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Acclaim pepmap100 separating column

Manufactured by Thermo Fisher Scientific
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The Acclaim PepMap100 separating column is a high-performance liquid chromatography (HPLC) column designed for the separation of peptides. It features a stationary phase of silica particles with a porous structure and a C18 reversed-phase coating. The column dimensions and particle size are optimized for effective peptide separation and analysis.

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Lab products found in correlation

2 cm guarding column, by Thermo Fisher Scientific (2 mentions) Dionex ultimate 3000 rslcnano system, by Thermo Fisher Scientific (2 mentions) Easy nlc 1200 instrument, by Thermo Fisher Scientific (1 mentions) Acclaim pepmap 100 pre column, by Thermo Fisher Scientific (1 mentions) Orbitrap velos pro, by Thermo Fisher Scientific (1 mentions) Orbitrap velos pro mass spectrometer, by Thermo Fisher Scientific (1 mentions) 2 cm guard column, by Thermo Fisher Scientific (1 mentions) Orbitrap fusion lumos, by Thermo Fisher Scientific (1 mentions) Ziptip, by Merck Group (1 mentions)

4 protocols using acclaim pepmap100 separating column

1

Intact Glycopeptides Analysis Protocol

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One microgram of glycopeptides was separated on an EASY-nLC™ 1200 instrument (Thermo Fisher Scientific, Germany) with the use of Acclaim PepMap100 precolumn (2 cm, 75 µm i.d., 3 µm) and Acclaim PepMap100 separating column (50 cm, 75 µm i.d., 3 µm) operating at 300 nL/min. The mobile phase A (0.1% FA) and mobile phase B (0.1% FA / 80% ACN) with a flow rate of 200 nL/min. The parameters used for intact glycopeptides analysis were the same as previously described [22 (link), 23 (link)].
Yu H., Li M., Shu J., Dang L., Wu X., Wang Y., Wang X., Chang X., Bao X., Zhu B., Ren X., Chen W, & Li Y. (2023). Characterization of aberrant glycosylation associated with osteoarthritis based on integrated glycomics methods. Arthritis Research & Therapy, 25, 102.
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2

Glycosite-Peptide Separation and Analysis

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The N-linked glycosite-containing peptides (~1 µg) were separated through a Dionex Ultimate 3000 RSLC nano system (Thermo Scientific) with a 75 µm × 15 cm Acclaim PepMap100 separating column (Thermo Scientific) protected by a 2 cm guarding column (Thermo Scientific). The mobile phase consisted of 0.1% formic acid in water (A) and 0.1% formic acid 95% acetonitrile (B). Flow rate was 300 nL/min. The gradient profile was set as following: 4–35% B for 70 min, 35–95% B for 5 min, 95% B for 10 min and equilibrated in 4% B for 15 min. MS analysis was performed using an Orbitrap Velos Pro mass spectrometer (Thermo Scientific). The spray voltage was set at 2.2 kV. Orbitrap spectra (AGC 1 × 106) were collected from 400–1800 m/z at a resolution of 60K followed by data-dependent HCD MS/MS (at a resolution of 7500, collision energy 35%, activation time 0.1 ms) of the ten most abundant ions using an isolation width of 2.0 Da. Charge state screening was enabled to reject unassigned and singly charged ions. A dynamic exclusion time of 35 sec was used to discriminate against previously selected ions.
Yang W., Jackson B, & Zhang H. (2016). Identification of glycoproteins associated with HIV latently infected cells using quantitative glycoproteomics. Proteomics, 16(13), 1872-1880.
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3

Peptide Separation and Mass Spectrometry

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Peptides were resuspended in 0.1% formic acid in water and subjected to LCMSMS analysis. Peptides from each fraction were separated on a Dionex Ultimate 3000 RSLCnano system (Thermo Scientific) with a 75 μm × 15 cm Acclaim PepMap100 separating column (Thermo Scientific) and with a 2 cm guarding column (Thermo Scientific). The flow rate was 300 nL/min with 0.1% formic acid in water (A) and 0.1% formic acid 95% acetonitrile (B). The gradient profile was: 5–40% B for 90 min. MS analysis was performed using an Orbitrap Velos Pro mass spectrometer (Thermo Scientific). The spray voltage was set at 2.2 kV. Orbitrap spectra (AGC 1×106) were collected with resolution of 30,000 followed by ten data-dependent HCD MS/MS (at a resolution of 7,500, collision energy 35%, activation time 0.1 ms). A dynamic exclusion time was set at 25 sec with a repeat count of 2.
Höti N., Yang S., Hu Y., Shah P., Haffner M.C, & Zhang H. (2018). Overexpression of α (1,6) fucosyltransferase in the development of castration-resistant prostate cancer cells. Prostate Cancer and Prostatic Diseases, 21(1), 137-146.
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4

SCX Fractionation and LC-MS Analysis

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Individual fractions from the strong cation exchange (SCX) chromatography were desalted using ZipTips (ZTC18S096, EMD Millipore), dried down and resuspended in 0.1% formic acid (Catalog no 94138, Honeywell). Fractions were analyzed by LC-MS on an Orbitrap Fusion Lumos (ThermoFisher) equipped with an Easy NanoLC1200 HPLC (ThermoFisher). Peptides were separated on a 75 μm × 15 cm Acclaim Pep-Map100 separating column (Thermo Scientific) downstream of a 2 cm guard column (Thermo Scientific). Buffer A was 0.1% formic acid in water. Buffer B was 0.1% formic acid in 80% acetonitrile. Peptides were separated on a two-hour gradient from 0% B to 35% B. Peptides were collisionally fragmented using HCD mode. Precursor ions were measured in the Orbitrap with a resolution of 120,000. Fragment ions were measured in the Orbitrap with a resolution of 50,000. The spray voltage was set at 2.2 kV. Orbitrap MS1 spectra (AGC 1×10 6 ) were acquired from 400-1800 m/z followed by data-dependent HCD MS/MS (collision energy 42%, isolation window of 0.7 Da) for a three second cycle time. Charge state screening was enabled to reject unassigned and singly charged ions. A dynamic exclusion time of 60 seconds was used to discriminate against previously selected ions.
Singh D., Fudickar A.M., Smiley T.M., & Ketterson E.D. (2020). Comparative proteomics reveals molecular correlates of population-level variation in reproductive timing in a North American songbird.
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