quadrupole time of flight tripletof 5600 mass spectrometer  (SCIEX)

 
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    Structured Review

    SCIEX quadrupole time of flight tripletof 5600 mass spectrometer
    Workflow for ErbB2 targeted proteomics using multiprotease digestion and high resolution mass spectrometry quantitation. ErbB2 immunopurified from four 15 cm plates of untreated SK-BR-3 cells was pooled into a single sample. The sample was split into 12 aliquots and separated by SDS-PAGE. Triplicate in-gel digestion was performed using either trypsin, Asp-N, chymotrypsin, or a double digestion with trypsin plus Asp-N. Each sample was analyzed using an AB SCIEX <t>TripleTOF</t> 5600 mass spectrometer. Two approaches for high resolution LC-MS/MS quantitation were employed, MS1 Filtering and SWATH MS2 acquisition.
    Quadrupole Time Of Flight Tripletof 5600 Mass Spectrometer, supplied by SCIEX, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/quadrupole time of flight tripletof 5600 mass spectrometer/product/SCIEX
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    quadrupole time of flight tripletof 5600 mass spectrometer - by Bioz Stars, 2022-05
    99/100 stars

    Images

    1) Product Images from "Label-Free Quantitation and Mapping of the ErbB2 Tumor Receptor by Multiple Protease Digestion with Data-Dependent (MS1) and Data-Independent (MS2) Acquisitions"

    Article Title: Label-Free Quantitation and Mapping of the ErbB2 Tumor Receptor by Multiple Protease Digestion with Data-Dependent (MS1) and Data-Independent (MS2) Acquisitions

    Journal: International Journal of Proteomics

    doi: 10.1155/2013/791985

    Workflow for ErbB2 targeted proteomics using multiprotease digestion and high resolution mass spectrometry quantitation. ErbB2 immunopurified from four 15 cm plates of untreated SK-BR-3 cells was pooled into a single sample. The sample was split into 12 aliquots and separated by SDS-PAGE. Triplicate in-gel digestion was performed using either trypsin, Asp-N, chymotrypsin, or a double digestion with trypsin plus Asp-N. Each sample was analyzed using an AB SCIEX TripleTOF 5600 mass spectrometer. Two approaches for high resolution LC-MS/MS quantitation were employed, MS1 Filtering and SWATH MS2 acquisition.
    Figure Legend Snippet: Workflow for ErbB2 targeted proteomics using multiprotease digestion and high resolution mass spectrometry quantitation. ErbB2 immunopurified from four 15 cm plates of untreated SK-BR-3 cells was pooled into a single sample. The sample was split into 12 aliquots and separated by SDS-PAGE. Triplicate in-gel digestion was performed using either trypsin, Asp-N, chymotrypsin, or a double digestion with trypsin plus Asp-N. Each sample was analyzed using an AB SCIEX TripleTOF 5600 mass spectrometer. Two approaches for high resolution LC-MS/MS quantitation were employed, MS1 Filtering and SWATH MS2 acquisition.

    Techniques Used: Mass Spectrometry, Quantitation Assay, SDS Page, Liquid Chromatography with Mass Spectroscopy

    2) Product Images from "Platform-independent and Label-free Quantitation of Proteomic Data Using MS1 Extracted Ion Chromatograms in Skyline"

    Article Title: Platform-independent and Label-free Quantitation of Proteomic Data Using MS1 Extracted Ion Chromatograms in Skyline

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.017707

    Standard concentration curves for stable isotope-labeled and acetyllysine containing peptides. A and B , YAPVA Kac DLAS R ( A , succinate dehydrogenase complex, subunit A) and LVSSVSDLP KacR ( B , 3-hydroxy-3-methylglutaryl-CoA synthase 2) spanning a concentration range from 4 attomoles to 25 femtomoles. Peptides were diluted into either a simple matrix ( red triangles , 25 fmol “six protein mix”) or a complex matrix ( blue circles , mitochondrial lysate from mouse liver, 0.3 μg on column), and acquired on a TripleTOF 5600 mass spectrometer in triplicates. MS1 filtered peak area curves for precursor ions M with m/z 621.8395 2+ ( A , heavy YAPVA Kac DLAS R ) and m/z 626.8604 2+ ( B , heavy LVSSVSDLP KacR ). Weighted regression lines and calculated LOQ are indicated (also see supplemental Table S3 ), and weighted linear regression slopes were determined as 1.03 and 1.03 for YAP and 0.99 and 1.00 for LVS peptides in the different matrices. C , peak area CVs across three replicates for each concentration point (0.037–25 fmol) in complex matrix are shown for six targeted acetyllysine peptides with 20 and 30% CV cutoffs indicated (also see supplemental Figs. S6, C and F ). D , high throughput analysis showing peak area CVs for 366 peptides across 27 independently acquired runs in a complex mitochondrial lysate background matrix. Peak area CVs are displayed against MS1 filtered precursor m/z .
    Figure Legend Snippet: Standard concentration curves for stable isotope-labeled and acetyllysine containing peptides. A and B , YAPVA Kac DLAS R ( A , succinate dehydrogenase complex, subunit A) and LVSSVSDLP KacR ( B , 3-hydroxy-3-methylglutaryl-CoA synthase 2) spanning a concentration range from 4 attomoles to 25 femtomoles. Peptides were diluted into either a simple matrix ( red triangles , 25 fmol “six protein mix”) or a complex matrix ( blue circles , mitochondrial lysate from mouse liver, 0.3 μg on column), and acquired on a TripleTOF 5600 mass spectrometer in triplicates. MS1 filtered peak area curves for precursor ions M with m/z 621.8395 2+ ( A , heavy YAPVA Kac DLAS R ) and m/z 626.8604 2+ ( B , heavy LVSSVSDLP KacR ). Weighted regression lines and calculated LOQ are indicated (also see supplemental Table S3 ), and weighted linear regression slopes were determined as 1.03 and 1.03 for YAP and 0.99 and 1.00 for LVS peptides in the different matrices. C , peak area CVs across three replicates for each concentration point (0.037–25 fmol) in complex matrix are shown for six targeted acetyllysine peptides with 20 and 30% CV cutoffs indicated (also see supplemental Figs. S6, C and F ). D , high throughput analysis showing peak area CVs for 366 peptides across 27 independently acquired runs in a complex mitochondrial lysate background matrix. Peak area CVs are displayed against MS1 filtered precursor m/z .

    Techniques Used: Concentration Assay, Labeling, Mass Spectrometry, High Throughput Screening Assay

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    SCIEX qqtof instrument
    Application of the two tandem mass spectral libraries to the analysis of wastewater samples collected at the WWTP in Innsbruck. Ten influent samples were analyzed. The <t>nontargeted</t> LC-MS/MS data was acquired on a <t>QqTOF</t> instrument using DDA. ( a ) Overview on the number of compounds identified in different compound classes, as well as ( b ) a Venn diagram characterizing the number of identified compounds obtained with the two libraries tested are provided.
    Qqtof Instrument, 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/qqtof instrument/product/SCIEX
    Average 86 stars, based on 1 article reviews
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    qqtof instrument - by Bioz Stars, 2022-05
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    SCIEX tripletof 5600 m z value
    Detection of truncated PtHMGR protein activity  in vitro  with a 1 ml reaction mixture (2.5 mM K 2 HPO 4 , 5 mM KCl, 1 mM EDTA, 5 mM DTT, 1 mg/ml PtHMGR, 3 mM NADPH as a coenzyme, and 0.3 mM of HMG-CoA as a substrate, pH 7.2).  (A)  Total ion chromatogram of reaction products of high-performance liquid chromatography (HPLC). The peak at retention time 2.2 was attributed to target production (MVA).  (B)  Extracted ion chromatography (XIC) analysis.  (C)  Time-of-flight mass spectrometry (TOFMS) analysis. The SCIEX TripleTOF 5600+ m/z value was 131.0710, consistent with MVA.
    Tripletof 5600 M Z Value, supplied by SCIEX, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Application of the two tandem mass spectral libraries to the analysis of wastewater samples collected at the WWTP in Innsbruck. Ten influent samples were analyzed. The nontargeted LC-MS/MS data was acquired on a QqTOF instrument using DDA. ( a ) Overview on the number of compounds identified in different compound classes, as well as ( b ) a Venn diagram characterizing the number of identified compounds obtained with the two libraries tested are provided.

    Journal: Metabolites

    Article Title: Annotating Nontargeted LC-HRMS/MS Data with Two Complementary Tandem Mass Spectral Libraries

    doi: 10.3390/metabo9010003

    Figure Lengend Snippet: Application of the two tandem mass spectral libraries to the analysis of wastewater samples collected at the WWTP in Innsbruck. Ten influent samples were analyzed. The nontargeted LC-MS/MS data was acquired on a QqTOF instrument using DDA. ( a ) Overview on the number of compounds identified in different compound classes, as well as ( b ) a Venn diagram characterizing the number of identified compounds obtained with the two libraries tested are provided.

    Article Snippet: The two sample sets were submitted to nontargeted LC-MS/MS on a QqTOF instrument (TripleTOF 5600+, Sciex, Framingham, MA, USA).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    Application of the two tandem mass spectral libraries to systematic toxicological analysis of 10 authentic plasma samples. Nontargeted LC-MS/MS data was acquired on a QqTOF instrument using DDA. ( a ) Overview on the number of compounds identified in different compound classes via the combined use of the two libraries tested, and ( b ) the Venn diagram illustrating the number of identified compounds obtained with the two libraries tested.

    Journal: Metabolites

    Article Title: Annotating Nontargeted LC-HRMS/MS Data with Two Complementary Tandem Mass Spectral Libraries

    doi: 10.3390/metabo9010003

    Figure Lengend Snippet: Application of the two tandem mass spectral libraries to systematic toxicological analysis of 10 authentic plasma samples. Nontargeted LC-MS/MS data was acquired on a QqTOF instrument using DDA. ( a ) Overview on the number of compounds identified in different compound classes via the combined use of the two libraries tested, and ( b ) the Venn diagram illustrating the number of identified compounds obtained with the two libraries tested.

    Article Snippet: The two sample sets were submitted to nontargeted LC-MS/MS on a QqTOF instrument (TripleTOF 5600+, Sciex, Framingham, MA, USA).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    Detection of truncated PtHMGR protein activity  in vitro  with a 1 ml reaction mixture (2.5 mM K 2 HPO 4 , 5 mM KCl, 1 mM EDTA, 5 mM DTT, 1 mg/ml PtHMGR, 3 mM NADPH as a coenzyme, and 0.3 mM of HMG-CoA as a substrate, pH 7.2).  (A)  Total ion chromatogram of reaction products of high-performance liquid chromatography (HPLC). The peak at retention time 2.2 was attributed to target production (MVA).  (B)  Extracted ion chromatography (XIC) analysis.  (C)  Time-of-flight mass spectrometry (TOFMS) analysis. The SCIEX TripleTOF 5600+ m/z value was 131.0710, consistent with MVA.

    Journal: Frontiers in Plant Science

    Article Title: Characterization and Function of 3-Hydroxy-3-Methylglutaryl-CoA Reductase in Populus trichocarpa: Overexpression of PtHMGR Enhances Terpenoids in Transgenic Poplar

    doi: 10.3389/fpls.2019.01476

    Figure Lengend Snippet: Detection of truncated PtHMGR protein activity in vitro with a 1 ml reaction mixture (2.5 mM K 2 HPO 4 , 5 mM KCl, 1 mM EDTA, 5 mM DTT, 1 mg/ml PtHMGR, 3 mM NADPH as a coenzyme, and 0.3 mM of HMG-CoA as a substrate, pH 7.2). (A) Total ion chromatogram of reaction products of high-performance liquid chromatography (HPLC). The peak at retention time 2.2 was attributed to target production (MVA). (B) Extracted ion chromatography (XIC) analysis. (C) Time-of-flight mass spectrometry (TOFMS) analysis. The SCIEX TripleTOF 5600+ m/z value was 131.0710, consistent with MVA.

    Article Snippet: Functional Identification of PtHMGR In Vitro The activity of purified truncated PtHMGR protein was analyzed using HPLC/MS ( and ), and the special peak or mass fragmentation pattern of target production (MVA) was detected at 2.2 min, and the SCIEX TripleTOF 5600+ m/z value was 131.0710 ( ).

    Techniques: Activity Assay, In Vitro, High Performance Liquid Chromatography, Ion Chromatography, Mass Spectrometry

    Standard concentration curves for stable isotope-labeled and acetyllysine containing peptides. A and B , YAPVA Kac DLAS R ( A , succinate dehydrogenase complex, subunit A) and LVSSVSDLP KacR ( B , 3-hydroxy-3-methylglutaryl-CoA synthase 2) spanning a concentration range from 4 attomoles to 25 femtomoles. Peptides were diluted into either a simple matrix ( red triangles , 25 fmol “six protein mix”) or a complex matrix ( blue circles , mitochondrial lysate from mouse liver, 0.3 μg on column), and acquired on a TripleTOF 5600 mass spectrometer in triplicates. MS1 filtered peak area curves for precursor ions M with m/z 621.8395 2+ ( A , heavy YAPVA Kac DLAS R ) and m/z 626.8604 2+ ( B , heavy LVSSVSDLP KacR ). Weighted regression lines and calculated LOQ are indicated (also see supplemental Table S3 ), and weighted linear regression slopes were determined as 1.03 and 1.03 for YAP and 0.99 and 1.00 for LVS peptides in the different matrices. C , peak area CVs across three replicates for each concentration point (0.037–25 fmol) in complex matrix are shown for six targeted acetyllysine peptides with 20 and 30% CV cutoffs indicated (also see supplemental Figs. S6, C and F ). D , high throughput analysis showing peak area CVs for 366 peptides across 27 independently acquired runs in a complex mitochondrial lysate background matrix. Peak area CVs are displayed against MS1 filtered precursor m/z .

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Platform-independent and Label-free Quantitation of Proteomic Data Using MS1 Extracted Ion Chromatograms in Skyline

    doi: 10.1074/mcp.M112.017707

    Figure Lengend Snippet: Standard concentration curves for stable isotope-labeled and acetyllysine containing peptides. A and B , YAPVA Kac DLAS R ( A , succinate dehydrogenase complex, subunit A) and LVSSVSDLP KacR ( B , 3-hydroxy-3-methylglutaryl-CoA synthase 2) spanning a concentration range from 4 attomoles to 25 femtomoles. Peptides were diluted into either a simple matrix ( red triangles , 25 fmol “six protein mix”) or a complex matrix ( blue circles , mitochondrial lysate from mouse liver, 0.3 μg on column), and acquired on a TripleTOF 5600 mass spectrometer in triplicates. MS1 filtered peak area curves for precursor ions M with m/z 621.8395 2+ ( A , heavy YAPVA Kac DLAS R ) and m/z 626.8604 2+ ( B , heavy LVSSVSDLP KacR ). Weighted regression lines and calculated LOQ are indicated (also see supplemental Table S3 ), and weighted linear regression slopes were determined as 1.03 and 1.03 for YAP and 0.99 and 1.00 for LVS peptides in the different matrices. C , peak area CVs across three replicates for each concentration point (0.037–25 fmol) in complex matrix are shown for six targeted acetyllysine peptides with 20 and 30% CV cutoffs indicated (also see supplemental Figs. S6, C and F ). D , high throughput analysis showing peak area CVs for 366 peptides across 27 independently acquired runs in a complex mitochondrial lysate background matrix. Peak area CVs are displayed against MS1 filtered precursor m/z .

    Article Snippet: In addition, mass spectrometric data from the TripleTOF 5600 and QSTAR Elite was also analyzed using the database search engine ProteinPilot ( ) (AB SCIEX Beta 4.1.46, revision 460) with the Paragon algorithm (4.0.0.0, 459).

    Techniques: Concentration Assay, Labeling, Mass Spectrometry, High Throughput Screening Assay

    Response curve for a digested 6 protein mix spiked into a complex matrix ( C. elegans whole cell lysate). (A) The mixture of six predigested proteins was spiked into digested C. elegans whole cell lysate (1 μ g/ μ L and 1 μ g on column) at 8 concentrations from 15 attomol/ μ L to 62.5 femtomol/ μ L (0 = blank, 0.015–62.5 fmol/ μ L, loading 1 μ L sample on column). Two replicate concentration curves were acquired on the TripleTOF 5600 (QqTOF in PRM mode, top) and on the QTRAP 5500 (QQQ in SRM mode, bottom), respectively. Peak areas of extracted fragment ion transitions are summed per peptide. Curves are displayed for peptides HLVDEPQNLIK 2+ ( m / z 653.36) and YSTDVSVDEVK 2+ ( m / z 621.30), respectively. (B) Peak area CV display for triplicate acquisitions of a digested 6 protein mix (50 fmol/ μ L) spiked into a complex C. elegans matrix (1 μ g/ μ ).

    Journal: Analytical chemistry

    Article Title: Multiplexed, Scheduled, High-Resolution Parallel Reaction Monitoring on a Full Scan QqTOF Instrument with Integrated Data-Dependent and Targeted Mass Spectrometric Workflows

    doi: 10.1021/acs.analchem.5b02983

    Figure Lengend Snippet: Response curve for a digested 6 protein mix spiked into a complex matrix ( C. elegans whole cell lysate). (A) The mixture of six predigested proteins was spiked into digested C. elegans whole cell lysate (1 μ g/ μ L and 1 μ g on column) at 8 concentrations from 15 attomol/ μ L to 62.5 femtomol/ μ L (0 = blank, 0.015–62.5 fmol/ μ L, loading 1 μ L sample on column). Two replicate concentration curves were acquired on the TripleTOF 5600 (QqTOF in PRM mode, top) and on the QTRAP 5500 (QQQ in SRM mode, bottom), respectively. Peak areas of extracted fragment ion transitions are summed per peptide. Curves are displayed for peptides HLVDEPQNLIK 2+ ( m / z 653.36) and YSTDVSVDEVK 2+ ( m / z 621.30), respectively. (B) Peak area CV display for triplicate acquisitions of a digested 6 protein mix (50 fmol/ μ L) spiked into a complex C. elegans matrix (1 μ g/ μ ).

    Article Snippet: Most of the PRM studies have used Orbitraps or hybrid Q-Exactive instruments (Thermo) for data acquisition, although, to our knowledge, this is the first large-scale PRM study carried out on an orthogonal quadrupole time-of-flight instrument (QqTOF), or TripleTOF 5600 (SCIEX).

    Techniques: Concentration Assay

    Standard concentration curves for stable isotope-labeled and acetyllysine-containing peptides. (A) Stable isotope-labeled acetylated peptide LVSSVSDLP Kac R* (HMGCS2) was monitored spanning a concentration range from 63 attomol/ μ L to 25 femtomol/ μ L ( m / z 626.86 2+ ), acquiring three replicates (1 μ L sample on column). Peptides were spiked into a simple matrix containing a six digested protein mix at 25 fmol/ μ L each, and acquired on a TripleTOF 5600 mass spectrometer (QqTOF) in PRM mode in triplicate. Extracted peak areas for the top 5 MS/MS fragment ions were summed per peptide. (B) Peak area CVs across three replicates for each concentration point (0.063–25 fmol/ μ ); K * = 13 C 6 15 N 2 -Lys and R * = 13 C 6 15 N 4 -Arg.

    Journal: Analytical chemistry

    Article Title: Multiplexed, Scheduled, High-Resolution Parallel Reaction Monitoring on a Full Scan QqTOF Instrument with Integrated Data-Dependent and Targeted Mass Spectrometric Workflows

    doi: 10.1021/acs.analchem.5b02983

    Figure Lengend Snippet: Standard concentration curves for stable isotope-labeled and acetyllysine-containing peptides. (A) Stable isotope-labeled acetylated peptide LVSSVSDLP Kac R* (HMGCS2) was monitored spanning a concentration range from 63 attomol/ μ L to 25 femtomol/ μ L ( m / z 626.86 2+ ), acquiring three replicates (1 μ L sample on column). Peptides were spiked into a simple matrix containing a six digested protein mix at 25 fmol/ μ L each, and acquired on a TripleTOF 5600 mass spectrometer (QqTOF) in PRM mode in triplicate. Extracted peak areas for the top 5 MS/MS fragment ions were summed per peptide. (B) Peak area CVs across three replicates for each concentration point (0.063–25 fmol/ μ ); K * = 13 C 6 15 N 2 -Lys and R * = 13 C 6 15 N 4 -Arg.

    Article Snippet: Most of the PRM studies have used Orbitraps or hybrid Q-Exactive instruments (Thermo) for data acquisition, although, to our knowledge, this is the first large-scale PRM study carried out on an orthogonal quadrupole time-of-flight instrument (QqTOF), or TripleTOF 5600 (SCIEX).

    Techniques: Concentration Assay, Labeling, Mass Spectrometry