Easy spray pepmap rslc c18 75μm 250mm column

Manufactured by Thermo Fisher Scientific

The EASY-Spray PepMap RSLC C18 75μm × 250mm column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of peptides and proteins. This column features a reversed-phase C18 stationary phase and a 75μm internal diameter, providing efficient chromatographic separation with low back pressure. The column length of 250mm enables high-resolution separations.

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Lab products found in correlation

Ultimate 3000 rslcnano system, by Thermo Fisher Scientific (8 mentions) Acclaim pepmap 100 20mm 0.075mm trapping column, by Thermo Fisher Scientific (4 mentions) Q exactive plus hybrid quadrupole orbitrap mass spectrometer, by Thermo Fisher Scientific (4 mentions)

Close spelling variants of this product

EASY-Spray PepMap RSLC C18 column EASY-Spray PepMap RSLC C18 PepMap RSLC EASY-Spray column EASY PepMapTM RSLC C18 column Easy-Spray RSLC C18 column Easy Spray PepMap C18 column Easy-Spray PepMap® RSLC Easy-Spray C18 PepMap Easy Spray PepMap column PepMap RSLC C18 column

4 protocols using easy spray pepmap rslc c18 75μm 250mm column

Peptide Quantification and Identification by nanoLC-MS/MS

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Final peptides were resuspended in 0.1% formic acid, quantified (ThermoFisher Cat# 23275), and then diluted to a final concentration of 0.25μg/μL. Samples were subjected to nanoLC-MS/MS analysis using an UltiMate 3000 RSLCnano system (ThermoFisher) coupled to a Q Exactive Plus Hybrid Quadrupole-Orbitrap mass spectrometer (ThermoFisher) via a nanoelectrospray ionization source. For each injection, 4μL (1μg) of sample was first trapped on an Acclaim PepMap 100 20mm × 0.075mm trapping column (ThermoFisher Cat# 164535; 5μL/min at 98/2 v/v water/acetonitrile with 0.1% formic acid). Analytical separation was performed over a 95min gradient (flow rate of 250nL/min) of 4–25% acetonitrile using a 2μm EASY-Spray PepMap RSLC C18 75μm × 250mm column (ThermoFisher Cat# ES802A) with a column temperature of 45°C. MS1 was performed at 70,000 resolution, with an AGC target of 3×10⁶ ions and a maximum injection time (IT) of 100ms. MS2 spectra were collected by data-dependent acquisition (DDA) of the top 15 most abundant precursor ions with a charge greater than 1 per MS1 scan, with dynamic exclusion enabled for 20s. Precursor ions isolation window was 1.5m/z and normalized collision energy was 27. MS2 scans were performed at 17,500 resolution, maximum IT of 50ms, and AGC target of 1×10⁵ ions.

Hagen J.T., Montgomery M.M., Biagioni E.M., Krassovskaia P., Jevtovic F., Shookster D., Sharma U., Tung K., Broskey N.T., May L., Huang H., Brault J.J., Neufer P.D., Cabot M.C, & Fisher-Wellman K.H. (2022). Intrinsic adaptations in OXPHOS power output and reduced tumorigenicity characterize doxorubicin resistant ovarian cancer cells. Biochimica et biophysica acta. Bioenergetics, 1863(8), 148915.

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Nanoflow LC-MS/MS Peptide Analysis

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Final peptides were resuspended in 0.1% formic acid, quantified (ThermoFisher Cat# 23275), and then diluted to a final concentration of 0.25 μg/μl. Samples were subjected to nanoLC-MS/MS analysis using an UltiMate 3000 RSLCnano system (ThermoFisher) coupled to a Q Exactive Plus Hybrid Quadrupole-Orbitrap mass spectrometer (ThermoFisher) via a nanoelectrospray ionization source. For each injection, 4 μL (1 μg) of the sample was first trapped on an Acclaim PepMap 100 20 mm × 0.075 mm trapping column (ThermoFisher Cat# 164535; 5 μl/min at 98/2 v/v water/acetonitrile with 0.1% formic acid). Analytical separation was performed over a 95 min gradient (flow rate of 250 nl/min) of 4%–25% acetonitrile using a 2 μm EASY-Spray PepMap RSLC C18 75 μm × 250 mm column (ThermoFisher Cat# ES802A) with a column temperature of 45°C. MS1 was performed at 70 000 resolution, with an AGC target of 3 × 10⁶ ions and a maximum injection time (IT) of 100 ms. MS2 spectra were collected by data-dependent acquisition (DDA) of the top 15 most abundant precursor ions with a charge greater than 1 per MS1 scan, with dynamic exclusion enabled for 20 s. Precursor ions isolation window was 1.5 m/z and the normalized collision energy was 27. MS2 scans were performed at 17 500 resolution, maximum IT of 50 ms, and AGC target of 1 × 10⁵ ions.

Fisher-Wellman K.H., Hagen J.T., Kassai M., Kao L.P., Nelson M.A., McLaughlin K.L., Coalson H.S., Fox T.E., Tan S.F., Feith D.J., Kester M., Loughran TP J.r., Claxton D.F, & Cabot M.C. (2022). Alterations in sphingolipid composition and mitochondrial bioenergetics represent synergistic therapeutic vulnerabilities linked to multidrug resistance in leukemia. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 36(1), e22094.

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Peptide Identification by Nano-LC-MS/MS

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Final peptides were resuspended in 0.1% formic acid, quantified (Thermo Fisher Scientific; 23275), and diluted to a final concentration of 0.25μg/μL. Samples were subjected to nanoLC-MS/MS analysis using an UltiMate 3000 RSLCnano system (Thermo Fisher Scientific) coupled to a Q Exactive Plus Hybrid Quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific) via a nanoelectrospray ionization source. For each injection, 4μL (1μg) of sample was first trapped on an Acclaim PepMap 100 20mm × 0.075mm trapping column (Thermo Fisher Scientific; 164535; 5μL/min at 98/2 v/v water/acetonitrile with 0.1% formic acid). Analytical separation was performed over a 95min gradient (flow rate of 250nL/min) of 4–25% acetonitrile using a 2μm EASY-Spray PepMap RSLC C18 75μm × 250mm column (Thermo Fisher Scientific; ES802A) with a column temperature of 45°C. MS1 was performed at 70,000 resolution, with an AGC target of 3×10⁶ ions and a maximum injection time (IT) of 100ms. MS2 spectra were collected by data-dependent acquisition (DDA) of the top 15 most abundant precursor ions with a charge greater than 1 per MS1 scan, with dynamic exclusion enabled for 20s. Precursor ions isolation window was 1.5m/z and normalized collision energy was 27. MS2 scans were performed at 17,500 resolution, maximum IT of 50ms, and AGC target of 1×10⁵ ions.

Hagen J.T., Montgomery M.M., Aruleba R.T., Chrest B.R., Green T.D., Kassai M., Zeczycki T.N., Schmidt C.A., Bhowmick D., Tan S.F., Feith D.J., Chalfant C.E., Loughran TP J.r., Liles D., Minden M.D., Schimmer A.D., Cabot M.C., Mclung J.M, & Fisher-Wellman K.H. (2024). Mitochondria inside acute myeloid leukemia cells hydrolyze ATP to resist chemotherapy. bioRxiv.

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Quantitative Proteomics by Nano-LC-MS/MS

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Final peptides were resuspended in 0.1% formic acid, quantified (ThermoFisher Cat# 23275), and then diluted to a final concentration of 0.25μg/μL. Samples were subjected to nanoLC-MS/MS analysis using an UltiMate 3000 RSLCnano system (ThermoFisher) coupled to a Q Exactive Plus Hybrid Quadrupole-Orbitrap mass spectrometer (ThermoFisher) via a nanoelectrospray ionization source. For each injection, 4μL (1μg) of sample was first trapped on an Acclaim PepMap 100 20mm × 0.075mm trapping column (ThermoFisher Cat# 164535; 5μL/min at 98/2 v/v water/acetonitrile with 0.1% formic acid). Analytical separation was performed over a 120min gradient (flow rate of 250nL/min) of 4–45% acetonitrile using a 2μm EASY-Spray PepMap RSLC C18 75μm × 250mm column (ThermoFisher Cat# ES802A) with a column temperature of 45°C. MS1 was performed at 70,000 resolution, with an AGC target of 3×10⁶ ions and a maximum injection time (IT) of 100ms. MS2 spectra were collected by data-dependent acquisition (DDA) of the top 15 most abundant precursor ions with a charge greater than 1 per MS1 scan, with dynamic exclusion enabled for 20s. Precursor ions isolation window was 1.5m/z and normalized collision energy was 27. MS2 scans were performed at 17,500 resolution, maximum IT of 50ms, and AGC target of 1×10⁵ ions.

Gu X, & Li W.H. (1998). Estimation of evolutionary distances under stationary and nonstationary models of nucleotide substitution. Proceedings of the National Academy of Sciences of the United States of America, 95(11), 5899-5905.

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