Plrp s reversed phase column

Manufactured by Agilent Technologies

The PLRP-S reversed phase column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of a wide range of analytes. The column features a polystyrene-divinylbenzene (PS-DVB) stationary phase, which provides excellent chemical and thermal stability, as well as a wide range of pH tolerance. The PLRP-S column is suitable for the separation of various organic compounds, including small molecules, peptides, and proteins.

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Lab products found in correlation

Q exactive plus orbitrap ms, by Thermo Fisher Scientific (1 mentions) Advancebio peptide mapping column, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

PLRP-S column (39 citations) PLRP-S (18 citations) PLRP-S polymeric reversed-phase column (3 citations) PLRP-S polymeric reversed phase preparatory column (2 citations)

3 protocols using plrp s reversed phase column

Glycosylation Profiling of BN.1 RBD

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Four micrograms of PNGase F-treated BN.1 RBD was used for each injection on the liquid chromatography–mass spectrometry (LC–MS) system to acquire intact mass spectrometry signal after separation of protease and protein by liquid chromatography (Agilent PLRP-S reversed phase column). Thermo MS (Q Exactive Plus Orbitrap) was used to acquire intact protein mass under denaturing conditions. BioPharma Finder 3.2 software was used to deconvolute the raw m/z data to protein average mass.
Peptide mapping with LC–MS was used to profile the site-specific glycosylation sites on BN.1 RBD. Glycopeptides containing only one specific glycan were achieved by selectively digesting with chymotrypsin protease. Twenty micrograms of each digest product (peptide with a single glycan) was analysed by LC–MS (Agilent AdvanceBio peptide mapping column and Thermo Q Exactive Plus Orbitrap MS). Peptide mapping data were analysed on Biopharma Finder 3.2 data analysis software.

Addetia A., Piccoli L., Case J.B., Park Y.J., Beltramello M., Guarino B., Dang H., de Melo G.D., Pinto D., Sprouse K., Scheaffer S.M., Bassi J., Silacci-Fregni C., Muoio F., Dini M., Vincenzetti L., Acosta R., Johnson D., Subramanian S., Saliba C., Giurdanella M., Lombardo G., Leoni G., Culap K., McAlister C., Rajesh A., Dellota E J.r., Zhou J., Farhat N., Bohan D., Noack J., Chen A., Lempp F.A., Quispe J., Kergoat L., Larrous F., Cameroni E., Whitener B., Giannini O., Cippà P., Ceschi A., Ferrari P., Franzetti-Pellanda A., Biggiogero M., Garzoni C., Zappi S., Bernasconi L., Kim M.J., Rosen L.E., Schnell G., Czudnochowski N., Benigni F., Franko N., Logue J.K., Yoshiyama C., Stewart C., Chu H., Bourhy H., Schmid M.A., Purcell L.A., Snell G., Lanzavecchia A., Diamond M.S., Corti D, & Veesler D. (2023). Neutralization, effector function and immune imprinting of Omicron variants. Nature, 621(7979), 592-601.

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Intact Mass Spectrometry for N-Glycan Analysis

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The purpose of intact MS was to verify the n-terminal sequence on four constructs. N-linked glycans were removed by PNGase F after overnight non-denaturing reaction at room temperature. 4 μg of deglycosylated protein was used for each injection on the LC-MS system to acquire intact MS signal after separation of protease and protein by LC (Agilent PLRP-S reversed phase column). Thermo MS (Q Exactive Plus Orbitrap) was used to acquire intact protein mass under denaturing condition. BioPharma Finder 3.2 software was used to deconvolute the raw m/z data to protein average mass.

McCallum M., De Marco A., Lempp F.A., Tortorici M.A., Pinto D., Walls A.C., Beltramello M., Chen A., Liu Z., Zatta F., Zepeda S., di Iulio J., Bowen J.E., Montiel-Ruiz M., Zhou J., Rosen L.E., Bianchi S., Guarino B., Fregni C.S., Abdelnabi R., Foo S.Y., Rothlauf P.W., Bloyet L.M., Benigni F., Cameroni E., Neyts J., Riva A., Snell G., Telenti A., Whelan S.P., Virgin H.W., Corti D., Pizzuto M.S, & Veesler D. (2021). N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2. Cell, 184(9), 2332-2347.e16.

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Rapid Protein Mass Spectrometry

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Protein mass spectra for WT and D146N RIP2 proteins were obtained using 6224 TOF MS/LC (Agilent Technologies) instrument. Samples (10-20 mg) were analyzed on a PLRP-S reversed phase column (Agilent, PL1912-1802) with a flow rate of 0.05 mL/min and a linear gradient of 5%-60% acetonitrile with 0.05% trifluoroacetic acid over 6 min.

Goncharov T., Hedayati S., Mulvihill M.M., Izrael-Tomasevic A., Zobel K., Jeet S., Fedorova A.V., Eidenschenk C., deVoss J., Yu K., Shaw A.S., Kirkpatrick D.S., Fairbrother W.J., Deshayes K, & Vucic D. (2018). Disruption of XIAP-RIP2 Association Blocks NOD2-Mediated Inflammatory Signaling. Molecular cell, 69(4).

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