C18 aq resin

Manufactured by Dr. Maisch

Sourced in Germany

C18-AQ resin is a type of reversed-phase chromatography media. It is designed for the separation and purification of a variety of organic compounds. The resin features a silica-based backbone with covalently bonded C18 alkyl chains, which provide a hydrophobic environment for analyte retention.

Automatically generated - may contain errors

Lab products found in correlation

Picofrit column, by New Objective (2 mentions) Xcalibur qual browser, by Thermo Fisher Scientific (1 mentions) Orbitrap fusion lumos, by Thermo Fisher Scientific (1 mentions) Ltq orbitrap velos, by Thermo Fisher Scientific (1 mentions) 6600 tripletof hybrid quadrupole time of flight mass spectrometer, by AB Sciex (1 mentions) 415 autosampler, by AB Sciex (1 mentions) Nanolc 415 system, by AB Sciex (1 mentions)

3 protocols using c18 aq resin

Validating AML1/ETO Splice Junction Peptide

Check if the same lab product or an alternative is used in the 5 most similar protocols

Tryptic peptide of the splice junction in AML1/ETO splice product was initially validated by manual inspection of chromatograms and MS1 spectra with theoretical m/z values of peptide candidates; m/z = 519.517 (z = 4) and m/z = 692.353 (z = 3)
Validated MS1 ions were further analyzed by “MS2 run only” mode to identify the splice junction peptide with the desired b- and y- ions. The LC-MS/MS experiment was performed with an Easy-nLC 1200 UPLC system employing a 45 cm × 75 μm (inner diameter) nano-capillary column packed with 1.9 μm C18-AQ resin (Dr. Maisch, Germany) mated to a metal emitter in-line with an Orbitrap Fusion Lumos (Thermo Scientific, USA). The column temperature was 45 °C, and a one-hour gradient method was run at a flow rate of 300 nL/min. The mass spectrometer was operated to scan MS2 from MS1 of the inclusion list with a 60,000 resolution (positive mode, profile mode, AGC target of 4 × 10⁵, maximum IT of 118 ms) in the Orbitrap, followed by HCD fragmentation in the ion trap with 30% collision energy. The isolation window for precursor ions was set to 0.4 m/z in the quadrupole.
Raw files were processed with Thermo XCalibur Qual Browser, and MS2 peaks were manually annotated.

Lee G, & Muir T.W. (2023). Distinct phases of cellular signaling revealed by time-resolved protein synthesis. bioRxiv.

+ Open protocol

+ Expand

HPLC-MS/MS Phosphopeptide Enrichment

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples were separated using a NanoAquity (waters) HPLC with a vented split on a 30mm 150 μM ID trap column with a Kasil frit packed with Magic C18AQ 3 mM 200Å resin (Bruker) and a 20cm 75 μM ID self-packed Pico-frit column (New Objective) packed with 1.9 μM 120Å reprosil-Pur C18-AQ resin (Dr. Maisch) on a non-linear 120min gradient from 5% ACN 0.1% formic acid to 95% ACN 0.1% formic acid and analyzed with a LTQ Orbitrap Velos (Thermo) using a Top 10 method. ERLIC samples were run in duplicate, with the first ERLIC fraction of each set of 3 run separately, while the 2^nd and 3^rd fraction of each set were pooled for a single run. In addition, for each sample 2 μg of the pre-enriched peptides and 2 μg of the total (unfractionated) enriched phosphopeptides were run using a non-linear 200min gradient from 5% ACN 0.1% formic acid to 95% ACN 0.1% formic acid.

Gassaway B.M., Cardone R.L., Padyana A.K., Petersen M.C., Judd E.T., Hayes S., Tong S., Barber K.W., Apostolidi M., Abulizi A., Sheetz J.B., K.s.h.i.t.i.z., Aerni H.R., Gross S., Kung C., Samuel V.T., Shulman G.I., Kibbey R.G, & Rinehart J. (2019). Distinct Hepatic PKA and CDK Signaling Pathways Control Activity-Independent Pyruvate Kinase Phosphorylation and Hepatic Glucose Production. Cell reports, 29(11), 3394-3404.e9.

+ Open protocol

+ Expand

Peptide Separation and Identification

Check if the same lab product or an alternative is used in the 5 most similar protocols

Using an Eksigent 415 autosampler connected to a 415 nanoLC system (Eksigent, USA), 5 µL of the sample was loaded at 300 nl/min with MS buffer A (2% Acetonitrile, 0.2% Formic Acid) by direct injection onto a PicoFrit column (75 µmID × 150 mm; New Objective, Woburn, MA) packed with C18AQ resin (1.9 µm, 200 Å; Dr Maisch, Germany). Peptides were eluted from the column and into the source of a 6600 TripleTOF hybrid quadrupole-time-of-flight mass spectrometer (Sciex, CA) using the following program: 2–35% MS buffer B (80% Acetonitrile, 0.2% Formic Acid) over 90 minutes, 35–95% MS buffer B over 9 minutes, 95% MS buffer B for 9 minutes, 80–2% for 2 min. The eluting peptides were ionised at 2300 V. An Intelligent Data Acquisition (IDA) experiment was performed, with a mass range of 350–1500 Da continuously scanned for peptides of charge state 2 + −5 + with an intensity of more than 400 counts/s. Up to 50 candidate peptide ions per cycle were selected and fragmented and the product ion fragment masses measured over a mass range of 100–2000 Da. The mass of the precursor peptide was then excluded for 15 seconds.

Berry I.J., Jarocki V.M., Tacchi J.L., Raymond B.B., Widjaja M., Padula M.P, & Djordjevic S.P. (2017). N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen. Scientific Reports, 7, 11063.

+ 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?

Revolutionizing how scientists
search and build protocols!