C18 reprosil particles

Manufactured by Dr. Maisch

Sourced in Germany

The C18 ReproSil particles are a type of reversed-phase chromatography material used for high-performance liquid chromatography (HPLC) and other analytical techniques. These particles are made of silica and have a chemically bonded C18 alkyl phase, which provides a hydrophobic surface for the separation and analysis of a wide range of compounds, including polar and non-polar molecules.

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Close spelling variants of this product

C18 particles (27 citations) Reprosil-Pur C18-AQ particles (10 citations) ReproSil-Pur 120 C18-AQ particles (6 citations) ReproSil particles (3 citations) ReproSil-Pur 130 C18-AQ 3 μm particles (2 citations)

5 protocols using c18 reprosil particles

Mass Spectrometry Analysis of Phosphopeptides

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Phosphopeptides (5 µL/10 µL) were loaded onto a 15 cm column packed in-house with 1.9 µm C18 ReproSil particles (Cat# r119.aq, Dr. Maisch GmbH, Ammerbuch, Germany). An Easy-nLC 1000 system (Cat# LC140, Thermo Fisher Scientific, Odense, Denmark) coupled to the MS (Q Exactive, Thermo Fisher Scientific, Bremen, Germany) was used to separate the (phospho)peptides with a binary buffer system of buffer A (0.1% formic acid) and buffer B (60% acetonitrile, 0.1% formic acid) at a flow rate of 300 nl/min. Phosphopeptides were introduced into the column with buffer A and eluted with 5 to 25% of buffer B, resulting in a 2 h gradient.
We used a data-dependent Top10 MS acquisition method in which one full scan (400–2000 m/z, MS resolution 70,000 at 200 m/z) at a target of 3 × 10⁶ ions was performed, followed by 10 data-dependent MS/MS scans with higher-energy collisional dissociation (HCD) with the following parameters: a target of 1 × 10⁵ ions, maximum ion fill time 80 ms (phosphopeptides), isolation window 2.2 m/z, normalized collision energy (NCE) of 25% and underfill ratio of 1% at MS/MS resolution of 17,500 at 200 m/z. Dynamic exclusion of 60 s was enabled.

Sampadi B., Mullenders L.H, & Vrieling H. (2021). Phosphoproteomics Sample Preparation Impacts Biological Interpretation of Phosphorylation Signaling Outcomes. Cells, 10(12), 3407.

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Single-shot DIA Peptide Identification

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Single-shot measurements were performed with 500 ng of purified peptides, determined by absorbance at 280 nm on a NanoDrop 2000. Peptides were loaded onto a 50-cm column, packed in-house with 1.9 µm C18 ReproSil particles (Dr. Maisch GmbH) with an EASY-nLC 1200 system (Thermo Fisher Scientific). Column temperature was kept at 60 °C using a column oven. Peptides were eluted over 60 min using a binary buffer system consisting of buffer A (0.1% formic acid) and buffer B (80% ACN, 0.1% formic acid). In brief, the gradient started with 5% buffer B and increased stepwise to 45% over 45 min, followed by a wash-out at 95% buffer B, all at a flowrate of 300 nl min⁻¹. Peptides were then transferred to the gas phase using electrospray ionization, prefiltered by a FAIMS device (coefficient of variation −50 V) before entering the Orbitrap Exploris 480 (Thermo Fisher Scientific) mass spectrometer. A data-independent (DIA) acquisition method was used, in which one full scan (300–1,650 m/z, maximum ion fill time of 45 ms, normalized AGC target 300%, R = 120.000 at 200 m/z) was followed by 66 tMS2 fragment scans of unequally spaced windows with 1 Th overlap, covering the same m/z range (fill time 22 ms, normalized AGC target 1,000%, normalized high-collision density energy of 30%, R = 15.000).

Quarta C., Stemmer K., Novikoff A., Yang B., Klingelhuber F., Harger A., Bakhti M., Bastidas-Ponce A., Baugé E., Campbell J.E., Capozzi M., Clemmensen C., Collden G., Cota P., Douros J., Drucker D.J., DuBois B., Feuchtinger A., Garcia-Caceres C., Grandl G., Hennuyer N., Herzig S., Hofmann S.M., Knerr P.J., Kulaj K., Lalloyer F., Lickert H., Liskiewicz A., Liskiewicz D., Maity G., Perez-Tilve D., Prakash S., Sanchez-Garrido M.A., Zhang Q., Staels B., Krahmer N., DiMarchi R.D., Tschöp M.H., Finan B, & Müller T.D. (2022). GLP-1-mediated delivery of tesaglitazar improves obesity and glucose metabolism in male mice. Nature Metabolism, 4(8), 1071-1083.

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Phosphopeptide Separation and MS Analysis

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Phosphopeptides were loaded onto a 40 cm column fabricated in-house with 75 μM inner diameter fused silica packed with 1.9 μM C18 ReproSil particles (Dr. Maisch GmBH). A column oven (Sonation) was used to maintain column temperature at 60°C, and a U3000 HPLC system (Dionex, Thermo Fisher Scientific) was connected to a Q Exactive HF X benchtop Orbitrap mass spectrometer (Thermo Fisher Scientific) with a NanoSpray Flex ion source (Thermo Fisher Scientific). For all samples, peptides were separated using a binary buffer system of 0.1% (v/v) formic acid (buffer A) and 80% (v/v) acetonitrile/0.1% (v/v) formic acid (buffer B). Peptides were eluted at a flow rate of 400 nl/min and separated with a gradient of 3 – 19% buffer B over 40 minutes, followed by 19 – 41% buffer B over 20 minutes, and peptides were analyzed with a full scan (350 – 1,400 m/z; R = 60,000 at 200 m/z) at a target of 3e6 ions, followed by up to ten data-dependent MS2 scans using HCD (target 1e5; max. IT 50 ms; isolation window 1.6 m/z; NCE 27%; min. AGC target 2e4), detected in the Orbitrap mass analyzer (R = 15,000 at 200 m/z). Dynamic exclusion (30 s) and Apex trigger (2 to 4 s) were enabled.

Mills R.J., Humphrey S.J., Fortuna P.R., Lor M., Foster S.R., Quaife-Ryan G.A., Johnston R.L., Dumenil T., Bishop C., Rudraraju R., Rawle D.J., Le T., Zhao W., Lee L., Mackenzie-Kludas C., Mehdiabadi N.R., Halliday C., Gilham D., Fu L., Nicholls S.J., Johansson J., Sweeney M., Wong N.C., Kulikowski E., Sokolowski K.A., Tse B.W., Devilée L., Voges H.K., Reynolds L.T., Krumeich S., Mathieson E., Abu-Bonsrah D., Karavendzas K., Griffen B., Titmarsh D., Elliott D.A., McMahon J., Suhrbier A., Subbarao K., Porrello E.R., Smyth M.J., Engwerda C.R., MacDonald K.P., Bald T., James D.E, & Hudson J.E. (2021). BET inhibition blocks inflammation-induced cardiac dysfunction and SARS-CoV-2 infection. Cell, 184(8), 2167-2182.e22.

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Quantitative Proteomics by FAIMS-DIA-MS

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0.5 μg of peptides were analyzed using the EASY-nLC 1200 (Thermo Fisher Scientific) connected to Orbitrap Exploris 480 Mass Spectrometer (Thermo Fisher Scientific) and a nano-electrospray ion source (Thermo Fisher Scientific). FAIMS Pro™ with Orbitrap Fusion ™ module was used with two different compensation voltages (CV) (−50V and −70V). Peptides were loaded at 60 °C onto a 50 cm, 75 μm inner diameter, in-house packed HPLC column with 1.9 μm with C18 Reprosil particles (Dr. Maisch GmbH). A binary buffer system [0.1 % formic acid (buffer A) and 80 % can, 0.1% formic acid (buffer B)] at a flow rate of 300 nl/min was used over a 60 min gradient: 5–20 % buffer B over 30 min, 20–29 % buffer B over 9 min, 29–45 % buffer B over 6 min, 45–95 % buffer B over 5 min, wash with 95 % buffer B for 5 min and 95-5% buffer B over 5 min. MS data were acquired in DIA (data-independent acquisition) mode using a 2 s cycle time scan method. Full scan MS targets were in a 300–1650 m/z scan range with 3 × 10⁶ charges and data was acquired in 120000 at m/z 200 resolution with 45 ms maximum injection time. Precursor ions for MS/MS scans were fragmented by higher-energy C-trap dissociation (HCD) with a normalized collision energy of 30. MS/MS scan sets were 15000 at m/z 200 resolution with an ion target value of %1000 and a maximum injection time of 22 ms.

Cota P., Caliskan Ö.S., Bastidas-Ponce A., Jing C., Jaki J., Saber L., Czarnecki O., Taskin D., Blöchinger A.K., Kurth T., Sterr M., Burtscher I., Krahmer N., Lickert H, & Bakhti M. (2023). Insulin regulates human pancreatic endocrine cell differentiation in vitro. Molecular Metabolism, 79, 101853.

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Liquid Chromatography-Orbitrap Mass Spectrometry

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The samples were analyzed in a liquid chromatography system (nano-UHPLC Dionex Ultimante 3.000) coupled online to the Orbitrap Elite™ hybrid ion trap-orbitrap mass spectrometer (Thermo Scientific, Germany). Two types of capillary columns were used in the chromatographic system, a 100 µm × 200 mm long internal diameter pre-column packed in the laboratory with 5 µm ReprosilPur 5 µm spherical silica particles with C18 Å (Dr. Maisch, Germany) and a 75 µm × 35 cm long analytical column, also packaged in the laboratory, with 3 µm C18 Reprosil particles with 120 Å pores (Dr. Maisch). Samples were eluted using a gradient of 98% solution A (0.1% formic acid in water) to 35% solution B (0.1% formic acid in ACN) over 155 min, 35 to 98% solution B for 5 min, and 98% solution B for 8 min (a total of 168 min at 230 nL/min). After each run, the column was equilibrated with 98% solution A. Mass spectra were acquired in positive mode by applying data-dependent automatic survey MS scan and tandem mass spectral acquisition (MS/MS). All MS scans in the orbitrap (mass range: m/z 350-1650, resolution: 120,000) were followed by MS/MS of the fifteen most intense ions. Fragmentation by collision-induced high energy dissociation (HCD) and repeated ion fragmentation were dynamically prevented.

Graziani D., Ribeiro J.V., Cruz V.S., Gomes R.M., Araújo E.G., Santos AC J.ú.n.i.o.r., Tomaz H.C., Castro C.H., Fontes W., Batista K.A., Fernandes K.F, & Xavier C.H. (2021). Oxidonitrergic and antioxidant effects of a low molecular weight peptide fraction from hardened bean (Phaseolus vulgaris) on endothelium. Brazilian Journal of Medical and Biological Research, 54(6), e10423.

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