C18 trap column

Manufactured by Waters Corporation

The C18 trap column is a type of chromatography column used for the separation and purification of organic compounds. It is filled with a stationary phase consisting of C18-bonded silica particles, which have a high affinity for non-polar or hydrophobic molecules. The primary function of the C18 trap column is to retain and concentrate analytes of interest, allowing for improved detection and analysis in subsequent chromatographic steps.

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Lab products found in correlation

6210a time of flight mass spectrometer, by Agilent Technologies (2 mentions) Q exactive hf x, by Thermo Fisher Scientific (1 mentions) Hss t3 c18 column, by Waters Corporation (1 mentions) Acquity uplc m class, by Waters Corporation (1 mentions) C18 column, by Waters Corporation (1 mentions) Nanoacquity, by Waters Corporation (1 mentions) Mascot server, by Matrix Science (1 mentions) Mass hunter qualitative analysis b 04, by Agilent Technologies (1 mentions) 1200 series hplc, by Agilent Technologies (1 mentions) 1200 series high performance liquid chromatography system, by Agilent Technologies (1 mentions)

Spelling variants of this product

C18 column (384 citations) Symmetry C18 trap column (19 citations) C18 trap column cartridge (5 citations) ACQUITY UPLC M-Class Symmetry C18 Trap column (3 citations) M-Class C18 trap column (2 citations) NanoEase Symmetry C18 trap column (2 citations) Symmetry 300 C18 UPLC Trap column (2 citations) Waters ACQUITY UPLC M-Class Symmetry C18 Trap Column (2 citations) MZ Symmetry C18 Trap Column (2 citations) NanoEase M/Z Symmetry C18 trap column (2 citations)

4 protocols using c18 trap column

Proteomics Analysis of Peptide Samples

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Samples were resuspended to 200–250 ng/μL in 0.1% (v/v) TFA. Peptides were analyzed using nanoLC-ESI- MS/MS platform consisting of an Acquity M-class UPLC (Waters) coupled to a Q Exactive HF-X (Thermo-Fisher) mass spectrometer. Mobile phase A consisted of water with 0.1% (v/v) formic acid (FA) and mobile phase B consisted of acetonitrile with 0.1% (v/v) FA. Approximately 800 ng of sample was injected onto a C18 trap column (100 Å, 5 μm, 180 μm × 20 mm; Waters) with a flow rate of 5 μL/min for 3 min using 99% (v/v) A and 1% (v/v) B. Peptides were separated on a HSS T3 C18 column (100 Å, 1.8 μm, 75 μm × 250 mm; Waters) using an increasing linear gradient of 5–40% (v/v) B over 90 min, then 85% (v/v) B for 5 min before returning to 5% (v/v) B in 2 min and re-equilibrating for 13 min. The mass spectrometer was operated in positive polarity mode. MS survey scans were collected from 350–2000 m/z at 120,000 resolution. MS/MS scans for the top 20 features were collected using NCE = 28 at 30,000 resolution. Dynamic exclusion for precursor m/z was set to a 10 s window.

Sadecki P.W., Balboa S.J., Lopez L.R., Kedziora K.M., Arthur J.C, & Hicks L.M. (2021). Evolution of polymyxin resistance regulates colibactin production in Escherichia coli. ACS chemical biology, 16(7), 1243-1254.

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LC-MS/MS Analysis of Protein Digestion

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Reduction and alkylation of the PLS were performed with DTT and iodoacetamide (IAM), respectively. The denatured PLS was further mixed with trypsin at a weight ratio of 1:20 for digestion at 37°C overnight. The resulting peptide fragments were analyzed using an ESI-Q-TOF mass spectrometer (Waters Synapt^TM G1 HDMS) equipped with an ultra-performance liquid chromatography (UPLC) system (nanoACQUITY, Waters). A sample volume of 5 μL was injected, concentrated with a C18 trap column (180 mm id x 20 mm, 5 μm, Waters) and then separated with a C18 column (75 μm id × 10 mm, 1.7 μm, Waters). The survey scan was performed from m/z 400 to 1600, and the MS/MS scan was performed from m/z 50 to 1990. The threshold to switch from MS to MS/MS was 40 counts, and the run was then switched back to MS until the signal reached less than 10 counts or until 2.4 s had passed. For protein identification, the raw data from the MS/MS spectra were transferred to the peak list (PKL) using MassLynx 4.0 Global ProteinLynx. The Mascot server (Matrix Science, version 2.4.1) was used for the database search. The mass tolerance for both precursor and fragment ions was set to 0.2 Da. Carbamidomethyl and oxidization were set as the fixed and variable modifications, respectively. One missed trypsin cleavage was allowed in the MS/MS ion search.

Lai C.C., Weng T.C., Chen P.L., Tseng Y.F., Lin C.Y., Chia M.Y., Sung W.C., Lee M.S, & Hu A.Y. (2020). Development and characterization of standard reagents for cell-based prepandemic influenza vaccine products. Human Vaccines & Immunotherapeutics, 16(9), 2245-2251.

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LC-MS Analysis of Megamolecules

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Megamolecule samples were prepared for LC−MS analysis by dilution to 1 μM in water. LC−MS analysis was performed on an Agilent 1200 series HPLC connected to an Agilent 6210A time-of-flight (TOF) mass spectrometer. A 10 μL injection of each sample was captured on a C18 trap column (Waters) and eluted using a gradient from 5% to 95% acetonitrile and 0.1% formic acid in water with a flow rate of 0.25 mL/min. Data were analyzed with Agilent MassHunter Qualitative Analysis B.04.00, and spectra were deconvoluted using a maximum entropy deconvolution calculation.

Taylor E.L., Metcalf K.J., Carlotti B., Lai C.T., Modica J.A., Schatz G.C., Mrksich M, & Goodson T I.I.I. (2018). Long-Range Energy Transfer in Protein Megamolecules. Journal of the American Chemical Society, 140(46), 15731-15743.

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LC/MS Analysis of Protein Samples

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To prepare samples for LC/MS analysis, protein samples were diluted in
water to a final concentration of 1 μM. LC/MS analysis
was performed using an Agilent 1200 series high-performance liquid
chromatography system connected to an Agilent 6210A time-of-flight (TOF) mass
spectrometer. A 10 μL injection of each sample was
captured on a C18 trap column (Waters) and eluted using a gradient from 5 to 95%
acetonitrile and 0.1% formic acid in water at a flow rate of 0.25 mL/min. Blank
injections were run before each sample, and the extracted mass spectrum of the
blank was subtracted from the mass spectrum of the sample. Each mass spectrum
was deconvoluted using a maximum entropy routine. Data was analyzed using
Agilent MassHunter Qualitative Analysis B.04.00.
For conjugation reactions, the SnapTag protein was coupled with compound
1 before and after UV irradiation of the sample. For the
UV-irradiated sample, compound 1 (250 μM in
dimethyl sulfoxide) was irradiated using a CL1000-L UV lamp (UVP) at a high
power for 5 min (365 nm, 1500 mJ/cm²) and quantitative deprotection
was assumed. Both ligand samples were incubated in a 50
μL reaction with 250 pmol of SnapTag and 2 equiv of
ligand (5 μM SnapTag and 10 μM
compound 1 in reaction) in PBS for 5 min at room temperature. The
reaction was quenched with the addition of 10 μL of 0.6%
v/v formic acid in water (the final concentration of formic acid was 0.1%
v/v).

Zhou S., Metcalf K.J., Bugga P., Grant J, & Mrksich M. (2018). Photoactivatable Reaction for Covalent Nanoscale Patterning of Multiple Proteins. ACS applied materials & interfaces, 10(47), 40452-40459.

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