Reprosil pur 120 c18 aq 1.9 μm beads

Manufactured by Dr. Maisch

ReproSil-Pur 120 C18-AQ 1.9 μm beads are a type of chromatographic material used in liquid chromatography. They are composed of silica-based particles with a C18 alkyl stationary phase and a pore size of 120 Angstroms. The beads have a particle size of 1.9 micrometers, which provides high separation efficiency. This product is commonly used in analytical and preparative chromatographic applications.

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Lab products found in correlation

Easy nlc 1000 system, by Thermo Fisher Scientific (1 mentions) Q exactive plus orbitrap mass spectrometer, by Thermo Fisher Scientific (1 mentions)

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ReproSil-Pur C18-AQ (72 citations) ReproSil-Pur 120 C18-AQ (58 citations) ReproSil-Pur C18 beads (32 citations) C18 beads (23 citations) Reprosil-Pur C18-AQ beads (21 citations) Reprosil-Pur C18 (21 citations) ReproSil-Pur C18-AQ 1.9 μm beads (7 citations) Reprosil-AQ Pur (3 citations) C18 ReproSil-Pur 1.9 μm (2 citations)

4 protocols using reprosil pur 120 c18 aq 1.9 μm beads

Quantitative L-Asp and D-isoAsp Peptide Analysis

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LC-MS data was acquired using a Thermo Fisher Ultimate 3000 RSLCnano
system coupled to an Orbitrap Fusion Lumos. Approximately 1 ng of
a 2:1 mixture of synthetic l-Asp and d-isoAsp standards
of the FAEDVGSNK peptide were injected and
separated on a column packed with ReproSil-Pur 120 C18-AQ 1.9 μm
beads (Dr. Maisch). The gradient was 0.875% B per minute where buffer
A was Optima water with 0.1% formic acid and buffer B was 80/20 acetonitrile/Optima
water with 0.1% formic acid. Flow rate was 0.3 μL/min. The MS
method used a tSIM scan of the doubly charged precursor followed by
data dependent CID MS² on the [M + 2H]²⁺ peak
in the ion trap, with one scan acquired per cycle. A targeted mass
filter was used to select the b5⁺ and y6⁺ fragment
ions for CID MS³ scans in the ion trap. Ten MS³ scans of each fragment ion were acquired per cycle by using rapid
scan speed.

Wu H.T., Van Orman B.L, & Julian R.R. (2024). Localizing Isomerized Residue Sites in Peptides with Tandem Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 35(4), 705-713.

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Chymotrypsin-Based Proteomic Analysis of CAT Variants

Cited 1 time

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In-gel digestion,
nano-LC–MS/MS, and peptide identification was performed as
previously described with the following modifications.^{45 (link)} Protein digestion was performed using chymotrypsin.
Reverse phase chromatography was performed using an in-house packed
column (40 cm long × 75 μm ID × 360 OD, Dr. Maisch
GmbH ReproSil-Pur 120 C18-AQ 1.9 μm beads) and a 120 min gradient.
Raw files were searched using the Mascot algorithm (version 2.5.1)
against a protein database constructed of combining the FASTA file
for CAT protein (modified to generate 20 versions each with a different
natural or modified amino acid at position 112) with a contaminant
database (cRAP, downloaded 11–21–16 from http://www.thegpm.org) via Proteome Discoverer 2.1. Variable modifications include
oxidation of Met, carboxyamidomethylation of Cys, and phosphorylation
of Ser, Thr, or Tyr. Only peptide spectral matches with an expectation
value of less than 0.01 (“High Confidence”) were used
(Table S6). As a control, wild-type CAT
protein was translated via wild-type EF-Tu and as
expected, only the wild-type amino acid, aspartic acid, was translated
at position 112 (Table S7). CAT protein
translation mediated by variants EF-coli, EF-N63A, EF-K263A, and EF-N273A
were not analyzed using mass spectrometry because protein expression
levels were too low to isolate purified CAT protein.

DeLey Cox V.E., Cole M.F, & Gaucher E.A. (2019). Incorporation of Modified Amino Acids by Engineered Elongation Factors with Expanded Substrate Capabilities. ACS Synthetic Biology, 8(2), 287-296.

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Reverse Phase Liquid Chromatography and Mass Spectrometry

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Peptides were separated by online reverse phase liquid chromatography using the EASY-nLC 1000 system (Thermo Scientific) in a 30-cm analytical column (inner diameter: 75 μm; heated at 50 °C) packed in-house with ReproSil-Pur 120 C18-AQ 1.9-μm beads (Dr. Maisch GmbH). The gradient separation was performed through a 105-min non-linear gradient of 1.6–32% acetonitrile with 0.1% formic acid at a nanoflow rate of 225 nl/min. The eluted peptides were sprayed directly by electrospray ionization into a Q Exactive Plus Orbitrap mass spectrometer (Thermo Scientific). Mass spectrometry measurement was conducted in data-dependent acquisition mode using a top 10 method with one full scan (mass range: 300–1650 m/z; resolution: 70,000, target value: 3 × 10⁶, maximum injection time: 20 ms) followed by 10 fragmentation scans via higher energy collision dissociation (HCD; normalized collision energy: 25%, resolution: 17,500 in profile mode, target value: 1 × 10⁵, maximum injection time: 120 ms, isolation window: 1.8 m/z). Precursor ions of unassigned or +1 charge state were rejected. Additionally, precursor ions already isolated for fragmentation were excluded dynamically for 20 s.

Martínez-Lumbreras S., Träger L.K., Mulorz M.M., Payr M., Dikaya V., Hipp C., König J, & Sattler M. (2024). Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs. Nature Communications, 15, 3888.

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Proteomic Profiling of Human Samples

Cited 1 time

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The proteins in each sample were reduced, alkylated and digested with trypsin according to the FASP protocol.^{[63 (link)]} The peptides were analyzed by nano-LC-MS/MS, and peptide identification as previously described with the following modifications.^{[64 (link)]} Reverse phase chromatography was performed using an in-house packed column (40 cm long X 75 μm ID X 360 OD, Dr. Maisch GmbH ReproSil-Pur 120 C18-AQ 1.9 μm beads) and a 120 min gradient. The Raw files were searched using the Mascot algorithm (ver. 2.5.1) against a protein database constructed by combining the human UniProt protein database (downloaded April 24, 2018, 20,303 entries), and a contaminant database (cRAP, downloaded 11–21-16 from http://www.thegpm.org) via Proteome Discoverer 2.1. Only peptide-spectrum matches with expectation value of less than 0.01 (“High Confidence”) were used. ^{[64 (link)]}

Liu A., Yu T., Young K., Stone N., Hanasoge S., Kirby T.J., Varadarajan V., Colonna N., Liu J., Raj A., Lammerding J., Alexeev A, & Sulchek T. (2019). Cell Mechanical and Physiological Behavior in the Regime of Rapid Mechanical Compressions that Lead to Cell Volume Change. Small (Weinheim an der Bergstrasse, Germany), 16(2), e1903857.

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