Tsq vantage

Manufactured by Thermo Fisher Scientific

Sourced in United States, Germany, France, United Kingdom

The TSQ Vantage is a triple quadrupole mass spectrometer designed for qualitative and quantitative analysis. It features high-performance ion optics, fast scanning, and robust construction to provide reliable and sensitive results.

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TSQ Vantage triple quadrupole mass spectrometer (74 citations) TSQ Vantage AM (6 citations) TSQ Vantage triple quadrupole (QQQ) mass spectrometer (4 citations) Thermo TSQ Vantage triple quadrupole mass spectrometer (4 citations) TSQ Vantage triple quadrupole (3 citations) TSQ Vantage triple quadrupole MS (3 citations) TSQ Vantage Extended Mass Range Mass Spectrometer (2 citations) TSQ Vantage MS (2 citations) TSQ Vantage triple stage (2 citations) TSQ-Vantage triple-quadrupole instrument (2 citations)

98 protocols using tsq vantage

Targeted Metabolite Profiling Using LC-MS/MS

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For detecting metabolites, a triple-quadrupole mass spectrometer (TSQ Vantage,
Thermo Scientific) coupled to an HPLC was used, which allows one to detect each
metabolite simultaneously using multiple reaction monitoring (MRM). Metabolites
were separated chromatographically using a Synergi Fusion column (150 × 2.0 mm,
4 μm, Phenomenex), using a Shimadzu Prominence HPLC (high-performance liquid
chromatography) autosampler coupled to the mass spectrometer. Extracted
metabolites were measured using targeted LC-MS/MS methods, detailed method
described previously 23 (link)42 (link). A library of common metabolites was
constructed using standards, and metabolites were detected using a TSQ Vantage
(Thermo Scientific) triple quadrupole-linear ion trap mass spectrometer for
quantitative optimized detection of daughter ions upon collision-induced
fragmentation of the parent ion. For each metabolite, parameters for
quantitation of the two most abundant daughter ions (that is, two MRMs per
metabolite) were included. To quantify metabolites, the area under each peak was
quantitated by using the Xcaliber software, inspected for accuracy, and
normalized against total ion count, after which relative amounts were
quantified.

Deshpande A.A., Bhatia M., Laxman S, & Bachhawat A.K. (2017). Thiol trapping and metabolic redistribution of sulfur metabolites enable cells to overcome cysteine overload. Microbial Cell, 4(4), 112-126.

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Quantifying Plant-Derived Alkaloid Compounds

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The PAs in the samples were measured using a LC-MS/MS system consisting of an UHPLC (Ultimate 3000, Thermo Scientific, San Jose, CA, USA) and a Triple Stage Quadrupole mass spectrometer (TSQ Vantage, Thermo Scientific, San Jose, CA, USA), as described previously with minor modifications [21 (link)]. Briefly, chromatographic separation was achieved on 150 × 2.1 mm, 1.9 μm particle sizes, C18 Hypersil Gold column fitted with a guard column (Thermo Scientific, Dreieich, Germany). Eluent A was 100% water with 0.1% formic acid and 5 mM of ammonium formate. Eluent B was 95% methanol and 5% water with 0.1% formic acid and 5 mM of ammonium formate. A stepwise gradient elution was conducted as follows: 0–0.5 min for 95% A/5% B, 7.0 min for 50% A/50% B, 7.5 min for 20% A/80% B, 7.6–9.0 min for 100% B and 9.1–15 min for 95% A/ 5% B. A flow rate of 300 μL/minute was applied and 10 μL of each sample was injected. The column temperature was maintained at 40 °C. Details of the mass parameters are listed in supporting data S1, Table S1.

Chen L., Zhang Q., Yi Z., Chen Y., Xiao W., Su D, & Shi W. (2022). Risk Assessment of (Herbal) Teas Containing Pyrrolizidine Alkaloids (PAs) Based on Margin of Exposure Approach and Relative Potency (REP) Factors. Foods, 11(19), 2946.

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Quantifying G Protein Subunits in Co-IP

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Co-IP samples containing Gβ and Gγ subunits were separated, digested, and analyzed by a TSQ Vantage triple quadrupole mass spectrometer (Thermo Scientific)^{28 (link)}. To allow comparisons between G proteins co-IPed from multiple mice, quantitative Gβ and Gγ subunits detected (fmol) were normalized by the amount of protein (mg) used in co-IPs. The amount of protein used in co-IPs was calculated using the volume of precleared lysate used and the protein concentration of precleared lysate from BCA assay.

Yim Y.Y., Betke K.M., McDonald W.H., Gilsbach R., Chen Y., Hyde K., Wang Q., Hein L, & Hamm H. (2019). The in vivo specificity of synaptic Gβ and Gγ subunits to the α2a adrenergic receptor at CNS synapses. Scientific Reports, 9, 1718.

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Targeted Lipid Analysis via MRM-MS

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Targeted analysis of lipid species was performed with Thermo Xcalibur 4.0 QF2 (ThermoFisher Scientific) using Multiple Reaction Monitoring (MRM) Mass Spectometry (MS)^{20 (link)}. A Triversa NanoMate (Advion, Ithaca, NY, USA) was used to infuse samples onto a TSQ Vantage triple quadrupole mass spectrometer (ThermoFisher Scientific, Waltham, USA). MRM-MS was used to identify and quantify lipid species as previously described^{48 (link)}. Data were converted and quantified relative to standard curves of internal standards that were incorporated to the samples before extraction. At least three independent biological replicates were analyzed, each of which was measured twice with three measurement cycles, leading to six technical replicates. Concentration values of lipid species were normalized to the total amount of inorganic phosphate as determined by colorimetric quantification with ammonium molybdate and ascorbic acid of pentachloroacetic acid hydrolyzed total lipid aliquots. To analyze the significance of the fold difference of each lipid species between two conditions, we performed an paired, two-tailed student’s t-test.

Castanon I., Hannich J.T., Abrami L., Huber F., Dubois M., Müller M., van der Goot F.G, & Gonzalez-Gaitan M. (2020). Wnt-controlled sphingolipids modulate Anthrax Toxin Receptor palmitoylation to regulate oriented mitosis in zebrafish. Nature Communications, 11, 3317.

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Bioavailability of Compound 5a in Mice

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To determine the bioavailability of compound 5a after i.p. injections, 12 WT mice were injected with 20 mg/kg of compound 5a and sacrificed at 12 successive time points. After decapitation, blood was sampled and transferred into BD Microtainer® SST tubes (Becton, Dickinson and Company, Plymouth, UK). Plasma was obtained according to the manufacturer’s protocol and stored at −80 °C.
Using an optimized Ultra Performance Liquid Chromatography with tandem mass spectrometry (UPLC-MS/MS), compound 5a was subsequently quantified in plasma. In short, proteins were precipitated using liquid/liquid extraction with ethyl acetate and supernatant was transferred into 40 µL DMSO/water/acetonitrile (12/44/44). Thereupon, UPLC separation was performed using a C18 column (HSS T3, Waters, Guyancourt, France) and a gradient mobile phase (acetonitrile and water with 0.1% formic acid), followed by triple quadrupole MS (TSQ Vantage, Thermo Scientific) with electrospray ionization. All samples were analyzed in triplicate.

Neumann F., Gourdain S., Albac C., Dekker A.D., Bui L.C., Dairou J., Schmitz-Afonso I., Hue N., Rodrigues-Lima F., Delabar J.M., Potier M.C., Le Caër J.P., Touboul D., Delatour B., Cariou K, & Dodd R.H. (2018). DYRK1A inhibition and cognitive rescue in a Down syndrome mouse model are induced by new fluoro-DANDY derivatives. Scientific Reports, 8, 2859.

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Targeted Quantification of Proteins Using 18O-Labeled Reference

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SRM-based targeted quantification using ¹⁸O-based reference²² was performed for 39 selected proteins. The peptides and SRM transitions was selected and screened as previously described²², and were listed in Supplemental Table 7. At least 6 transitions of each peptide were monitored in initial screening to ensure the confident identification and detection of the targeted peptides. The best two transitions (without interference) for each peptide were selected for final quantification. The predicted collision energies from Skyline were used for all peptides. Prior to LC-SRM analyses, the ¹⁸O-labeled reference sample was spiked into each peptide sample in 1:1 mixing ratio. All peptide samples were analyzed on a Waters nanoACQUITY UPLC system (Waters Corporation, Milford MA) directly coupled to coupled on-line to a triple quadrupole mass spectrometer (TSQ Vantage; Thermo Fisher Scientific) using a 25-cm-long, 75-μm-inner diameter fused silica capillary column. 1 μl aliquots of each sample containing ~ 0.5 μg/μl peptides were injected onto the analytical column with a 40-min linear gradient of 10–50% acetonitrile and 0.1% formic acid. A fixed dwell time of 10 ms and a scan window of 0.002 m/z were employed. All datasets were analyzed by Skyline software. The peak area ratios were used for the evaluation of protein abundance changes.

El Ouaamari A., Zhou J.Y., Liew C.W., Shirakawa J., Dirice E., Gedeon N., Kahraman S., De Jesus D.F., Bhatt S., Kim J.S., Clauss T.R., Camp DG I.I., Smith R.D., Qian W.J, & Kulkarni R.N. (2015). Compensatory Islet Response to Insulin Resistance Revealed by Quantitative Proteomics. Journal of proteome research, 14(8), 3111-3122.

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Quantification of Purine Nucleosides by LC-MS/MS

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MS-MS detection of the analytes and their respective internal standards was accomplished on a Thermo Scientific TSQ Vantage^® triple quadrupole mass spectrometer coupled with a Thermo Scientific Accela 1250^® pump and CTC Analytics HTC PAL^® autosampler. The mobile phase was aqueous with 4% acetonitrile and 0.1% formic acid pumped at a flow rate of 200 μL/min. Chromatographic separation was accomplished with Develosil C₃₀ Reversed-Phase-Aqueous, 140Å, 150–2.0mm, 3μm particle size column purchased from Phenomenex (Torrance, CA). Adenosine, guanosine and inosine analysis was operated in ESI + and the analytes SRM [precursor/product] ⁺ transitions (m/z) were detected as described in Table I. The adenosine+1 m/z transition was used for detection of adenosine to avoid signal saturation at the upper range of quantification.

Jimmerson L.C., Bushman L.R., Ray M.L., Anderson P.L, & Kiser J.J. (2016). A LC-MS/MS method for quantifying adenosine, guanosine and inosine nucleotides in human cells. Pharmaceutical research, 34(1), 73-83.

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Targeted Quantification of Histone Peptides by SRM/MRM MS

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Example 6

SRM/MRM Assay on a Triple Quadrupole Mass Spectrometer for Individual Fragment Peptides

SRM is a MS-based technique for the targeted detection and quantification of previously selected proteotypic peptides with defined fragmentation properties detectable in a highly complex background such as blood-derived serum or plasma.

The quantitative SRM assay described in the following was developed to measure the quantitative levels of unmodified histone-derived peptides generated by tryptic digestion of plasma or serum proteins.

Specific peptides derived from histone H4 and histone H2A, referred to as H4 and H2A, were detected by LC-MS/MS technology (TSQ vantage and TSQ Quantiva mass spectrometers (MS); ThermoFisher Scientific). Identified peptide sequences and fragmentation ions thereof, so-called transitions, for each peptide were found to be useful surrogates for monitoring H4 and H2A protein levels in a blood sample.

Optimization was done on recombinant proteins purchased from Sigma. All possible tryptic peptides were screened and best peptides regarding signal to noise were selected (see Tables 4 and 5). Optimal retention time, dwell time and collision energy for at least 4 best transitions were set up.

Relative quantification and/or absolute quantification can be performed on clinical samples and assay performances were evaluated using Normal curves or Reverse curves.

US11391742B2. Free histone proteins as biomarkers (2022-07-19). B.R.A.H.M.S GMBH [DE]. Inventors: Maryann Stephanie Vogelsang [US], Bryan Krastins [US], Anne Incamps [FR], Andre Schoenichen [DE], Tim Ziera [DE].

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Multiplexed SRM Quantification of Proteins

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SRM assays were developed on a triple-quadrupole mass spectrometer (TSQ Vantage; Thermo Fisher Scientific, USA) using a nanoelectrospray ionization source (nano-ESI, Proxeon Biosystems, FL), as previously described [52 (link)]. Briefly, a 60-minute, three-step gradient was used to load peptides onto the column via an EASY-nLC pump (Proxeon Biosystems, FL), and peptides were analyzed by a multiplexed SRM method using the following parameters: predicted CE values, 0.002 m/z scan width, 0.01 s scan time, 0.3 Q1, 0.7 Q3, 1.5 mTorr Q2 pressure and tuned tube lens values. Quantification, in SF set I, was executed after normalization against a set of 4 peptides corresponding to 2 housekeeping proteins (Table 2), to offset technical variations. Each sample was analyzed in duplicate, using a 60-minute method, whereby 63 transitions were monitored. Quantification in SF set II was executed following normalization against the added heavy-labelled peptides, as described earlier. Each sample was analyzed in duplicate, using a 60-minute method, whereby 114 transitions were monitored. Reproducibility of the SRM signal was confirmed by running a quality control solution of 0.1 fmol/μL BSA, every 10 runs.

Cretu D., Prassas I., Saraon P., Batruch I., Gandhi R., Diamandis E.P, & Chandran V. (2014). Identification of psoriatic arthritis mediators in synovial fluid by quantitative mass spectrometry. Clinical Proteomics, 11(1), 27.

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Quantification of EE2 in Water

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Water samples were collected from different tanks at nine separate occasions during the exposure and stored in darkness at −20°C until analysis. EE₂ concentrations were analyzed in single or duplicate samples as previously described in Volkova et al. (2015b (link)). Briefly, water samples (100 mL) were extracted on 100 mg Strata X-33μ Polymeric Reversed Phase cartridges, reconditioned with MeOH. Dionex ultimate 3000 LC system (Thermo Scientific, San Jose, CA, USA), coupled to a triple quadruple mass spectrometer (TSQ Vantage, Thermo Scientific, San Jose, CA, USA) was used for quantitation of EE₂ content. The quantification range was 0.5–100 ng/L, using EE₂-d4 as internal standard.

Porseryd T., Volkova K., Reyhanian Caspillo N., Källman T., Dinnetz P, & Porsh Hällström I. (2017). Persistent Effects of Developmental Exposure to 17α-Ethinylestradiol on the Zebrafish (Danio rerio) Brain Transcriptome and Behavior. Frontiers in Behavioral Neuroscience, 11, 69.

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