsc70-myc). Lysates were used as input control. C. Neuronal proteins influence the interaction of NF-κB p65 with Hsc70. IP (αmyc) was performed in presence of cross-linker (DSP) and/or brain lysates with subsequent analysis by western blot. Interaction bands (WB: αFlag) were detectable in cross-linked samples for myc-tagged IκBε and flag tagged NF-κB p65 as well as for Hsc70-myc and NF-κB p65-flag. Combination of cross-linker and brain lysates resulted in stronger interaction band (WB: αFlag) for Hsc70-myc and NF-κB p65-flag. Without cross-linker no interaction bands was detectable.

    Journal: PLoS ONE

    Article Title: Hsc70 Is a Novel Interactor of NF-kappaB p65 in Living Hippocampal Neurons

    doi: 10.1371/journal.pone.0065280

    Figure Lengend Snippet: Hsc70 is a novel neuronal interaction partner of NF-κB. A. Porcine brain extracts were immunoprecipitated with anti NF-κB p65 antibody or isotype control on protein G sepharose in presence of cross-linker. The IP were separated in a 1D SDS gel. Each lane (p65 precipitate and control) were cut into 36 slices and prepared for MS by trypsin digestion. All 36 slices were analyzed by MS. Seven samples in range of 95 to 60 and 27 to 24 kDa were additionally analyzed by LC-ESI-MS/MS. The hits identified by MS included the heat shock cognate Hsc70 as a potential interaction partner of NF-κB p65. B. HEK293 co-transfected with p65-flag and Hsc70-myc or IκBε-myc were lysed followed by co-immunoprecipitation in presence of cross-linker using αmyc (IP) antibody with subsequent WB analysis. A clear interaction band (WB: αFlag) was detectable if myc-tagged IκBε and flag-tagged NF-κB p65 were co-transfected. Similarly, co-transfection of p65-flag and Hsc70-myc resulted in a clear interaction band (WB: αFlag), whereas no band was observed in negative controls (no p65-flag, or no IκBε-myc or Hsc70-myc). Lysates were used as input control. C. Neuronal proteins influence the interaction of NF-κB p65 with Hsc70. IP (αmyc) was performed in presence of cross-linker (DSP) and/or brain lysates with subsequent analysis by western blot. Interaction bands (WB: αFlag) were detectable in cross-linked samples for myc-tagged IκBε and flag tagged NF-κB p65 as well as for Hsc70-myc and NF-κB p65-flag. Combination of cross-linker and brain lysates resulted in stronger interaction band (WB: αFlag) for Hsc70-myc and NF-κB p65-flag. Without cross-linker no interaction bands was detectable.

    Article Snippet: MALDI-MS and LC-ESI-MS/MS revealed an interaction of p65 with compounds of the endocytosis network: clathrin and dynamin-1, microtubule subunits or associated proteins like beta 5-tubulin, tubulin alpha 6, beta actin, dihydropyrimidinase-related protein 2, neurofilament and light polypeptide (NEFL) and heat shock proteins HSP90 alpha class A and B (data not shown).

    Techniques: Immunoprecipitation, SDS-Gel, Mass Spectrometry, Transfection, Western Blot, Cotransfection

    Analysis of a hair sample proving exposure to the nerve agent sarin. a – c Detection of hydrolyzed sarin (IMPA) by LC–ESI(−)-MS/MS MRM (procedure I) in a positive control ( b ) and the sample ( c ). For reasons of clarity, only two transitions for monitoring deprotonated IMPA (from m/z 136.9 to 94.6, solid line ) and the IS (nBPA) (from m/z 137.1 to 79.1, dotted line ) are depicted. d – f Detection of DIMP, a by-product of sarin synthesis, by LC–ESI(+)-HR-MS ( m/z 97.005) is illustrated for a blank ( d ), positive control ( e ) and sample ( f ). Blank hair ( a ) and solvent blank ( d ) were free of interferences

    Journal: Forensic Toxicology

    Article Title: Fatal sarin poisoning in Syria 2013: forensic verification within an international laboratory network

    doi: 10.1007/s11419-017-0376-7

    Figure Lengend Snippet: Analysis of a hair sample proving exposure to the nerve agent sarin. a – c Detection of hydrolyzed sarin (IMPA) by LC–ESI(−)-MS/MS MRM (procedure I) in a positive control ( b ) and the sample ( c ). For reasons of clarity, only two transitions for monitoring deprotonated IMPA (from m/z 136.9 to 94.6, solid line ) and the IS (nBPA) (from m/z 137.1 to 79.1, dotted line ) are depicted. d – f Detection of DIMP, a by-product of sarin synthesis, by LC–ESI(+)-HR-MS ( m/z 97.005) is illustrated for a blank ( d ), positive control ( e ) and sample ( f ). Blank hair ( a ) and solvent blank ( d ) were free of interferences

    Article Snippet: Samples were analyzed by LC–ESI(+)-MS/MS in MRM mode as well as by LC–ESI(+)-MS/HR-MS to detect the intact adducted nonapeptide and its aged variant with injecting 10 µL each.

    Techniques: Mass Spectrometry, Positive Control

    Analysis of a blood sample proving incorporation of the nerve agent sarin by diverse biomarkers. a – c Detection of hydrolyzed sarin (IMPA) by LC–ESI(−)-MS/MS MRM (procedure I) in a positive control ( b ) and the sample ( c ). For reasons of clarity, only two transitions for monitoring deprotonated IMPA (from m/z 136.9 to 94.6, solid line ) and the internal standard (IS) n -butylphosphonic acid (nBPA, from m/z 137.1 to 79.1, dotted line ) are depicted. d – f Detection of tyrosine adduct (Y-GB), most presumably derived from albumin. Analysis was performed by micro LC–ESI(+)-MS/MS MRM (procedure IV). Transition from m/z 302.1 to 214.1 is depicted exemplarily for a blank sample ( d ), positive control ( e ) and the sample ( f ). g – i Detection of sarin after fluoride-induced reactivation by GC–EI-MS/MS MRM (procedure II). Transition from m/z 125 to 99 is illustrated for blank ( g ), positive control ( h ) and sample ( i ). j – l Detection of the modified nonapeptide FGESAGAAS derived from the aged adduct of butyrylcholinesterase and sarin. Analysis was carried out by LC–ESI(+)-MS/MS MRM (procedure III). Transition from m/z 874 to 778 is shown for measurement of blank ( j ), positive control ( k ) and sample ( l ). Blank blood was free of interferences for each method ( a , d , g , j )

    Journal: Forensic Toxicology

    Article Title: Fatal sarin poisoning in Syria 2013: forensic verification within an international laboratory network

    doi: 10.1007/s11419-017-0376-7

    Figure Lengend Snippet: Analysis of a blood sample proving incorporation of the nerve agent sarin by diverse biomarkers. a – c Detection of hydrolyzed sarin (IMPA) by LC–ESI(−)-MS/MS MRM (procedure I) in a positive control ( b ) and the sample ( c ). For reasons of clarity, only two transitions for monitoring deprotonated IMPA (from m/z 136.9 to 94.6, solid line ) and the internal standard (IS) n -butylphosphonic acid (nBPA, from m/z 137.1 to 79.1, dotted line ) are depicted. d – f Detection of tyrosine adduct (Y-GB), most presumably derived from albumin. Analysis was performed by micro LC–ESI(+)-MS/MS MRM (procedure IV). Transition from m/z 302.1 to 214.1 is depicted exemplarily for a blank sample ( d ), positive control ( e ) and the sample ( f ). g – i Detection of sarin after fluoride-induced reactivation by GC–EI-MS/MS MRM (procedure II). Transition from m/z 125 to 99 is illustrated for blank ( g ), positive control ( h ) and sample ( i ). j – l Detection of the modified nonapeptide FGESAGAAS derived from the aged adduct of butyrylcholinesterase and sarin. Analysis was carried out by LC–ESI(+)-MS/MS MRM (procedure III). Transition from m/z 874 to 778 is shown for measurement of blank ( j ), positive control ( k ) and sample ( l ). Blank blood was free of interferences for each method ( a , d , g , j )

    Article Snippet: Samples were analyzed by LC–ESI(+)-MS/MS in MRM mode as well as by LC–ESI(+)-MS/HR-MS to detect the intact adducted nonapeptide and its aged variant with injecting 10 µL each.

    Techniques: Mass Spectrometry, Positive Control, Derivative Assay, Modification

    Biological fate of sarin and targets for biomedical verification of poisoning. Sarin undergoes two major biotransformation processes, i.e., hydrolysis and adduct formation. The resulting reaction products are unequivocal biomarkers of exposure, which can be assessed by modern mass spectrometric methods. BChE butyrylcholinesterase, CI chemical ionization, DIMP diisopropylmethylphosphonate, EI electron ionization, ESI electrospray ionization, GC gas chromatography, HR high resolution, IMPA O -isopropyl methylphosphonic acid, LC liquid chromatography, MRM multiple reaction monitoring, MS mass spectrometry, MS/MS tandem mass spectrometry

    Journal: Forensic Toxicology

    Article Title: Fatal sarin poisoning in Syria 2013: forensic verification within an international laboratory network

    doi: 10.1007/s11419-017-0376-7

    Figure Lengend Snippet: Biological fate of sarin and targets for biomedical verification of poisoning. Sarin undergoes two major biotransformation processes, i.e., hydrolysis and adduct formation. The resulting reaction products are unequivocal biomarkers of exposure, which can be assessed by modern mass spectrometric methods. BChE butyrylcholinesterase, CI chemical ionization, DIMP diisopropylmethylphosphonate, EI electron ionization, ESI electrospray ionization, GC gas chromatography, HR high resolution, IMPA O -isopropyl methylphosphonic acid, LC liquid chromatography, MRM multiple reaction monitoring, MS mass spectrometry, MS/MS tandem mass spectrometry

    Article Snippet: Samples were analyzed by LC–ESI(+)-MS/MS in MRM mode as well as by LC–ESI(+)-MS/HR-MS to detect the intact adducted nonapeptide and its aged variant with injecting 10 µL each.

    Techniques: Gas Chromatography, Liquid Chromatography, Mass Spectrometry

    Stereoisomers of 12-HETE. ( a ) Chromatogram of 12(R)-HETE and 12(S)-HETE standards separated on a chiral column and detected by UV detection. ( b ) Chromatogram of 15-, 11-, 12- and 5-HETE separated on a reverse phase C 18 column and detected by ESI-MS. Note : The LC-ESI-MS technique used in this study cannot differentiate the 12-HETE stereoisomers. Chromatograms of ( c ) 12(S)-HETE and ( d ) 12(R)-HETE in PC-3 cells treated with exogenous 2-AG (1 μM). 12-HETE mixtures were first separated on an HPLC chiral column as in ( a ) and subsequently analyzed by LC-ESI-MS.

    Journal: International journal of cancer. Journal international du cancer

    Article Title: Diverse roles of 2-arachidonoylglycerol in invasion of prostate carcinoma cells: Location, hydrolysis and 12-lipoxygenase metabolism

    doi: 10.1002/ijc.22761

    Figure Lengend Snippet: Stereoisomers of 12-HETE. ( a ) Chromatogram of 12(R)-HETE and 12(S)-HETE standards separated on a chiral column and detected by UV detection. ( b ) Chromatogram of 15-, 11-, 12- and 5-HETE separated on a reverse phase C 18 column and detected by ESI-MS. Note : The LC-ESI-MS technique used in this study cannot differentiate the 12-HETE stereoisomers. Chromatograms of ( c ) 12(S)-HETE and ( d ) 12(R)-HETE in PC-3 cells treated with exogenous 2-AG (1 μM). 12-HETE mixtures were first separated on an HPLC chiral column as in ( a ) and subsequently analyzed by LC-ESI-MS.

    Article Snippet: To demonstrate the presence of exogenous 2-AG, AA and 12-HETE that may influence the invasion of prostate carcinoma cells, these lipids in the conditioned media of PC-3 cells and WPMY-1 cells were determined by LC-ESI-MS. shows the LC-MS chromatograms of 12-HETE, 2-AG, and AA standards (upper panel), in conditioned media of PC-3 cells (middle panel), and in conditioned media of WPMY-1 cells (lower panel), respectively.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography

    Structures of the identified compounds by LC-ESI-MS analysis in the avocado seeds extracts and the tested HSCCC fractions.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Persea americana Mill. Seed: Fractionation, Characterization, and Effects on Human Keratinocytes and Fibroblasts

    doi: 10.1155/2013/391247

    Figure Lengend Snippet: Structures of the identified compounds by LC-ESI-MS analysis in the avocado seeds extracts and the tested HSCCC fractions.

    Article Snippet: As detected by LC-ESI-MS the HSCCC fraction M.6 was principally composed of salidroside ( 17 ), hydroxy salidroside ( 13 ), ABA derivatives ( 18 , 21 ), and structurally unknown compounds.

    Techniques: Mass Spectrometry, High Speed Counter-current Chromatography

    LC-ESI-MS (negative mode) of the methanol-water partition M and the recovered HSCCC fractions ( M.2 , M.3 , M.6, and M.7 ). Intensity × 10 5 when not another is written.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Persea americana Mill. Seed: Fractionation, Characterization, and Effects on Human Keratinocytes and Fibroblasts

    doi: 10.1155/2013/391247

    Figure Lengend Snippet: LC-ESI-MS (negative mode) of the methanol-water partition M and the recovered HSCCC fractions ( M.2 , M.3 , M.6, and M.7 ). Intensity × 10 5 when not another is written.

    Article Snippet: As detected by LC-ESI-MS the HSCCC fraction M.6 was principally composed of salidroside ( 17 ), hydroxy salidroside ( 13 ), ABA derivatives ( 18 , 21 ), and structurally unknown compounds.

    Techniques: Mass Spectrometry, High Speed Counter-current Chromatography

    Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by MRM analysis using LC-ESI MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.

    Journal: Scientific Reports

    Article Title: A thraustochytrid-specific lipase/phospholipase with unique positional specificity contributes to microbial competition and fatty acid acquisition from the environment

    doi: 10.1038/s41598-019-52854-7

    Figure Lengend Snippet: Involvement of 145138 in the extracellular lipid degradation. ( A ) Amounts of extracellular TGs. Culture supernatants of WT and Δ145138 were collected by centrifugation, and lipids were extracted to subject to MS analysis. Major molecular species, TG48:0, TG54:6, TG60:12, and TG66:18, in WT (white bars) and Δ145138 (black bars) were measured by MRM analysis using LC-ESI MS/MS. ( B ) Lipase activities in the medium of WT and Δ145138. The culture supernatant was collected by centrifugation from 1-, 3-, 5-, and 7-day cultures of WT and Δ145138. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( C ) mRNA expression levels of 145138. Cells were harvested from 2- and 7-day cultures of WT and Δ145138. A standard curve to determine the copy numbers of 145138 was made from a plasmid containing 145138. ( D ) Western blotting analysis showing the localization of 145138-FLAG. After cultivation for 3 days, the culture supernatant and cells of WT and 145138-FLAG-OE were separated by centrifugation. Cell lysate, culture supernatant, and 5-times concentrated supernatant were subjected to western blotting using an antibody against DYKDDDDK. (E) Lipase activities in the supernatant of WT and 145138-FLAG-OE. Culture supernatants were collected from 1-, 3-, 5-, and 7-day cultures of WT and 145138-FLAG-OE. Lipase activities were measured by using 4MU-palmitic acid as a substrate. ( F ) Western blotting analysis showing the expression level of full length 145138 [145138 (Full)] and N-terminal deleted mutants, 145138 (Δ1–126) and 145128 (Δ1–210) in the culture medium. All constructs were expressed as C-terminal FLAG-fused proteins. Error bars represent means ± S.D. of three separate experiments.

    Article Snippet: Oleic acid-containing PC and TG were measured using MRM with LC-ESI MS/MS.

    Techniques: Centrifugation, Mass Spectrometry, Expressing, Plasmid Preparation, Western Blot, Construct

    BmNPV polyhedra matrix proteins were separated on 12% ( A ) and 15% ( B ) SDS-PAGE gels. Purified polyhedra were treated with an alkaline solution. Undissolved polyhedra were removed by low-speed centrifugation at 500 × g. The resulting supernatant was collected and then centrifuged by continuous sucrose gradients to remove the ODVs. Protein sample over the upper gradient was separated by SDS-PAGE. Proteins on the gel were excised into five contiguous sections (M1 to M5) and subjected to in-gel digestion and LC-ESI-MS/MS analysis. Two M5 sections shown in ( A ) and ( B ) were combined for the determination. Lane M, protein marker.

    Journal: Scientific Reports

    Article Title: Protein composition analysis of polyhedra matrix of Bombyx mori nucleopolyhedrovirus (BmNPV) showed powerful capacity of polyhedra to encapsulate foreign proteins

    doi: 10.1038/s41598-017-08987-8

    Figure Lengend Snippet: BmNPV polyhedra matrix proteins were separated on 12% ( A ) and 15% ( B ) SDS-PAGE gels. Purified polyhedra were treated with an alkaline solution. Undissolved polyhedra were removed by low-speed centrifugation at 500 × g. The resulting supernatant was collected and then centrifuged by continuous sucrose gradients to remove the ODVs. Protein sample over the upper gradient was separated by SDS-PAGE. Proteins on the gel were excised into five contiguous sections (M1 to M5) and subjected to in-gel digestion and LC-ESI-MS/MS analysis. Two M5 sections shown in ( A ) and ( B ) were combined for the determination. Lane M, protein marker.

    Article Snippet: In this report, HSP70–4 was identified by an LC-ESI-MS/MS analysis to be associated with the BmNPV polyhedra matrix.

    Techniques: SDS Page, Purification, Centrifugation, Mass Spectrometry, Marker

    HPLC/ESI/MS/MS analysis of OHdiA adduct production in the reaction of KOHA-PC with Ac-Gly-Lys-OMe dipeptide. (A) Authentic 4-oxoheptanedioic acid ( 1 ) standard. (B) Reaction product mixture after 48 h incubation at room temperature.

    Journal: Chemical research in toxicology

    Article Title: Bioactive 4-Oxoheptanedioic Monoamide Derivatives of Proteins and Ethanolaminephospholipids: Products of Docosahexaenoate Oxidation

    doi: 10.1021/acs.chemrestox.6b00218

    Figure Lengend Snippet: HPLC/ESI/MS/MS analysis of OHdiA adduct production in the reaction of KOHA-PC with Ac-Gly-Lys-OMe dipeptide. (A) Authentic 4-oxoheptanedioic acid ( 1 ) standard. (B) Reaction product mixture after 48 h incubation at room temperature.

    Article Snippet: LC-ESI/MS/MS analysis of OHdiA adducts was performed on a Quattro Ultima triple-quadrupole mass spectrometer (Micromass, Wythenshawe, UK) equipped with a Waters Alliance 2690 HPLC system with an auto-injector (Waters, Milford, MA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Incubation

    LC/ESI/MS/MS evidence for OHdiA derivatives in human plasma. OHdiA-diPFB was detected after acid hydrolysis followed by PFB esterification. (A) MRM for synthetic authentic standard OHdiA-diPFB. (B) MRM for PFB derivative of 4-oxoheptanedioic acid from

    Journal: Chemical research in toxicology

    Article Title: Bioactive 4-Oxoheptanedioic Monoamide Derivatives of Proteins and Ethanolaminephospholipids: Products of Docosahexaenoate Oxidation

    doi: 10.1021/acs.chemrestox.6b00218

    Figure Lengend Snippet: LC/ESI/MS/MS evidence for OHdiA derivatives in human plasma. OHdiA-diPFB was detected after acid hydrolysis followed by PFB esterification. (A) MRM for synthetic authentic standard OHdiA-diPFB. (B) MRM for PFB derivative of 4-oxoheptanedioic acid from

    Article Snippet: LC-ESI/MS/MS analysis of OHdiA adducts was performed on a Quattro Ultima triple-quadrupole mass spectrometer (Micromass, Wythenshawe, UK) equipped with a Waters Alliance 2690 HPLC system with an auto-injector (Waters, Milford, MA).

    Techniques: Mass Spectrometry

    HPLC/ESI/MS/MS analysis after acid hydrolysis and pentafluorobenzyl esterification of the OHdiA monoamide produced by the reaction of KOHA-PC with Ac-Gly-Lys-OMe dipeptide. (A) Authentic OHdiA-diPFB standard. (B) Reaction product mixture from incubation

    Journal: Chemical research in toxicology

    Article Title: Bioactive 4-Oxoheptanedioic Monoamide Derivatives of Proteins and Ethanolaminephospholipids: Products of Docosahexaenoate Oxidation

    doi: 10.1021/acs.chemrestox.6b00218

    Figure Lengend Snippet: HPLC/ESI/MS/MS analysis after acid hydrolysis and pentafluorobenzyl esterification of the OHdiA monoamide produced by the reaction of KOHA-PC with Ac-Gly-Lys-OMe dipeptide. (A) Authentic OHdiA-diPFB standard. (B) Reaction product mixture from incubation

    Article Snippet: LC-ESI/MS/MS analysis of OHdiA adducts was performed on a Quattro Ultima triple-quadrupole mass spectrometer (Micromass, Wythenshawe, UK) equipped with a Waters Alliance 2690 HPLC system with an auto-injector (Waters, Milford, MA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Produced, Incubation

    HPLC/ESI/MS/MS analysis of OHdiA produced by copper-catalyzed oxidation of DHA-PC for 48 h (A) without DPPE or (B) with DPPE after 0 h incubation or (C) with DPPE after 48 h incubation followed by hydrolysis with 6 N HCl at 100 °C for 5 h.

    Journal: Chemical research in toxicology

    Article Title: Bioactive 4-Oxoheptanedioic Monoamide Derivatives of Proteins and Ethanolaminephospholipids: Products of Docosahexaenoate Oxidation

    doi: 10.1021/acs.chemrestox.6b00218

    Figure Lengend Snippet: HPLC/ESI/MS/MS analysis of OHdiA produced by copper-catalyzed oxidation of DHA-PC for 48 h (A) without DPPE or (B) with DPPE after 0 h incubation or (C) with DPPE after 48 h incubation followed by hydrolysis with 6 N HCl at 100 °C for 5 h.

    Article Snippet: LC-ESI/MS/MS analysis of OHdiA adducts was performed on a Quattro Ultima triple-quadrupole mass spectrometer (Micromass, Wythenshawe, UK) equipped with a Waters Alliance 2690 HPLC system with an auto-injector (Waters, Milford, MA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Produced, Incubation

    KLA induces time-dependent increases in ceramide and dihydroceramide. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC ESI-MS/MS. A , amounts of the major chain length subspecies of DHCer. Data represent the means ( n = 9). B , amounts of total DHCer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001. C , amounts of the major chain length subspecies of Cer. Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (9 pmol/μg DNA); C18 (0.4 pmol/μg DNA); C20 (0.2 pmol/μg DNA); C22 (1.9 pmol/μg DNA); C24:1 (5.4 pmol/μg DNA); C24 (5.5 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); and C26 (0.1 pmol/μg DNA). Data represent the means ± S.E. ( n = 9). D , amounts of total Cer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001.

    Journal: The Journal of Biological Chemistry

    Article Title: Kdo2-Lipid A, a TLR4-specific Agonist, Induces de Novo Sphingolipid Biosynthesis in RAW264.7 Macrophages, Which Is Essential for Induction of Autophagy *

    doi: 10.1074/jbc.M110.170621

    Figure Lengend Snippet: KLA induces time-dependent increases in ceramide and dihydroceramide. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC ESI-MS/MS. A , amounts of the major chain length subspecies of DHCer. Data represent the means ( n = 9). B , amounts of total DHCer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001. C , amounts of the major chain length subspecies of Cer. Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (9 pmol/μg DNA); C18 (0.4 pmol/μg DNA); C20 (0.2 pmol/μg DNA); C22 (1.9 pmol/μg DNA); C24:1 (5.4 pmol/μg DNA); C24 (5.5 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); and C26 (0.1 pmol/μg DNA). Data represent the means ± S.E. ( n = 9). D , amounts of total Cer (a summation of all chain lengths) in KLA versus control conditions. Data represent the means ± S.E. ( n = 9); *, p ≤ 0.05; **, p ≤ 0.001.

    Article Snippet: Materials The suppliers for the reagents were as follows: Kdo2 -lipid A and the internal standard mixture for SL analysis by LC ESI-MS/MS (ceramide/sphingoid internal standard mixture II, LM-6005) (Avanti Polar Lipids, Alabaster, AL); [U-13 C]palmitic acid (98%) (Cambridge Isotopes, Andover, MA); fatty acid-free BSA (Calbiochem) ; Hoechst 33342 (Invitrogen); ISP1 (Biomol, Plymouth Meeting, PA); mouse monoclonal antibody to SPT1 (anti-LCB1), anti-BiP/GRP78, and anti-GM130 (BD Biosciences); rabbit monoclonal anti-HA tag and rabbit polyclonal LC3B antibody (Cell Signaling Technology, Boston); mouse monoclonal anti-Cer antibody clone 15B4 (Alexis Biochemicals, San Diego) This antibody clone has been successfully used in immunocytochemistry applications with no indication of nonspecific reactions with other lipids ( ) The secondary Alexa Fluor-conjugated F(ab)2 fragment goat anti-mouse antibody and goat anti-rabbit antibody were from Molecular Probes, Inc. (Eugene, OR.).

    Techniques: Incubation, Mass Spectrometry

    Effect of ISP1 on sphingolipid biosynthesis in KLA-treated RAW264.7 cells. RAW264.7 cells were incubated for 24 h with vehicle control (PBS), KLA (100 ng/ml), ISP1 (1 μ m ), or KLA + ISP1. For cells treated with KLA + ISP1, ISP1 was added 1 h prior to the addition of KLA. Following treatment, cells were harvested for lipid extraction and analysis by LC ESI-MS/MS. A , change in the amounts of Cer, HexCer, and SM for cells treated with KLA or KLA + ISP1. Data represent the means ± S.E. ( n = 3). B , amounts of the major chain length subspecies of ceramide in cells treated with KLA + ISP1. Data represent the means ( n = 3).

    Journal: The Journal of Biological Chemistry

    Article Title: Kdo2-Lipid A, a TLR4-specific Agonist, Induces de Novo Sphingolipid Biosynthesis in RAW264.7 Macrophages, Which Is Essential for Induction of Autophagy *

    doi: 10.1074/jbc.M110.170621

    Figure Lengend Snippet: Effect of ISP1 on sphingolipid biosynthesis in KLA-treated RAW264.7 cells. RAW264.7 cells were incubated for 24 h with vehicle control (PBS), KLA (100 ng/ml), ISP1 (1 μ m ), or KLA + ISP1. For cells treated with KLA + ISP1, ISP1 was added 1 h prior to the addition of KLA. Following treatment, cells were harvested for lipid extraction and analysis by LC ESI-MS/MS. A , change in the amounts of Cer, HexCer, and SM for cells treated with KLA or KLA + ISP1. Data represent the means ± S.E. ( n = 3). B , amounts of the major chain length subspecies of ceramide in cells treated with KLA + ISP1. Data represent the means ( n = 3).

    Article Snippet: Materials The suppliers for the reagents were as follows: Kdo2 -lipid A and the internal standard mixture for SL analysis by LC ESI-MS/MS (ceramide/sphingoid internal standard mixture II, LM-6005) (Avanti Polar Lipids, Alabaster, AL); [U-13 C]palmitic acid (98%) (Cambridge Isotopes, Andover, MA); fatty acid-free BSA (Calbiochem) ; Hoechst 33342 (Invitrogen); ISP1 (Biomol, Plymouth Meeting, PA); mouse monoclonal antibody to SPT1 (anti-LCB1), anti-BiP/GRP78, and anti-GM130 (BD Biosciences); rabbit monoclonal anti-HA tag and rabbit polyclonal LC3B antibody (Cell Signaling Technology, Boston); mouse monoclonal anti-Cer antibody clone 15B4 (Alexis Biochemicals, San Diego) This antibody clone has been successfully used in immunocytochemistry applications with no indication of nonspecific reactions with other lipids ( ) The secondary Alexa Fluor-conjugated F(ab)2 fragment goat anti-mouse antibody and goat anti-rabbit antibody were from Molecular Probes, Inc. (Eugene, OR.).

    Techniques: Incubation, Mass Spectrometry

    KLA induces time-dependent increases in ceramide metabolites. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC ESI-MS/MS. Amounts of the major chain length subspecies of Cer metabolites as follows: sphingomyelins ( A ), monohexosylceramides ( B ), and ceramide 1-phosphates ( C ) are shown. Data represent the means ( n = 9).

    Journal: The Journal of Biological Chemistry

    Article Title: Kdo2-Lipid A, a TLR4-specific Agonist, Induces de Novo Sphingolipid Biosynthesis in RAW264.7 Macrophages, Which Is Essential for Induction of Autophagy *

    doi: 10.1074/jbc.M110.170621

    Figure Lengend Snippet: KLA induces time-dependent increases in ceramide metabolites. RAW264.7 cells were incubated with vehicle control (PBS) or KLA (100 ng/ml). Following treatment, cells were harvested at the indicated time points for lipid extraction and analysis by LC ESI-MS/MS. Amounts of the major chain length subspecies of Cer metabolites as follows: sphingomyelins ( A ), monohexosylceramides ( B ), and ceramide 1-phosphates ( C ) are shown. Data represent the means ( n = 9).

    Article Snippet: Materials The suppliers for the reagents were as follows: Kdo2 -lipid A and the internal standard mixture for SL analysis by LC ESI-MS/MS (ceramide/sphingoid internal standard mixture II, LM-6005) (Avanti Polar Lipids, Alabaster, AL); [U-13 C]palmitic acid (98%) (Cambridge Isotopes, Andover, MA); fatty acid-free BSA (Calbiochem) ; Hoechst 33342 (Invitrogen); ISP1 (Biomol, Plymouth Meeting, PA); mouse monoclonal antibody to SPT1 (anti-LCB1), anti-BiP/GRP78, and anti-GM130 (BD Biosciences); rabbit monoclonal anti-HA tag and rabbit polyclonal LC3B antibody (Cell Signaling Technology, Boston); mouse monoclonal anti-Cer antibody clone 15B4 (Alexis Biochemicals, San Diego) This antibody clone has been successfully used in immunocytochemistry applications with no indication of nonspecific reactions with other lipids ( ) The secondary Alexa Fluor-conjugated F(ab)2 fragment goat anti-mouse antibody and goat anti-rabbit antibody were from Molecular Probes, Inc. (Eugene, OR.).

    Techniques: Incubation, Mass Spectrometry