Qtrap 4500

Manufactured by AB Sciex

Sourced in United States, Japan, Canada

The QTRAP 4500 is a high-performance triple quadrupole mass spectrometer designed for a wide range of analytical applications. It offers high sensitivity, resolution, and mass accuracy, providing reliable results for quantitative and qualitative analysis.

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Lab products found in correlation

Absoluteidq p180 kit, by Biocrates (5 mentions) Pre column securityguard, by Phenomenex (5 mentions) 1260 series hplc, by Agilent Technologies (4 mentions) Nexera xr lc 20 ad uhplc system, by Shimadzu (3 mentions) Omix c18 tips, by Agilent Technologies (3 mentions) Massview1, by AB Sciex (3 mentions) Nicolet 6700, by Thermo Fisher Scientific (3 mentions) Nanolc400nano hplc system, by AB Sciex (2 mentions) Nanospray 3, by AB Sciex (2 mentions) Analyst software, by AB Sciex (2 mentions) Tripletof 6600, by AB Sciex (2 mentions) Qtrap 5500, by AB Sciex (2 mentions) Nexera x2, by Shimadzu (2 mentions) Nexera x2 lc 30ad, by Shimadzu (2 mentions) Agilent 1260 series hplc, by Agilent Technologies (2 mentions) Analytical balance, by Mettler Toledo (2 mentions) Peakview software, by AB Sciex (2 mentions) K alpha spectrometer, by Thermo Fisher Scientific (2 mentions) Analyst 1, by AB Sciex (2 mentions) Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

QTRAP 4500 mass spectrometer (43 citations) QTRAP 4500 system (9 citations) QTRAP 4500 triple quadrupole mass spectrometer (9 citations) QTRAP 4500 MD triple quadrupole mass spectrometer (8 citations) QTRAP® 4500 MS/MS system (7 citations) QTRAP 4500 LC-MS/MS system (6 citations) QTRAP 4500 MS (4 citations) SCIEX 4500 QTRAP mass spectrometer (4 citations) API 4500 QTrap (3 citations) API 4500 QTrap LC/MS/MS system (3 citations)

94 protocols using qtrap 4500

Quantification of Vitamin D Metabolites

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Venous blood samples for vitamin D metabolites were collected at three time points (1 h before, and 1 h and 3 h after the exercise) into tubes containing a coagulation accelerator. The serum was separated using a laboratory centrifuge, aliquotted into 1.5-mL centrifuge tubes, and frozen at −80 °C until further analysis.
Before the analysis, serum proteins were precipitated and derivatized using a Cookson-type reagent (DAPTAD). Proteins were precipitated using acetonitrile. For 1,25(OH)₂D₃ determination, the sample preparation involved liquid–liquid extraction with ethyl acetate. Quantitative analyses were performed using liquid chromatography coupled with tandem mass spectrometry (Exion LC system coupled with QTRAP4500, Sciex, Framingham, MA, USA). Chromatographic separation was carried out using an XDB-C18 column (50 × 4.6 mm, 1.7 μm; Agilent, Santa Clara, CA, USA). Serum samples were analyzed in the positive ion mode, using electrospray ionization. The concentrations of the following vitamin D metabolites were determined: 25(OH)D₃, 24,25(OH)₂D₃, 1,25(OH)₂D₃, 3-epi-25(OH)D₃, and 25(OH)D₂. The concentration range was 1–100 ng/mL for 25(OH)D₃; 0.1–10 ng/mL for 25(OH)D₂, 3-epi-25(OH)D₃, and 24,25(OH)₂D₃; and 10–200 pg/mL for 1,25(OH)₂D₃. In addition, the ratios of 25(OH)D₃ to 24,25(OH)₂D₃, and 25(OH)D₃ to epi-25(OH)D₃ were calculated.

Żychowska M., Rola R., Borkowska A., Tomczyk M., Kortas J., Anczykowska K., Pilis K., Kowalski K., Pilch W, & Antosiewicz J. (2021). Fasting and Exercise Induce Changes in Serum Vitamin D Metabolites in Healthy Men. Nutrients, 13(6), 1963.

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Quantification of FAM-UNO in Tumor Lysate

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High-performance liquid chromatography (Agilent 1200 series, USA) – mass spectrometry (Sciex Q-Trap 4500, Canada) analysis was done using a C18 column (Kinetex 2.6 µm EVO C18 100 × 4.6 mm, Phenomenex, USA). Ionization was performed at 300 °C with declustering potential set 30 V. Chromatography gradient started with 2 min 5% acetonitrile in water, followed by linear increase to 95% acetonitrile in 10 min and finally 10 min isocratic flow of 95% acetonitrile in water. Both eluents, water and acetonitrile, contained 0.2% formic acid. Flow rate was 0.3 ml/min. Column temperature was maintained at 40 °C. Autosampler temperature was set to 37 °C.
Retention times and m/z signals of FAM-UNO, were determined from 30 µM FAM-UNO solution in PBS. Tumor lysate was split into two aliquotes of 200 µL in each. From one aliquot, 20 µL were injected and the LC-MS profile obtained. The second aliquot was mixed with 50 µL of 30 µM FAM-UNO in PBS and injected within 1 min to LC-MS and the LC-MS profile obtained.

Scodeller P., Simón-Gracia L., Kopanchuk S., Tobi A., Kilk K., Säälik P., Kurm K., Squadrito M.L., Kotamraju V.R., Rinken A., De Palma M., Ruoslahti E, & Teesalu T. (2017). Precision Targeting of Tumor Macrophages with a CD206 Binding Peptide. Scientific Reports, 7, 14655.

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PAMPA Assay for Metabolite Permeability

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Chromatography fraction G from the original rarefication of the crude cyanobacterial extract was evaluated using PAMPA. The same method was used as described above. Following the PAMPA protocol, the plates were evaluated using LC-MS/MS with MRM on a SCIEX Qtrap 4500 mass spectrometer. The transitions for each monitored metabolite were determined utilizing the product ion function of a SCIEX HIRES TripleTOF 4600 mass spectrometer with Analyst TF software. The relative quantity of metabolites was measured using the area under the curve (AUC) for each metabolite. The closer the AUC of the donor and the acceptor plate shows higher permeability.

Kirk R.D., Picard K., Christian J.A., Johnson S.L., DeBoef B, & Bertin M.J. (2020). Unnarmicin D, an Anti-inflammatory Cyanobacterial Metabolite with Delta and Mu Opioid Binding Activity Discovered via a Pipeline Approach Designed to Target Neurotherapeutics. ACS chemical neuroscience, 11(24), 4478-4488.

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Evaluating MIP Leaching in SPE

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To examine the applicability of developed MIPs as SPE extraction materials, we checked the potential leaching of the template from the MIP. As reported under the upscale experiment (Section 2.7), 50 mg of each MIP was packed in the SPE column, conditioned, loaded, and eluted with 5 mL 1% TFA in MeOH. The extract was dried under nitrogen at 40 °C and the amount of leaching was quantified with a Nexera X2 ultra high performance liquid chromatograph (UHPLC, Schimadzu, Kyoto, Japan) coupled to the hybrid quadrupole-linear ion trap mass spectrometry analyzer QTRAP 4500 (Sciex, Framingham, MA, USA) following the method developed by Gornik et al., (2020a) [9 (link)].

Gornik T., Shinde S., Lamovsek L., Koblar M., Heath E., Sellergren B, & Kosjek T. (2020). Molecularly Imprinted Polymers for the Removal of Antide-Pressants from Contaminated Wastewater. Polymers, 13(1), 120.

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Fungal Amino Acid Quantification

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We transferred 100 mg fungal biomass into Eppendorf tubes containing glass beads and 1 mL ethanol (80%) solution in water. Homogenization with FastPrep-24 (MP-Biomedicals) was conducted for 2 min. Next, the sample was centrifuged (2 min, 6,000×g) and 50 μL of the supernatant was diluted with deionized water. Fungal amino acid concentrations were determined in duplicates by an aTRAQ Kit for amino acid analysis of physiological fluids (Sciex) with a QTRAP 4500 (Sciex) mass spectrometer connected to an Eksigent microLC 200 (Sciex). Detailed analysis was performed according to the manufacturer’s instructions.

Bernat P., Nykiel-Szymańska J., Stolarek P., Słaba M., Szewczyk R, & Różalska S. (2018). 2,4-dichlorophenoxyacetic acid-induced oxidative stress: Metabolome and membrane modifications in Umbelopsis isabellina, a herbicide degrader. PLoS ONE, 13(6), e0199677.

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Untargeted and Targeted Metabolomics Analysis

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For untargeted analyses, the pre-prepared EBC and serum samples were randomized and analyzed on a QTRAP 3200 (Sciex, Framingham, MA, USA) mass spectrometer. Ten μL of redissolved serum and 50 μL of EBC was directly injected and analyzed in isocratic flow of 0.05 mL/min water, 0.15 mL/min methanol, and 0.1% formic acid. Electrospray ionization MS scans were performed in negative and positive modes with a rate of 1000 amu/s between the mass ranges of 90 to 1400 Da. Ionspray voltage, declustering potential, and entrance potential were set to 4500 V, 20 V, and 10 V, respectively with the use of corresponding negative voltages in the negative scanning mode.
For targeted analysis, serum samples were measured on QTRAP 4500 (Sciex, Framingham, MA, USA), coupled to a high-performance liquid chromatography (HPLC) (Agilent 1260 series, Agilent Technologies, Waldbronn, Germany) using the AbsoluteIDQ p180 kit (Biocrates Life Sciences AG, Innsbruck, Austria) according to the manufacturer’s specifications. The resulting data were absolutely quantified concentrations of amino acids, acylcarnitines, biogenic amines, glycerophospholipids, hexose, and sphingolipids.

Kilk K., Aug A., Ottas A., Soomets U., Altraja S, & Altraja A. (2018). Phenotyping of Chronic Obstructive Pulmonary Disease Based on the Integration of Metabolomes and Clinical Characteristics. International Journal of Molecular Sciences, 19(3), 666.

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Quantifying Kynurenine and Tryptophan in Tumors

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To measure Kyn and Trp in tumor tissues, the tumor tissues were dried with filter paper, weighed, and put into 2 mL FastPrep® homogenization tubes with three stainless steel beads (2 mm), and 500 µL of methanol was added. Subsequently, the tumor tissue samples were homogenized at 9391 g for 2 min, performed with 10 s of homogenization at 10 s intervals. After centrifugation (10,000 g, 10 min), the contents of Kyn and Trp in the supernatant were then examined by using a highly sensitive series triple quadrupole mass spectrometer (SCIEX, QTRAP 4500).

Cao Z., Li D., Zhao L., Liu M., Ma P., Luo Y, & Yang X. (2022). Bioorthogonal in situ assembly of nanomedicines as drug depots for extracellular drug delivery. Nature Communications, 13, 2038.

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Metabolite Profiling of Murine Kidneys

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Phase extraction of metabolites from the frozen kidney samples of mice was performed as previously described (64 (link)). The AbsoluteID p180 Kit (Biocrates Life Sciences) was used to determine 186 metabolites. The samples were measured on mass spectrometer QTRAP 4500 (Sciex), in combination with a high-performance liquid chromatography (Agilent Technologies). The concentrations of the metabolites were calculated automatically by the MetIDQ software (Biocrates Life Sciences). The levels of reduced glutathione and oxidized glutathione were quantified with a luminescence-based glutathione assay (GSH-Glo; Promega). See Supplemental Table 3 for the summary of all significantly altered metabolites in the kidneys from Stk25^–/– versus WT mice.

Cansby E., Caputo M., Gao L., Kulkarni N.M., Nerstedt A., Ståhlman M., Borén J., Porosk R., Soomets U., Pedrelli M., Parini P., Marschall H.U., Nyström J., Howell B.W, & Mahlapuu M. (2020). Depletion of protein kinase STK25 ameliorates renal lipotoxicity and protects against diabetic kidney disease. JCI Insight, 5(24), e140483.

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Quantitative Mass Spectrometry-based Proteomics

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Analysis was performed as previously dicribed55 (link). For protein identification, wiff data files were analyzed with ProteinPilot 4.5 revision 1656 (Sciex, USA) using search algorithm Paragon 4.5.0.0 revision 1654 (Sciex, USA) and a standard set of identification settings to search against M. gallisepticum S6 CP006916.2NCBI protein database supplied with common contaminants. The following parameters were used: alkylation of cysteine-iodoacetamide, trypsin digestion, TripleTOF 5600 equipment, species: none, thorough search with additional statistical FDR analysis. Peptide identifications were processed with default settings by a ProteinPilot software built-in ProGroup algorithm. The final protein identification list was obtained with the threshold reliable protein ID unused score calculated by ProteomicS Performance Evaluation Pipeline Software (PSPEP) algorithm for 1% global FDR from fit.
Quantitative LC-MS protein analysis was performed on the basis of MRM methodology on QTRAP 4500 (Sciex, USA) triple quadrupole mass spectrometer equipped with a NanoSpray III ion source (Sciex, USA) coupled to an expertNanoLC400nano-HPLC system (Eksigent, USA). The details of the MRM analysis are described in the Supplementary Information.

Matyushkina D., Pobeguts O., Butenko I., Vanyushkina A., Anikanov N., Bukato O., Evsyutina D., Bogomazova A., Lagarkova M., Semashko T., Garanina I., Babenko V., Vakhitova M., Ladygina V., Fisunov G, & Govorun V. (2016). Phase Transition of the Bacterium upon Invasion of a Host Cell as a Mechanism of Adaptation: a Mycoplasma gallisepticum Model. Scientific Reports, 6, 35959.

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Extraction and Mass Spectrometry Analysis of Sphingolipids

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We extracted 100-mg biomass samples with 4 mL ethyl acetate/isopropanol/water mixture (60:30:10, v/v/v) [25 (link)]. Qualitative analysis of sphingolipids from evaporated extracts was obtained by examining their mass spectrum using a triple quad mass spectrometer QTRAP 4500 (Sciex) operating in the MRM positive ionization mode as previously described [26 (link)]. For the reversed-phase chromatographic analysis, 10 μL of the lipid extract was injected on a C18 column (the same model as mentioned above). The solvents and gradient elution were identical to that applied for the determination of phospholipids.

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