Reverse phase column

Manufactured by Waters Corporation

Sourced in United States

A reverse phase column is a type of chromatography column used for the separation and purification of compounds. It consists of a stationary phase that has a non-polar functional group, typically a hydrocarbon chain, which interacts with the non-polar components of the sample. This allows for the separation of molecules based on their hydrophobicity.

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Lab products found in correlation

Uv 975, by Jasco (1 mentions) 1200 infinity, by Agilent Technologies (1 mentions) Oasis mcx, by Waters Corporation (1 mentions) Ultimate 3000 system, by Thermo Fisher Scientific (1 mentions) Sequence grade modified trypsin, by Promega (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions)

4 protocols using reverse phase column

Quantitative HPLC Analysis of DOX and FA Loading

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The CAD loading degree
(LC) and FA loading efficiency (LE) were calculated
according to the following formulas (1) and (2): The DOX
loading contents were quantified by
gradient analytical HPLC assay. An HPLC assay was performed on an
Agilent 1100 instrument, and 20 μL of solution was loaded onto
a Waters reverse phase column (250 × 4.6 mm). Acetonitrile (TFA
0.1%):water (TFA 0.1%) (Acetonitrile increase from 5 to 95% with 20
min) was eluted at a flow rate of 1 mL/min at 490 nm by a UV detector
(UV-975, Jasco). FA was detected by UV–vis absorption at 282
nm.

Yan J., Liu C., Wu Q., Zhou J., Xu X., Zhang L., Wang D., Yang F, & Zhang H. (2020). Mineralization of pH-Sensitive Doxorubicin Prodrug in ZIF-8 to Enable Targeted Delivery to Solid Tumors. Analytical Chemistry, 92(16), 11453-11461.

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Heme b Quantification in BS Cells

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A total of 5 × 10⁸ BS cells was harvested by centrifugation at 1000 × g at 4 °C for 10 min and washed 3 times with PBS on ice. Cells were resuspended in 60 μl H₂O, extracted with 400 μl acetone/0.2% HCl, and the supernatant was collected after centrifugation at 1000 × g at 4 °C for 5 min. The pellet was resuspended in 200 μl acetone/0.2% HCl and centrifuged as described above. Both supernatants were combined, and 150 μl of each sample was immediately injected into a high-performance liquid chromatography system (Infinity 1200, Agilent Technologies) and separated using a reverse-phase column (4 μm particle size, 3.9 × 75 mm) (Waters) with 0.1% trifluoroacetic acid and acetonitrile/0.1% trifluoroacetic acid as solvents A and B, respectively. Heme b was eluted with a linear gradient of solvent B (30–100% in 12 min) followed by 100% of B at a flow rate of 0.8 ml/min at 40 °C. Heme was detected by diode array detector (Infinity 1200, Agilent Technologies) and identified by retention time and absorbance spectra according to commercially available standard (Sigma-Aldrich).

Horáková E., Lecordier L., Cunha P., Sobotka R., Changmai P., Langedijk C.J., Abbeele J.V., Vanhollebeke B, & Lukeš J. (2022). Heme-deficient metabolism and impaired cellular differentiation as an evolutionary trade-off for human infectivity in Trypanosoma brucei gambiense. Nature Communications, 13, 7075.

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Plasma Lyso-Gb3 Quantification

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Plasma Lyso‐Gb3 was measured in EDTA plasma samples. Briefly, Lyso‐Gb3 was extracted from plasma by solid phase (Waters Oasis McX). The separation and detection were done by ultra‐performance liquid chromatography system coupled with a tandem mass spectrometer (UPLC‐MS/MS) operated in MRM mode with a reverse phase column (Waters Corp. Milford, MA). Reference value for men was established as <1.0 nmol/L.

Frabasil J., Durand C., Sokn S., Gaggioli D., Carozza P., Carabajal R., Politei J, & Schenone A.B. (2019). Prevalence of Fabry disease in male dialysis patients: Argentinean screening study. JIMD Reports, 48(1), 45-52.

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Protein extraction and fractionation

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Samples were thawed and transferred into lysis buffer (2% SDS, 7 M urea, 1 mg/ml protease inhibitor cocktail (Roche Ltd. Basel, Switzerland)). The homogenated samples were then centrifuged at 3000g for 15 min at 4 °C to collect the supernatant. BCA Protein Assay Kit was applied to determine the proteins concentrations. The extracted proteins were finally digested with sequence-grade modified trypsin (Promega, Madison, WI) at 37 °C for 16 h and the peptide mixture was collected.
3 μg peptides dissolved with buffer A (0.1% formic acid in water) was fractionated by high pH separation with Ultimate 3000 system (Thermo Fisher scientific, MA, USA), which was connected to a reverse phase column (4.6 mm × 250 mm, 5 μm, (Waters Corporation, MA, USA)). The column was maintained at 1 ml/min flow rate at 30 °C. Six fractions were collected, and each fraction was dried in a vacuum concentrator for further analysis.

Yu F., Chen Y., Liu B., Wang T., Ding Z., Yi Z., Zhu Y, & Li J. (2022). DIA mass spectrometry characterizes urinary proteomics in neonatal and adult donkeys. Scientific Reports, 12, 22590.

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