C18 beads

Manufactured by Waters Corporation

C18 beads are a type of chromatography media used in liquid chromatography. They are composed of silica particles with a chemically bonded octadecyl (C18) functional group. C18 beads are designed to separate, purify, and analyze a wide range of organic compounds based on their hydrophobic interactions with the stationary phase.

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Lab products found in correlation

Nanoacquity, by Waters Corporation (3 mentions) Laser puller, by Sutter Instruments (3 mentions) Ultimate 3000 rslcnano system, by Thermo Fisher Scientific (2 mentions) Xbridge peptide beh 25 cm column, by Waters Corporation (2 mentions) Pierce high ph reversed phase peptide fractionation kit, by Thermo Fisher Scientific (2 mentions) Ltq velos, by Thermo Fisher Scientific (2 mentions) Prominence hplc system, by Shimadzu (1 mentions) Qe hf, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Magic C18 AQ beads (2 citations)

6 protocols using c18 beads

Redox Proteomics Fractionation Protocol

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For the redox proteomics experiments 70 μg of proteins were resuspended into 300 μL of 0.1% TFA and fractionated using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo Fischer Scientific) according to manufacturer's protocol, resulting in 8 fractions per sample. Samples were then dried overnight in a Speedvac.
For FITExP and PISA experiments, 150 μg of proteins were resuspended into 20 mM NH₄OH. Then, samples were off-line high-pH reversed-phase fractionated using an UltimateTM 3000 RSLCnano System (Dionex) equipped with a XBridge Peptide BEH 25 cm column of 2.1 mm internal diameter, packed with 3.5 μm C18 beads having 300 Å pores (Waters). The mobile phase consisted of buffer A (20 mM NH₄OH) and buffer B (100% ACN). The gradient started from 1% B to 23.5% in 42 min, then to 54% B in 9 min, 63% B in 2 min and stayed at 63% B for 5 min and finally back to 1% B and stayed at 1% B for 7 min. This resulted in 96 fractions that were concatenated into 24 fractions and dried overnight using miVac DNA.

Sabatier P., Beusch C.M., Gencheva R., Cheng Q., Zubarev R, & Arnér E.S. (2021). Comprehensive chemical proteomics analyses reveal that the new TRi-1 and TRi-2 compounds are more specific thioredoxin reductase 1 inhibitors than auranofin. Redox Biology, 48, 102184.

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High-Resolution Protein Profiling by LC-MS/MS

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Samples were analyzed by HPLC-ESI-MS/MS using a system consisting of a high-performance liquid chromatograph (nanoAcquity, Waters) connected to an electrospray ionization (ESI) Orbitrap mass spectrometer (LTQ Velos, Thermo Fisher Scientific). HPLC separation employed a 100×365 mm fused silica capillary micro-column packed with 20 cm of 1.7-µm-diameter, 130 Å pore size, C18 beads (Waters BEH), with an emitter tip pulled to approximately 1 µm using a laser puller (Sutter Instruments). Peptides were loaded on-column at a flow rate of 400 nL/min for 30 min and then eluted over 120 min at a flow rate of 300 nL/min with a gradient of 2–30% acetonitrile in 0.1% formic acid. Full-mass profile scans were performed in the orbitrap between 300 and 1500 m/z at a resolution of 60,000, followed by 10 MS/MS HCD scans of the 10 highest intensity parent ions at 42% relative collision energy and 7500 resolution, with a mass range starting at 100 m/z. Dynamic exclusion was enabled with a repeat count of two over the duration of 30 s and an exclusion window of 120 s.

Hansen S.R., White D.S., Scalf M., Corrêa I.R., Smith L.M, & Hoskins A.A. (2022). Multi-step recognition of potential 5' splice sites by the Saccharomyces cerevisiae U1 snRNP. eLife, 11, e70534.

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High-pH Reversed-Phase Peptide Fractionation

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We performed high-pH reversed-phase peptide prefractionation with fraction concatenation on 175 μg HeLa or cerebellum peptides on a 2.1 × 300 mm Acquity UPLC Peptide BEH column packed with 130 Å pore, 1.7 μm particle size C₁₈ beads (Part No. 186005792, Waters). A gradient of basic reversed-phase buffers (Buffer A: 0.1% formic acid, ammonium hydroxide pH 10; Buffer B: 0.1% formic acid, 80% acetonitrile, ammonium hydroxide pH 10) was run on a Prominence HPLC system (Shimadzu, Duisburg, Germany) at a flow rate of 150 μl/min at 60 °C. The LC run lasted for 240 min with a starting concentration of 5% buffer B increasing to 30% over the initial 120 min and a further increase in concentration to 60% over 70 min. This elution gradient was followed by a 95% wash and re-equilibration. Fraction collection started after 0.2 ml elution and fractions were collected every 140 s resulting in 72 fractions used for concatenation into 24 fractions as described previously (31 (link)).

Beck S., Michalski A., Raether O., Lubeck M., Kaspar S., Goedecke N., Baessmann C., Hornburg D., Meier F., Paron I., Kulak N.A., Cox J, & Mann M. (2015). The Impact II, a Very High-Resolution Quadrupole Time-of-Flight Instrument (QTOF) for Deep Shotgun Proteomics. Molecular & Cellular Proteomics : MCP, 14(7), 2014-2029.

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Peptide Fractionation for Proteomic Analysis

Cited 1 time

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For experiments 2–5 and 10 (Supplementary Table 2) 70 µg of peptides were resuspended into 300 µL of 0.1% TFA and fractionated using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo Fischer Scientific) according to manufacturer’s protocol, resulting in 8 fractions per samples. Samples were then dried overnight in a Speedvac.
For experiments 1, 7–9, 11, and 12 (Supplementary Table 2), 150 µg of peptides were resuspended into 20 mM NH₄OH. Then, samples were off-line high-pH reversed-phase fractionated^{63 ,64 (link)} using an UltimateTM 3000 RSLCnano System (Dionex) equipped with a XBridge Peptide BEH 25 cm column of 2.1 mm internal diameter, packed with 3.5 µm C18 beads having 300 Å pores (Waters). The mobile phase consisted of buffer A (20 mM NH4OH) and buffer B (100% ACN). The gradient started from 1% B to 23.5% in 42 min, then to 54% B in 9 min, 63% B in 2 min and stayed at 63% B for 5 min and finally back to 1% B and stayed at 1% B for 7 min. This resulted in 96 fractions that were concatenated into 24 fractions and dried o/n using miVac DNA.

Sabatier P., Beusch C.M., Saei A.A., Aoun M., Moruzzi N., Coelho A., Leijten N., Nordenskjöld M., Micke P., Maltseva D., Tonevitsky A.G., Millischer V., Carlos Villaescusa J., Kadekar S., Gaetani M., Altynbekova K., Kel A., Berggren P.O., Simonson O., Grinnemo K.H., Holmdahl R., Rodin S, & Zubarev R.A. (2021). An integrative proteomics method identifies a regulator of translation during stem cell maintenance and differentiation. Nature Communications, 12, 6558.

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Peptide Analysis by HPLC-MS/MS

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The samples were analyzed using an HPLC-ESI-MS/MS system consisting of a high performance liquid chromatograph (nanoAcquity, Waters) set in line with an electrospray ionization (ESI) Orbitrap mass spectrometer (QE HF, ThermoFisher Scientific). A 100 μm id × 365 μm od fused silica capillary microcolumn packed with 20 cm of 1.7 μm diameter, 130 Å pore size, C18 beads (Waters BEH), and an emitter tip pulled to approximately 1 μm using a laser puller (Sutter Instruments) was used for HPLC separation of peptides. Peptides were loaded on-column with 2% acetonitrile in 0.1% formic acid at a flow rate of 400 nL/min for 30 min. Peptides were then eluted at a flow-rate of 400 nL/min over 120 min with a gradient from 5% to 35% acetonitrile, in 0.1% formic acid. Full-mass profile scans (375−1500 m/z) were performed in the FT orbitrap at a resolution of 120,000 followed by 20 MS/MS HCD scans of the 20 highest intensity parent ions at 30% relative collision energy and 15,000 resolution with a mass range starting at 100 m/z. Dynamic exclusion was enabled with a repeat count of one over a duration of 30 s.

Spiniello M., Knoener R.A., Steinbrink M.I., Yang B., Cesnik A.J., Buxton K.E., Scalf M., Jarrard D.F, & Smith L.M. (2018). HyPR-MS for Multiplexed Discovery of MALAT1, NEAT1, and NORAD lncRNA Protein Interactomes. Journal of proteome research, 17(9), 3022-3038.

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High-Resolution Proteomics Analysis

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Samples were analyzed by HPLC-ESI-MS/MS using a system consisting of a highperformance liquid chromatograph (nanoAcquity, Waters) connected to an electrospray ionization (ESI) Orbitrap mass spectrometer (LTQ Velos, ThermoFisher Scientific). HPLC separation employed a 100 x 365 mm fused silica capillary micro-column packed with 20 cm of 1.7µm-diameter, 130 Angstrom pore size, C18 beads (Waters BEH), with an emitter tip pulled to approximately 1 µm using a laser puller (Sutter Instruments). Peptides were loaded oncolumn at a flow-rate of 400nL/min for 30 minutes and then eluted over 120 min at a flow-rate of 300 nl/minute with a gradient of 2-30% acetonitrile in 0.1% formic acid. Full-mass profile scans were performed in the orbitrap between 300-1500 m/z at a resolution of 60,000, followed by ten MS/MS HCD scans of the ten highest intensity parent ions at 42% relative collision energy and 7,500 resolution, with a mass range starting at 100 m/z. Dynamic exclusion was enabled with a repeat count of two over the duration of 30 seconds and an exclusion window of 120 seconds.

Hansen S.R., Corrêa I.R., Scalf M., Smith L.M., & Hoskins A.A. (2021). Multi-Factor Authentication of Potential 5′ Splice Sites by the Saccharomyces cerevisiae U1 snRNP.

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