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Sciex 5600 plus tripletof mass spectrometer

Manufactured by AB Sciex
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The SCIEX 5600 plus TripleTOF mass spectrometer is a high-resolution, accurate-mass (HRAM) system designed for advanced analytical applications. It features a TripleTOF configuration, combining a triple quadrupole and a time-of-flight (TOF) mass analyzer, providing both quantitative and qualitative capabilities. The instrument is capable of performing fast data acquisition and high-resolution mass measurements to enable comprehensive compound identification and structural elucidation.

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Lab products found in correlation

Nanolc ultra 2d plus hplc system, by AB Sciex (2 mentions) Magic c18 aq, by New Objective (2 mentions) Picofrit emitter, by New Objective (2 mentions)

Close spelling variants of this product

TripleTOF 5600 plus mass spectrometer TripleTOF 5600 mass spectrometer Sciex 5600 mass spectrometer Sciex TripleTOF 5600+, TripleTOF 5600 SCIEX 5600 5600-plus

2 protocols using sciex 5600 plus tripletof mass spectrometer

1

Mass Spectrometry-Based Proteomics of iPSCs

Cited 1 time
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The peptides digested from two biological replicates of iPSC cells at time zero (cells in light medium) were both measured on an AB SCIEX 5600 plus TripleTOF mass spectrometer operated in DDA mode. The mass spectrometer was interfaced with an Eksigent NanoLC Ultra 2D Plus HPLC system as previously described [48 (link), 49 (link)]. Peptides were directly injected onto a 20-cm PicoFrit emitter (New Objective, self-packed to 20 cm with Magic C18 AQ 3-µm 200-Å material), and then separated using a 120-min linear gradient of 2 % buffer B to 35 % buffer B (buffer A 0.1 % (v/v) formic acid, 2 % (v/v) acetonitrile, buffer B 0.1 % (v/v) formic acid, 90 % (v/v) acetonitrile) at a flow rate of 300 nL/min. MS1 spectra were collected in the range 360–1,460 m/z. The 20 most intense precursors with charge state 2–5 which exceeded 250 counts per second were selected for fragmentation, and MS2 spectra were collected in the range 50–2,000 m/z for 100 ms. The precursor ions were dynamically excluded from reselection for 20 s.
Röst H.L., Liu Y., D’Agostino G., Zanella M., Navarro P., Rosenberger G., Collins B.C., Gillet L., Testa G., Malmström L, & Aebersold R. (2016). TRIC: an automated alignment strategy for reproducible protein quantification in targeted proteomics. Nature methods, 13(9), 777-783.
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2

Mass Spectrometry-Based Proteomics of iPSCs

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
The peptides digested from two biological replicates of iPSC cells at time zero (cells in light medium) were both measured on an AB SCIEX 5600 plus TripleTOF mass spectrometer operated in DDA mode. The mass spectrometer was interfaced with an Eksigent NanoLC Ultra 2D Plus HPLC system as previously described [48 (link), 49 (link)]. Peptides were directly injected onto a 20-cm PicoFrit emitter (New Objective, self-packed to 20 cm with Magic C18 AQ 3-µm 200-Å material), and then separated using a 120-min linear gradient of 2 % buffer B to 35 % buffer B (buffer A 0.1 % (v/v) formic acid, 2 % (v/v) acetonitrile, buffer B 0.1 % (v/v) formic acid, 90 % (v/v) acetonitrile) at a flow rate of 300 nL/min. MS1 spectra were collected in the range 360–1,460 m/z. The 20 most intense precursors with charge state 2–5 which exceeded 250 counts per second were selected for fragmentation, and MS2 spectra were collected in the range 50–2,000 m/z for 100 ms. The precursor ions were dynamically excluded from reselection for 20 s.
Röst H.L., Liu Y., D’Agostino G., Zanella M., Navarro P., Rosenberger G., Collins B.C., Gillet L., Testa G., Malmström L, & Aebersold R. (2016). TRIC: an automated alignment strategy for reproducible protein quantification in targeted proteomics. Nature methods, 13(9), 777-783.
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