Structured Review

SCIEX protein esi
Whole protein <t>ESI-MS</t> and LC-MS/MS characterization of <t>HMGB1</t> isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.
Protein Esi, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/protein esi/product/SCIEX
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
protein esi - by Bioz Stars, 2020-09
86/100 stars

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1) Product Images from "High Mobility Group Box-1 (HMGB1) Participates in the Pathogenesis of Alcoholic Liver Disease (ALD) *"

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

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M114.552141

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

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

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

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

Related Articles

Mass Spectrometry:

Article Title: High Mobility Group Box-1 (HMGB1) Participates in the Pathogenesis of Alcoholic Liver Disease (ALD) *
Article Snippet: .. Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 was performed as described previously by whole protein ESI or tandem mass spectrometry (MS/MS) ( ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc., Framingham, MA). .. Peptide analysis was determined using an AB Sciex QTRAP 5500 equipped with a NanoSpray II source by in-line liquid chromatography using a U3000 HPLC system (Dionex, Sunnyvale, CA), connected to a 180-μm × 20-mm nanoAcquity UPLC C18 trap column and a 75-μm × 15-cm nanoAcquity UPLC BEH130 C18 column (Waters, Milford, MA) via reducing unions.

Article Title: DAMP Signaling is a Key Pathway Inducing Immune Modulation after Brain Injury
Article Snippet: .. Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 were determined as described previously by whole protein electrospray ionization or tandem mass spectrometry ( ; ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc.). .. Peptide analysis was determined using an AB Sciex QTRAP 5500 equipped with a NanoSpray II source by in-line liquid chromatography using a U3000 HPLC System (Dionex), connected to a 180 μm × 20 mm nanoAcquity UPLC C18 trap column and a 75 μm × 15 cm nanoAcquity UPLC BEH130 C18 column via reducing unions.

Tandem Mass Spectroscopy:

Article Title: High Mobility Group Box-1 (HMGB1) Participates in the Pathogenesis of Alcoholic Liver Disease (ALD) *
Article Snippet: .. Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 was performed as described previously by whole protein ESI or tandem mass spectrometry (MS/MS) ( ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc., Framingham, MA). .. Peptide analysis was determined using an AB Sciex QTRAP 5500 equipped with a NanoSpray II source by in-line liquid chromatography using a U3000 HPLC system (Dionex, Sunnyvale, CA), connected to a 180-μm × 20-mm nanoAcquity UPLC C18 trap column and a 75-μm × 15-cm nanoAcquity UPLC BEH130 C18 column (Waters, Milford, MA) via reducing unions.

Article Title: Molecular isoforms of high-mobility group box 1 are mechanistic biomarkers for epilepsy
Article Snippet: .. Characterization of whole protein molecular weights, acetylated lysine residues, or redox modifications on cysteine residues within HMGB1 were determined by whole protein electrospray ionization or MS-MS as described previously ( , ) using either an AB Sciex QTRAP 5500 or an AB Sciex TripleTOF 5600 (Sciex Inc.). .. Peptide analysis was determined using an AB Sciex QTRAP 5500 equipped with a NanoSpray II source by in-line liquid chromatography using a U3000 HPLC System (Dionex, Thermo Fisher UK Ltd.) connected to a 180 μm × 20 mm nanoAcquity UPLC C18 trap column and a 75 μm × 15 cm nanoAcquity UPLC BEH130 C18 column via reducing unions.

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    SCIEX protein esi
    Whole protein <t>ESI-MS</t> and LC-MS/MS characterization of <t>HMGB1</t> isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.
    Protein Esi, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protein esi/product/SCIEX
    Average 86 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    protein esi - by Bioz Stars, 2020-09
    86/100 stars
      Buy from Supplier

    86
    SCIEX esi ms ms proteins
    Whole protein <t>ESI-MS</t> and LC-MS/MS characterization of <t>HMGB1</t> isoforms in healthy volunteers and in patients with ALD. Representative spectra of whole protein ESI-MS of HMGB1 isoforms isolated from serum of healthy volunteers ( A ) or patients with ALD ( B ) are shown. Molecular weights and a schematic representation of each isoform are indicated on each spectra where required. Representative spectra of the tandem MS characterization of a peptide containing lysine residues (Lys-28, -29, and -30) within NLS1 ( C ) and lysine residues (Lys-180, -182, -183, -184, and -185) within NLS2 ( D ) after Glu-C digestion of the 25,467- and 25,549-Da human HMGB1 isoforms following extraction from the serum of ALD patients are shown. HMGB1 was enzymatically cleaved with endopeptidase Glu-C to confirm the presence or absence of acetyl modifications on specific lysine residues (shown as K(Ac) ) as described under “Experimental Procedures.” The one-letter amino acid code is given for each peptide sequence, and b and y ions are labeled with molecular weights and amino acid code where appropriate. Data are representative of either 10 healthy volunteers or 10 ALD patients.
    Esi Ms Ms Proteins, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/esi ms ms proteins/product/SCIEX
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    esi ms ms proteins - by Bioz Stars, 2020-09
    86/100 stars
      Buy from Supplier

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

    Journal: The Journal of Biological Chemistry

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

    doi: 10.1074/jbc.M114.552141

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

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

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

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

    Journal: The Journal of Biological Chemistry

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

    doi: 10.1074/jbc.M114.552141

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

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

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