Qstar xl

Manufactured by AB Sciex

Sourced in United States, Canada

The QSTAR XL is a liquid chromatography-tandem mass spectrometry (LC-MS/MS) system. It is designed for targeted and untargeted quantitative and qualitative analysis of small molecules, peptides, and proteins. The system features a hybrid quadrupole time-of-flight (QTOF) mass analyzer that provides high mass resolution and accurate mass measurements.

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Lab products found in correlation

Chromasolv, by Merck Group (1 mentions) Methanol, by Merck Group (1 mentions) Inca energy 300, by Oxford Instruments (1 mentions) Su5000, by JEOL (1 mentions) Avatar 370, by Thermo Fisher Scientific (1 mentions) D max 2200, by Rigaku (1 mentions) 1750 ftir spectrometer, by PerkinElmer (1 mentions) Silica gel 60 f254, by Merck Group (1 mentions) Anti flag m2 agarose bead, by Merck Group (1 mentions) Lys c, by Fujifilm (1 mentions) Flag peptide, by Merck Group (1 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (1 mentions) Acquity uplc beh c18, by Waters Corporation (1 mentions) Nanolc system, by AB Sciex (1 mentions) Mascot, by Matrix Science (1 mentions) Agilent 1100 hplc, by Agilent Technologies (1 mentions) Uv 1800 uv vis spectrophotometer, by Shimadzu (1 mentions)

Close spelling variants of this product

QSTAR XL mass spectrometer ABSCIEX QSTAR XL

12 protocols using qstar xl

LC-MS Analysis of OSTE+ Polymer

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To obtain standards for the LC-MS analysis, an exact amount of each chemical used for the production of OSTE+ was dissolved in methanol (Sigma Aldrich) overnight (except acetone and D.E.N 431). The following day the solutions were diluted to a concentration of 500 μg/ml using 50 % MilliQ water and 50 % methanol. This was followed by a second dilution step to 50 μg/ml using MilliQ water. Acetone was not tested since it is not detectable in the LC-MS system used; D.E.N 431 was not tested since it is not water-soluble. To simulate the UV-lithography process of the fabrication of OSTE+, all standards were exposed to UV-light using a Karl Suss MA4 mask aligner for 40 min. All standards, extractions (described above) of OSTE+, extractions of OSTE+H₂O as well as blank samples, were analyzed using LC-MS.
A LC-MS system (QStar XL, Sciex, together with an Agilent 1100 LC system) was used with an Acquity CHS C18 1.7 μm 2.1x50 mm column and a sample volume of 5 μl. The mass spectrometer was configured to scan 120–1000 Da at 2 scans/s. Acetonitrile (LC-MS, Chromasolv, Sigma Aldrich) and MilliQ water were used at a flow rate of 250 μl/min. The concentration of acetonitrile in the mobile phase was: starting at 5 % for 1 min, ramp to 95 % over 3 min, hold for 2 min, ramp down to 5 % in 0.1 min.

Ejserholm F., Stegmayr J., Bauer P., Johansson F., Wallman L., Bengtsson M, & Oredsson S. (2015). Biocompatibility of a polymer based on Off-Stoichiometry Thiol-Enes + Epoxy (OSTE+) for neural implants. Biomaterials Research, 19, 19.

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Mass Spectrometric Analysis of Ce-10

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Mass spectra
were collected by using nanospray ionization and a quadrupole time-of-flight
instrument (QStar XL, Sciex, Ontario, Canada). Crystals of Ce-10 (4.5 mg) were dissolved in acetonitrile, and the solution was diluted
to approximately 50 μM. The sample solution was then loaded
into a pulled borosilicate capillary (1 mm o.d. 0.75 mm i.d. pulled
to 5 μm tip size) with its tip placed ∼1 cm from the
curtain plate inlet of the mass spectrometer. A platinum electrode
was inserted into the back of the capillary to make electrical contact
with the solution for nanospray generation. Voltages of 2200–2400
V were applied to the solution while the spectrometer plate was held
at 1100 V. The instrument was operated in TOF mode without any collision-induced
dissociation gas in Q2 using DP1 = 50 V and DP2 = 10 V. These conditions
produced a gentle ion sampling while helping desolvate the noncovalently
bound solvent molecules.

Blanes-Díaz A., Shohel M., Rice N.T., Piedmonte I., McDonald M.A., Jorabchi K., Kozimor S.A., Bertke J.A., Nyman M, & Knope K.E. (2023). Synthesis and Characterization of Cerium-Oxo Clusters Capped by Acetylacetonate. Inorganic Chemistry, 63(21), 9406-9417.

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Characterization of Al Particle Morphology

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The morphologies of Al particles were observed via scanning electron microscope (SEM, SU-5000, JEOL). The element analyses on Al particle surfaces before and after dye removal test were performed by energy dispersive X-ray spectrometer (EDS, INCA Energy 300, Oxford Instruments) equipped on SEM. X-ray diffractometry (XRD, D/max-2200, Rigaku) was used to analyze the phase composition of Al powder. The chemical bonds and functional groups of dye and those on OM-Al before and after reaction were observed by Fourier transform infrared spectrometer (FTIR, AVATAR 370, Thermo Nicolet). The byproducts by the reaction of M-orange and M-blue with Al were identified by a liquid chromatograph fitted with a mass spectrometer (LC/MS, Qstar XL, AB SCIEX) with a Z-spray electrospray ionization (ESI) source in positive and negative mode, respectively.

Xie S., Yang Y., Gai W.Z, & Deng Z.Y. (2021). Oxide modified aluminum for removal of methyl orange and methyl blue in aqueous solution. RSC Advances, 11(2), 867-875.

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Analytical techniques for compound isolation

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Electrospray ionization mass spectrometry (ESIMS) was recorded on QSTARXL of AB Sciex Company. Melting points of the isolated compounds were determined using an Electrothermal IA9000 Series digital melting point apparatus (Bibby scientific, Great Britain). UV and visible spectra were recorded in MeOH at 25 °C using a Kontron Uvikon spectrophotometer. The IR spectra were measured on a PerkinElmer 1750 FTIR spectrometer. The NMR spectra were measured on Bruker 500 MHz NMR Avance II spectrometers equipped with cryoprobe. Chemical shifts were recorded in δ (ppm) and the coupling constants (J) are in hertz relative to the internal standard tetramethylsilane (TMS). Silica gel 60 F254 (70-230; Merck; Darmstadt, Germany) was used as stationary phase for column chromatography. Precoated silica gel Kieselgel 60 F254 plates (0.25 mm thick) were used for TLC to monitor the purity of isolates and spots detected by spraying with 50% H2SO4 followed by heating at 100 °C. All solvents were distilled before using.

Lah F.C.W., Tchamgoué A.D., Abdou J.P., Kowa T.K., Wabo H.K., Tchinda A.T., Agbor G.A., Frédérich M., & Dongo É. (2020). Anti-inflammatory activity of chemical constituents from Echinops gracilis (Asteraceae). The Journal of Phytopharmacology, 9(3), 169-174.

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Affinity Purification of Tankyrase Protein

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HEK293T cells were transfected with the FLAG-tagged tankyrase plasmid using Lipofectamine 2000 (Lifetechnologies, Carlsbad, CA) according to the manufacturer's protocol. The cells were lysed with lysis buffer (20 mM Hepes, pH 7.5, 150 mM NaCl, 50 mM NaF, 1 mM Na₃VO₄, 0.5% digitonin, 1 mM PMSF, 5 μg/ml leupeptin, 5 μg/ml aprotinin, and 3 μg/ml pepstatin A). After centrifugation, the supernatant was incubated with anti-FLAG M2-agarose beads (Sigma-Aldrich, St. Louis, MO) and the beads were washed with wash buffer (10 mM Hepes, pH 7.5, 150 mM NaCl, and 0.1% Triton X-100). The immunoprecipitants were eluted with a FLAG peptide (0.5 mg/ml; Sigma-Aldrich) dissolved in wash buffer and digested with lysyl endopeptidase (Lys-C; Wako Chemicals USA). The immunoprecipitated proteins were analyzed by a direct nanoflow liquid chromatography/tandem mass spectrometry system coupled to a time-of-flight mass spectrometer (Q-STAR XL; AB Sciex, Foster City, CA), as described previously [52 (link)].

Okamoto K., Ohishi T., Kuroiwa M., Iemura S.I., Natsume T, & Seimiya H. (2018). MERIT40-dependent recruitment of tankyrase to damaged DNA and its implication for cell sensitivity to DNA-damaging anticancer drugs. Oncotarget, 9(88), 35844-35855.

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Synthetic Peptide Characterization by HPLC-MS

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Amino acids and nicotinic acid were coupled to the resin by general 1-hydroxybenzotriazole-diisopropylcarbodiimide (HOBt-DIC) mediated solid-phase peptide synthesis (SPPS) protocol [33 (link)] and then purified by reverse-phase HPLC (Waters, MA, USA; pump 600E, UV-484 detector, Gemini RP-C18 column 250 × 21.2 mm) in a gradient of acetonitrile in 0.1% trifluoroacetic acid. A MALDI-TOF mass spectrometry assay was performed to determine the quality of the synthetic NA–IVH. All of the mass spectrometry (MS) or MS/MS experiments were performed on a mass spectrometer (Q-Star XL, AB Sciex, Foster City, CA, USA) with a turboionspray source. The electrospray ionization (ESI) ion source parameters were a spray voltage 5.0 kV, curtain gas 25 L/min, and nebulizer gas 20 L/min. Synthetic peptides were confirmed for the molecular weights in full scan mode, and then sequenced by MS/MS scans. The collision energies were varied from 20 to 40 to efficiently get the fragments. The results were manually interpreted by Analyst QS 1.1 with Bioanalyst extensions (or all MS or MS/MS experiments followed the methods described in previous report [35 (link)]).

Son D.H., Yang D.J., Sun J.S., Kim S.K., Kang N., Kang J.Y., Choi Y.H., Lee J.H., Moh S.H., Shin D.M, & Kim K.W. (2018). A Novel Peptide, Nicotinyl–Isoleucine–Valine–Histidine (NA–IVH), Promotes Antioxidant Gene Expression and Wound Healing in HaCaT Cells. Marine Drugs, 16(8), 262.

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Identifying Active Compounds by Mass Spectrometry

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The active fraction F4 was subjected to electrospray ionization-mass spectrometry using a hybrid quadrupole-TOF mass spectrometry system (QSTAR XL; AB Sciex Instruments, San Diego, CA, USA) to identify its active compounds. All mass spectrometric analyses were performed by positive/negative electrospray ionization (ESI+/ESI−) with Ultra Performance Liquid Chromatography using a C18 reversed-phase column (Acquity UPLC BEH C18, 1.7 μm particle size, 2.1 × 100 mm; Waters, MA, USA). Active compounds were eluted by two solvent systems, including solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in acetonitrile). The flow rate for the two elution programs was 300 μl/min, and the column temperature was maintained at 40°C. A 5-μl aliquot was injected into the system and the gradient program was conducted as follows: 0–1 min and 16–20 min, 95% A and 5% B; 10–15 min, 100% B. Liquid chromatography mass spectrometry full-scan spectra were acquired.

Han V.C., Yu N.H., Yoon H., Ahn N.H., Son Y.K., Lee B.H, & Kim J.C. (2022). Identification, Characterization, and Efficacy Evaluation of Bacillus velezensis for Shot-Hole Disease Biocontrol in Flowering Cherry. The Plant Pathology Journal, 38(2), 115-130.

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Integrated nanoLC-MS/MS Protein Identification

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LC-MS/MS analysis was performed on an integrated nanoLC-MS/MS system (QSTAR XL, AB SCIEX, Framingham, MA, USA) comprising a LC Packings NanoLC system with an autosampler, and a QSTAR XL Q-Tof mass spectrometer (AB SCIEX, Framingham, MA, USA) fitted with nano-LC sprayer. Injected samples were first trapped and desalted on a LC-Packings PepMap™ C18 μ-Precolumn™ Cartidge (5 μm, 30 μm inner diameter × 5mm, ThermoFisher Scientific Inc., Waltham, MA, USA). Peptides were separated on an analytical LC-Packings PepMap C18column (3μm, 75 mm inner diameter × 15 cm, ThermoFisher Scientific Inc.) connected inline to the mass spectrometer, using a 45 min gradient of 5% to 60% acetonitrile in 0.1% formic acid. Data of MS/MS were fully automated and synchronized with AnalystQS (version 1.0) software. For protein identification analysis, the one second survey scans were acquired over the mass range m/z 400–1600 and a maximum of 10 concurrent MS/MS acquisitions could be triggered for 2+, 3+ and 4+ charged precursors detected at an intensity above the predefined threshold. The peak list files were used to query the NCBI database using the Mascot for web search (Matrix Science, Boston, MA, USA).

Wang C.M., Jhan Y.L., Tsai S.J, & Chou C.H. (2016). The Pleiotropic Antibacterial Mechanisms of Ursolic Acid against Methicillin-Resistant Staphylococcus aureus (MRSA). Molecules, 21(7), 884.

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Analyzing Gln103 MauG Variant Proteins

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The Gln103 MauG variant proteins
were analyzed by whole protein mass spectrometry. Samples were prepared
and analyzed as described previously.^{25 (link)} The data were obtained with a QSTAR XL (AB Sciex) quadrupole time-of-flight
mass spectrometer with the IonSpray electrospray source, and Analyst
QS version 1.0 (AB Sciex) and BioAnalyst extensions version 1.1 (AB
Sciex) were used for the acquisition and analysis of the data.

Shin S., Yukl E.T., Sehanobish E., Wilmot C.M, & Davidson V.L. (2014). Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauG. Biochemistry, 53(8), 1342-1349.

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Mass Spectrometry Analysis of MR-Inhibitor Complex

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Samples of MR were prepared for MS by exchanging assay buffer with ammonium acetate (10 mM, pH 7.5). The final concentrations of both the enzyme and the inhibitor were 10 μM. Mass spectra were recorded on an AB/Sciex QStarXL mass spectrometer equipped with an ion spray source operated in positive ion mode. Ions were scanned in the range of m/z 800-4000 with accumulation times of 1 s per spectrum with no interscan time delay. Experiments were conducted to trap the imine adduct using NaCNBH3. Wild-type MR (10 μM) in assay buffer was incubated with 2-FPBA (10 or 100 μM) for 30 min and then reacted with NaCNBH3 (2.5 mM) overnight at 4 °C.

Douglas C.D., Grandinetti L., Easton N.M., Kuehm O.P., Hayden J.A., Hamilton M.C., St Maurice M, & Bearne S.L. (2021). Slow-Onset, Potent Inhibition of Mandelate Racemase by 2-Formylphenylboronic Acid. An Unexpected Adduct Clasps the Catalytic Machinery. Biochemistry.

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