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Aqua c18 reverse phase resin

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Aqua C18 reverse phase resin is a silica-based packing material used in liquid chromatography. It features a chemically bonded C18 alkyl functional group, providing a hydrophobic stationary phase for the separation of a wide range of analytes.

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Lab products found in correlation

Agilent 1200 series hplc, by Agilent Technologies (5 mentions) Ltq orbitrap discovery mass spectrometer, by Thermo Fisher Scientific (3 mentions) Partisphere strong cation exchange resin scx, by Cytiva (3 mentions) Whatman, by Cytiva (3 mentions) Ltq orbitrap discovery mass, by Thermo Fisher Scientific (2 mentions) Ltq orbitrap discovery, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Aqua C18 (15 citations) C18 resin (6 citations) Aqua C18 resin (4 citations)

8 protocols using aqua c18 reverse phase resin

1

LC-MS/MS Workflow for Proteomics Analysis

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Liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) analysis was performed with an LTQ-Orbitrap Discovery mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) coupled to an Easy-nLC HPLC (Thermo Fisher Scientific, Waltham, MA, USA). Samples were pressure loaded onto a 250-μm fused-silica capillary hand packed with 4-cm Aqua C18 reverse phase resin (Phenomenex). Samples were separated on a hand packed 100-μm fused-silica capillary column with a 5-μm tip packed with 10 cm Aqua C18 reverse phase resin (Phenomenex). Peptides were eluted using a 10-h gradient of 0–100% Buffer B in Buffer A (Buffer A: 95% water, 5% acetonitrile, 0.1% formic acid; Buffer B: 20% water, 80% acetonitrile, 0.1% formic acid). The flow rate through the column was set to ~400 nL/min, and the spray voltage was set to 2.5 kV. One full MS scan (FTMS) was followed by 7 data-dependent MS2 scans (ITMS) of the nth most abundant ions. The tandem MS data were searched by the SEQUEST algorithm using a concatenated target/decoy variant of the human and viral UniProt database. A static modification of +57.02146 on cysteine was specified to account for alkylation by iodoacetamide. SEQUEST output files were filtered using DTASelect 2.0.
Pasquero S., Gugliesi F., Biolatti M., Dell’Oste V., Albano C., Bajetto G., Griffante G., Trifirò L., Brugo B., Raviola S., Lacarbonara D., Yang Q., Sudeshna S., Barasa L., Haniff H., Thompson P.R., Landolfo S, & De Andrea M. (2023). Citrullination profile analysis reveals peptidylarginine deaminase 3 as an HSV-1 target to dampen the activity of candidate antiviral restriction factors. PLOS Pathogens, 19(12), e1011849.
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2

LC-MS/MS Proteomics for Mouse Lungs

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Liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) analysis was performed on an LTQ-Orbitrap Discovery mass spectrometer (ThermoFisher) coupled to an Easy-nLC HPLC (ThermoFisher). Samples were pressure loaded onto a 250 μm fused-silica capillary hand packed with 4 cm Aqua C18 reverse phase resin (Phenomenex). Samples were separated on a hand packed 100 μm fused-silica capillary column with a 5 μm tip packed with 10 cm Aqua C18 reverse phase resin (Phenomenex). Peptides were eluted using a 10-hour gradient of 0-100% Buffer B in Buffer A (Buffer A: 95% water, 5% acetonitrile, 0.1% formic acid; Buffer B: 20% water, 80% acetonitrile, 0.1% formic acid). The flow rate through the column was set to ~400 nL/min and the spray voltage was set to 2.5 kV. One full MS scan (FTMS) was followed by 7 data-dependent MS2 scans (ITMS) of the nth most abundant ions.
The tandem MS data of mouse lungs was searched using the SEQUEST algorithm using a concatenated target/decoy variant of the mouse UniProt database. A static modification of +57.02146 on cysteine was specified to account for alkylation by iodoacetamide. SEQUEST output files were filtered using DTASelect 2.0.
Sun B., Tomita B., Salinger A., Tilvawala R.R., Li L., Hakami H., Liu T., Tsoyi K., Rosas I.O., Reinhardt D.P., Thompson P.R, & Ho I.C. (2021). PAD2-mediated citrullination of Fibulin-5 promotes elastogenesis. Matrix biology : journal of the International Society for Matrix Biology, 102, 70-84.
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3

Comprehensive Proteomics Analysis by LC-MS/MS

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Liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) analysis was performed with an LTQ-Orbitrap Discovery mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) coupled to an Easy-nLC HPLC (Thermo Fisher Scientific, Waltham, MA, USA). Samples were pressure-loaded onto a 250-µm fused-silica capillary hand-packed with 4 cm Aqua C18 reverse-phase resin (Phenomenex). Samples were separated on a hand-packed 100-µm fused-silica capillary column with a 5-µm tip packed with 10 cm Aqua C18 reverse-phase resin (Phenomenex). Peptides were eluted using a 10-h gradient of 0–100% Buffer B in Buffer A (Buffer A: 95% water, 5% acetonitrile, 0.1% formic acid; Buffer B: 20% water, 80% acetonitrile, 0.1% formic acid). The flow rate through the column was set to ~400 nL/min, and the spray voltage was set to 2.5 kV. One full MS scan (FTMS) was followed by seven data-dependent MS2 scans (ITMS) of the nth most abundant ions. The tandem MS data were searched by the SEQUEST algorithm using a concatenated target/decoy variant of the human and viral UniProt database. A static modification of +57.02146 on cysteine was specified to account for alkylation by iodoacetamide. SEQUEST output files were filtered using DTASelect 2.0.
Griffante G., Gugliesi F., Pasquero S., Dell’Oste V., Biolatti M., Salinger A.J., Mondal S., Thompson P.R., Weerapana E., Lebbink R.J., Soppe J.A., Stamminger T., Girault V., Pichlmair A., Oroszlán G., Coen D.M., De Andrea M, & Landolfo S. (2021). Human cytomegalovirus-induced host protein citrullination is crucial for viral replication. Nature Communications, 12, 3910.
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4

Liquid Chromatography-Mass Spectrometry Protocol

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LC-MS analysis was performed on an LTQ Orbitrap Discovery mass spectrometer (ThermoFisher) coupled to an Agilent 1200 series HPLC. Digests were pressure-loaded onto a 250-μm fused silica desalting column packed with 4 cm of Aqua C18 reverse phase resin (Phenomenex). Digests of affinity-purified samples were loaded in their entirety, whereas unfractionated sample digests were centrifuged (16,873 × g, 4 °C, 2 min) before loading half of each sample onto the column. The peptides were eluted onto a biphasic column (100-μm fused silica with a 5 μm tip, packed with 10 cm C18 and 3 cm Partisphere strong cation exchange resin (SCX, Whatman)). The peptides were eluted from the SCX onto the C18 resin and into the mass spectrometer as previously described20 (link).
Hatzios S.K., Abel S., Martell J., Hubbard T., Sasabe J., Munera D., Clark L., Bachovchin D.A., Qadri F., Ryan E.T., Davis B.M., Weerapana E, & Waldor M.K. (2016). Chemoproteomic profiling of host and pathogen enzymes active in cholera. Nature chemical biology, 12(4), 268-274.
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5

Liquid Chromatography-Mass Spectrometry Protocol

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LC-MS analysis was performed on an LTQ Orbitrap Discovery mass spectrometer (ThermoFisher) coupled to an Agilent 1200 series HPLC. Digests were pressure-loaded onto a 250-μm fused silica desalting column packed with 4 cm of Aqua C18 reverse phase resin (Phenomenex). Digests of affinity-purified samples were loaded in their entirety, whereas unfractionated sample digests were centrifuged (16,873 × g, 4 °C, 2 min) before loading half of each sample onto the column. The peptides were eluted onto a biphasic column (100-μm fused silica with a 5 μm tip, packed with 10 cm C18 and 3 cm Partisphere strong cation exchange resin (SCX, Whatman)). The peptides were eluted from the SCX onto the C18 resin and into the mass spectrometer as previously described20 (link).
Hatzios S.K., Abel S., Martell J., Hubbard T., Sasabe J., Munera D., Clark L., Bachovchin D.A., Qadri F., Ryan E.T., Davis B.M., Weerapana E, & Waldor M.K. (2016). Chemoproteomic profiling of host and pathogen enzymes active in cholera. Nature chemical biology, 12(4), 268-274.
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6

LC-MS/MS Proteomic Analysis of Citrullinated Peptides

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LC-MS/MS analysis was performed on an LTQ-Orbitrap Discovery mass spectrometer (ThermoFisher) coupled to an Agilent 1200 series HPLC. Samples were pressure loaded onto a hand-pulled 100 µm fused-silica capillary column with a 5 µm tip packed with 10 cm Aqua C18 reverse phase resin (Phenomenex). Peptides were eluted using a 3-hour gradient 0–100% Buffer B in Buffer A (Buffer A: 95% water, 5% acetonitrile, 0.1% formic acid; Buffer B: 20% water, 80% acetonitrile, 0.1% formic acid). The flow rate through the column was set to ~0.25 µL/min and the spray voltage was set to 2.75 kV. One full MS scan (FTMS) was followed by 7 data dependent scans (ITMS) of the 7 most abundant ions. For high resolution runs, a full scan (FTMS) was followed by 4 data dependent scans (FTMS) limited to an inclusion mass list containing the masses of previously identified citrullinated peptides.
The tandem MS data were searched using the SEQUEST algorithm using a concatenated target/decoy variant of the human UniProt database. A static modification of +57.02146 on cysteine was specified to account for alkylation by iodoacetamide and a differential modification of 0.984 was specified on arginine. SEQUEST output files were filtered using DTASelect.
Sun B., Dwivedi N., Bechtel T.J., Paulsen J.L., Muth A., Bawadekar M., Li G., Thompson P.R., Shelef M.A., Schiffer C.A., Weerapana E, & Ho I.C. (2017). Citrullination of NF-kB p65 enhances its nuclear localization and TLR-induced expression of IL-1β and TNFα. Science immunology, 2(12), eaal3062.
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7

Proteomic Analysis by LC-MS/MS

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LC-MS/MS analysis was performed on an LTQ-Orbitrap Discovery mass spectrometer (ThermoFisher) coupled to an Agilent 1200 series HPLC. Samples were loaded via HPLC autosampler onto a hand-pulled 100 μm fused-silica capillary column with a 5 μm tip packed with 10 cm Aqua C18 reverse phase resin (Phenomenex). Peptides were eluted over a 5 h elution using a gradient from 100% Buffer A (95% water, 5% acetonitrile, 0.1% formic acid) to 100% Buffer B (20% water, 80% acetonitrile, 0.1% formic acid). The flow rate through the column was set to ~0.25 μL/min and the spray voltage was set to 2.75 kV. One full MS scan was followed by 8 data dependent scans of the 8 most abundant ions. For high resolution runs, a full scan was followed by 4 data dependent scans limited to an inclusion mass list containing the masses of previously identified modified peptides. The tandem MS data were searched using the SEQUEST algorithm using a concatenated target/decoy variant of the human UniProt database. A static modification of +57.02146 on cysteine was specified to account for alkylation by iodoacetamide and a differential modification of +117.0102 was specified on arginine. SEQUEST output files were filtered using DTA-Select.
Nemmara V.V., Tilvawala R., Salinger A.J., Miller L., Nguyen S.H., Weerapana E, & Thompson P.R. (2018). Citrullination Inactivates Nicotinamide-N-methyltransferase. ACS chemical biology, 13(9), 2663-2672.
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8

Proteomic analysis using LC-MS

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LC-MS analysis was performed on an LTQ Orbitrap Discovery mass spectrometer (ThermoFisher, Waltham MA) coupled to an Agilent 1200 series HPLC. Digests were pressure loaded onto a 250 μm fused silica desalting column packed with 4 cm of Aqua C18 reverse phase resin (Phenomenex, Torrance CA). The peptides were eluted onto a biphasic column (100 μm fused silica with a 5 μm tip, packed with 10 cm C18 and 3 cm Partisphere strong cation exchange resin (SCX, Whatman, United Kingdom) using a gradient 5–100% Buffer B in Buffer A (Buffer A: 95% water, 5% acetonitrile, 0.1% formic acid; Buffer B: 20% water, 80% acetonitrile, 0.1% formic acid). The peptides were eluted from the SCX onto the C18 resin and into the mass spectrometer following the four salt steps outlined in Weerapana et al., 2007 (link). The flow rate through the column was set to ~0.25 μL/min and the spray voltage was set to 2.75 kV. One full MS scan (400–1800 MW) was followed by 8 data dependent scans of the nth most intense ions with dynamic exclusion enabled.
Sanman L.E., Qian Y., Eisele N.A., Ng T.M., van der Linden W.A., Monack D.M., Weerapana E, & Bogyo M. (2016). Disruption of glycolytic flux is a signal for inflammasome signaling and pyroptotic cell death. eLife, 5, e13663.
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