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Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a <t>Mascot</t> search engine (Matrix Science) through the <t>BioTools</t> 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p
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1) Product Images from "Outer Membrane Protein of Gut Commensal Microorganism Induces Autoantibody Production and Extra-Intestinal Gland Inflammation in Mice"

Article Title: Outer Membrane Protein of Gut Commensal Microorganism Induces Autoantibody Production and Extra-Intestinal Gland Inflammation in Mice

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19103241

Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a Mascot search engine (Matrix Science) through the BioTools 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p
Figure Legend Snippet: Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a Mascot search engine (Matrix Science) through the BioTools 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p

Techniques Used: Polyacrylamide Gel Electrophoresis, Western Blot, Mouse Assay, Mass Spectrometry, Peptide Mass Fingerprinting, Injection

2) Product Images from "Long-chain saturated fatty acids induce annexin II translocation to detergent-resistant membranes"

Article Title: Long-chain saturated fatty acids induce annexin II translocation to detergent-resistant membranes

Journal: Biochemical Journal

doi: 10.1042/BJ20031083

SDS/PAGE of DRM with or without stearate treatment and identification of the 36 kDa protein by MS ( A ) Human breast cancer cells (Hs578T) were incubated with or without 50 μM stearate for 6 h, lysed and DRM and DSM were prepared as described in the Experimental section. Proteins were resolved by SDS/PAGE and stained with Coomassie Blue. Molecular-mass standards are indicated in kDa. The arrow indicates the band (approx. 36 kDa), which was excised for enzymic digestion by trypsin and subsequent MS analysis. ( B ) The gel slice from SDS/polyacrylamide was excised and subjected to in-gel digestion by trypsin. After digestion, a portion of the supernatant was removed and analysed by high-accuracy peptide mass mapping using MALDI–TOF-MS analysis. The band excised from the gel contained a single identifiable component. ( C ) The peptide masses obtained by MALDI–TOF-MS were used to search the NCBI database using MASCOT search engine from Matrixscience.com. The two peptide masses with the highest scores (accession numbers 4757756 and 113948) indicated that the 36 kDa protein was annexin II.
Figure Legend Snippet: SDS/PAGE of DRM with or without stearate treatment and identification of the 36 kDa protein by MS ( A ) Human breast cancer cells (Hs578T) were incubated with or without 50 μM stearate for 6 h, lysed and DRM and DSM were prepared as described in the Experimental section. Proteins were resolved by SDS/PAGE and stained with Coomassie Blue. Molecular-mass standards are indicated in kDa. The arrow indicates the band (approx. 36 kDa), which was excised for enzymic digestion by trypsin and subsequent MS analysis. ( B ) The gel slice from SDS/polyacrylamide was excised and subjected to in-gel digestion by trypsin. After digestion, a portion of the supernatant was removed and analysed by high-accuracy peptide mass mapping using MALDI–TOF-MS analysis. The band excised from the gel contained a single identifiable component. ( C ) The peptide masses obtained by MALDI–TOF-MS were used to search the NCBI database using MASCOT search engine from Matrixscience.com. The two peptide masses with the highest scores (accession numbers 4757756 and 113948) indicated that the 36 kDa protein was annexin II.

Techniques Used: SDS Page, Mass Spectrometry, Incubation, Staining

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Article Snippet: .. Mass spectrometry data analysis After pre-processing the raw data with Mascot Distiller software (version 2.3, Matrix Science, London, UK), obtained peak lists were used to search the nonredundant protein database of the National Centre for Biotechnology Information (NCBI-NR) (23919380 sequences; 8216485116 residues) using the Mascot search engine (version 2.4, 8-processors onsite license) (Matrix Science) with the following search parameters: taxonomy restriction—Viridiplantae (Green Plants, 1249273 sequences), enzyme specificity—trypsin, permitted number of missed cleavages—1, fixed modification—carbamidomethylation (C), variable modifications—carboxymethyl (K), oxidation (M), protein mass—unrestricted, peptide mass tolerance—±30 ppm, fragment mass tolerance—±0.6 Da. ..

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Mass Spectrometry:

Article Title: Maize proteomic responses to separate or overlapping soil drought and two-spotted spider mite stresses
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Software:

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    Matrix Science mascot search engine
    Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a <t>Mascot</t> search engine (Matrix Science) through the <t>BioTools</t> 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p
    Mascot Search Engine, supplied by Matrix Science, used in various techniques. Bioz Stars score: 93/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mascot search engine/product/Matrix Science
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    Matrix Science mascot 2 3 02 search engine
    Identification and analysis of DEPs from roots and leaves in cotton. (A) Total spectra, spectra, unique spectra, peptides, unique peptide, and proteins identified from iTRAQ proteomic analysis. (B) Identified proteins were grouped according to the protein mass. (C) Number of peptides that match to proteins as indicated by MASCOT 2.3.02.
    Mascot 2 3 02 Search Engine, supplied by Matrix Science, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 5 article reviews
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    Matrix Science mascot search engine ms ms ion search program
    Sequence analysis of Flag-LC3B G120A by MALDI ISD. Flag-LC3B G120A expression vector was transfected into HEK293 cell for 48 hours. Cells were harvested and lysed with protease inhibitor cocktail. The lysates were centrifuged at 10,000 g for 30 min. Supernatants were then used for affinity purification of Flag-LC3B G120A by Flag antibody conjugated beads in column according to the proposed protocol. A, 20 µl of elution (from total 1 ml) from Flag antibody based affinity column was loaded onto 12.5% of SDS-polyacrylamide gel. Gel was stained with PageBlue Protein Staining Solution. Elution number 2 and 3 were combined and concentrated. Purified Flag-LC3B G120A was used to run MALDI ISD. Intact mass spectra are shown in B and in-source decay spectra are shown in C . For database searching selected ISD fragments (* in the spectra) were used as virtual precursors and submitted to the <t>Mascot</t> <t>search</t> <t>engine</t> <t>MS/MS</t> <t>ion</t> search <t>program</t> (Matrix Science, Ltd. Version 2.3) through the Shimadzu Biotech Launchpad software. D, peptide view of Mascot Search results MS/MS Fragmentation of N-terminal: MDYKDHDGDYKDHDIDYKDDDDKLQVDPSEKTFKQRRTFEQRVED (Found in IPI00953817; Data file: Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5622.8801; Ions Score: 168 Expect: 2.1e-012; Matches : 28/88 fragment ions using 47 most intense peaks.). E, peptide view of Mascot Search results: MS/MS Fragmentation of C-terminal: LLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFAMKLSV(Found in IPI00953817; Data file Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5017.6143; Ions Score: 34 Expect: 53;Matches : 30/88 fragment ions using 134 most intense peaks.). F, Theoretical fragment ions for the peptide sequence. The matched fragment ions are highlighted in red typed. G, Protein view: Match to: IPI00953817 Score: 297. Found in search of Automatically uploaded data. Nominal mass (M r ): 17870; Calculated pI value: 5.38. NCBI BLAST search of IPI00953817 against nr Unformatted sequence string for pasting into other applications. Sequence Coverage: 59%. Matched peptides shown in Bold Red. The N-terminal 3xFlag tag and C-terminal last five amino acids of Flag-LC3B G120A are underlined. The downward pointing arrow shows the LC3B start amino acid in the recombinant protein (first amino acid methionine was removed in the fusion protein). The arrow pointing upward shows the G120A point mutation in the Flag-LC3B G120A .
    Mascot Search Engine Ms Ms Ion Search Program, supplied by Matrix Science, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Matrix Science s pneumoniae
    Proteomic analysis of S. <t>pneumoniae</t> after YycF overproduction.
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    Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a Mascot search engine (Matrix Science) through the BioTools 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p

    Journal: International Journal of Molecular Sciences

    Article Title: Outer Membrane Protein of Gut Commensal Microorganism Induces Autoantibody Production and Extra-Intestinal Gland Inflammation in Mice

    doi: 10.3390/ijms19103241

    Figure Lengend Snippet: Immunogenic protein in E. coli -treated mouse model. Cell surface proteins of E. coli were separated on 2-D PAGE ( A ). Western blotting of 2-D gel-transferred nitrocellulose membrane was probed with serum of E. coli -treated mouse ( B ), or serum of mouse treated with PBS alone ( C ). Representative membranes of similar Western blotting results with sera of three sets of mice are shown. A spot of 41 kDa/pI 6.24 in E. coli -surface extract reacting with sera from E. coli -treated mouse was excised from the 2-D gel (arrow head in A). OmpA was identified by MALDI-TOF/MS using peptide mass fingerprinting (Matrix Science, London, UK) and the non-redundant National Center for Biotechnology Information (NCBI) database (US National Library of Medicine, Bethesda, MD, USA) with a Mascot search engine (Matrix Science) through the BioTools 3.0 interface (Bruker Daltonics, Billerica, MA, USA). Matched peptides from the MS-fit data are shown in bold red ( D ). Anti-OmpA antibodies in sera of mice were compared between those of E. coli -treated mice ( n = 5), and those of PBS-treated mice ( n = 5) at indicated time after the final injection ( p = 0.02 at 1 month, p

    Article Snippet: Peptide mass fingerprint (Matrix Science) was conducted using the non-redundant NCBI database (US National Library of Medicine) with MASCOT search engine (Matrix Science), through BioTools 3.0 interface (Bruker Daltonics).

    Techniques: Polyacrylamide Gel Electrophoresis, Western Blot, Mouse Assay, Mass Spectrometry, Peptide Mass Fingerprinting, Injection

    Identification and analysis of DEPs from roots and leaves in cotton. (A) Total spectra, spectra, unique spectra, peptides, unique peptide, and proteins identified from iTRAQ proteomic analysis. (B) Identified proteins were grouped according to the protein mass. (C) Number of peptides that match to proteins as indicated by MASCOT 2.3.02.

    Journal: PLoS ONE

    Article Title: iTRAQ-Based Quantitative Proteomic Analysis of Cotton Roots and Leaves Reveals Pathways Associated with Salt Stress

    doi: 10.1371/journal.pone.0148487

    Figure Lengend Snippet: Identification and analysis of DEPs from roots and leaves in cotton. (A) Total spectra, spectra, unique spectra, peptides, unique peptide, and proteins identified from iTRAQ proteomic analysis. (B) Identified proteins were grouped according to the protein mass. (C) Number of peptides that match to proteins as indicated by MASCOT 2.3.02.

    Article Snippet: iTRAQ protein identification and quantification Protein identification and quantification was performed using the Mascot 2.3.02 search engine (Matrix Science, Boston, MA).

    Techniques:

    Sequence analysis of Flag-LC3B G120A by MALDI ISD. Flag-LC3B G120A expression vector was transfected into HEK293 cell for 48 hours. Cells were harvested and lysed with protease inhibitor cocktail. The lysates were centrifuged at 10,000 g for 30 min. Supernatants were then used for affinity purification of Flag-LC3B G120A by Flag antibody conjugated beads in column according to the proposed protocol. A, 20 µl of elution (from total 1 ml) from Flag antibody based affinity column was loaded onto 12.5% of SDS-polyacrylamide gel. Gel was stained with PageBlue Protein Staining Solution. Elution number 2 and 3 were combined and concentrated. Purified Flag-LC3B G120A was used to run MALDI ISD. Intact mass spectra are shown in B and in-source decay spectra are shown in C . For database searching selected ISD fragments (* in the spectra) were used as virtual precursors and submitted to the Mascot search engine MS/MS ion search program (Matrix Science, Ltd. Version 2.3) through the Shimadzu Biotech Launchpad software. D, peptide view of Mascot Search results MS/MS Fragmentation of N-terminal: MDYKDHDGDYKDHDIDYKDDDDKLQVDPSEKTFKQRRTFEQRVED (Found in IPI00953817; Data file: Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5622.8801; Ions Score: 168 Expect: 2.1e-012; Matches : 28/88 fragment ions using 47 most intense peaks.). E, peptide view of Mascot Search results: MS/MS Fragmentation of C-terminal: LLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFAMKLSV(Found in IPI00953817; Data file Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5017.6143; Ions Score: 34 Expect: 53;Matches : 30/88 fragment ions using 134 most intense peaks.). F, Theoretical fragment ions for the peptide sequence. The matched fragment ions are highlighted in red typed. G, Protein view: Match to: IPI00953817 Score: 297. Found in search of Automatically uploaded data. Nominal mass (M r ): 17870; Calculated pI value: 5.38. NCBI BLAST search of IPI00953817 against nr Unformatted sequence string for pasting into other applications. Sequence Coverage: 59%. Matched peptides shown in Bold Red. The N-terminal 3xFlag tag and C-terminal last five amino acids of Flag-LC3B G120A are underlined. The downward pointing arrow shows the LC3B start amino acid in the recombinant protein (first amino acid methionine was removed in the fusion protein). The arrow pointing upward shows the G120A point mutation in the Flag-LC3B G120A .

    Journal: PLoS ONE

    Article Title: The Carboxyl-Terminal Amino Acids Render Pro-Human LC3B Migration Similar to Lipidated LC3B in SDS-PAGE

    doi: 10.1371/journal.pone.0074222

    Figure Lengend Snippet: Sequence analysis of Flag-LC3B G120A by MALDI ISD. Flag-LC3B G120A expression vector was transfected into HEK293 cell for 48 hours. Cells were harvested and lysed with protease inhibitor cocktail. The lysates were centrifuged at 10,000 g for 30 min. Supernatants were then used for affinity purification of Flag-LC3B G120A by Flag antibody conjugated beads in column according to the proposed protocol. A, 20 µl of elution (from total 1 ml) from Flag antibody based affinity column was loaded onto 12.5% of SDS-polyacrylamide gel. Gel was stained with PageBlue Protein Staining Solution. Elution number 2 and 3 were combined and concentrated. Purified Flag-LC3B G120A was used to run MALDI ISD. Intact mass spectra are shown in B and in-source decay spectra are shown in C . For database searching selected ISD fragments (* in the spectra) were used as virtual precursors and submitted to the Mascot search engine MS/MS ion search program (Matrix Science, Ltd. Version 2.3) through the Shimadzu Biotech Launchpad software. D, peptide view of Mascot Search results MS/MS Fragmentation of N-terminal: MDYKDHDGDYKDHDIDYKDDDDKLQVDPSEKTFKQRRTFEQRVED (Found in IPI00953817; Data file: Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5622.8801; Ions Score: 168 Expect: 2.1e-012; Matches : 28/88 fragment ions using 47 most intense peaks.). E, peptide view of Mascot Search results: MS/MS Fragmentation of C-terminal: LLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFAMKLSV(Found in IPI00953817; Data file Automatically uploaded data; Average mass of neutral peptide Mr(calc): 5017.6143; Ions Score: 34 Expect: 53;Matches : 30/88 fragment ions using 134 most intense peaks.). F, Theoretical fragment ions for the peptide sequence. The matched fragment ions are highlighted in red typed. G, Protein view: Match to: IPI00953817 Score: 297. Found in search of Automatically uploaded data. Nominal mass (M r ): 17870; Calculated pI value: 5.38. NCBI BLAST search of IPI00953817 against nr Unformatted sequence string for pasting into other applications. Sequence Coverage: 59%. Matched peptides shown in Bold Red. The N-terminal 3xFlag tag and C-terminal last five amino acids of Flag-LC3B G120A are underlined. The downward pointing arrow shows the LC3B start amino acid in the recombinant protein (first amino acid methionine was removed in the fusion protein). The arrow pointing upward shows the G120A point mutation in the Flag-LC3B G120A .

    Article Snippet: For database searching selected ISD fragments (* in the spectra) were used as virtual precursors and submitted to the Mascot search engine MS/MS ion search program (Matrix Science, Ltd.

    Techniques: Sequencing, Expressing, Plasmid Preparation, Transfection, Protease Inhibitor, Affinity Purification, Affinity Column, Staining, Purification, Mass Spectrometry, Software, Recombinant, Mutagenesis

    Proteomic analysis of S. pneumoniae after YycF overproduction.

    Journal: Journal of Bacteriology

    Article Title: Evidence that the Essential Response Regulator YycF in Streptococcus pneumoniae Modulates Expression of Fatty Acid Biosynthesis Genes and Alters Membrane Composition †

    doi: 10.1128/JB.187.7.2357-2367.2005

    Figure Lengend Snippet: Proteomic analysis of S. pneumoniae after YycF overproduction.

    Article Snippet: Peptide peak lists were searched against databases of S. pneumoniae (Mascot software; Matrix Science).

    Techniques:

    Transcriptional analysis of S. pneumoniae after induction of yycF .

    Journal: Journal of Bacteriology

    Article Title: Evidence that the Essential Response Regulator YycF in Streptococcus pneumoniae Modulates Expression of Fatty Acid Biosynthesis Genes and Alters Membrane Composition †

    doi: 10.1128/JB.187.7.2357-2367.2005

    Figure Lengend Snippet: Transcriptional analysis of S. pneumoniae after induction of yycF .

    Article Snippet: Peptide peak lists were searched against databases of S. pneumoniae (Mascot software; Matrix Science).

    Techniques:

    Fatty acid biosynthesis in S. pneumoniae . (A) Pathway of saturated (SFA) and unsaturated (UFA) fatty acid biosynthesis in pneumococci. (B) Pneumococcal biosynthetic gene cluster. Black arrows indicate genes with increased protein levels, as detected by

    Journal: Journal of Bacteriology

    Article Title: Evidence that the Essential Response Regulator YycF in Streptococcus pneumoniae Modulates Expression of Fatty Acid Biosynthesis Genes and Alters Membrane Composition †

    doi: 10.1128/JB.187.7.2357-2367.2005

    Figure Lengend Snippet: Fatty acid biosynthesis in S. pneumoniae . (A) Pathway of saturated (SFA) and unsaturated (UFA) fatty acid biosynthesis in pneumococci. (B) Pneumococcal biosynthetic gene cluster. Black arrows indicate genes with increased protein levels, as detected by

    Article Snippet: Peptide peak lists were searched against databases of S. pneumoniae (Mascot software; Matrix Science).

    Techniques:

    Growth curve analysis and detection of GFP fluorescence. Cultures of S. pneumoniae JNR7/87(pPL100) (•) and JNR7/87(pLS1RGFP) (○) in exponential growth phase were induced with maltose at time point zero. The optical densities of the cultures

    Journal: Journal of Bacteriology

    Article Title: Evidence that the Essential Response Regulator YycF in Streptococcus pneumoniae Modulates Expression of Fatty Acid Biosynthesis Genes and Alters Membrane Composition †

    doi: 10.1128/JB.187.7.2357-2367.2005

    Figure Lengend Snippet: Growth curve analysis and detection of GFP fluorescence. Cultures of S. pneumoniae JNR7/87(pPL100) (•) and JNR7/87(pLS1RGFP) (○) in exponential growth phase were induced with maltose at time point zero. The optical densities of the cultures

    Article Snippet: Peptide peak lists were searched against databases of S. pneumoniae (Mascot software; Matrix Science).

    Techniques: Fluorescence

    Proteomic analysis of long-term maltose induction of S. pneumoniae strains JNR7/87(pLS1RGFP) and JNR7/87(pPL100). Protein extracts of long-term induced JNR7/87(pLS1RGFP) (control strain) (A) and JNR7/87(pPL100) (B) cultures were analyzed by 2D gel electrophoresis

    Journal: Journal of Bacteriology

    Article Title: Evidence that the Essential Response Regulator YycF in Streptococcus pneumoniae Modulates Expression of Fatty Acid Biosynthesis Genes and Alters Membrane Composition †

    doi: 10.1128/JB.187.7.2357-2367.2005

    Figure Lengend Snippet: Proteomic analysis of long-term maltose induction of S. pneumoniae strains JNR7/87(pLS1RGFP) and JNR7/87(pPL100). Protein extracts of long-term induced JNR7/87(pLS1RGFP) (control strain) (A) and JNR7/87(pPL100) (B) cultures were analyzed by 2D gel electrophoresis

    Article Snippet: Peptide peak lists were searched against databases of S. pneumoniae (Mascot software; Matrix Science).

    Techniques: Two-Dimensional Gel Electrophoresis, Electrophoresis