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C18 beads

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C18 beads are a type of chromatographic sorbent material used in various analytical and purification techniques. They consist of silica particles coated with octadecyl (C18) functional groups, providing a hydrophobic surface for the retention of nonpolar or weakly polar analytes. The core function of C18 beads is to facilitate the separation, extraction, and purification of compounds based on their affinity for the hydrophobic stationary phase.

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Lab products found in correlation

Q exactive hf hybrid quadrupole orbitrap mass spectrometer, by Thermo Fisher Scientific (3 mentions) Picochip column, by New Objective (3 mentions) Dionex ultimate 3000 rapid separation nanolc, by Thermo Fisher Scientific (3 mentions)

3 protocols using c18 beads

1

Peptide Identification by LC-MS/MS

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Peptides were analyzed by LC-MS/MS using a Dionex UltiMate 3000 Rapid Separation nanoLC and a Q Exactive™ HF Hybrid Quadrupole-Orbitrap™ Mass Spectrometer (Thermo Fisher Scientific). Approximately 1 μg of peptide samples was loaded onto the trap column, which was 150 μm × 3 cm in-house packed with 3 μm C18 beads. The analytical column was a 75 μm × 10.5 cm PicoChip column packed with 3 μm C18 beads (New Objective, Inc.). The flow rate was kept at 300 nL/min. Solvent A was 0.1% FA in water and Solvent B was 0.1% FA in ACN. The peptide was separated on a 120-min analytical gradient from 5% ACN/0.1% FA to 40% ACN/0.1% FA. The mass spectrometer was operated in data-dependent mode. The source voltage was 2.10 kV and the capillary temperature was 320 °C. MS1 scans were acquired from 300–2000 m/z at 60,000 resolving power and automatic gain control (AGC) set to 3 × 106. The top 15 most abundant precursor ions in each MS1 scan were selected for fragmentation. Precursors were selected with an isolation width of 2 Da and fragmented by higher-energy collisional dissociation (HCD) at 30% normalized collision energy in the HCD cell. Previously selected ions were dynamically excluded from re-selection for 20 seconds. The MS2 AGC was set to 1 × 105. All samples were run in duplicate.
Henning N.F., LeDuc R.D., Even K.A, & Laronda M.M. (2019). Proteomic analyses of decellularized porcine ovaries identified new matrisome proteins and spatial differences across and within ovarian compartments. Scientific Reports, 9, 20001.
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2

Peptide Analysis by LC-MS/MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were analyzed by LC-MS/MS using a Dionex UltiMate 3000 Rapid Separation nanoLC and a Q Exactive™ HF Hybrid Quadrupole-Orbitrap™ Mass Spectrometer (Thermo Fisher Scientific Inc, San Jose, CA). Approximately 2 μg of peptide samples was loaded onto the trap column, which was 150 μm × 3 cm in-house packed C18 beads. The analytical column was a 75 μm × 10.5 cm PicoChip column packed with 3 μm C18 beads (New Objective, Inc. Woburn, MA). The flow rate was kept at 300 nL/min. Solvent A was 0.1% FA in water and Solvent B was 0.1% FA in ACN. The peptide was separated on a 120-min analytical gradient from 5% ACN/0.1% FA to 40% ACN/0.1% FA. The mass spectrometer was operated in data-dependent mode. The source voltage was 2.40 kV. MS1 scans were acquired from 300 to 2000 m/z at 60,000 resolving power and automatic gain control (AGC) set to 3 × 106. The top 20 most abundant precursor ions in each MS1 scan were selected for fragmentation. Precursors were selected with an isolation width of 2 m/z and fragmented by Higher-energy collisional dissociation (HCD) at 30% normalized collision energy in the HCD cell. Previously selected ions were dynamically excluded from re-selection for 20 s. The MS2 minimum AGC was set to 1 × 103. Data was acquired in technical duplicates.
Mondal C., Gacha-Garay M.J., Larkin K.A., Adikes R.C., Di Martino J.S., Chien C.C., Fraser M., Eni-aganga I., Agullo-Pascual E., Cialowicz K., Ozbek U., Naba A., Gaitas A., Fu T.M., Upadhyayula S., Betzig E., Matus D.Q., Martin B.L, & Bravo-Cordero J.J. (2022). A proliferative to invasive switch is mediated by srGAP1 downregulation through the activation of TGF-β2 signaling. Cell reports, 40(12), 111358.
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3

Peptide Analysis by LC-MS/MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were analyzed by LC-MS/MS using a Dionex UltiMate 3000 Rapid Separation nanoLC and a Q Exactive™ HF Hybrid Quadrupole-Orbitrap™ Mass Spectrometer (Thermo Fisher Scientific Inc, San Jose, CA). Approximately 2 μg of peptide samples was loaded onto the trap column, which was 150 μm × 3 cm in-house packed C18 beads. The analytical column was a 75 μm × 10.5 cm PicoChip column packed with 3 μm C18 beads (New Objective, Inc. Woburn, MA). The flow rate was kept at 300 nL/min. Solvent A was 0.1% FA in water and Solvent B was 0.1% FA in ACN. The peptide was separated on a 120-min analytical gradient from 5% ACN/0.1% FA to 40% ACN/0.1% FA. The mass spectrometer was operated in data-dependent mode. The source voltage was 2.40 kV. MS1 scans were acquired from 300 to 2000 m/z at 60,000 resolving power and automatic gain control (AGC) set to 3 × 106. The top 20 most abundant precursor ions in each MS1 scan were selected for fragmentation. Precursors were selected with an isolation width of 2 m/z and fragmented by Higher-energy collisional dissociation (HCD) at 30% normalized collision energy in the HCD cell. Previously selected ions were dynamically excluded from re-selection for 20 s. The MS2 minimum AGC was set to 1 × 103. Data was acquired in technical duplicates.
Mondal C., Gacha-Garay M.J., Larkin K.A., Adikes R.C., Di Martino J.S., Chien C.C., Fraser M., Eni-aganga I., Agullo-Pascual E., Cialowicz K., Ozbek U., Naba A., Gaitas A., Fu T.M., Upadhyayula S., Betzig E., Matus D.Q., Martin B.L, & Bravo-Cordero J.J. (2022). A proliferative to invasive switch is mediated by srGAP1 downregulation through the activation of TGF-β2 signaling. Cell reports, 40(12), 111358.
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