ltq velos tandem mass spectrometer  (Thermo Fisher)


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    Thermo Fisher ltq velos tandem mass spectrometer
    Ltq Velos Tandem Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq velos tandem mass spectrometer/product/Thermo Fisher
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ltq velos tandem mass spectrometer - by Bioz Stars, 2020-05
    84/100 stars

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    Mass Spectrometry:

    Article Title: Indirect sexual selection drives rapid sperm protein evolution in abalone
    Article Snippet: .. Individually purified proteins were analyzed by LC/MS-MS using data-dependent acquisition on an LTQ Velos tandem mass spectrometer (Thermo Scientific, Waltham, MA) for determination of intact protein and fragment ion masses. .. Sequence analysis of FITZAP and estimation of molecular evolutionary rates Draft genome assemblies are available for disk abalone (Haliotis discus ) ( ) and red abalone (H. rufescens ) ( ).

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    Article Title: Indirect sexual selection drives rapid sperm protein evolution in abalone
    Article Snippet: .. Individually purified proteins were analyzed by LC/MS-MS using data-dependent acquisition on an LTQ Velos tandem mass spectrometer (Thermo Scientific, Waltham, MA) for determination of intact protein and fragment ion masses. .. Sequence analysis of FITZAP and estimation of molecular evolutionary rates Draft genome assemblies are available for disk abalone (Haliotis discus ) ( ) and red abalone (H. rufescens ) ( ).

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    Thermo Fisher ltq orbitrap velos mass spectrometer
    Overview of phosphoproteome upon palmella formation of Dunaliella salina . (A) Overlap of phosphorylation sites among three biological replicates. All phosphorylated sites having a reported localization probability of at least 0.75 were considered to be assigned to a specific residue, and we refer to these as phosphorylated sites. 137 phosphorylated sites were identified. (B) Among the 137 identified sites, 54 phosphorylated sites were quantified. Three biological replicates for each sample were performed by <t>LTQ-Orbitrap</t> <t>Velos</t> MS/MS analysis, and the obtained results were given in Supplemental Table S3 . We compared the overlap of identified phosphorylated sites and quantified phosphorylated sites among the three biological replicates. Biol.1/2/3 represent the first/second/third biological replicate. (C) Functional category of 100 identified phosphoproteins (containing 137 identified phosphorylated sites) in D. salina . The numbers inside the parentheses shows how many phosphorylated sites identified in phosphoproteins. (D) Functional category of 40 quantified phosphoproteins (containing 54 quantified phosphorylated sites). The numbers inside the parentheses show how many phosphorylated sites quantified in phosphoproteins. (E) A representative MS/MS spectra of 35 salinity-responsive phosphoproteins. The peptide GYLTDLK from PRP1 splicing factor (gi|307110542).
    Ltq Orbitrap Velos Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 253 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq orbitrap velos mass spectrometer/product/Thermo Fisher
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    99
    Thermo Fisher ltq orbitrap velos
    Venn Diagrams depicting the total number of unique T . pallidum proteins identified per rabbit biological replicate (N = 3) analyzed by (A) Matrix-assisted laser desorption/ionization time of flight and (B) Electrospray Ionization <t>LTQ-</t> <t>Orbitrap</t> <t>Velos</t> MS/MS. All spectra were screened against the UniProt databases (ID: UP000000811 UP000014259), with a peptide and protein identification confidence interval of 95%. There was considerable overlap between the complementary MS analytical methods whereby an additional 42 treponemal proteins were found in the Orbitrap analysis as depicted in diagram (C).
    Ltq Orbitrap Velos, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 743 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 743 article reviews
    Price from $9.99 to $1999.99
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    Overview of phosphoproteome upon palmella formation of Dunaliella salina . (A) Overlap of phosphorylation sites among three biological replicates. All phosphorylated sites having a reported localization probability of at least 0.75 were considered to be assigned to a specific residue, and we refer to these as phosphorylated sites. 137 phosphorylated sites were identified. (B) Among the 137 identified sites, 54 phosphorylated sites were quantified. Three biological replicates for each sample were performed by LTQ-Orbitrap Velos MS/MS analysis, and the obtained results were given in Supplemental Table S3 . We compared the overlap of identified phosphorylated sites and quantified phosphorylated sites among the three biological replicates. Biol.1/2/3 represent the first/second/third biological replicate. (C) Functional category of 100 identified phosphoproteins (containing 137 identified phosphorylated sites) in D. salina . The numbers inside the parentheses shows how many phosphorylated sites identified in phosphoproteins. (D) Functional category of 40 quantified phosphoproteins (containing 54 quantified phosphorylated sites). The numbers inside the parentheses show how many phosphorylated sites quantified in phosphoproteins. (E) A representative MS/MS spectra of 35 salinity-responsive phosphoproteins. The peptide GYLTDLK from PRP1 splicing factor (gi|307110542).

    Journal: Frontiers in Plant Science

    Article Title: Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics

    doi: 10.3389/fpls.2017.00810

    Figure Lengend Snippet: Overview of phosphoproteome upon palmella formation of Dunaliella salina . (A) Overlap of phosphorylation sites among three biological replicates. All phosphorylated sites having a reported localization probability of at least 0.75 were considered to be assigned to a specific residue, and we refer to these as phosphorylated sites. 137 phosphorylated sites were identified. (B) Among the 137 identified sites, 54 phosphorylated sites were quantified. Three biological replicates for each sample were performed by LTQ-Orbitrap Velos MS/MS analysis, and the obtained results were given in Supplemental Table S3 . We compared the overlap of identified phosphorylated sites and quantified phosphorylated sites among the three biological replicates. Biol.1/2/3 represent the first/second/third biological replicate. (C) Functional category of 100 identified phosphoproteins (containing 137 identified phosphorylated sites) in D. salina . The numbers inside the parentheses shows how many phosphorylated sites identified in phosphoproteins. (D) Functional category of 40 quantified phosphoproteins (containing 54 quantified phosphorylated sites). The numbers inside the parentheses show how many phosphorylated sites quantified in phosphoproteins. (E) A representative MS/MS spectra of 35 salinity-responsive phosphoproteins. The peptide GYLTDLK from PRP1 splicing factor (gi|307110542).

    Article Snippet: The LTQ-Orbitrap Velos mass spectrometer (Thermo Fisher Scientific) was operated in data-dependent MS/MS acquisition mode.

    Techniques: Mass Spectrometry, Functional Assay

    Urinary ApoA-Ib contains 3 extra amino acids at the N-Terminal end compared to plasmatic mature ApoA-I (form 0). Urine ( A ) and plasma samples ( B ) of ApoA-Ib positive FSGS recurrent patients were resolved in 24-cm 2D SDS-PAGE gels using a 4–7 Ph range and stained with colloidal coomassie. The complete 2DE gels obtained using urine and plasma samples are depicted in panels A and B, respectively. A zoom box of the ApoA-I region detailing the spots analysed in urine (panel A) and in plasma (panel B) is shown. Retinol-binding protein 4 (RET4) is highlighted as a reference spot. The spots corresponding to different forms of ApoA-I were excised, digested with trypsin and run on an LTQ-Orbitrap mass spectrometer. The sequence obtained in each case is shown in bold red and the detected N-Terminal end of each form is marked with an arrow. As can be observed in panel A, ApoA-Ib sequence contained 3 extra aminoacids (WQQ, underlined) at the N-Terminal end that were not present in the ApoA-I form 0.These three amino acids are part of the propeptide sequence that was observed complete in plasma proApoA-I (form +2) (RHFWQQ, underlined) (Panel B). A representative MS/MS scan of the N-terminal peptide of ApoA-Ib can be found in Supplemental Fig. 3 . RET4: Retinol binding protein 4 .

    Journal: Scientific Reports

    Article Title: A misprocessed form of Apolipoprotein A-I is specifically associated with recurrent Focal Segmental Glomerulosclerosis

    doi: 10.1038/s41598-020-58197-y

    Figure Lengend Snippet: Urinary ApoA-Ib contains 3 extra amino acids at the N-Terminal end compared to plasmatic mature ApoA-I (form 0). Urine ( A ) and plasma samples ( B ) of ApoA-Ib positive FSGS recurrent patients were resolved in 24-cm 2D SDS-PAGE gels using a 4–7 Ph range and stained with colloidal coomassie. The complete 2DE gels obtained using urine and plasma samples are depicted in panels A and B, respectively. A zoom box of the ApoA-I region detailing the spots analysed in urine (panel A) and in plasma (panel B) is shown. Retinol-binding protein 4 (RET4) is highlighted as a reference spot. The spots corresponding to different forms of ApoA-I were excised, digested with trypsin and run on an LTQ-Orbitrap mass spectrometer. The sequence obtained in each case is shown in bold red and the detected N-Terminal end of each form is marked with an arrow. As can be observed in panel A, ApoA-Ib sequence contained 3 extra aminoacids (WQQ, underlined) at the N-Terminal end that were not present in the ApoA-I form 0.These three amino acids are part of the propeptide sequence that was observed complete in plasma proApoA-I (form +2) (RHFWQQ, underlined) (Panel B). A representative MS/MS scan of the N-terminal peptide of ApoA-Ib can be found in Supplemental Fig. 3 . RET4: Retinol binding protein 4 .

    Article Snippet: The tryptic peptides were extracted in a two-step procedure using sonication and were analyzed on an LTQ-Orbitrap Velos Pro mass spectrometer (Thermo Scientific) coupled to a nanoAcquity UPLC system (Waters) using a 45 min method.

    Techniques: SDS Page, Staining, Two-Dimensional Gel Electrophoresis, Binding Assay, Mass Spectrometry, Sequencing, Tandem Mass Spectroscopy

    Reversed-phase profile and spectra of three gymnosperm taxa. ( A ) RP-HPLC profiles of two Larix × marschlinsii ovular secretion samples. One sample was collected at the beginning of the secretion period (red trace) and the other collected seven days later (black trace). In each experiment, 20 μL of whole sample was loaded onto a C8 column and separation occurred in a linear gradient of increasing acetonitrile concentration. UV absorbance of eluent was monitored at 220 nm. Asterisks denote fractions shown by SDS-PAGE to contain protein. (B) MS/MS fragmentation data. Tryptic peptide from chitinase protein found in Welwitschia mirabilis pollination drops introduced by nanospray electrospray ionization into a QSTAR Pulsar I Hybrid Quadrupole-TOF MS/MS mass spectrometer (Applied Biosystems/MDS Sciex). Data were managed with PEAKS (Bioinformatics Solutions) and Bioanalyst software (Applied Biosystems/MDS Sciex). (C) MS/MS fragmentation data. Peptide (VYSGDTDGRVP) from serine carboxypeptidase II-3 protein found in Ephedra monosperma pollination drops introduced by nanospray electrospray ionization into the LTQ Orbitrap Velos mass spectrometer (Thermo Fisher Scientific). Data were managed with Proteome Discoverer (Thermo Fisher Scientific) and Mascot version 2.2.1 (Matrix Science) software.

    Journal: Applications in Plant Sciences

    Article Title: Application of proteomics to the study of pollination drops 1

    doi: 10.3732/apps.1300008

    Figure Lengend Snippet: Reversed-phase profile and spectra of three gymnosperm taxa. ( A ) RP-HPLC profiles of two Larix × marschlinsii ovular secretion samples. One sample was collected at the beginning of the secretion period (red trace) and the other collected seven days later (black trace). In each experiment, 20 μL of whole sample was loaded onto a C8 column and separation occurred in a linear gradient of increasing acetonitrile concentration. UV absorbance of eluent was monitored at 220 nm. Asterisks denote fractions shown by SDS-PAGE to contain protein. (B) MS/MS fragmentation data. Tryptic peptide from chitinase protein found in Welwitschia mirabilis pollination drops introduced by nanospray electrospray ionization into a QSTAR Pulsar I Hybrid Quadrupole-TOF MS/MS mass spectrometer (Applied Biosystems/MDS Sciex). Data were managed with PEAKS (Bioinformatics Solutions) and Bioanalyst software (Applied Biosystems/MDS Sciex). (C) MS/MS fragmentation data. Peptide (VYSGDTDGRVP) from serine carboxypeptidase II-3 protein found in Ephedra monosperma pollination drops introduced by nanospray electrospray ionization into the LTQ Orbitrap Velos mass spectrometer (Thermo Fisher Scientific). Data were managed with Proteome Discoverer (Thermo Fisher Scientific) and Mascot version 2.2.1 (Matrix Science) software.

    Article Snippet: The second example is an MS/MS spectrum showing a y-ion series from a peptide (VYSGDTDGRVP) from a serine carboxypeptidase II-3 found in E. monosperma pollination drops ( ) that had been generated by tandem mass spectrometry using an LTQ Orbitrap Velos mass spectrometer (Thermo Fisher Scientific).

    Techniques: High Performance Liquid Chromatography, Concentration Assay, SDS Page, Mass Spectrometry, Software

    Venn Diagrams depicting the total number of unique T . pallidum proteins identified per rabbit biological replicate (N = 3) analyzed by (A) Matrix-assisted laser desorption/ionization time of flight and (B) Electrospray Ionization LTQ- Orbitrap Velos MS/MS. All spectra were screened against the UniProt databases (ID: UP000000811 UP000014259), with a peptide and protein identification confidence interval of 95%. There was considerable overlap between the complementary MS analytical methods whereby an additional 42 treponemal proteins were found in the Orbitrap analysis as depicted in diagram (C).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Characterizing the Syphilis-Causing Treponema pallidum ssp. pallidum Proteome Using Complementary Mass Spectrometry

    doi: 10.1371/journal.pntd.0004988

    Figure Lengend Snippet: Venn Diagrams depicting the total number of unique T . pallidum proteins identified per rabbit biological replicate (N = 3) analyzed by (A) Matrix-assisted laser desorption/ionization time of flight and (B) Electrospray Ionization LTQ- Orbitrap Velos MS/MS. All spectra were screened against the UniProt databases (ID: UP000000811 UP000014259), with a peptide and protein identification confidence interval of 95%. There was considerable overlap between the complementary MS analytical methods whereby an additional 42 treponemal proteins were found in the Orbitrap analysis as depicted in diagram (C).

    Article Snippet: The LTQ Orbitrap Velos (Thermo Scientific, San Jose, CA) was set up in a data dependent MS/MS mode where a full scan spectrum (350–5000 m/z, resolution 60000) was followed by a maximum of ten CID tandem mass spectra (100 to 2000 m/z).

    Techniques: Mass Spectrometry