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  • 99
    Thermo Fisher invitrosol lc ms protein solubilizer kit
    Invitrosol Lc Ms Protein Solubilizer Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Shimadzu Corporation lc esi ms
    Lc Esi Ms, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies lc esi ms ms analysis
    Lc Esi Ms Ms Analysis, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 181 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: 92/100, based on 133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation lc esi ms ms analysis
    In vitro SOAT activity of sCASD1 monitored by <t>DMB-HPLC</t> and <t>LC-ESI-MS.</t> ( a ) HPLC elution profile of the DMB-derivatized Sia reference panel, which included also two non-human Sia species, that is, Neu5Gc (5- N -glycolyl neuraminic acid) and 9- O -acetylated Neu5Gc (Neu5Gc9Ac). Asterisks denote that the indicated Sia species are labelled with DMB. ( b-d ) HPLC elution profiles of DMB-derivatized samples obtained after incubation of CMP-Neu5Ac and acetyl-CoA without enzyme ( b ), with sCASD1-wt ( c ) or with sCASD1-S94A ( d ). In all profiles, the retention time corresponding to DMB-Neu5,9Ac 2 of the reference panel is highlighted by a grey box. ( e ) SOAT activity of sCASD1 towards different acceptor substrates. Purified sCASD1-wt and sCASD1-S94A were incubated with acetyl-CoA and the indicated acceptor substrates. Product analysis was performed by DMB-HPLC analysis and the amount of DMB-Neu5,9Ac 2 was quantified by integrating the corresponding peak areas. Parallel HPLC runs of reactions without CASD1 were used to measure the background, and data are presented as background subtracted data with the values obtained for CMP-Neu5Ac in the presence of sCASD1-wt and acetyl-CoA set to 100% (mean±s.d., n =3). ( f ) Scheme showing sCASD1-catalysed 9- O -acetylation of CMP-Neu5Ac, subsequent DMB labelling of the reaction product, and the calculated m / z value ([M+H] + ) for DMB-derivatized Neu5,9Ac 2 . Structures and calculated m / z values ([M+H] + ) of the fragmentation compounds of DMB-Neu5,9Ac 2 are given according to Klein et al. 45 . ( g ) LC-ESI-MS/MS analysis. In the HPLC runs shown in ( b – d ), the peak material eluting at the retention time of DMB-Neu5,9Ac 2 was collected and subjected to LC-ESI-MS/MS. Ions at m / z 468.16 ([M+H] + ), indicating DMB-Neu5,9Ac 2 , were obtained only for the material collected from c and subsequent fragmentation revealed the three ions ( m / z 313, 295 and 229) that are characteristic for DMB-Neu5,9Ac 2 (ref. 45 ). Numbers in brackets above the spectrum refer to the structures given in f . DMB, 1,2-diamino - 4,5-methylenedioxy-benzene.
    Lc Esi Ms Ms Analysis, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher lc esi ms ms system
    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 <t>kDa</t> were additionally analyzed by <t>LC-ESI-MS/MS.</t> 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.
    Lc Esi Ms Ms System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 322 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies esi tuning mix
    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 <t>kDa</t> were additionally analyzed by <t>LC-ESI-MS/MS.</t> 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.
    Esi Tuning Mix, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 98/100, based on 141 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies chromatography electrospray ionization mass spectrometry
    Representative of liquid <t>chromatography-electrospray</t> ionization mass spectrometry (LC-ESI-MS) selected ion chromatogram ( m / z = 353) of vTP+ vessels incubated in HEPES buffer with and without angiotensin II [0.1 μM; aorta ( A ) or mesentery artery
    Chromatography Electrospray Ionization Mass Spectrometry, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 151 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher q star elite esi lc ms ms mass spectrometer
    Representative of liquid <t>chromatography-electrospray</t> ionization mass spectrometry (LC-ESI-MS) selected ion chromatogram ( m / z = 353) of vTP+ vessels incubated in HEPES buffer with and without angiotensin II [0.1 μM; aorta ( A ) or mesentery artery
    Q Star Elite Esi Lc Ms Ms Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 73 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies esi tof lc ms 6200 system
    Representative of liquid <t>chromatography-electrospray</t> ionization mass spectrometry (LC-ESI-MS) selected ion chromatogram ( m / z = 353) of vTP+ vessels incubated in HEPES buffer with and without angiotensin II [0.1 μM; aorta ( A ) or mesentery artery
    Esi Tof Lc Ms 6200 System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Diatech Korea Co Ltd esi lc ms
    MEF2 methylation decreases during C2C12 cell differentiation. ( a ) <t>HA-MEF2D,</t> transiently expressed in HEK293 cells, was immunoprecipitated with anti-methylated K267 MEF2D (anti-K267me) and subjected to <t>ESI-LC-MS</t> analysis. Dimethylation (upper panel) and monomethylation (lower panel) of MEF2D were detected. ( b ) Transiently expressed HA-MEF2D wild-type (WT) or K267R mutant (K267R) was immunoprecipitated with anti-K267me, followed by immunoblotting with anti-HA. ( c ) Transiently expressed Flag-MEF2D (WT) was immunoprecipitated with anti-Flag, followed by immunoblotting with anti-K267me with or without chemically methylated K267 containing peptide blocking. ( d ) Endogenous MEF2D was immunoprecipitated from C2C12 cells with anti-K267me and immunoblotted with anti-MEF2D. ( e ) C2C12 whole-cell lysates were immunoprecipitated with anti-K267me or IgG. Supernatants of immunodepleted C2C12 cell lysates were analyzed by immunoblotting with anti-MEF2D (upper panel). Quantification of MEF2D after normalization to input (lower panel). ( f ) C2C12 cells, differentiated for up to 4 days, were immunoprecipitated with anti-MEF2D and western blotted with anti-K267me (GM, DM2, DM4; DM for 2 or 4 days).
    Esi Lc Ms, supplied by Diatech Korea Co Ltd, used in various techniques. Bioz Stars score: 89/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    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

    In vitro SOAT activity of sCASD1 monitored by DMB-HPLC and LC-ESI-MS. ( a ) HPLC elution profile of the DMB-derivatized Sia reference panel, which included also two non-human Sia species, that is, Neu5Gc (5- N -glycolyl neuraminic acid) and 9- O -acetylated Neu5Gc (Neu5Gc9Ac). Asterisks denote that the indicated Sia species are labelled with DMB. ( b-d ) HPLC elution profiles of DMB-derivatized samples obtained after incubation of CMP-Neu5Ac and acetyl-CoA without enzyme ( b ), with sCASD1-wt ( c ) or with sCASD1-S94A ( d ). In all profiles, the retention time corresponding to DMB-Neu5,9Ac 2 of the reference panel is highlighted by a grey box. ( e ) SOAT activity of sCASD1 towards different acceptor substrates. Purified sCASD1-wt and sCASD1-S94A were incubated with acetyl-CoA and the indicated acceptor substrates. Product analysis was performed by DMB-HPLC analysis and the amount of DMB-Neu5,9Ac 2 was quantified by integrating the corresponding peak areas. Parallel HPLC runs of reactions without CASD1 were used to measure the background, and data are presented as background subtracted data with the values obtained for CMP-Neu5Ac in the presence of sCASD1-wt and acetyl-CoA set to 100% (mean±s.d., n =3). ( f ) Scheme showing sCASD1-catalysed 9- O -acetylation of CMP-Neu5Ac, subsequent DMB labelling of the reaction product, and the calculated m / z value ([M+H] + ) for DMB-derivatized Neu5,9Ac 2 . Structures and calculated m / z values ([M+H] + ) of the fragmentation compounds of DMB-Neu5,9Ac 2 are given according to Klein et al. 45 . ( g ) LC-ESI-MS/MS analysis. In the HPLC runs shown in ( b – d ), the peak material eluting at the retention time of DMB-Neu5,9Ac 2 was collected and subjected to LC-ESI-MS/MS. Ions at m / z 468.16 ([M+H] + ), indicating DMB-Neu5,9Ac 2 , were obtained only for the material collected from c and subsequent fragmentation revealed the three ions ( m / z 313, 295 and 229) that are characteristic for DMB-Neu5,9Ac 2 (ref. 45 ). Numbers in brackets above the spectrum refer to the structures given in f . DMB, 1,2-diamino - 4,5-methylenedioxy-benzene.

    Journal: Nature Communications

    Article Title: 9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate

    doi: 10.1038/ncomms8673

    Figure Lengend Snippet: In vitro SOAT activity of sCASD1 monitored by DMB-HPLC and LC-ESI-MS. ( a ) HPLC elution profile of the DMB-derivatized Sia reference panel, which included also two non-human Sia species, that is, Neu5Gc (5- N -glycolyl neuraminic acid) and 9- O -acetylated Neu5Gc (Neu5Gc9Ac). Asterisks denote that the indicated Sia species are labelled with DMB. ( b-d ) HPLC elution profiles of DMB-derivatized samples obtained after incubation of CMP-Neu5Ac and acetyl-CoA without enzyme ( b ), with sCASD1-wt ( c ) or with sCASD1-S94A ( d ). In all profiles, the retention time corresponding to DMB-Neu5,9Ac 2 of the reference panel is highlighted by a grey box. ( e ) SOAT activity of sCASD1 towards different acceptor substrates. Purified sCASD1-wt and sCASD1-S94A were incubated with acetyl-CoA and the indicated acceptor substrates. Product analysis was performed by DMB-HPLC analysis and the amount of DMB-Neu5,9Ac 2 was quantified by integrating the corresponding peak areas. Parallel HPLC runs of reactions without CASD1 were used to measure the background, and data are presented as background subtracted data with the values obtained for CMP-Neu5Ac in the presence of sCASD1-wt and acetyl-CoA set to 100% (mean±s.d., n =3). ( f ) Scheme showing sCASD1-catalysed 9- O -acetylation of CMP-Neu5Ac, subsequent DMB labelling of the reaction product, and the calculated m / z value ([M+H] + ) for DMB-derivatized Neu5,9Ac 2 . Structures and calculated m / z values ([M+H] + ) of the fragmentation compounds of DMB-Neu5,9Ac 2 are given according to Klein et al. 45 . ( g ) LC-ESI-MS/MS analysis. In the HPLC runs shown in ( b – d ), the peak material eluting at the retention time of DMB-Neu5,9Ac 2 was collected and subjected to LC-ESI-MS/MS. Ions at m / z 468.16 ([M+H] + ), indicating DMB-Neu5,9Ac 2 , were obtained only for the material collected from c and subsequent fragmentation revealed the three ions ( m / z 313, 295 and 229) that are characteristic for DMB-Neu5,9Ac 2 (ref. 45 ). Numbers in brackets above the spectrum refer to the structures given in f . DMB, 1,2-diamino - 4,5-methylenedioxy-benzene.

    Article Snippet: LC-ESI-MS MS analysis of peptides and DMB-labelled sugars was performed on a nanoACQUITY UPLC system (Waters) equipped with an analytical column (Waters, BEH130C18, 100 μm × 100 mm, 1.7-μm particle size) coupled online with an ESI Q-TOF (Q-TOF Ultima, Waters).

    Techniques: In Vitro, Activity Assay, High Performance Liquid Chromatography, Mass Spectrometry, Incubation, Purification

    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: Seven samples in the range of 95 to 60 and 27 to 24 kDa were additionally analyzed by LC-ESI-MS/MS (Thermo Scientific).

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

    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

    Representative of liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS) selected ion chromatogram ( m / z = 353) of vTP+ vessels incubated in HEPES buffer with and without angiotensin II [0.1 μM; aorta ( A ) or mesentery artery

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Role of superoxide and thromboxane receptors in acute angiotensin II-induced vasoconstriction of rabbit vessels

    doi: 10.1152/ajpheart.01135.2010

    Figure Lengend Snippet: Representative of liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS) selected ion chromatogram ( m / z = 353) of vTP+ vessels incubated in HEPES buffer with and without angiotensin II [0.1 μM; aorta ( A ) or mesentery artery

    Article Snippet: Samples were analyzed by using liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS, Agilent 1100 LC/MSD, SL model) using a modification of a method previously described by Nithipatikom et al. ( ).

    Techniques: Liquid Chromatography, Mass Spectrometry, Incubation

    MEF2 methylation decreases during C2C12 cell differentiation. ( a ) HA-MEF2D, transiently expressed in HEK293 cells, was immunoprecipitated with anti-methylated K267 MEF2D (anti-K267me) and subjected to ESI-LC-MS analysis. Dimethylation (upper panel) and monomethylation (lower panel) of MEF2D were detected. ( b ) Transiently expressed HA-MEF2D wild-type (WT) or K267R mutant (K267R) was immunoprecipitated with anti-K267me, followed by immunoblotting with anti-HA. ( c ) Transiently expressed Flag-MEF2D (WT) was immunoprecipitated with anti-Flag, followed by immunoblotting with anti-K267me with or without chemically methylated K267 containing peptide blocking. ( d ) Endogenous MEF2D was immunoprecipitated from C2C12 cells with anti-K267me and immunoblotted with anti-MEF2D. ( e ) C2C12 whole-cell lysates were immunoprecipitated with anti-K267me or IgG. Supernatants of immunodepleted C2C12 cell lysates were analyzed by immunoblotting with anti-MEF2D (upper panel). Quantification of MEF2D after normalization to input (lower panel). ( f ) C2C12 cells, differentiated for up to 4 days, were immunoprecipitated with anti-MEF2D and western blotted with anti-K267me (GM, DM2, DM4; DM for 2 or 4 days).

    Journal: Nucleic Acids Research

    Article Title: Modulation of lysine methylation in myocyte enhancer factor 2 during skeletal muscle cell differentiation

    doi: 10.1093/nar/gkt873

    Figure Lengend Snippet: MEF2 methylation decreases during C2C12 cell differentiation. ( a ) HA-MEF2D, transiently expressed in HEK293 cells, was immunoprecipitated with anti-methylated K267 MEF2D (anti-K267me) and subjected to ESI-LC-MS analysis. Dimethylation (upper panel) and monomethylation (lower panel) of MEF2D were detected. ( b ) Transiently expressed HA-MEF2D wild-type (WT) or K267R mutant (K267R) was immunoprecipitated with anti-K267me, followed by immunoblotting with anti-HA. ( c ) Transiently expressed Flag-MEF2D (WT) was immunoprecipitated with anti-Flag, followed by immunoblotting with anti-K267me with or without chemically methylated K267 containing peptide blocking. ( d ) Endogenous MEF2D was immunoprecipitated from C2C12 cells with anti-K267me and immunoblotted with anti-MEF2D. ( e ) C2C12 whole-cell lysates were immunoprecipitated with anti-K267me or IgG. Supernatants of immunodepleted C2C12 cell lysates were analyzed by immunoblotting with anti-MEF2D (upper panel). Quantification of MEF2D after normalization to input (lower panel). ( f ) C2C12 cells, differentiated for up to 4 days, were immunoprecipitated with anti-MEF2D and western blotted with anti-K267me (GM, DM2, DM4; DM for 2 or 4 days).

    Article Snippet: Sliced gel pieces or MEF2D peptides were digested with trypsin or chymotrypsin and analyzed by ESI-LC-MS (Diatech Korea, Co. LTD).

    Techniques: Methylation, Cell Differentiation, Immunoprecipitation, Liquid Chromatography with Mass Spectroscopy, Mutagenesis, Blocking Assay, Western Blot

    G9a methylates MEF2D at K267 through their interaction. ( a ) In vitro methylation of MEF2D peptide (263–271) (me0) by G9a was analyzed by dot blot assay. Chemically methylated MEF2D peptide (me1) was used as a positive control for antibody detection. ( b ) In vitro methylation of bacterially purified full-length His-MEF2D with G9a was analyzed by ESI-LC-MS. ( c ) C2C12 cells were treated with BIX01294 at the indicated concentrations. MEF2D and its methylation levels were analyzed by immunoprecipitation. ( d ) MEF2D methylation in C2C12 cells infected with shMock or shG9a was analyzed by immunoprecipitation. ( e ) Whole-cell lysates of C2C12 cells in GM were immunoprecipitated with anti-G9a or rabbit normal IgG. ( f ) Colocalization of G9a and MEF2D in proliferating C2C12 cells was analyzed by immunostaining.

    Journal: Nucleic Acids Research

    Article Title: Modulation of lysine methylation in myocyte enhancer factor 2 during skeletal muscle cell differentiation

    doi: 10.1093/nar/gkt873

    Figure Lengend Snippet: G9a methylates MEF2D at K267 through their interaction. ( a ) In vitro methylation of MEF2D peptide (263–271) (me0) by G9a was analyzed by dot blot assay. Chemically methylated MEF2D peptide (me1) was used as a positive control for antibody detection. ( b ) In vitro methylation of bacterially purified full-length His-MEF2D with G9a was analyzed by ESI-LC-MS. ( c ) C2C12 cells were treated with BIX01294 at the indicated concentrations. MEF2D and its methylation levels were analyzed by immunoprecipitation. ( d ) MEF2D methylation in C2C12 cells infected with shMock or shG9a was analyzed by immunoprecipitation. ( e ) Whole-cell lysates of C2C12 cells in GM were immunoprecipitated with anti-G9a or rabbit normal IgG. ( f ) Colocalization of G9a and MEF2D in proliferating C2C12 cells was analyzed by immunostaining.

    Article Snippet: Sliced gel pieces or MEF2D peptides were digested with trypsin or chymotrypsin and analyzed by ESI-LC-MS (Diatech Korea, Co. LTD).

    Techniques: In Vitro, Methylation, Dot Blot, Positive Control, Purification, Liquid Chromatography with Mass Spectroscopy, Immunoprecipitation, Infection, Immunostaining