2 μm c18 beads

Manufactured by Thermo Fisher Scientific

2 μm C18 beads are a type of chromatography media used for the separation and purification of various compounds. These beads have a particle size of 2 micrometers and a stationary phase consisting of C18 alkyl chains bonded to a silica support. The primary function of these beads is to facilitate the separation and isolation of analytes based on their hydrophobic interactions with the C18 stationary phase.

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Lab products found in correlation

4 protocols using 2 μm c18 beads

Orbitrap Fusion Lumos Nano-LC-MS/MS Protocol

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All MS experiments were performed on a nanoscale EASY-nLC 1200 UHPLC system (Thermo Fisher Scientific) connected to an Orbitrap Fusion Lumos equipped with a nanoelectrospray ion source (Thermo Fisher Scientific). Mobile phase A contained 0.1% formic acid (v/v) in water; mobile phase B contained 0.1% formic acid in 80% acetonitrile. The peptides were dissolved in 0.1% formic acid with 2% acetonitrile and separated on a RP-HPLC analytical column (75 μm×25 cm) packed with 2 μm C18 beads (Thermo Fisher Scientific) using a linear gradient ranging from 6% to 26% B in 90 min and followed by a linear increase to 44% B in 15 min at a flow rate of 300 nL/min. The Orbitrap Fusion Lumos acquired data in a manner that alternated between full-scan MS and MS2 scans. The spray voltage was set at 2.2 kV and the temperature of ion transfer capillary was 300 °C. The MS spectra (350−1750 m/z) were collected with a resolution of 60,000, AGC target of 600,000 charges, and a maximal injection time of 60 ms. Precursor ions were isolated with a window of 1.3 m/z, with an AGC target of 200,000 charges, a resolution of 60,000, and a maximal injection time of 120 ms. The precursor fragmentation was accomplished using electron transfer dissociation (ETD) in positive ion mode.

Fu H., Liu R., Jia Z., Li R., Zhu F., Zhu W., Shao Y., Jin Y., Xue Y., Huang J., Luo K., Gao X., Lu H, & Zhou Q. (2022). Poly(ADP-ribosylation) of P-TEFb by PARP1 disrupts phase separation to inhibit global transcription upon DNA damage. Nature cell biology, 24(4), 513-525.

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Peptide Separation and Analysis by Nano-UPLC-MS

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Peptides were injected into an Ultimate 3000 RSLC system (Thermo Scientific, Sunnyvale, California, USA) connected to a Q Exactive HF equipped with a nanospray Flex ion source (Thermo Scientific, Bremen, Germany). The samples were loaded on an Acclaim PepMap 100, 2cm x 75μm i.d. nanoViper pre-column, packed with 3μm C18 beads at a flow rate of 5μl/min for 5 min with 0.1% TFA (trifluoroacetic acid, vol/vol). Peptides were separated during a biphasic ACN gradient from two nanoflow UPLC pumps (flow rate of 0.250 μl/min) on a 50 cm analytical column (Easy-Spray 803, 50cm x 75μm i.d. PepMap RSLC column, packed with 2μm C18 beads (Thermo Scientific). Solvent A was 0.1% FA (vol/vol) in water, and solvent B was 100% ACN, 0.1% FA. The following gradient was used; 0 min 5% B, 5 min 5% B, 140 min 35% B, 155 min 80% B, 170 min 80% B, 175 min 5% B, 195 min 5% B. Samples were a maximum of 48 hours in the autosampler at 10˚C prior to injection.

Lereim R.R., Nytrova P., Guldbrandsen A., Havrdova E.K., Myhr K.M., Barsnes H, & Berven F.S. (2024). Natalizumab promotes anti-inflammatory and repair effects in multiple sclerosis. PLOS ONE, 19(3), e0300914.

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Orbitrap Fusion Lumos LC-MS/MS Protocol

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All MS experiments were performed on a nanoscale EASY-nLC 1200UHPLC system (Thermo Fisher Scientific) connected to an Orbitrap Fusion Lumos equipped with a nanoelectrospray source (Thermo Fisher Scientific). Mobile phase A contained 0.1% formic acid (v/v) in water; mobile phase B contained 0.1% formic acid in 80% acetonitrile (ACN). The peptides were dissolved in 0.1% formic acid (FA) with 2% acetonitrile and separated on a RP-HPLC analytical column (75 μm×25 cm) packed with 2 μm C18 beads (Thermo Fisher Scientific) using a linear gradient ranging from 5% to 22% ACN in 90 mins and followed by a linear increase to 35% B in 20 mins at a flow rate of 300 nL/min. The Orbitrap Fusion Lumos acquired data in a data-dependent manner alternating between full-scan MS and MS2 scans. The spray voltage was set at 2.2 kV and the temperature of ion transfer capillary was 300°C. The MS spectra (350-1500 m/z) were collected with 120,000 resolutions, AGC of 4 × 10⁵, and 50 ms maximal injection time. Selected ions were sequentially fragmented in a 3 seconds (s) cycle by HCD with 30% normalized collision energy, specified isolated windows 1.6m/z, 30,000 resolutions. AGC of 5 × 10⁴ and 150 ms maximal injection time were used. Dynamic exclusion was set to 15 s. Unassigned ions or those with a charge of 1+ and >7+ were rejected for MS/MS.

Peng B.L., Li W.J., Ding J.C., He Y.H., Ran T., Xie B.L., Wang Z.R., Shen H.F., Xiao R.Q., Gao W.W., Ye T.Y., Gao X, & Liu W. (2020). A hypermethylation strategy utilized by enhancer-bound CARM1 to promote estrogen receptor α-dependent transcriptional activation and breast carcinogenesis. Theranostics, 10(8), 3451-3473.

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Nanoscale TMT Mass Spectrometry

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TMT MS experiments were performed on a nanoscale EASY-nLC 1200UHPLC system or nanoU3000UHPLC system (Thermo Fisher Scientific) connected to an Orbitrap Fusion Lumos equipped with a nanoelectrospray source (Thermo Fisher Scientific). Mobile phase A contained 0.1% formic acid (v/v) in water; mobile phase B contained 0.1% formic acid in 80% acetonitrile (ACN). The peptides were dissolved in 0.1% formic acid (FA) with 2% ACN and separated on a RP-HPLC analytical column (75 μm × 25 cm) packed with 2 μm C18 beads (Thermo Fisher Scientific) using a linear gradient ranging from 9 to 32% ACN in 100 min and followed by a linear increase to 50% B in 20 min at a flow rate of 300 nL/min. The Orbitrap Fusion Lumos acquired data in a data-dependent manner alternating between full-scan MS and MS2 scans. The spray voltage was set at 2.2 kV and the temperature of ion transfer capillary was 300 °C. The MS spectra (350−1500 m/z) were collected with 60,000 resolution, AGC of 4 × 10⁵ and 50 ms maximal injection time. Selected ions were sequentially fragmented in a 3 s cycle by HCD with 38% normalized collision energy, specified isolated windows 0.7 m/z, 50,000 resolution. AGC of 1 × 10⁵ and 105 ms maximal injection time were used. Dynamic exclusion was set to 30 s. Unassigned ions or those with a charge of 1+ and >7+ were rejected for MS/MS.

Liu W., Xie L., He Y.H., Wu Z.Y., Liu L.X., Bai X.F., Deng D.X., Xu X.E., Liao L.D., Lin W., Heng J.H., Xu X., Peng L., Huang Q.F., Li C.Y., Zhang Z.D., Wang W., Zhang G.R., Gao X., Wang S.H., Li C.Q., Xu L.Y., Liu W, & Li E.M. (2021). Large-scale and high-resolution mass spectrometry-based proteomics profiling defines molecular subtypes of esophageal cancer for therapeutic targeting. Nature Communications, 12, 4961.

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