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Accucore 50 resin

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The Accucore 50 resin is a high-performance chromatographic material designed for use in liquid chromatography. It features a spherical particle size of 50 µm and a pore size of 100 Å, providing efficient separation capabilities. The resin's composition and characteristics are optimized for various analytical and purification applications.

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Accucore resin (2 citations)

5 protocols using accucore 50 resin

1

High-Throughput Quantitative Proteomics Workflow

Cited 2 times
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Mass spectrometric data were collected on an Orbitrap Fusion Lumos mass spectrometer coupled to a Proxeon NanoLC-1200 UHPLC. The 100 µm capillary column was packed with 35 cm of Accucore 50 resin (2.6 µm, 150Å; ThermoFisher Scientific). Peptides were separated using a 2.5 h gradient of 9~35% acetonitrile gradient in 0.125% formic acid with a flow rate of ~400nl min 1. The scan sequence began with an MS1 spectrum (Orbitrap analysis, resolution 120,000, 350 1400 Th, automatic gain control (AGC) target 5E5, maximum injection time 50 ms). SPS-MS3 analysis was used to reduce ion interference.71 (link),72 (link) The top 10 precursors were then selected for MS2/MS3 analysis. MS2 analysis consisted of collision-induced dissociation (CID), quadrupole ion trap analysis, automatic gain control (AGC) 1E4, NCE (normalized collision energy) 35, q-value < 0.25, maximum injection time 60 ms), and isolation window at 0.5. Following acquisition of each MS2 spectrum, we collected an MS3 spectrum in which multiple MS2 fragment ions are captured in the MS3 precursor population using isolation waveforms with multiple frequency notches. MS3 precursors were fragmented by HCD and analyzed using the Orbitrap (NCE 65, AGC 3E5, maximum injection time 150 ms, resolution was 50,000 at 400 Th).
Keele G.R., Zhang T., Pham D.T., Vincent M., Bell T.A., Hock P., Shaw G.D., Paulo J.A., Munger S.C., Pardo-Manuel de Villena F., Ferris M.T., Gygi S.P, & Churchill G.A. (2021). Regulation of protein abundance in genetically diverse mouse populations. Cell Genomics, 1(1), 100003.
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2

Orbitrap Fusion Lumos Mass Spectrometry Protocol

Cited 1 time
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The data acquisition method was as described previously (Navarrete-Perea et al., 2018 (link)). Briefly, mass spectrometric data were collected on an Orbitrap Fusion Lumos mass spectrometer coupled to a Proxeon NanoLC-1200 UHPLC. The 100 μm capillary column was packed in-house with 35 cm of Accucore 50 resin (2.6 μm, 150Å; ThermoFisher Scientific). The mobile phase was 5% acetonitrile, 0.125% formic acid and 95% acetonitrile, 0.125% formic acid. The data were collected using a DDA-SPS-MS3 method. Each fraction was eluted across a 120 min method with a gradient from 6% to 30% B. Peptides were ionized with a spray voltage of 2,600 kV. The instrument method included Orbitrap MS1 scans (resolution of 120K; mass range 350–1,400 m/z; automatic gain control (AGC) target 5 × 105, max injection time of 50 ms) and ion trap MS2 scans (isolation window: 0.5, CID collision energy of 35%; AGC target 1 × 104; rapid scan mode; max injection time of 60 ms). MS3 precursors were fragmented by HCD and analyzed using the Orbitrap (NCE 65%, AGC 3 × 105, maximum injection time 150 ms, resolution was 50,000 at 400 Th). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE (Perez-Riverol et al., 2019 (link)) partner repository with the dataset identifier Database: PXD030072.
Verdaguer M.P., Zhang T., Surve S., Paulo J.A., Wallace C., Watkins S.C., Gygi S.P, & Sorkin A. (2022). Time-resolved proximity labeling of protein networks associated with ligand-activated EGFR. Cell reports, 39(11), 110950.
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3

Orbitrap Mass Spectrometry Proteomic Pipeline

Cited 2 times
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Mass spectrometric data were collected on an Orbitrap Fusion Lumos mass spectrometer coupled to a Proxeon NanoLC-1200 UHPLC. The 100 μm capillary column was packed with 35 cm of Accucore 50 resin (2.6 μm, 150Å; ThermoFisher Scientific). Peptides were separated using a 2.5 h gradient of 9∼35% acetonitrile gradient in 0.125% formic acid with a flow rate of ∼400nl min−1. The scan sequence began with an MS1 spectrum (Orbitrap analysis, resolution 120,000, 350−1400 Th, automatic gain control (AGC) target 5E5, maximum injection time 50 ms). SPS-MS3 analysis was used to reduce ion interference.71 (link),72 (link) The top 10 precursors were then selected for MS2/MS3 analysis. MS2 analysis consisted of collision-induced dissociation (CID), quadrupole ion trap analysis, automatic gain control (AGC) 1E4, NCE (normalized collision energy) 35, q-value < 0.25, maximum injection time 60 ms), and isolation window at 0.5. Following acquisition of each MS2 spectrum, we collected an MS3 spectrum in which multiple MS2 fragment ions are captured in the MS3 precursor population using isolation waveforms with multiple frequency notches. MS3 precursors were fragmented by HCD and analyzed using the Orbitrap (NCE 65, AGC 3E5, maximum injection time 150 ms, resolution was 50,000 at 400 Th).
Keele G.R., Zhang T., Pham D.T., Vincent M., Bell T.A., Hock P., Shaw G.D., Paulo J.A., Munger S.C., Pardo-Manuel de Villena F., Ferris M.T., Gygi S.P, & Churchill G.A. (2021). Regulation of protein abundance in genetically diverse mouse populations. Cell Genomics, 1(1), 100003.
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4

Orbitrap Fusion Lumos Mass Spectrometry Protocol

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
The data acquisition method was as described previously (Navarrete-Perea et al., 2018 (link)). Briefly, mass spectrometric data were collected on an Orbitrap Fusion Lumos mass spectrometer coupled to a Proxeon NanoLC-1200 UHPLC. The 100 μm capillary column was packed in-house with 35 cm of Accucore 50 resin (2.6 μm, 150Å; ThermoFisher Scientific). The mobile phase was 5% acetonitrile, 0.125% formic acid and 95% acetonitrile, 0.125% formic acid. The data were collected using a DDA-SPS-MS3 method. Each fraction was eluted across a 120 min method with a gradient from 6% to 30% B. Peptides were ionized with a spray voltage of 2,600 kV. The instrument method included Orbitrap MS1 scans (resolution of 120K; mass range 350–1,400 m/z; automatic gain control (AGC) target 5 × 105, max injection time of 50 ms) and ion trap MS2 scans (isolation window: 0.5, CID collision energy of 35%; AGC target 1 × 104; rapid scan mode; max injection time of 60 ms). MS3 precursors were fragmented by HCD and analyzed using the Orbitrap (NCE 65%, AGC 3 × 105, maximum injection time 150 ms, resolution was 50,000 at 400 Th). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE (Perez-Riverol et al., 2019 (link)) partner repository with the dataset identifier Database: PXD030072.
Verdaguer M.P., Zhang T., Surve S., Paulo J.A., Wallace C., Watkins S.C., Gygi S.P, & Sorkin A. (2022). Time-resolved proximity labeling of protein networks associated with ligand-activated EGFR. Cell reports, 39(11), 110950.
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5

Quantitative Proteomics with Orbitrap Fusion

Cited 2 times
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Mass spectrometric data were collected on an Orbitrap Fusion mass spectrometer coupled to a Proxeon NanoLC-1200 UHPLC. The 100 μm capillary column was packed with 35 cm of Accucore 50 resin (2.6 μm, 150Å; ThermoFisher Scientific). The scan sequence began with an MS1 spectrum (Orbitrap analysis, resolution 120,000, 350–1400 Th, automatic gain control (AGC) target 4E5, maximum injection time 50 ms). SPS-MS3 analysis was used to reduce ion interference (Gygi et al., 2019 (link); Paulo et al., 2016 (link)). The top ten precursors were then selected for MS2/MS3 analysis. MS2 analysis consisted of collision-induced dissociation (CID), quadrupole ion trap analysis, automatic gain control (AGC) 1E4, NCE (normalized collision energy) 35, q-value 0.25, maximum injection time 60 ms), and isolation window at 0.7. Following acquisition of each MS2 spectrum, we collected an MS3 spectrum in which multiple MS2 fragment ions are captured in the MS3 precursor population using isolation waveforms with multiple frequency notches. MS3 precursors were fragmented by HCD and analyzed using the Orbitrap (NCE 65, AGC 3E5, maximum injection time 150 ms, resolution was 50,000 at 400 Th).
Takahashi N., Cho P., Selfors L.M., Kuiken H.J., Kaul R., Fujiwara T., Harris I.S., Zhang T., Gygi S.P, & Brugge J.S. (2020). 3D Culture Models with CRISPR Screens Reveal Hyperactive NRF2 as a Prerequisite for Spheroid Formation via Regulation of Proliferation and Ferroptosis. Molecular cell, 80(5), 828-844.e6.
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