Acclaim pepmap rslc c18 nano column

Manufactured by Thermo Fisher Scientific

The Acclaim PepMap RSLC C18 nano-column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of peptides and proteins. It features a reversed-phase C18 stationary phase with a small particle size, which provides efficient and high-resolution separation. The column is suitable for use in nano-LC applications, where small sample volumes and high sensitivity are required.

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Lab products found in correlation

Q exactive hybrid quadrupole orbitrap mass spectrometer, by Thermo Fisher Scientific (1 mentions) Acclaim pepmap100 c18 nano trap column, by Thermo Fisher Scientific (1 mentions) Acclaim pepmap c18 trap column, by Thermo Fisher Scientific (1 mentions) Easy nanolc 1000 system, by Thermo Fisher Scientific (1 mentions) Acclaim pepmap 100 trap column, by Thermo Fisher Scientific (1 mentions) Orbitrap velos pro, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

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4 protocols using acclaim pepmap rslc c18 nano column

Nano-LC-MS/MS Proteomics Workflow

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The LC-MS/MS system consisted of a nanoAcquity Ultra Performance LC (UPLC, Ultimate 3000, Thermo Fisher Scientific) coupled with a Q Exactive™ Hybrid Quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific). The samples were loaded to an Acclaim PepMap 100 C18 nano-trap column (75μm×2cm, 3μm particles; Thermo Fisher Scientific) using solvent A at a flow rate of 2.5 μL/min for 5min. Peptide separation was then conducted using an Acclaim PepMap RSLC C18 nano-column (75μm×50cm, 2μm particles; Thermo Fisher Scientific). The mobile phase solvent consisted of solvents A and B (0.1% FA in ACN: water [80:20, v/v]), and the flow rate was fixed at 300nL/min. The gradient was set up as follows: solvent B, equilibration at 5% for 15 min, 5–20% for 60 min, 20–50% for 80 min, 50–96% for 1 min, holding at 96% for 10 min, 96–4% for 1 min, and holding at 4% for 17 min for column re-equilibration. The operation parameters were set as follows: the spray voltage was 2.2kV, scan range (m/z) was from 500–2000, resolution of full-MS scan was 60, 000, MS/MS scans at 200 m/z and the resolution was 15, 000. Peptides were selected for tandem mass spectrometry using normalized collision energy (NCE) setting as 28%. Dynamic exclusion was set at 20 s to minimize repeated analyses of the same abundant precursor ions.

Han Y., Zhong L, & Ren F. (2022). A simple method for the preparation of positive samples to preliminarily determine the quality of phosphorylation-specific antibody. PLoS ONE, 17(7), e0272138.

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LC-MS/MS Analysis of Protein Peptides

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For on-line LC-MS/MS analyses, a labeled sample containing approximately 0.5 μg ubiquitin peptides or 2 μg β2m or hGH peptides was loaded on a Thermo Scientific Easy-NanoLC 1000 system (Waltham, MA). Samples were loaded, trapped, and desalted on a Thermo Scientific Acclaim™ PepMap™ C18 trap column (2 cm × 75 μm, 3 μm particle size). Separation of peptides was performed using an Acclaim™ PepMap™ RSLC C18 nanocolumn (15 cm × 75 μm, 3 μm particle size; Thermo Scientific) with a flow rate of 300 nL/min. LC/MS-grade water (solvent A) and acetonitrile (solvent B), each containing 0.1% formic acid, were used as mobile phases. A linear gradient for separation of the peptides consisted of 0% B to 50% B over 60 min (β2m), 0% B to 50% B over 30 min (ubiquitin), and 0% B to 45% B over 35 min (hGH).

Limpikirati P., Pan X, & Vachet R.W. (2019). Covalent Labeling with Diethylpyrocarbonate is Sensitive to Residue Microenvironment, Providing Improved Analysis of Protein Higher Order Structure by Mass Spectrometry. Analytical chemistry, 91(13), 8516-8523.

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Fc Glycopeptide Identification by LC-MS

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Glycopeptides were separated with an Ultimate 3000 RSLCnano high-performance liquid chromatography system (Thermo Scientific, Waltham, MA) equipped with an Acclaim PepMap 100 trap column (100 μm × 20 mm, 5 μm particle size; Thermo Scientific) and an Acclaim PepMap RSLC C18 nano-column (75 μm × 150 mm, 2 μm particle size) analytical column. Five hundred nL of total IgG and two hundred nL of HLA-A2-specific IgG was injected and separated with a gradient from 97% solvent A (0.1% formic acid in water) and 3% solvent B (95% ACN) down to 27% solvent B, at a flowrate of 700 nL/min over 15 minutes. The LC-MS system was hyphenated to a maXis HD quadrupole time-of-flight mass spectrometer (Bruker Daltonics, Billerica, MA) via an electrospray ionization interface, which was equipped with a CaptiveSpray nanoBooster using ACN-enriched nitrogen gas (at 0.2 bar pressure and a dry gas flow rate of 3 L/min). A frequency of 1 Hz was used for recording the spectra in the m/z range of 550–1800 in positive ion polarity mode. The transfer time was set to 130 μs, the pre-pulse storage time to 10 μs, while the collision energy was set to 5 eV.¹¹³ (link) This method allowed unambiguous identification of IgG Fc glycopeptides in a subclass specific manner based on accurate mass (MS1) and specific migration positions in liquid chromatography.

Bharadwaj P., Shrestha S., Pongracz T., Concetta C., Sharma S., Le Moine A., de Haan N., Murakami N., Riella L.V., Holovska V., Wuhrer M., Marchant A, & Ackerman M.E. (2022). Afucosylation of HLA-specific IgG1 as a potential predictor of antibody pathogenicity in kidney transplantation. Cell Reports Medicine, 3(11), 100818.

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3D Spheroid Proteome Analysis using C18 Enrichment and LC-MS/MS

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3D spheroid cell culture samples were concentrated on an enrichment column (C18, 5 μm, 100 Å, 20 × 0.1 mm, Thermo Fisher Scientific) for 6 min with the flow rate of 5 μl/min. Chromatographic separation was carried out on an Acclaim PepMap RSLC C18 nanocolumn (2 μm, 50 × 75 μm) (Thermo Fisher Scientific) at 60 °C with the flow rate of 0.3 μl/min and the following gradient: 6 to 154 min: 4 to 25% B, 154 to 159 min: 25 to 95% B, 159 to 169 min: 95% B, 169.1 to 184 min: 4% B.
For spheroids cultured on CAM, chromatographic separation was carried out on an Aurora Series UHPLC C18 column (250 mm × 75 μm, 1.6 μm) (Ionopticks) with the flow of 0.25 μl/min and the following gradient: 0 to 18 min: 2% B, 18 to 160 min: 2 to 25% B, 160 to 167 min: 25 to 35% B, 167 to 168 min: 35 to 95% B, 168 to 178 min: 95 to 2% B. Mass spectrometry was performed on Orbitrap Velos Pro (Thermo Fisher Scientific) operated in positive ion mode by alternating full scan MS (m/z 300–2000, 60,000 resolution) in the ion cyclotron resonance cell and MS/MS by collision-induced dissociation of the ten most intense peaks in the ion trap (with dynamic exclusion enabled for 35 s). The mass spectrometry proteomics data were deposited to the ProteomeXchange Consortium via the PRIDE (23 (link)) partner repository with the data set identifier PXD021105 and doi:10.6019/PXD021105.

Honeder S., Tomin T., Nebel L., Gindlhuber J., Fritz-Wallace K., Schinagl M., Heininger C., Schittmayer M., Ghaffari-Tabrizi-Wizsy N, & Birner-Gruenberger R. (2021). Adipose Triglyceride Lipase Loss Promotes a Metabolic Switch in A549 Non–Small Cell Lung Cancer Cell Spheroids. Molecular & Cellular Proteomics : MCP, 20, 100095.

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