nano electrospray ion trap mass spectrometers  (Thermo Fisher)


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    Thermo Fisher nano electrospray ion trap mass spectrometers
    Nano Electrospray Ion Trap Mass Spectrometers, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano electrospray ion trap mass spectrometers/product/Thermo Fisher
    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    nano electrospray ion trap mass spectrometers - by Bioz Stars, 2020-08
    85/100 stars

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    Article Title: Calculations of relative intensities of fragment ions in the MSMS spectra of a doubly charged penta-peptide
    Article Snippet: .. MSMS spectra of doubly charged GAVLK were collected on nano-electrospray ion trap mass spectrometers (LCQ Deca XP Plus and LTQ-Orbitrap Velos; THERMO), by direct sample injection (flow 500 nl.min-1 ), using low energy modes of fragmentation (CID-Collision Induced Decay, PQD-Pulsed-Q Dissociation). ..

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    Article Title: Calculations of relative intensities of fragment ions in the MSMS spectra of a doubly charged penta-peptide
    Article Snippet: .. MSMS spectra of doubly charged GAVLK were collected on nano-electrospray ion trap mass spectrometers (LCQ Deca XP Plus and LTQ-Orbitrap Velos; THERMO), by direct sample injection (flow 500 nl.min-1 ), using low energy modes of fragmentation (CID-Collision Induced Decay, PQD-Pulsed-Q Dissociation). ..

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    Thermo Fisher nano reverse phase rp lc esi ion trap ms ms
    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. <t>Nano-RP-LC-ESI-ion</t> trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.
    Nano Reverse Phase Rp Lc Esi Ion Trap Ms Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano reverse phase rp lc esi ion trap ms ms/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
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    90
    Thermo Fisher nano rp lc esi ion trap ms ms
    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. <t>Nano-RP-LC-ESI-ion</t> trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.
    Nano Rp Lc Esi Ion Trap Ms Ms, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano rp lc esi ion trap ms ms/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
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    nano rp lc esi ion trap ms ms - by Bioz Stars, 2020-08
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    93
    Thermo Fisher nano hplc esi ion trap ms ms analysis
    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. <t>Nano-RP-LC-ESI-ion</t> trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.
    Nano Hplc Esi Ion Trap Ms Ms Analysis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano hplc esi ion trap ms ms analysis/product/Thermo Fisher
    Average 93 stars, based on 3 article reviews
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    92
    Thermo Fisher nano liquid chromatography nlc electrospray ionization esi linear ion trap lit tandem ms ms mass spectrometry analysis
    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. <t>Nano-RP-LC-ESI-ion</t> trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.
    Nano Liquid Chromatography Nlc Electrospray Ionization Esi Linear Ion Trap Lit Tandem Ms Ms Mass Spectrometry Analysis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano liquid chromatography nlc electrospray ionization esi linear ion trap lit tandem ms ms mass spectrometry analysis/product/Thermo Fisher
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    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Tegument Glycoproteins and Cathepsins of Newly Excysted Juvenile Fasciola hepatica Carry Mannosidic and Paucimannosidic N-glycans

    doi: 10.1371/journal.pntd.0004688

    Figure Lengend Snippet: Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.

    Article Snippet: The proteomics analysis of the NEJTeg extract was performed by nano reverse-phase (RP) LC-ESI-ion trap MS/MS, consisting of an Ultimate 3000 RSLC nano LC system (Thermo Fisher Scientific) coupled to a Captive Spray nano Booster (Bruker Daltonics) according to previous protocol [ ].

    Techniques: Mass Spectrometry

    Identification of short N- glycans occupying an N- glycosylation site of FhCB1. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide Y 79 NVSENDLPESFDAR 93 from FhCB1 (BN1106_s6570B000050). The [M+3H] 3+ parent ions (blue diamonds) at m/z 829.50 ( A ) and 878.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle), pep (peptide moiety).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Tegument Glycoproteins and Cathepsins of Newly Excysted Juvenile Fasciola hepatica Carry Mannosidic and Paucimannosidic N-glycans

    doi: 10.1371/journal.pntd.0004688

    Figure Lengend Snippet: Identification of short N- glycans occupying an N- glycosylation site of FhCB1. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide Y 79 NVSENDLPESFDAR 93 from FhCB1 (BN1106_s6570B000050). The [M+3H] 3+ parent ions (blue diamonds) at m/z 829.50 ( A ) and 878.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle), pep (peptide moiety).

    Article Snippet: The proteomics analysis of the NEJTeg extract was performed by nano reverse-phase (RP) LC-ESI-ion trap MS/MS, consisting of an Ultimate 3000 RSLC nano LC system (Thermo Fisher Scientific) coupled to a Captive Spray nano Booster (Bruker Daltonics) according to previous protocol [ ].

    Techniques: Mass Spectrometry

    Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Tegument Glycoproteins and Cathepsins of Newly Excysted Juvenile Fasciola hepatica Carry Mannosidic and Paucimannosidic N-glycans

    doi: 10.1371/journal.pntd.0004688

    Figure Lengend Snippet: Identification of short N- glycans occupying an N- glycosylation site of on the YNVSENDLPESFDAR tryptic peptide. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide YNVSENDLPESFDAR from FhProCB2 (gi|27526823). The [M+3H] 3+ parent ions (blue diamonds) at m/z 824.70 ( A ) and 873.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle).pep, peptide moiety.

    Article Snippet: For nano-RP-LC-ESI-ion trap-MS/MS the peptides and glycopeptides extracted from the cathepsin bands were loaded on a trap column (Acclaim PepMap100 C18 column, 100 μm × 2 cm, C18 particle size 5 μm, pore size 100 Å, Thermo Fisher Scientific) for concentration prior to separation on an Acclaim PepMap RSLCnano-column (75 μm × 15 cm, C18 particle size 2 μm, pore size 100 Å, Thermo Fisher Scientific).

    Techniques: Mass Spectrometry

    Identification of short N- glycans occupying an N- glycosylation site of FhCB1. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide Y 79 NVSENDLPESFDAR 93 from FhCB1 (BN1106_s6570B000050). The [M+3H] 3+ parent ions (blue diamonds) at m/z 829.50 ( A ) and 878.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle), pep (peptide moiety).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Tegument Glycoproteins and Cathepsins of Newly Excysted Juvenile Fasciola hepatica Carry Mannosidic and Paucimannosidic N-glycans

    doi: 10.1371/journal.pntd.0004688

    Figure Lengend Snippet: Identification of short N- glycans occupying an N- glycosylation site of FhCB1. Nano-RP-LC-ESI-ion trap-MS/MS with collision-induced dissociation ( A and B ) and with electron transfer dissociation ( C ) of the tryptic glycopeptide Y 79 NVSENDLPESFDAR 93 from FhCB1 (BN1106_s6570B000050). The [M+3H] 3+ parent ions (blue diamonds) at m/z 829.50 ( A ) and 878.70 ( B ) of the glycopeptide carrying a glycan of composition H2N2 and F1H2N2 respectively were selected. Fragment ions are indicated. The residual signals at the m/z corresponding to [H+3H] 3+ ( Δ ), to the doubly charged ions that result from capture of 1 electron without dissociation [H+3H] 2+· ( X ) and to the singly charged ions that result from capture of 2 electrons without dissociation [H+3H] +·· (*) are indicated ( C ). Monoisotopic masses are given. Man (green circle), GlcNAc (blue square) and Fuc (red triangle), pep (peptide moiety).

    Article Snippet: For nano-RP-LC-ESI-ion trap-MS/MS the peptides and glycopeptides extracted from the cathepsin bands were loaded on a trap column (Acclaim PepMap100 C18 column, 100 μm × 2 cm, C18 particle size 5 μm, pore size 100 Å, Thermo Fisher Scientific) for concentration prior to separation on an Acclaim PepMap RSLCnano-column (75 μm × 15 cm, C18 particle size 2 μm, pore size 100 Å, Thermo Fisher Scientific).

    Techniques: Mass Spectrometry