Advancebio peptide mapping column

Manufactured by Thermo Fisher Scientific

The AdvanceBio peptide mapping column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of peptides. It features a specialized stationary phase optimized for the efficient separation of complex peptide mixtures. The column's core function is to provide efficient and reproducible peptide separation, which is essential for applications such as peptide mapping, protein characterization, and bioanalytical studies.

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Lab products found in correlation

Q exactive plus orbitrap ms, by Thermo Fisher Scientific (2 mentions) Plrp s reversed phase column, by Agilent Technologies (1 mentions) Exactive plus orbitrap ms, by Thermo Fisher Scientific (1 mentions)

3 protocols using advancebio peptide mapping column

Peptide Mapping of Cysteine Modifications

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The purpose of peptide mapping was to identify the post modification on unpaired cysteines. Tryptic digestion was used without adding reducing reagent. 50 μg of deglycosyated protein was denatured (6 M guanidine hydrochloride), alkylated (Iodoacetamide), and buffer exchanged (Zeba spin desalting column) before trypsin digestion. 10 μg of digested peptide was analyzed on the LC-MS system (Agilent AdvanceBio peptide mapping column and Thermo Q Exactive Plus Orbitrap MS) to acquire both MS1 and MS2 data under HCD fragmentation. Peptide mapping data was analyzed on Biopharma Finder 3.2 by searching the possible modifications such as cysteinylation and carbamidomethylation on the cysteines.

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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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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Site-Specific Glycosylation Mapping of NAs

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Peptide mapping with liquid chromatography–mass spectrometry (LC–MS) was used to profile the site-specific glycosylation sites on two NAs (A/Tanzania/205/2010 and A/Hong Kong/2671/2019). Glycopeptides containing only one specific glycan were achieved by selectively digesting with trypsin, Glu-C, Lys-C or Asp-N protease, depending on the sequence context. Of each digest product (peptide with a single glycan), 25 µg 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. Technical replicates were performed by injecting 25 µg of digested product three times from the same sample vial into the LC–MS.

Momont C., Dang H.V., Zatta F., Hauser K., Wang C., di Iulio J., Minola A., Czudnochowski N., De Marco A., Branch K., Donermeyer D., Vyas S., Chen A., Ferri E., Guarino B., Powell A.E., Spreafico R., Yim S.S., Balce D.R., Bartha I., Meury M., Croll T.I., Belnap D.M., Schmid M.A., Schaiff W.T., Miller J.L., Cameroni E., Telenti A., Virgin H.W., Rosen L.E., Purcell L.A., Lanzavecchia A., Snell G., Corti D, & Pizzuto M.S. (2023). A pan-influenza antibody inhibiting neuraminidase via receptor mimicry. Nature, 618(7965), 590-597.

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