Q exactive hf mass spectrometer

Manufactured by Waters Corporation

The Q Exactive HF mass spectrometer is a high-resolution, quadrupole-Orbitrap hybrid mass spectrometer designed for advanced analytical applications. It provides high-quality data and accurate mass measurements for a wide range of analytes.

Automatically generated - may contain errors

Lab products found in correlation

Nanoacquity uplc, by Waters Corporation (1 mentions) Acquity uplc peptide beh c18 analytical column, by Waters Corporation (1 mentions) Nanoacquity nplc symmetry c18 trap column, by Waters Corporation (1 mentions) Triversa nanomate source, by Advion (1 mentions) Q exactive hf mass spectrometer, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Q Exactive (14 citations) Exactive mass spectrometer (2 citations)

2 protocols using q exactive hf mass spectrometer

Extracellular Vesicle Proteome Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

EV samples were lysed with 100 µL of 8 M urea. Following protein determination, 10 µg of the protein was reduced with TCEP to a final concentration of 10 mM at room temperature for 30 min. Samples were then alkylated with CAA to a final concentration of 40 mM for 30 min at room temperature. Samples were diluted with 50 mM ammonium bicarbonate buffer to obtain a final urea concentration of <1 M. Samples were digested overnight with Lys-C-Trypsin mix (1:100 enzyme: protein ratio) and trypsin (Promega V5073, USA; 1:50 enzyme: protein ratio). Peptides were desalted on C18 stage tips, vacuum dried and resuspended in 2% acetonitrile, 0.1% TFA. The peptide samples were analyzed in the De Botton Protein Profiling Institute of the Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science. Peptides were loaded onto a Waters ACQ M-Class HSS T3 column (1.8 µm, 75 µm × 250 mm) coupled to a Waters nanoACQUITY UPLC and Q Exactive HF mass spectrometer. Peptides were separated using a 180-min linear gradient of water and acetonitrile.

Nudelman A., Shenoy A., Allouche-Arnon H., Fisler M., Rosenhek-Goldian I., Dayan L., Abou Karam P., Porat Z., Solomonov I., Regev-Rudzki N., Bar-Shir A, & Sagi I. (2024). Proteolytic Vesicles Derived from Salmonella enterica Serovar Typhimurium-Infected Macrophages: Enhancing MMP-9-Mediated Invasion and EV Accumulation. Biomedicines, 12(2), 434.

+ Open protocol

+ Expand

Glycopeptide Characterization by Mass Spectrometry

Check if the same lab product or an alternative is used in the 5 most similar protocols

As a comparison, along with the intact glycopeptide analyses with timsTOF Pro MS, we characterized both AGP and influenza samples in parallel using a Q Exactive HF mass spectrometer (Thermo-Fisher, San Jose, CA). The Q Exactive HF mass spectrometer was equipped with a nanoAcquity UPLC system: nanoAcquity NPLC Symmetry C₁₈ trap column and ACQUITY UPLC Peptide BEH C₁₈ analytical column (Waters, Milford, MA) and a Triversa Nanomate source (Advion, Ithaca, NY). The sample separation and elution gradient were implemented the same as those used for timsTOF Pro.
Data for both nonenriched glycopeptides and HILIC-enriched glycopeptides were acquired using data-independent acquisition (DIA) methods. MS1 spectra were acquired at a 30,000 resolution at m/z 400, scan range m/z 350–1800, 1 microscan per spectrum, AGC target of 3e6, maximum injection time 32 ms. For MS2 acquisition, the range of m/z 800–1600 was divided into 50 nonoverlapping windows, each with an isolation width of m/z 16. The resolution was 30,000 at m/z 400, and we acquired 2 microscans per spectrum, AGC target 1e6, maximum injection time 32 ms, and NCE 35. Profile and centroid data were recorded for MS1 and MS2 scans, respectively.

Wong T.L., Mooney B.P., Cavallero G.J., Guan M., Li L., Zaia J, & Wan X.F. (2022). Glycoproteomic Analyses of Influenza A Viruses Using timsTOF Pro MS. Journal of proteome research, 22(1), 62-77.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!