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Nano acquity capillary uplc

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The Nano-Acquity capillary UPLC is a high-performance liquid chromatography (HPLC) system designed for the separation and analysis of small-volume samples. It utilizes ultra-high pressure liquid chromatography (UPLC) technology to provide efficient and high-resolution separations. The core function of the Nano-Acquity capillary UPLC is to enable the separation and detection of analytes from micro- and nano-scale samples.

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Lab products found in correlation

Beh c18 column, by Waters Corporation (3 mentions) Orbitrap xl, by Thermo Fisher Scientific (2 mentions) Orbitrap xl instrument, by Thermo Fisher Scientific (1 mentions) Winnonlin version 5, by Pharsight (1 mentions)

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Acquity UPLC (716 citations) Acquity nano-UPLC (3 citations)

4 protocols using nano acquity capillary uplc

1

Proteomics Analysis of Protein Samples

Cited 1 time
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Elution of proteins from acrylamide gels, trypsin digestion and separation of peptides were performed as previously described [17 (link)]. The resulting peptides were analysed by LC-MS/MS using an Orbitrap XL instrument (Thermo Fisher Scientific) equipped with a nano-ESI source coupled with a nano-Acquity capillary UPLC (Waters). Briefly, peptides were separated with a capillary BEH C18 column (0.075×100 mm, 1.7 μM, Waters) using aqueous 0.1% formic acid (A) and CH3CN containing 0.1% formic acid (B) as mobile phases. Peptides were eluted by means of a linear gradient from 5 to 50% of B in 90 min, at a 300 nl/min flow rate. Mass spectra were acquired over an m/z range from 400 to 1800. To achieve protein identification, MS and MS/MS data underwent Mascot Search Engine software analysis to interrogate the National Center for Biotechnology Information nonredundant (NCBInr) protein database. Parameters sets were: trypsin cleavage; carbamidomethylation of cysteines as a fixed modification and methionine oxidation as a variable modification; a maximum of two missed cleavages; false discovery rate, calculated by searching the decoy database, 0.05.
Randi L., Perrone A., Maturi M., Dal Piaz F., Camerani M, & Hochkoeppler A. (2016). The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity. Bioscience Reports, 36(6), e00419.
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2

Mass Spectrometry Analysis of Amyloid-β

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Mass spectra of reacted and unreacted Aβ42 were acquired using a MALDI-TOF Micro (Waters) instrument operating in reflectron mode. Mass calibration was achieved using a peptide mixture derived from trypsin digestion of BSA. The peptide was digested overnight by trypsin under stirring at 37 °C, and the resulting fragments were analyzed by nano-LC-MS using a Orbitrap XL instrument (Thermo Fisher Scientific) equipped by a nano-ESI source coupled with a nano-ACQUITY capillary UPLC (Waters). Peptide separation was performed on a capillary BEH C18 column (0.075 × 100 mm, 1.7 μm; Waters) using aqueous 0.1% formic acid (A) and acetonitrile containing 0.1% formic acid (B) as mobile phases. Peptides were eluted by means of a linear gradient from 5 to 50% B in 45 min and a 300 nl/min flow rate. Mass spectra were acquired over an m/z range from 400 to 1800.
Emendato A., Milordini G., Zacco E., Sicorello A., Dal Piaz F., Guerrini R., Thorogate R., Picone D, & Pastore A. (2018). Glycation affects fibril formation of Aβ peptides. The Journal of Biological Chemistry, 293(34), 13100-13111.
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3

Mass Spectrometry-based Proteomic Analysis

Cited 1 time
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Elution of proteins from acrylamide gels, trypsin digestion, and separation of peptides were performed as previously described [21] (link). The resulting peptides were analyzed by LC-MS/MS using an Orbitrap XL instrument (Thermo Fisher, Waltham, MA, USA) equipped with a nano-ESI source coupled with a nano-Acquity capillary UPLC (Waters, Milford, MA, USA). Briefly, peptides were separated with a capillary BEH C18 column (0.075×100 mm, 1.7 μM, Waters) using aqueous 0.1% formic acid (A) and CH3CN containing 0.1% formic acid (B) as mobile phases. Peptides were eluted by means of a linear gradient from 5% to 50% of B in 90 min, at a 300 nL/min flow rate. Mass spectra were acquired over an m/z range from 400 to 1800. To achieve protein identification, MS and MS/MS data underwent Mascot Search Engine software analysis to interrogate the National Center for Biotechnology Information nonredundant (NCBInr) protein database. Parameters sets were: trypsin cleavage; carbamidomethylation of cysteines as a fixed modification and methionine oxidation as a variable modification; a maximum of two missed cleavages; false discovery rate, calculated by searching the decoy database, 0.05.
Caramia S., Gatius A.G., dal Piaz F., Gaja D, & Hochkoeppler A. (2017). Dual role of imidazole as activator/inhibitor of sweet almond (Prunus dulcis) β-glucosidase. Biochemistry and Biophysics Reports, 10, 137-144.
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4

Pharmacokinetics of Lupeol in Mice

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Female C57BL/6 mice (8-weeks old) were used for pharmacokinetics studies. Blood samples from the mandibular vein were collected in lithium-heparin coated tubes (at 0, 0.25, 0.5, 1, 2, 4, 6, 12, and 24 h) after a single-dose administration of Lupeol (200 mg/kg) by oral or intraperitoneal routes. The samples were prepared as described in Supplementary data. The quantitative analysis of Lupeol in plasma samples was performed on a TSQ Quantum Ultra Mass Spectrometer (MS) coupled with a Waters Nano-Acquity capillary UPLC. Lanosterol was used as an internal control. The detailed MS/UPLC method for Lupeol is provided in Supplementary data. The PK parameters (Tmax, AUCinf, AUClast) were determined by using WinNonlin Version 5.3 from Pharsight (Mountain View, CA).
Ganaie A.A., Siddique H.R., Sheikh I.A., Parray A., Wang L., Panyam J., Villalta P.W., Deng Y., Konety B.R, & Saleem M. (2020). A novel terpenoid class for prevention and treatment of KRAS-driven cancers: Comprehensive analysis using in situ, in vitro and in vivo model systems. Molecular carcinogenesis, 59(8), 886-896.
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