Acquity uplc beh130 c18 column

Manufactured by Waters Corporation

Sourced in United States

The Acquity UPLC BEH130 C18 column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of a wide range of compounds. The column features a C18 stationary phase and a particle size of 1.7 μm, which provides efficient and high-resolution separations. The column is compatible with ultra-high performance liquid chromatography (UPLC) systems and can be used for a variety of applications, including pharmaceutical, environmental, and food analysis.

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Lab products found in correlation

Symmetry c18 precolumn, by Waters Corporation (4 mentions) Nanoacquity uplc device, by Waters Corporation (2 mentions) Tripletof 5600 mass spectrometer, by AB Sciex (1 mentions) Speedvac, by Thermo Fisher Scientific (1 mentions) Triple tof 5600 system, by AB Sciex (1 mentions) Q exactive hf x mass spectrometer, by Thermo Fisher Scientific (1 mentions) Nanoacquity, by Waters Corporation (1 mentions) Nanoacquity ultra performance lc, by Waters Corporation (1 mentions) Optima lc ms grade solvents, by Thermo Fisher Scientific (1 mentions) Q exactive plus mass spectrometer, by Thermo Fisher Scientific (1 mentions) Ultimate 3000 uhplc system, by Thermo Fisher Scientific (1 mentions)

6 protocols using acquity uplc beh130 c18 column

Nanoflow LC-MS/MS Proteomic Analysis

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NanoLC-MS/MS analysis was performed on a nanoAcquity UPLC device (Waters, Milford, USA) coupled to a TripleTOF 5600 mass spectrometer (Sciex, Framingham, MA, USA). Peptide separation was performed on an ACQUITY UPLC BEH130 C18 column (250 mm × 75 μm with 1.7 μm diameter particles) and a Symmetry C18 precolumn (20 mm × 180 μm with 5 μm diameter particles, Waters). The solvent system consisted of 0.1% FA in water (solvent A) and 0.1% FA in ACN (solvent B). The samples (1 μL) were loaded into the enrichment column over 3 min at 5 μL/min with 99% of solvent A and 1% of solvent B. The peptides were eluted at 300 μL/min with the following gradient of solvent B: from 3 to 35% over 110 min, and 35 to 85% over 5 min.
The Ion Spray Voltage Floating was set to 2.6 kV and the interface heater at 100 °C. The system was operated in data-dependent-acquisition mode with automatic switching between MS (mass range 400–1250 m/z) and MS/MS (mass range 100–1800 m/z in high sensitivity mode) modes. The fifty most abundant peptides (intensity threshold of 150 counts), were selected on each MS spectrum for further isolation and collision induced dissociation fragmentation, preferably from 2+ to 5+ charged ions. The dynamic exclusion time was set to 6 s. Complete datasets are available via ProteomeXchange with identifier PXD008656.

Muller L., Fornecker L., Chion M., Van Dorsselaer A., Cianférani S., Rabilloud T, & Carapito C. (2018). Extended investigation of tube-gel sample preparation: a versatile and simple choice for high throughput quantitative proteomics. Scientific Reports, 8, 8260.

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Peptide Mass Fingerprinting of Lipase from C. crenata

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Peptide mass fingerprinting of the purified lipase from C. crenata was performed using a Dionex Ultimate 3000 HPLC system (Thermo Fisher) equipped with an Acquity UPLC BEH 130 C18 column (1.7 μm, 2.1 × 50 mm; Waters, Milford, MA, USA) and TripleTOF 5600+ System (AB Sciex, Framingham, MA, USA) at 50 °C. For sample preparation, the enzyme fraction in SDS-PAGE was separated and destained with acetonitrile solvent for 15 min. One microgram of trypsin was added to the in-gel piece, and the gel was incubated for 18 h at 37 °C. The hydrolyzed peptide was collected through dehydration of the gel with SpeedVac (Thermo Fisher).
The swollen Sep-Pak C18 cartridge with 100% acetonitrile was equilibrated by desalting with distilled water. The bound peptide was eluted with 3 mL of 80% acetonitrile, dried with SpeedVac, and stored at 4 °C. It was then dissolved in 15 μL of distilled water with 0.1% formic acid and injected into a liquid chromatography coupled with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS) system. Distilled water with 0.1% formic acid and acetonitrile with 0.1% formic acid were used for elution of the sample with a flow rate of 0.3 mL/min.

Heo J., Kwon C.W., Lee J., Park H., Yu H, & Chang P.S. (2022). A jacalin-related lectin domain-containing lipase from chestnut (Castanea crenata): Purification, characterization, and protein identification. Current Research in Food Science, 5, 2081-2093.

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DIA and DDA Mass Spectrometry Workflow

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DDA and DIA acquisitions were performed on a NanoAcquity ultra-high performance liquid chromatography (UPLC) device (Waters) coupled to a Q-Exactive HF-X mass spectrometer (Thermo Fisher Scientific Inc., Bremen, Germany). Mobile phase A was 0.1% (V/V) FA in water and mobile phase B was 0.1% (V/V) FA in ACN. The equivalent of 400 ng of proteins was trapped onto a Symmetry C₁₈ precolumn (20 mm × 180 μm, 5 μm; Waters) and eluted on an Acquity UPLC BEH130 C₁₈ column (250 mm × 75 μm, 1.7 μm; Waters). A 115 min chromatographic gradient (2%–35% B in 95 min, 35%–80% B in 1 min, 80% B for 5 min, 80%–2% B in 1 min and maintained 2% B for 13 min) was applied at 400 nL/min, with a column temperature set at 60 °C. The Q-Exactive HF-X source temperature was set at 250 °C and spray voltage to 2 kV. The system was fully controlled by XCalibur software v4.0.27.19, 2013 (Thermo Fisher Scientific Inc.) and NanoAcquity UPLC console v1.51.3347 (Waters). The three injection replicates of DIA and DDA were performed in a randomized injection sequence. The MS proteomics data have been deposited to the ProteomeXchange consortium via the PRIDE partner repository with the dataset identifier PXD029305 [24 (link)].

Hessmann S., Chery C., Sikora A.S., Gervais A, & Carapito C. (2023). Host cell protein quantification workflow using optimized standards combined with data-independent acquisition mass spectrometry. Journal of Pharmaceutical Analysis, 13(5), 494-502.

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Peptide Separation via UPLC-MS

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The analysis was performed on a nanoACQUITY Ultra-Performance-LC (UPLC, Waters Corporation, Milford, USA). The samples were trapped on a 20 × 0.18 mm, 5 µm Symmetry C18 precolumn (Waters Corporation, Milford, USA), and the peptides were separated on a ACQUITY UPLC^® BEH130 C18 column (Waters Corporation, Milford, USA), 75 µm × 250 mm, 1.7 µm particle size. The solvent system consisted of 0.1% formic acid in water (solvent A) and 0.1% formic acid in acetonitrile (solvent B). Trapping was performed during 3 min at 5 µL/min with 97% of solvent A and 3% of solvent B. Elution was performed at a flow rate of 300 nL/min, using 3–40% gradient (solvent B) over 79 min followed by 80% (solvent B) over 10 min at 60 °C.

Bragantini B., Charron C., Bourguet M., Paul A., Tiotiu D., Rothé B., Marty H., Terral G., Hessmann S., Decourty L., Chagot M.E., Strub J.M., Massenet S., Bertrand E., Quinternet M., Saveanu C., Cianférani S., Labialle S., Manival X, & Charpentier B. (2021). The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity. Nature Communications, 12, 1859.

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NanoLC-PRM Analysis of Peptides

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NanoLC-PRM analyses were performed on a NanoAcquity UPLC device (Waters, Milford, Massachusetts, United State) coupled to a Q-Exactive Plus mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). Solvent system consisted of 0.1% FA in H2O (solvent A) and 0.1% FA in ACN (solvent B) (Optima LC/MS grade solvents, Fisher Chemical, Illkirch, France). Peptides (500ng) were separated onto a Symmetry C18 precolumn (20 mm × 180 µm, 5 µm diameter particles; Waters, Milford, Massachusetts, United State) over 3 min at 5 µL/min with 1% solvent B. Peptides were eluted on a Acquity UPLC BEH130 C18 column (250 mm × 75 µm, 1.70 µm particles; Waters, Milford, Massachusetts, United State) at 0.45 µL/min with the following gradient of solvent B: from 1% to 3% in 0.5 min, linear from 3% to 26% in 54.5 min, linear from 26% to 35% in 5 min, and up to 90% in 1 min. A scheduled PRM method consisting of one full MS1 scan and 16 targeted MS2 scans was developed. The full MS1 scan was collected from 300-1,800 m/z at a resolution of 17,500 at 200 m/z (AGC target: 3e6, maximum IT: 50 ms). Targeted MS2 scans were collected at a resolution of 35,000 at 200 m/z (AGC target: 1e6, maximum IT: 128 ms) and scheduled with 6-min time windows. Precursors were isolated within a 2-m/z window and fragmented with a NCE of 27.

Bonnet M., Soulat J., Bons J., Léger S., De Koning L., Carapito C, & Picard B. (2020). Quantification of biomarkers for beef meat qualities using a combination of Parallel Reaction Monitoring- and antibody-based proteomics. Food chemistry, 317.

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Peptide Characterization by Q-TOF Mass Spectrometry

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The molecular mass distribution and amino acid sequence of the purified peptides were determined by Q‐TOF mass spectrometer (AB Sciex Triple TOF 5600+, Foster City, CA, USA) with a Thermo UHPLC Ultimate 3000 system through an electrospray ionization source (Thermo Fisher Scientific, Waltham, MA, USA). Solution A (0.1% formic acid in distilled water) and solution B (0.1% formic acid in acetonitrile) were used in the elution and loaded onto an ACQUITY UPLC BEH 130 C₁₈column (1.7 µm, 2.1 mm × 50 mm, Waters Co.). The flow rate was set to 0.3 ml/min using the following conditions: 0–3 min, 99% eluent A; 3–70 min, 50% eluent A; 70–75 min, 0% eluent A; 75–80 min, 0% eluent A; 80–81 min, 99% eluent A; and 81–90 min, 99% eluent A. All experiments were carried out using positive mode with a capillary voltage of 3,500 V. The data were gathered in the centroid mode covering the mass/charge range of 100–2,500 m/z. The MS/MS spectra were examined using Protein Pilot (AB Sciex) software against the Uniprot sequence database (http://www.uniprot.org).

Kim J.M., Liceaga A.M, & Yoon K.Y. (2019). Purification and identification of an antioxidant peptide from perilla seed (Perilla frutescens) meal protein hydrolysate. Food Science & Nutrition, 7(5), 1645-1655.

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