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q10 (strong anion exchange) proteinchip arrays  (Ciphergen inc)

 
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    Ciphergen inc q10 (strong anion exchange) proteinchip arrays
    Q10 (Strong Anion Exchange) Proteinchip Arrays, supplied by Ciphergen inc, 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/product/q10+(strong+anion+exchange)+proteinchip+arrays/sax+2+proteinchip+/pm18384103-57-9-28
    Average 90 stars, based on 1 article reviews
    q10 (strong anion exchange) proteinchip arrays - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Incubation:

    Article Title: Mass Spectometry-Based Protein Patterns in the Diagnosis of Sepsis/Systemic Inflammatory Response Syndrome
    Article Snippet: .. Early differential diagnosis of systemic inflammatory reactions in critically ill patients is essential for timely implementation of lifesaving therapies.. Despite many efforts made, reliable biomarkers to discriminate between infectious and noninfectious causes of systemic inflammatory response syndrome (SIRS) are currently not available.. Recent advances in mass spectrometryYbased methods have raised hopes that identification of spectral patterns from serum/ plasma samples can be instrumental in this context. .. Early differential diagnosis of systemic inflammatory reactions in critically ill patients is essential for timely implementation of lifesaving therapies.. Despite many efforts made, reliable biomarkers to discriminate between infectious and noninfectious causes of systemic inflammatory response syndrome (SIRS) are currently not available.. Recent advances in mass spectrometryYbased methods have raised hopes that identification of spectral patterns from serum/ plasma samples can be instrumental in this context.

    Protein Purification:

    Article Title: A Proteomic Analysis Reveals Differential Regulation of the σS-Dependent yciGFE(katN) Locus by YncC and H-NS in Salmonella and Escherichia coli K-12
    Article Snippet: .. A strong anion exchange ProteinChip array (Q10, Bio-Rad), for which the complementary resin Q Ceramic HYPERD F (BioSepra-Pall, Cergy St Christophe, France) can be used for protein purification, was employed to capture negatively charged proteins. ..



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    q10 (strong anion exchanger) proteinchip array  (Bio-Rad)
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    Bio-Rad q10 (strong anion exchanger) proteinchip array
    Mass spectra of representative single biomarker candidate proteins in CSF under different pH conditions. Protein profiles of the MMD and control groups were generated using <t>Q10</t> (strong anion exchanger) array. For each pH condition, the upper two spectra are protein profiles obtained between m/z 2,000 and 10,000, and the lower two spectra are expansions showing the peak intensities around m/z 4473, 4588 and 4476 for pH 5, 7 and 9, respectively. All representative peaks (red arrows) are larger for the MMD than control group under each pH condition, as determined by SELDI-TOF-MS.
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    strong anion exchange proteinchip array  (Bio-Rad)
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    Bio-Rad strong anion exchange proteinchip array
    FIG. 1. Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto <t>Q10</t> <t>ProteinChip</t> Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (A) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 l) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.
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    strong anion exchange proteinchip array (q10  (Bio-Rad)
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    Bio-Rad strong anion exchange proteinchip array (q10
    Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto <t>Q10</t> <t>ProteinChip</t> Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 μl) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.
    Strong Anion Exchange Proteinchip Array (Q10, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    q10 (strong anion exchange) proteinchip arrays  (Ciphergen inc)
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    Ciphergen inc q10 (strong anion exchange) proteinchip arrays
    Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto <t>Q10</t> <t>ProteinChip</t> Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 μl) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.
    Q10 (Strong Anion Exchange) Proteinchip Arrays, supplied by Ciphergen inc, 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/product/q10+(strong+anion+exchange)+proteinchip+arrays/sax+2+proteinchip+/pm18384103-57-9-28
    Average 90 stars, based on 1 article reviews
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    strong anion exchange (q10) proteinchip array  (Ciphergen inc)
    90
    Ciphergen inc strong anion exchange (q10) proteinchip array
    Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto <t>Q10</t> <t>ProteinChip</t> Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 μl) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.
    Strong Anion Exchange (Q10) Proteinchip Array, supplied by Ciphergen inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    strong anion exchange (q10) proteinchip array - by Bioz Stars, 2026-09
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    Mass spectra of representative single biomarker candidate proteins in CSF under different pH conditions. Protein profiles of the MMD and control groups were generated using Q10 (strong anion exchanger) array. For each pH condition, the upper two spectra are protein profiles obtained between m/z 2,000 and 10,000, and the lower two spectra are expansions showing the peak intensities around m/z 4473, 4588 and 4476 for pH 5, 7 and 9, respectively. All representative peaks (red arrows) are larger for the MMD than control group under each pH condition, as determined by SELDI-TOF-MS.

    Journal: BMC Neurology

    Article Title: Identification of novel biomarker candidates by proteomic analysis of cerebrospinal fluid from patients with moyamoya disease using SELDI-TOF-MS

    doi: 10.1186/1471-2377-10-112

    Figure Lengend Snippet: Mass spectra of representative single biomarker candidate proteins in CSF under different pH conditions. Protein profiles of the MMD and control groups were generated using Q10 (strong anion exchanger) array. For each pH condition, the upper two spectra are protein profiles obtained between m/z 2,000 and 10,000, and the lower two spectra are expansions showing the peak intensities around m/z 4473, 4588 and 4476 for pH 5, 7 and 9, respectively. All representative peaks (red arrows) are larger for the MMD than control group under each pH condition, as determined by SELDI-TOF-MS.

    Article Snippet: Q10 (strong anion exchanger) ProteinChip array (Bio-Rad Laboratories) was used for protein profile analysis.

    Techniques: Biomarker Assay, Generated

    CART analysis using peaks obtained by SELDI-TOF-MS to discriminate between patients with MMD and control patients. The decision tree was constructed using CSF samples from 32 patients with MMD and control patients. The classification is determined starting at the roof node, following by appropriate splitting decisions based on the peak intensity at each node. If the peak intensity is lower than the cutoff intensity value, the left node is selected. This splitting process is continued until no further classification is achieved and terminal nodes are produced. Using m/z 4473, 2406 and 6338 peaks (pH 5), m/z 4588 and 7250 peaks (pH 7), and m/z 4746 and 1044 peaks (pH 9), CART for Q10 ProteinChip was applied to identify patients with MMD and control patients. The analysis correctly classified all 20 patients with MMD under pH 5 condition and 19 of 20 under the pH 7 and 9 conditions; all 12 control patients were classified under all pH conditions.

    Journal: BMC Neurology

    Article Title: Identification of novel biomarker candidates by proteomic analysis of cerebrospinal fluid from patients with moyamoya disease using SELDI-TOF-MS

    doi: 10.1186/1471-2377-10-112

    Figure Lengend Snippet: CART analysis using peaks obtained by SELDI-TOF-MS to discriminate between patients with MMD and control patients. The decision tree was constructed using CSF samples from 32 patients with MMD and control patients. The classification is determined starting at the roof node, following by appropriate splitting decisions based on the peak intensity at each node. If the peak intensity is lower than the cutoff intensity value, the left node is selected. This splitting process is continued until no further classification is achieved and terminal nodes are produced. Using m/z 4473, 2406 and 6338 peaks (pH 5), m/z 4588 and 7250 peaks (pH 7), and m/z 4746 and 1044 peaks (pH 9), CART for Q10 ProteinChip was applied to identify patients with MMD and control patients. The analysis correctly classified all 20 patients with MMD under pH 5 condition and 19 of 20 under the pH 7 and 9 conditions; all 12 control patients were classified under all pH conditions.

    Article Snippet: Q10 (strong anion exchanger) ProteinChip array (Bio-Rad Laboratories) was used for protein profile analysis.

    Techniques: Construct, Produced

    FIG. 1. Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto Q10 ProteinChip Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (A) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 l) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.

    Journal: Molecular & Cellular Proteomics

    Article Title: A Proteomic Analysis Reveals Differential Regulation of the σS-Dependent yciGFE(katN) Locus by YncC and H-NS in Salmonella and Escherichia coli K-12

    doi: 10.1074/mcp.m110.002493

    Figure Lengend Snippet: FIG. 1. Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto Q10 ProteinChip Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (A) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 l) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.

    Article Snippet: A strong anion exchange ProteinChip array (Q10, Bio-Rad), for which the complementary resin Q Ceramic HYPERD F (BioSepra-Pall, Cergy St Christophe, France) can be used for protein purification, was employed to capture negatively charged proteins.

    Techniques: Mutagenesis, Mass Spectrometry, Purification, Molecular Weight, Sequencing

    FIG. 4. Expression of the yciGFE locus in E. coli K-12 strains. A, SELDI-TOF-MS profiles of E. coli MG1655 and its mutant derivatives using the Q10 ProteinChip array. Clear lysates from MG1655 (WT) and its mutants MG655hns, MG1655hnsyciE, and MG1655hnsyciF were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were de- tected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. Normalized mass (m/z) for each peak (in Daltons (Da)) is demonstrated on the x-axis, whereas intensity (A) is plotted on the y-axis. A laser energy of 3200 nJ was used. The relevant portion of the spectra is shown. The arrows indicate the YciE and YciF proteins. B, Expression of the yciE-lacZ fusion in the E. coli strains indicated was determined in overnight LB cultures at 37 °C. Lanes 1 to 5: (1) MC4100 yciE-lacZ, (2) MC4100hns yciE-lacZ, (3) MC4100mcbR yciE-lacZ, (4) MC4100hnsmcbR yciE-lacZ, (5) MC4100hnsrpoS yciE-lacZ. Lanes 6 to 15: MC4100 yciE-lacZ harbor- ing pCABg (6), pmcbRHIS (7), pQE30 (12), and pyncCHIS (13); MC4100hns yciE-lacZ harboring pCABg (8), pmcbRHIS (9), pQE30 (14), and pyncCHIS (15); and MC4100hnsmcbR yciE-lacZ harboring pCABg (10), and pmcbRHIS (11).

    Journal: Molecular & Cellular Proteomics

    Article Title: A Proteomic Analysis Reveals Differential Regulation of the σS-Dependent yciGFE(katN) Locus by YncC and H-NS in Salmonella and Escherichia coli K-12

    doi: 10.1074/mcp.m110.002493

    Figure Lengend Snippet: FIG. 4. Expression of the yciGFE locus in E. coli K-12 strains. A, SELDI-TOF-MS profiles of E. coli MG1655 and its mutant derivatives using the Q10 ProteinChip array. Clear lysates from MG1655 (WT) and its mutants MG655hns, MG1655hnsyciE, and MG1655hnsyciF were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were de- tected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. Normalized mass (m/z) for each peak (in Daltons (Da)) is demonstrated on the x-axis, whereas intensity (A) is plotted on the y-axis. A laser energy of 3200 nJ was used. The relevant portion of the spectra is shown. The arrows indicate the YciE and YciF proteins. B, Expression of the yciE-lacZ fusion in the E. coli strains indicated was determined in overnight LB cultures at 37 °C. Lanes 1 to 5: (1) MC4100 yciE-lacZ, (2) MC4100hns yciE-lacZ, (3) MC4100mcbR yciE-lacZ, (4) MC4100hnsmcbR yciE-lacZ, (5) MC4100hnsrpoS yciE-lacZ. Lanes 6 to 15: MC4100 yciE-lacZ harbor- ing pCABg (6), pmcbRHIS (7), pQE30 (12), and pyncCHIS (13); MC4100hns yciE-lacZ harboring pCABg (8), pmcbRHIS (9), pQE30 (14), and pyncCHIS (15); and MC4100hnsmcbR yciE-lacZ harboring pCABg (10), and pmcbRHIS (11).

    Article Snippet: A strong anion exchange ProteinChip array (Q10, Bio-Rad), for which the complementary resin Q Ceramic HYPERD F (BioSepra-Pall, Cergy St Christophe, France) can be used for protein purification, was employed to capture negatively charged proteins.

    Techniques: Expressing, Mutagenesis, Mass Spectrometry

    Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto Q10 ProteinChip Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 μl) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: A Proteomic Analysis Reveals Differential Regulation of the ? S -Dependent yciGFE ( katN ) Locus by YncC and H-NS in Salmonella and Escherichia coli K-12

    doi: 10.1074/mcp.M110.002493

    Figure Lengend Snippet: Identification of protein targets for YncC regulation in Salmonella. A, Selective capture of proteins from cell lysates of S. Typhimurium wild-type and mutant strains onto Q10 ProteinChip Array. Clear lysates from ATCC14028 (WT) and its mutant derivatives ATCCyncC, ATCCrpoS and ATCCyci were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. The normalized mass (m/z) for each peak (in Da) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. Extracts were examined several times at different laser energies, and energies of 4500 nJ and 3200 nJ were found to be optimal for detection of peaks 1, 2, and peak 3, respectively. To pick out peak 3, the first pass peak detection was performed with a s/n threshold of two instead of five (Experimental Procedures). The relevant portion of the spectra from a representative experiment is shown. Similar results were obtained in two other experiments. The arrows indicate proteins expressed at different levels in the wild-type and the mutant strains. B, Partial purification of proteins of interest for identification by mass spectrometry. The pH 5 fraction (25 μl) of the Q Ceramic HYPERD F exchange resin from lysates of 2: ATCCkatN-lacZ, 3: ATCC14028; 4: ATCC-F1; 5: ATCC-F12; and 6: ATCCrpoS were loaded on the gel. 1: molecular weight markers (in kDa). The stars indicate the protein bands that were excised from the gel and identified as the YciF and YciE proteins by mass spectrometry. C, Schematic representation of the yciGFE(katN) loci in Salmonella (STM) and E. coli K-12 (ECO). The molecular sizes of the gene products are indicated in Daltons (Da). D, The yciG promoters in Salmonella and E. coli K-12. The relevant portion of the sequence in Salmonella ATCC14028 (STM) and E. coli MG1655 (ECO) is shown.

    Article Snippet: A strong anion exchange ProteinChip array (Q10, Bio-Rad), for which the complementary resin Q Ceramic HYPERD F (BioSepra-Pall, Cergy St Christophe, France) can be used for protein purification, was employed to capture negatively charged proteins.

    Techniques: Mutagenesis, Mass Spectrometry, Purification, Molecular Weight, Sequencing

    Expression of the yciGFE locus in E. coli K-12 strains. A, SELDI-TOF-MS profiles of E. coli MG1655 and its mutant derivatives using the Q10 ProteinChip array. Clear lysates from MG1655 (WT) and its mutants MG655hns, MG1655hnsyciE, and MG1655hnsyciF were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. Normalized mass (m/z) for each peak (in Daltons (Da)) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. A laser energy of 3200 nJ was used. The relevant portion of the spectra is shown. The arrows indicate the YciE and YciF proteins. B, Expression of the yciE-lacZ fusion in the E. coli strains indicated was determined in overnight LB cultures at 37 °C. Lanes 1 to 5: (1) MC4100 yciE-lacZ, (2) MC4100hns yciE-lacZ, (3) MC4100mcbR yciE-lacZ, (4) MC4100hnsmcbR yciE-lacZ, (5) MC4100hnsrpoS yciE-lacZ. Lanes 6 to 15: MC4100 yciE-lacZ harboring pCABg (6), pmcbRHIS (7), pQE30 (12), and pyncCHIS (13); MC4100hns yciE-lacZ harboring pCABg (8), pmcbRHIS (9), pQE30 (14), and pyncCHIS (15); and MC4100hnsmcbR yciE-lacZ harboring pCABg (10), and pmcbRHIS (11).

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: A Proteomic Analysis Reveals Differential Regulation of the ? S -Dependent yciGFE ( katN ) Locus by YncC and H-NS in Salmonella and Escherichia coli K-12

    doi: 10.1074/mcp.M110.002493

    Figure Lengend Snippet: Expression of the yciGFE locus in E. coli K-12 strains. A, SELDI-TOF-MS profiles of E. coli MG1655 and its mutant derivatives using the Q10 ProteinChip array. Clear lysates from MG1655 (WT) and its mutants MG655hns, MG1655hnsyciE, and MG1655hnsyciF were applied to the surface of a Q10 ProteinChip as described in the Experimental Procedures section. The captured proteins were detected using surface enhanced laser desorption/ionization (SELDI) time-of-flight mass spectrometry. Normalized mass (m/z) for each peak (in Daltons (Da)) is demonstrated on the x-axis, whereas intensity (μA) is plotted on the y-axis. A laser energy of 3200 nJ was used. The relevant portion of the spectra is shown. The arrows indicate the YciE and YciF proteins. B, Expression of the yciE-lacZ fusion in the E. coli strains indicated was determined in overnight LB cultures at 37 °C. Lanes 1 to 5: (1) MC4100 yciE-lacZ, (2) MC4100hns yciE-lacZ, (3) MC4100mcbR yciE-lacZ, (4) MC4100hnsmcbR yciE-lacZ, (5) MC4100hnsrpoS yciE-lacZ. Lanes 6 to 15: MC4100 yciE-lacZ harboring pCABg (6), pmcbRHIS (7), pQE30 (12), and pyncCHIS (13); MC4100hns yciE-lacZ harboring pCABg (8), pmcbRHIS (9), pQE30 (14), and pyncCHIS (15); and MC4100hnsmcbR yciE-lacZ harboring pCABg (10), and pmcbRHIS (11).

    Article Snippet: A strong anion exchange ProteinChip array (Q10, Bio-Rad), for which the complementary resin Q Ceramic HYPERD F (BioSepra-Pall, Cergy St Christophe, France) can be used for protein purification, was employed to capture negatively charged proteins.

    Techniques: Expressing, Mutagenesis, Mass Spectrometry