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Reprosil pur c18 aq materials

Manufactured by Dr. Maisch
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Sourced in Germany

ReproSil-Pur C18-AQ materials are a type of reversed-phase chromatographic media used for liquid chromatography. They are composed of silica particles with a chemically bonded C18 alkyl stationary phase, which is suitable for the separation and purification of a wide range of analytes, including polar and non-polar compounds.

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Lab products found in correlation

Htc pal autosampler, by CTC Analytics (3 mentions) Ultimate 3000 rslcnano liquid chromatograph, by Thermo Fisher Scientific (2 mentions) Orbitrap fusion lumos tribrid mass spectrometer, by Thermo Fisher Scientific (2 mentions) Orbitrap fusion lumos, by Thermo Fisher Scientific (2 mentions) Ultimate 3000 pump, by Thermo Fisher Scientific (1 mentions) Q exactive mass spectrometer, by Thermo Fisher Scientific (1 mentions)

5 protocols using reprosil pur c18 aq materials

1

Nanoflow LC-MS/MS Proteomics Analysis

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A nanoLC/MS/MS system consisting of an UltiMate™ 3000 RSLCnano liquid chromatograph and an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) was employed. The purified peptides (250 ng) were injected onto a self-pulled analytical column (150 mm length × 100 μm i.d.) packed with ReproSil-Pur C18-AQ materials (3 μm, Dr. Maisch GmbH, Ammerbuch-Entringen, Germany). A gradient condition with flow rate of 500 nL/min was employed, that is, 5–10% B in 1 min, 10–40% B in 64 min, 40–100% B in 5 min, 100% B for 10 min, and 5% B for 30 min (Solvent A was 0.5% acetic acid, and solvent B was 0.5% acetic acid in 80% acetonitrile). Peptides were ionized at 2400 V. The MS scan range was m/z 300–1500 at a resolution of 120,000 (at m/z 200) at orbitrap using an automatic gain control (AGC) set to 4 × 105 ions and the maximum injection time (IT) set to 50 ms, followed by product ion scans of the 20 most intense precursors for 3 s with 1.6 m/z isolation at quadrupole, normalized HCD collision energy of 30%, and a resolution of 15,000 (at m/z 200), 5 × 104 AGC and 100 ms maximum IT. Dynamic exclusion was applied for 20 s.
Tajima K., Ikeda K., Chang H.Y., Chang C.H., Yoneshiro T., Oguri Y., Jun H., Wu J., Ishihama Y, & Kajimura S. (2019). Mitochondrial lipoylation integrates age-associated decline in brown fat thermogenesis. Nature metabolism, 1(9), 886-898.
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2

Nano-LC/MS/MS for Proteome Analysis

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Nano-LC/MS/MS was conducted using a Q Exactive mass spectrometer (Thermo Fisher Scientific) or an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific) equipped with an Ultimate 3000 pump (Thermo Fisher Scientific) and an HTC-PAL autosampler (CTC Analytics). Peptides were separated by a self-pulled analytical column (150 mm length by 100 μm internal diameter) packed with ReproSil-Pur C18-AQ materials (3 μm, Dr. Maisch, Germany). The injection volume was set to 5 μl, and the flow rate was 500 nl/min. The mobile phases consisted of (A) 0.5% acetic acid and (B) 0.5% acetic acid in 80% acetonitrile. Two-step linear gradient programs ranging from 5 to 99% B over 50 to 90 min were used. An MS1 survey scan followed by MS2 scans were performed according to the data-dependent acquisition mode.
Oda Y., Takahashi C., Harada S., Nakamura S., Sun D., Kiso K., Urata Y., Miyachi H., Fujiyoshi Y., Honigmann A., Uchida S., Ishihama Y, & Toyoshima F. (2021). Discovery of anti-inflammatory physiological peptides that promote tissue repair by reinforcing epithelial barrier formation. Science Advances, 7(47), eabj6895.
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3

Nanoflow LC-MS/MS Proteomics Analysis

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A nanoLC/MS/MS system consisting of an UltiMate™ 3000 RSLCnano liquid chromatograph and an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) was employed. The purified peptides (250 ng) were injected onto a self-pulled analytical column (150 mm length × 100 μm i.d.) packed with ReproSil-Pur C18-AQ materials (3 μm, Dr. Maisch GmbH, Ammerbuch-Entringen, Germany). A gradient condition with flow rate of 500 nL/min was employed, that is, 5–10% B in 1 min, 10–40% B in 64 min, 40–100% B in 5 min, 100% B for 10 min, and 5% B for 30 min (Solvent A was 0.5% acetic acid, and solvent B was 0.5% acetic acid in 80% acetonitrile). Peptides were ionized at 2400 V. The MS scan range was m/z 300–1500 at a resolution of 120,000 (at m/z 200) at orbitrap using an automatic gain control (AGC) set to 4 × 105 ions and the maximum injection time (IT) set to 50 ms, followed by product ion scans of the 20 most intense precursors for 3 s with 1.6 m/z isolation at quadrupole, normalized HCD collision energy of 30%, and a resolution of 15,000 (at m/z 200), 5 × 104 AGC and 100 ms maximum IT. Dynamic exclusion was applied for 20 s.
Tajima K., Ikeda K., Chang H.Y., Chang C.H., Yoneshiro T., Oguri Y., Jun H., Wu J., Ishihama Y, & Kajimura S. (2019). Mitochondrial lipoylation integrates age-associated decline in brown fat thermogenesis. Nature metabolism, 1(9), 886-898.
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4

Nanoflow LC-MS/MS for Deep Proteome Profiling

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Nano-scale reversed-phase liquid chromatography coupled with tandem mass spectrometry (nanoLC/MS/MS) was performed by an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific), connected to a Thermo Ultimate 3000 RSLCnano pump and an HTC-PAL autosampler (CTC Analytics, Zwingen, Switzerland) equipped with a self-pulled analytical column (150 mm length × 100 μm i.d.) (14) packed with ReproSil-Pur C18-AQ materials (3 μm, Dr. Maisch GMBH, Ammerbuch, Germany). The mobile phases consisted of (A) 0.5% acetic acid and (B) 0.5% acetic acid and 80% acetonitrile. Peptides were eluted from the analytical column at a flow rate of 500 nL/min by altering the gradient: 5-10% B in 5 min, 10-40% B in 60 min, 40-99% B in 5 min and 99% for 5 min. The Orbitrap Fusion Lumos instrument was operated in the datadependent mode with a full scan in the Orbitrap followed by MS/MS scans for 3 sec using higherenergy collisional dissociation (HCD). The applied voltage for ionization was 2.4 kV. The full scans were performed with a resolution of 120,000, a target value of 4x10 5 ions and a maximum injection time of 50 ms. The MS scan range was m/z 300-1,500. The MS/MS scans were performed with a 15,000 resolution, a 5x10 4 target value and a 50 ms maximum injection time. The isolation window was set to 1.6, and the normalized HCD collision energy was 30. Dynamic exclusion was applied for 20 sec.
Uchiyama J., Ishihama Y., & Imami K. (2020). Quantitative nascent proteome profiling by dual pulse labeling with O-propargyl-puromycin and stable isotope labeled amino acids.
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5

Nanoflow LC-MS/MS for Deep Proteome Profiling

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nano-scale reversed-phase liquid chromatography coupled with tandem mass spectrometry (nanoLC/MS/MS) was performed by an Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific), connected to a Thermo Ultimate 3000 RSLCnano pump and an HTC-PAL autosampler (CTC Analytics, Zwingen, Switzerland) equipped with a self-pulled analytical column (150 mm length × 100 μm i.d.) (14) packed with ReproSil-Pur C18-AQ materials (3 μm, Dr. Maisch GMBH, Ammerbuch, Germany). The mobile phases consisted of (A) 0.5% acetic acid and (B) 0.5% acetic acid and 80% acetonitrile. Peptides were eluted from the analytical column at a flow rate of 500 nL/min by altering the gradient: 5-10% B in 5 min, 10-40% B in 60 min, 40-99% B in 5 min and 99% for 5 min. The Orbitrap Fusion Lumos instrument was operated in the datadependent mode with a full scan in the Orbitrap followed by MS/MS scans for 3 sec using higherenergy collisional dissociation (HCD). The applied voltage for ionization was 2.4 kV. The full scans were performed with a resolution of 120,000, a target value of 4x10 5 ions and a maximum injection time of 50 ms. The MS scan range was m/z 300-1,500. The MS/MS scans were performed with a 15,000 resolution, a 5x10 4 target value and a 50 ms maximum injection time. The isolation window was set to 1.6, and the normalized HCD collision energy was 30. Dynamic exclusion was applied for 20 sec.
Uchiyama J., Ishihama Y, & Imami K. (2021). Quantitative nascent proteome profiling by dual-pulse labelling with O-propargyl-puromycin and stable isotope-labelled amino acids. Journal of biochemistry, 169(2).
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