nano-electrospray ion source Search Results


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  • 99
    Thermo Fisher easy spray nano electrospray ion source
    Easy Spray Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 109 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/easy spray nano electrospray ion source/product/Thermo Fisher
    Average 99 stars, based on 109 article reviews
    Price from $9.99 to $1999.99
    easy spray nano electrospray ion source - by Bioz Stars, 2020-03
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    99
    Thermo Fisher nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1014 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1014 article reviews
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    89
    Bruker Corporation nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 89/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano electrospray ion source/product/Bruker Corporation
    Average 89 stars, based on 20 article reviews
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    nano electrospray ion source - by Bioz Stars, 2020-03
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    86
    New Objective Inc nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 86/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano electrospray ion source/product/New Objective Inc
    Average 86 stars, based on 48 article reviews
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    nano electrospray ion source - by Bioz Stars, 2020-03
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    84
    Michrom nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Michrom, used in various techniques. Bioz Stars score: 84/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 84 stars, based on 28 article reviews
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    nano electrospray ion source - by Bioz Stars, 2020-03
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    84
    Waters Corporation nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 84/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 84 stars, based on 21 article reviews
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    87
    SCIEX nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by SCIEX, used in various techniques. Bioz Stars score: 87/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 87 stars, based on 13 article reviews
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    96
    Thermo Fisher flex nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Flex Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 66 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 66 article reviews
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    flex nano electrospray ion source - by Bioz Stars, 2020-03
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    93
    Thermo Fisher easy1000 nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Easy1000 Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 11 article reviews
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    90
    Thermo Fisher nanoesi nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nanoesi Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 11 article reviews
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    89
    Advion triversa nanomate nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Triversa Nanomate Nano Electrospray Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 89 stars, based on 6 article reviews
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    92
    New Objective Inc picoview pv550 nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Picoview Pv550 Nano Electrospray Ion Source, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 7 article reviews
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    89
    Advion nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 89/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 89 stars, based on 20 article reviews
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    78
    New Objective Inc dpv 566 picoview nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Dpv 566 Picoview Nano Electrospray Ion Source, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 78/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 78 stars, based on 1 article reviews
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    84
    MDS Proteomics nano electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nano Electrospray Ion Source, supplied by MDS Proteomics, used in various techniques. Bioz Stars score: 84/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 84 stars, based on 4 article reviews
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    76
    Bruker Corporation nano flow electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nano Flow Electrospray Ion Source, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano flow electrospray ion source/product/Bruker Corporation
    Average 76 stars, based on 1 article reviews
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    75
    Thermo Fisher nano electrospray ion source thermofisher
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nano Electrospray Ion Source Thermofisher, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 75 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    78
    Thermo Fisher proxeon nano electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Proxeon Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proxeon nano electrospray ion source/product/Thermo Fisher
    Average 78 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    proxeon nano electrospray ion source - by Bioz Stars, 2020-03
    78/100 stars
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    83
    Advion triversa chip based nano electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Triversa Chip Based Nano Electrospray Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 83/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/triversa chip based nano electrospray ion source/product/Advion
    Average 83 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    triversa chip based nano electrospray ion source - by Bioz Stars, 2020-03
    83/100 stars
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    89
    Biosystems S.A nano electrospray ion source esi
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nano Electrospray Ion Source Esi, supplied by Biosystems S.A, used in various techniques. Bioz Stars score: 89/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano electrospray ion source esi/product/Biosystems S.A
    Average 89 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    nano electrospray ion source esi - by Bioz Stars, 2020-03
    89/100 stars
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    79
    Waters Corporation z spray nano electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Z Spray Nano Electrospray Ion Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 79/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/z spray nano electrospray ion source/product/Waters Corporation
    Average 79 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
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    79/100 stars
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    80
    New Objective Inc pv 550 nano electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Pv 550 Nano Electrospray Ion Source, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 80/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pv 550 nano electrospray ion source/product/New Objective Inc
    Average 80 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    pv 550 nano electrospray ion source - by Bioz Stars, 2020-03
    80/100 stars
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    80
    Biosystems S.A nano electrospray ion esi source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Advion nano flow electrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Advion chip based nano electrospray ionization ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Chip Based Nano Electrospray Ionization Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Advion chip based nano electrospray ionization nesi ion source ion source triversananomate
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Thermo Fisher nanospray ion source 1
    Reproducibility test for the integrated <t>Micro-CF/nano-HPLC-ESI-MS/MS.</t> Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).
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    New Objective Inc picoslide nano electrospray
    Reproducibility test for the integrated <t>Micro-CF/nano-HPLC-ESI-MS/MS.</t> Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).
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    Advion chipmatetm nanoelectrospray ion source
    Reproducibility test for the integrated <t>Micro-CF/nano-HPLC-ESI-MS/MS.</t> Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).
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    Michrom thermo captivespray nanoelectrospray ion source
    Reproducibility test for the integrated <t>Micro-CF/nano-HPLC-ESI-MS/MS.</t> Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).
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    Image Search Results


    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.

    Journal: International Journal of Molecular Sciences

    Article Title: Antioxidant Properties and the Formation of Iron Coordination Complexes of 8-Hydroxyquinoline

    doi: 10.3390/ijms19123917

    Figure Lengend Snippet: Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.

    Article Snippet: Mass Spectrometry Direct infusion nano-electrospray ionization mass spectrometry was carried out in positive ionization mode on a Thermo Electron LTQ-Orbitrap XL mass spectrometer equipped with a nano electrospray ion source (ThermoFisher Scientific, Bremen, Germany) and operated under Xcalibur software 2.2 (ThermoFisher Scientific, Bremen, Germany) as described by Kubicova et al. [ ].

    Techniques: Mass Spectrometry

    Ideication of the UV cross-linked amino acid residue in SSB by nanoelectrospray tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Mass spectrometric analysis of a UV-cross-linked protein-DNA complex: Tryptophans 54 and 88 of E. coli SSB cross-link to DNA

    doi:

    Figure Lengend Snippet: Ideication of the UV cross-linked amino acid residue in SSB by nanoelectrospray tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.

    Article Snippet: Analytical properties of the nanoelectrospray ion source.

    Techniques: Mass Spectrometry, Purification, Sequencing, Labeling

    Reproducibility test for the integrated Micro-CF/nano-HPLC-ESI-MS/MS. Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).

    Journal: Journal of chromatography. A

    Article Title: Micro - Proteome Analysis Using Micro-Chromatofocusing In Intact Protein Separations

    doi: 10.1016/j.chroma.2008.03.065

    Figure Lengend Snippet: Reproducibility test for the integrated Micro-CF/nano-HPLC-ESI-MS/MS. Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).

    Article Snippet: The digested peptide mixture was analyzed by nano-flow reverse-phase LC/MS/MS using the LTQ mass spectrometer with a nano-spray ESI ion source (Thermo, San Jose, CA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry