LC-MS/MS analyses were conducted using a Velos Pro Elite Orbitrap mass spectrometer (Thermo) coupled online to a nanoAcquity UPLC system (Waters Corporation) through an EASY-Spray nanoESI ion source (Thermo). An EASY-Spray PepMap RSLC C18, 3 μm, 75 μm × 15 cm column (Thermo Scientific) was used to resolve peptides using 0.1% formic acid in water as mobile phase A and 0.1% formic acid in acetonitrile as mobile phase B. Peptides were loaded at 2% B for 20 min at a flow rate of 600nL/min. Peptides were separated at 400nL/min using a gradient from 2% to 25% B over 48 or 220 min followed by a second gradient from 25% to 37% B over 8 minutes and then a column wash at 75% B and reequilibration at 2% B. Precursor scans were acquired in the Orbitrap analyzer (300–1800 m/z, resolution: 60,000@400 m/z, AGC target: 2e6. The top 6 most intense, doubly charged or higher ions were isolated (4 m/z isolation window), subjected to high-energy collisional dissociation (27.5 NCE), and the product ions measured in the Orbitrap analyzer (15,000@400 m/z, AGC target: 9e4).
Easy spray nanoesi ion source
Manufactured by Thermo Fisher Scientific
The EASY-Spray nanoESI ion source is a laboratory equipment designed for the generation of electrospray ionization (ESI) for mass spectrometry applications. It provides a reliable and consistent spray of charged analyte particles from liquid samples for introduction into a mass spectrometer.
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Lab products found in correlation
2 protocols using easy spray nanoesi ion source
1
Quantitative Peptide Analysis by LC-MS/MS
2
Quantitative Proteomics via Orbitrap LC-MS/MS
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LC-MS/MS analyses were conducted using a QExactive Plus Orbitrap (QE) mass spectrometer (Thermo Fisher) coupled online to a nanoAcquity UPLC system (Waters Corporation) through an EASY-Spray nanoESI ion source (Thermo Fisher). Peptides were loaded onto an EASY-Spray column (75 μm x 15 cm column packed with 3 μm, 100 Å PepMap C18 resin) at 2% B (0.1% formic acid in acetonitrile) for 20 min at a flow rate of 600 nl/min. Peptides were separated at 400 nL/min using a gradient from 2% to 25% B over 48 min (QE) followed by a second gradient from 25% to 37% B over 8 minutes and then a column wash at 75% B and reequilibration at 2% B. Precursor scans were acquired in the Orbitrap analyzer (350–1500 m/z, resolution: 70,000@200 m/z, AGC target: 3 × 106). The top 10 most intense, doubly charged or higher ions were isolated (4 m/z isolation window), subjected to high-energy collisional dissociation (25 NCE), and the product ions measured in the Orbitrap analyzer (17,500@200 m/z, AGC target: 5e4).
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