Peptide beh c18 column

Manufactured by Waters Corporation

Sourced in United States

The Peptide BEH C18 column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of peptides. It features a bonded stationary phase composed of hybrid silica particles with a C18 alkyl chain ligand. The column is intended for use in HPLC applications that require the separation and purification of peptides.

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Lab products found in correlation

Q exactive mass spectrometer, by Thermo Fisher Scientific (1 mentions) H class uplc, by Waters Corporation (1 mentions) Synapt g2 si hdms, by Waters Corporation (1 mentions) Vanquish uhplc, by Thermo Fisher Scientific (1 mentions) Sq detector 2 mass spectrometer, by Waters Corporation (1 mentions) Xevo g2 xs system, by Waters Corporation (1 mentions) Xevo tq s, by Waters Corporation (1 mentions) Acquity ultra performance liquid chromatography system, by Waters Corporation (1 mentions)

9 protocols using peptide beh c18 column

Peptide Analysis via Nano-LC-MS/MS

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Peptides were analyzed with a Waters
NanoAcquity liquid chromatograph (LC) paired with a Q-Exactive mass
spectrometer (Thermo Scientific). 200 ng of peptides was injected
into the LC system equipped with a peptide BEH C18 column (Waters,
100 μm × 100 mm, 1.7 μm particle size). Peptides
were separated over a 48 min gradient with a flow rate of 0.9 μL/min
with a two-solvent system, where solvent A was water containing 0.1%
FA and solvent B was ACN containing 0.1% FA. The following linear
gradient was used for all samples: 4% B from 0 to 8 min, 4–7%
B from 8 to 10 min, 7–33% B from 10 to 30 min, 33–90%
B from 30 to 33 min, 90% B until 36 min, 90–4% B for 1 min,
and reequilibration at 4% B from 37 to 48 min. The mass spectrometer
settings were identical to those described previously.^{40 (link)}

DeRosa C.M., Weaver S.D., Wang C.W., Schuster-Little N, & Whelan R.J. (2023). Simultaneous N-Deglycosylation and Digestion of Complex Samples on S-Traps Enables Efficient Glycosite Hypothesis Generation. ACS Omega, 8(4), 4410-4418.

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UPLC-MS Analysis of Microbial Metabolites

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One-fourth volume of butanol was used to extract 200 μl of culture supernatants, which was subsequently lyophilized to dryness. Samples were analyzed by UPLC-MS (Waters Acquity UPLC H-Class and Waters Synapt G2-Si HDMS, USA) at the positive detection mode after dissolving in 10 L of a solvent mixture (H2O: 5% CH3CN+ 1% HCOOH). Then, 7.5 μl of the sample was loaded onto a Waters Acquity Peptide BEH C18 column (2.1 mm × 100 mm) equilibrated in a solution mixture (1% CH3CN + 0.1% HCOOH + H2O) with a flow rate of 0.2 ml/ min, and a column temperature that was kept at 65°C. Bound compounds were eluted using the following gradient: Solution A (0.1% HCOOH:H2O) and Solution B (CH3CN): 1% Solution B for 1 min, 1–40% of Solution B over 10 min, 40–80% Solution B over 1 min and kept for 2 min, 80–1% of Solution B over 50 s, and re-equilibration with 1% Solution B for 10 min before loading the following sample.

Abdulmalek H.W, & Yazgan-Karataş A. (2022). Improvement of Bacilysin Production in Bacillus subtilis by CRISPR/Cas9-Mediated Editing of the 5’-Untranslated Region of the bac Operon. Journal of Microbiology and Biotechnology, 33(3), 410-418.

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Glass Composition Analysis by HPLC-MS

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We analyzed the composition changes before and after the glass formation using an Orbitrap mass spectrometry (Thermo Fisher Scientific, USA). The high-performance liquid chromatography–MS (HPLC-MS) conditions were listed as follows. For HPLC, the chromatographic separation was carried out in a Peptide BEH C18 column (2.1 × 150 mm, 1.7 μm) (Waters, USA). The used HPLC system was the Vanquish UHPLC (Thermo Fisher Scientific, USA). The mobile phase A and B were 0.1% formic acid–water and 0.1% formic acid–acetonitrile, respectively. The gradient elution procedure was performed as follows: 0 to 1 min, 5% B; 1 to 3 min, 5 to 40% B; 3 to 5 min, 40 to 100% B; 5 to 20 min, 100% B; 20 to 30 min, 5% B. The flow rate was 0.1 ml min⁻¹. The injection volume was 5 μl. The column temperature was kept at 30°C. For MS, electron spray ionization positive mode was used. The spray voltage was 4.5 kV. The capillary temperature and vaporizer temperature were 320° and 300°C, respectively. The sheath gas and aux gas were 19.8 ml min⁻¹ and 5 psi, respectively. The MS scan range was set from m/z 100 to 600. The samples including the powder and glass were dissolved in ethanol solution.

Xing R., Yuan C., Fan W., Ren X, & Yan X. (2023). Biomolecular glass with amino acid and peptide nanoarchitectonics. Science Advances, 9(11), eadd8105.

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High-pH Peptide Fractionation for Proteome Depth

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In order to decrease the complexity of labeled peptides mixtures and increase the identified depth of proteome, the labeled peptide mixtures were fractionated by a high-pH RPLC. Firstly, the labeled peptides mixtures (400μg) from frontal and temporal cortex were re-dissolved in 100μL 0.1% ammonium hydroxide solution (pH 10), then injected into an X-bridge Peptide BEH C18 column (4.6 mm×250 mm, C18, 3μm, 100 Å, Waters, MA, USA), fractionated with mobile phase A₁ (0.1% NH₃·H₂O, pH=10) and mobile phase B₁ (90%ACN/10%H₂O/0.1%NH₃·H₂O, pH=10) at a 60-min gradient at flow rate of 1 mL/min. The eluted gradient was 5–30% buffer B₁ for 60 min. The eluted peptides fractions were collected every minute and then concatenated into 20 fractions by combining fractions 1, 21, 41; 2, 22, 42, and so on. The 20 combined fractions were then dried by a refrigerated centrifugal vacuum concentrator and stored at −80 °C until analysis by LC-MS/MS.

Xu L., Sun H., Zhang Y., Guo Z., Xiao X., Zhou X., Hu K., Sun W., Wang B, & Liu W. (2021). Proteomic analysis of human frontal and temporal cortex using iTRAQ-based 2D LC-MS/MS. Chinese Neurosurgical Journal, 7, 27.

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Glutathione Adducts Characterization

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1 mM Glutathione(GSH) is reacted with 1 mM HNE in Tris-HCl buffer (pH=7.4) for 1 h at room temperature. The reaction is then adjusted to pH 5.0 and added with 5 mM AOyne for another 30 min. The reaction solutions are filtered through a 0.22 µm membrane. The samples are analyzed on an ACQUITY H-Class ultra performance liquid chromatography-electrospray ionization-mass spectrometry (UPLC-ESI-MS) system (Waters Corp.) with a peptide BEH C18 column (Waters 300, 1.7 2.1 100 mm) and a quadrupole rods SQ Detector 2 mass spectrometer (Waters Corp.) The ultra-pure water and acetonitrile are used as the mobile phase in a 7 min gradient and the ion chromatographic traces are extracted at m/z 306 for GSH, 462 for GSH-HNE, 557 for GSH-HNE-OAyne, and 572 for GSH-HNE-HZyne.

Chen Y., Cong Y., Quan B., Lan T., Chu X., Ye Z., Hou X, & Wang C. (2017). Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe. Redox Biology, 12, 712-718.

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Separation and Analysis of Posttranslational Modifications

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The pellet of the product of chemical posttranslational modification was resuspended in 30 µL of 5% TFA aq. An aliquot (10 µL) of the resulting solution was separated on an Acquity UPLC (Waters) equipped with a C18 column (Peptide BEH C18 Column, 300 Å, 1.7 µm, 2.1 mm × 150 mm, Waters) using a gradient of 5–40% B over 10 min (A = water containing 0.1% formic acid, B = acetonitrile containing 0.1% formic acid), and directly subjected to an ESI-qTOF mass spectrometer (Waters Xevo G2-XS system, under control of MassLynx v.4.1). Nitrogen was used as cone gas (50 L/min) and desolvation gas (1000 L/min). The capillary voltage was set to 0.7 kV. The ionization source and desolvation gas were heated to 120 and 400 °C, respectively. The eluent from the UPLC system on Rt = 0–2 min was diverted from the mass spectrometer. For the analysis of Pep6, the HPLC gradient conditions were modified to 1–80% B over 10 min. For the analyses of Pep7, the injection volume was modified to 5 µL. For tandem mass spectrometry, MS/MS spectra were acquired with a 0.3 s scan time, with 25 eV collision energy. The obtained LC–MS data were analyzed with MassLynx v.4.1.

Tsutsumi H., Kuroda T., Kimura H., Goto Y, & Suga H. (2021). Posttranslational chemical installation of azoles into translated peptides. Nature Communications, 12, 696.

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Glycopeptide Characterization by LC-MS/MS

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An aliquot of 7.5 μg of the digest was injected onto a Waters Peptide BEH C18 column (300A, 1.7 μm, 2.1 mm x 150 mm) at 55oC. Mobile phase A was 0.1 % formic acid in water, and mobile phase B was 0.1 % formic acid in acetonitrile. The gradient started at 0 % B for 2 min and was stepped to 7 % where it was then increased gradually to 32 % in 6 min. The column was then washed with 90 % B for 1.6 min followed by equilibration at 0 % B for 0.2 min.
Mass spectrometer data was acquired on a Waters Xevo TQ-S instrument on positive ion unit mass resolution mode with the following settings: electrospray capillary voltage 3 kV, cone voltage 20 V, source temperature 70oC, desolvation temperature 400oC and desolvation gas flow 800 L/h. MS1 was set at monoisotopic masses of the tryptic glycopeptides and MS2 was set at 138 m/z (GlcNAc oxonium ion) with collision energy at 60 V and dwell time of 27 ms. Automatic peak integration was performed in TargetLynx and percentage glycan species calculated in Microsoft Excel.

Chi B., Veyssier C., Kasali T., Uddin F, & Sellick C.A. (2020). At-line high throughput site-specific glycan profiling using targeted mass spectrometry. Biotechnology Reports, 25, e00424.

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UPLC-MS Analysis of Microbial Metabolites

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Two hundred microliter of culture supernatants were extracted with one-fourth volume of butanol and lyophilized to dryness. After dissolved in 10 μl of a solvent mixture (H 2 O: 5% CH 3 CN + 1% HCOOH), samples were analyzed by UPLC-MS (Waters Acquity UPLC H-Class and Water Synapt G2-Si HDMS) at the positive detection mode. 7.5 μl of sample was injected onto a Waters Acquity Peptide BEH C18 column (2.1 mm × 100 mm) equilibrated in solution mixture (1% CH 3 CN + 0.1% HCOOH + H 2 O) with a flow rate 0.2 ml/ min, and column temperature was kept at 65°C. Bound compounds were eluted with a gradient prepared with Solution A (0.1% HCOOH:H 2 O) and Solution B (CH 3 CN) as follows: 1% Solution B for 1 min, 1-40% of Solution B over 10 min, 40-80% Solution B over 1 min and kept for 2 min, 80-1% of Solution B over 50 sec, and 1% Solution B reequilibration for 10 min before loading the next sample.

Ertekin O., Kutnu M., Taşkin A.A., Demir M., Karataş A.Y, & Özcengiz G. (2020). Analysis of a bac operon-silenced strain suggests pleiotropic effects of bacilysin in Bacillus subtilis. Journal of microbiology (Seoul, Korea), 58(4).

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Peptide Analysis by UPLC-PDA-FLD-MS

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Tryptic peptides were analyzed using a Waters (Waltham, MA) Acquity ultra-performance liquid chromatography system coupled with a photodiode array detector, a fluorescence detector, and a QDa mass detector. The LC column used for peptide separation is an Acquity ultra-performance liquid chromatography Peptide BEH C18 column (2.1 mm Â 150 mm) from Waters. The mobile phases consisted of 0.1% formic acid in water (solvent A) and 0.1% TFA in acetonitrile (solvent B). The separation was performed using a gradient from 17% to 18.5% solvent B in 5 min at a flow rate of 300 mL/min. Column temperature was set at 50 C, and UV detection was performed at the wavelength of 280 nm. For fluorescence detection, peptides were monitored using an excitation wavelength of 290 nm and an emission wavelength of 372 nm. The QDa mass range was set from m/z 100 to 1250.

Zhou K., Cao X., Bautista J., Chen Z., Hershey N., Ludwig R., Tao L., Zeng M, & Das T.K. (2020). Structure-Function Assessment and High-Throughput Quantification of Site-Specific Aspartate Isomerization in Monoclonal Antibody Using a Novel Analytical Tool Kit. Journal of pharmaceutical sciences, 109(1).

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