Log In Sign up
The largest database of trusted experimental protocols

Reprosil pur c18 aq 3.0 m resin

Manufactured by Dr. Maisch
Visit Supplier
Sourced in United States

ReproSil-Pur C18-AQ 3.0 μm resin is a silica-based stationary phase with a bonded C18 alkyl functionality and an aqueous endcapping. It is designed for use in high-performance liquid chromatography (HPLC) and ultra-high-performance liquid chromatography (UHPLC) applications.

Automatically generated - may contain errors

Lab products found in correlation

Dionex ultimate 3000 lc system, by Thermo Fisher Scientific (3 mentions) Orbitrap elite, by Thermo Fisher Scientific (2 mentions) Eksigent ekspert nanolc 425 system, by AB Sciex (2 mentions) Fusion lumos mass spectrometer, by Thermo Fisher Scientific (2 mentions) Ltq orbitrap elite mass spectrometer, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

ReproSil-Pur C18-AQ (72 citations) Reprosil-Pur C18 (21 citations) ReproSil-Pur C18-AQ resin (19 citations) ReproSil-Pur C18 resin (17 citations) C18 resin (14 citations) Reprosil C18 resin (8 citations) ReproSil-Pur C18-AQ 3 µm resin (6 citations) Reprosil-AQ Pur (3 citations)

6 protocols using reprosil pur c18 aq 3.0 m resin

1

Nano-LC-MS/MS Peptide Fractionation Workflow

Check if the same lab product or an alternative is used in the 5 most similar protocols
Each concatenated peptide fraction was resuspended in 20 μl 0.1 % formic acid. In total 10 % of the material was injected and separated on a 18 cm reversed phase column (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH) over a total run of 160 min using a two-step linear gradient with 4–25 % buffer B (0.2% (v/v) formic acid, 5% DMSO, and 94.8% (v/v) acetonitrile) for 120 min followed by 25–40 % buffer B for 30 min using the Eksigent ekspert nanoLC-425 system (Sciex, Framingham, U.S.A). The LC system was coupled on-line with an Orbitrap Elite instrument (Thermo Fisher Scientific, Bremen, Germany) via a nano-electrospray source. Full scans were acquired in the Orbitrap mass analyzer with resolution 60,000 at 340–1600 m/z. Unassigned charge states were rejected and the top 20 most intense ions with charge states 2 and up were sequentially isolated for MS/MS analysis using CID fragmentation. A minimal signal of 500 was required, the normalized collision energy was set to 35% and the fragmented peptide masses were collected in the ion-trap. Dynamic exclusion was enabled with a repeat count of 1 with the repeat duration set to 30 seconds.
Khodadoust M.S., Olsson N., Wagar L.E., Haabeth O.A., Chen B., Swaminathan K., Rawson K., Liu C.L., Steiner D., Lund P., Rao S., Zhang L., Marceau C., Stehr H., Newman A.M., Czerwinski D.K., Carlton V.E., Moorhead M., Faham M., Kohrt H.E., Carette J., Green M.R., Davis M.M., Levy R., Elias J.E, & Alizadeh A.A. (2017). Antigen Presentation Profiling Reveals Recognition of Lymphoma Immunoglobulin Neoantigens. Nature, 543(7647), 723-727.
+ Open protocol
+ Expand
2

Nano-LC-MS/MS Peptide Fractionation Workflow

Check if the same lab product or an alternative is used in the 5 most similar protocols
Each concatenated peptide fraction was resuspended in 20 μl 0.1 % formic acid. In total 10 % of the material was injected and separated on a 18 cm reversed phase column (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH) over a total run of 160 min using a two-step linear gradient with 4–25 % buffer B (0.2% (v/v) formic acid, 5% DMSO, and 94.8% (v/v) acetonitrile) for 120 min followed by 25–40 % buffer B for 30 min using the Eksigent ekspert nanoLC-425 system (Sciex, Framingham, U.S.A). The LC system was coupled on-line with an Orbitrap Elite instrument (Thermo Fisher Scientific, Bremen, Germany) via a nano-electrospray source. Full scans were acquired in the Orbitrap mass analyzer with resolution 60,000 at 340–1600 m/z. Unassigned charge states were rejected and the top 20 most intense ions with charge states 2 and up were sequentially isolated for MS/MS analysis using CID fragmentation. A minimal signal of 500 was required, the normalized collision energy was set to 35% and the fragmented peptide masses were collected in the ion-trap. Dynamic exclusion was enabled with a repeat count of 1 with the repeat duration set to 30 seconds.
Khodadoust M.S., Olsson N., Wagar L.E., Haabeth O.A., Chen B., Swaminathan K., Rawson K., Liu C.L., Steiner D., Lund P., Rao S., Zhang L., Marceau C., Stehr H., Newman A.M., Czerwinski D.K., Carlton V.E., Moorhead M., Faham M., Kohrt H.E., Carette J., Green M.R., Davis M.M., Levy R., Elias J.E, & Alizadeh A.A. (2017). Antigen Presentation Profiling Reveals Recognition of Lymphoma Immunoglobulin Neoantigens. Nature, 543(7647), 723-727.
+ Open protocol
+ Expand
3

Histone H3 Cleavage Product Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein bands corresponding to cleaved H3 products were cut and digested with Glu-C endoproteinase in 50 mM NH4HCO3 buffer. Samples were reconstituted in 0.1% formic acid and analyzed on a Fusion Lumos mass spectrometer (Thermo Fisher Scientific, San Jose, USA) equipped with a Dionex Ultimate 3000 LC-system. Peptides were separated by capillary reverse phase chromatography on a 24 cm reversed phase column (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH)). Full MS scans, data dependent HCD (higher-energy collisional dissociation) and EThcD (electron transfer dissociation with 25% of supplemental collision energy) MS/MS scans were all acquired in the Orbitrap mass analyzer. H3 cleavage products with cleavage sites range from H3K14 to H3R42 were analyzed. Peptide sequences were confirmed based on the EThcD spectra manually. In cases where multiple cleavage products were found, peak area of the precursor peptides were used to compare the relative abundance of each cleavage product.
Cheung P., Schaffert S., Chang S.E., Dvorak M., Donato M., Macaubas C., Foecke M.H., Li T.M., Zhang L., Coan J.P., Schulert G.S., Grom A.A., Henderson L.A., Nigrovic P.A., Elias J.E., Gozani O., Mellins E.D., Khatri P., Utz P.J, & Kuo A.J. (2021). REPRESSION OF CTSG, ELANE, AND PRTN3-MEDIATED HISTONE H3 PROTEOLYTIC CLEAVAGE PROMOTES MONOCYTE-TO-MACROPHAGE DIFFERENTIATION. Nature immunology, 22(6), 711-722.
+ Open protocol
+ Expand
4

Mass Spectrometry Analysis of AML Immunopeptidomes

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
MHC-Class I and II immunopeptidomes were measured in parallel from primary AML tumor samples (1 X 108 cells per MHC preparation) and AML cell lines (1 X 109 cells per MHC preparation) as previously described (see S1 File) [8 (link),20 (link),21 ]. Isolated HLA peptides were reconstituted in 12 μl of 0.1% formic acid and analyzed on an LTQ Orbitrap Elite mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) or a Fusion Lumos mass spectrometer (Thermo Fisher Scientific, San Jose, USA). Peptides were separated by capillary reverse phase chromatography on 20–24 cm reversed phase columns (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH)) using two-step linear gradients with increasing acetonitrile as previously described (see S1 File) [8 (link),21 ]. All primary AML tumor samples were measured with the Orbitrap Elite mass spectrometer and analyzed three times with complementary acquisition methods. The two cell line specimens (OCI-AML3 and MV4-11) were analyzed with the Fusion Lumos tribrid mass spectrometer.
Narayan R., Olsson N., Wagar L.E., Medeiros B.C., Meyer E., Czerwinski D., Khodadoust M.S., Zhang L., Schultz L., Davis M.M., Elias J.E, & Levy R. (2019). Acute myeloid leukemia immunopeptidome reveals HLA presentation of mutated nucleophosmin. PLoS ONE, 14(7), e0219547.
+ Open protocol
+ Expand
5

Peptide Analysis via Fusion Lumos Mass Spectrometry

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptide samples were analyzed using a Fusion Lumos mass spectrometer (Thermo Fisher Scientific, San Jose, CA) equipped with Dionex Ultimate 3000 LC systems (Thermo Fisher Scientific, San Jose, CA). Peptides were separated by capillary reverse phase chromatography on a 25 cm reversed phase column (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH)). Liquid chromatography was performed using a two-step linear gradient with 4–25 % buffer B (0.1% (v/v) formic acid in acetonitrile) for 90 min followed by 25–40 % buffer B for 10 min. Data was acquired in top 20 data dependent mode. Full MS scans were acquired in the Orbitrap mass analyzer with a resolution of 120,000 (FWHM) and m/z scan range of 340–1500. Selected precursor ions were subjected to fragmentation using higher-energy collisional dissociation (HCD) with quadrupole isolation, isolation window of 1.6 m/z, and normalized collision energy of 30%. HCD fragments were analyzed in the Orbitrap mass analyzer with a resolution of 15,000 (FWHM). Fragmented ions were dynamically excluded from further selection for a period of 15 seconds. The AGC target was set to 400,000 and 50,000 for full FTMS scans and FTMS2 scans, respectively. The maximum injection time was set to 50 ms for full FTMS scans and dynamic for FTMS2 scans.
Lanz M.C., Zatulovskiy E., Swaffer M.P., Zhang L., Ilerten I., Zhang S., You D.S., Marinov G., McAlpine P., Elias J.E, & Skotheim J.M. (2022). Increasing cell size remodels the proteome and promotes senescence. Molecular cell, 82(17), 3255-3269.e8.
+ Open protocol
+ Expand
6

Histone H3 Cleavage Product Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein bands corresponding to cleaved H3 products were cut and digested with Glu-C endoproteinase in 50 mM NH4HCO3 buffer. Samples were reconstituted in 0.1% formic acid and analyzed on a Fusion Lumos mass spectrometer (Thermo Fisher Scientific, San Jose, USA) equipped with a Dionex Ultimate 3000 LC-system. Peptides were separated by capillary reverse phase chromatography on a 24 cm reversed phase column (100 μm inner diameter, packed in-house with ReproSil-Pur C18-AQ 3.0 m resin (Dr. Maisch GmbH)). Full MS scans, data dependent HCD (higher-energy collisional dissociation) and EThcD (electron transfer dissociation with 25% of supplemental collision energy) MS/MS scans were all acquired in the Orbitrap mass analyzer. H3 cleavage products with cleavage sites range from H3K14 to H3R42 were analyzed. Peptide sequences were confirmed based on the EThcD spectra manually. In cases where multiple cleavage products were found, peak area of the precursor peptides were used to compare the relative abundance of each cleavage product.
Cheung P., Schaffert S., Chang S.E., Dvorak M., Donato M., Macaubas C., Foecke M.H., Li T.M., Zhang L., Coan J.P., Schulert G.S., Grom A.A., Henderson L.A., Nigrovic P.A., Elias J.E., Gozani O., Mellins E.D., Khatri P., Utz P.J, & Kuo A.J. (2021). REPRESSION OF CTSG, ELANE, AND PRTN3-MEDIATED HISTONE H3 PROTEOLYTIC CLEAVAGE PROMOTES MONOCYTE-TO-MACROPHAGE DIFFERENTIATION. Nature immunology, 22(6), 711-722.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!