The largest database of trusted experimental protocols

Xcalibur qualbrowser 4

Manufactured by Thermo Fisher Scientific

The XCalibur QualBrowser 4.0.27.10 is a software tool designed for the analysis and interpretation of mass spectrometry data. It provides a user-friendly interface for visualizing and processing complex data sets generated by Thermo Fisher Scientific mass spectrometry instruments.

Automatically generated - may contain errors

7 protocols using xcalibur qualbrowser 4

1

Mycotoxin Quantification via UPLC-MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Use Thermo Xcalibur Qual Browser 4.0 to recognize UPLC-MS raw data. Mycotoxin recoveries for each solvent mixture and purification method were evaluated using two-way ANOVA at a significance level of 0.05; Tukey’s multiple comparisons testing was used to evaluate the significance of difference within each group. GraphPad Prism 5.0 software is used for all statistical analysis and graphic production.
+ Open protocol
+ Expand
2

Determination of Mycotoxins in Wheat Flour

Check if the same lab product or an alternative is used in the 5 most similar protocols
The UPLC-MS raw data were recognized by Thermo Xcalibur Qual Browser 4.0. Nonparametric statistics were used after the normality and lognormality testing for each group. Distribution characteristics and differences of mycotoxins in various types of wheat flour samples were compared and evaluated using the Kruskal-Wallis or Mann-Whitney test at a significance level of 0.05. All statistical analyses and drawings were performed using GraphPad Prism 9.0 software.
+ Open protocol
+ Expand
3

Quantitative Proteomics and Glycomics of Viral Spike Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
For the proteomics experiment, data collected was submitted to MaxQuant for protein identification and quantitation. Proteins were searched against SARS-CoV S protein, SARS-CoV-2 S protein, MERS S protein and human proteome UP000005640. The identification FDR was 0.01. The MaxQuant score was set to 60. The assignment of glycoproteins was based on UniprotKB. The abundance of viral spike proteins relative to human proteins were calculated. Human glycoproteins which might affect the quantitation of viral spike protein N-glycans were investigated.
For glycomics experiment, acquired .raw files were processed Skyline (MacCoss Lab Software) with in-house glycan library. All possible m/z values of each glycan adduct forms were evaluated manually. Relative quantitation of glycans was performed using Microsoft Excel. Chromatograms and MS2 spectra were generated with Skyline and XCalibur Qual Browser 4.3 (Thermo Scientific). MS2 spectra were carefully examined with GlycoWorkbench 2. Other figures were made with GraphPad Prism 8.4.3. Workflow scheme was made with biorender.com.
+ Open protocol
+ Expand
4

Blinded LC-MS Analysis of Pharmacological Treatments

Check if the same lab product or an alternative is used in the 5 most similar protocols
LC-MS data were collected and processed using Thermo Xcalibur Qual Browser 4.3, and then MS/MS spectra were used to identify the chemical structures.
All data and images were analyzed unbiasedly. A random number was assigned to each group to ensure the investigator was blind to the pharmacological treatment grouping information. Statistical analysis was performed by using Graphpad Prism software 9.0, and T-test and one-way ANOVA were used for two- or multiple-group comparisons. p < 0.05 was considered statistically significant.
+ Open protocol
+ Expand
5

Native Mass Spectrometry of Nucleosomes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nucleosomes samples at a concentration of 2 μM and desalted into 150 mM ammonium acetate using 30 kDa MWCO 0.5 mL spin filters (Millipore-Sigma). Samples were analyzed using a Q Exactive HF mass spectrometer with Extended Mass Range (QE-EMR) and a Q Exactive HF Ultra-High Mass Range (QE-UHMR), both by Thermo Fisher Scientific. Data were collected using XCalibur QualBrowser 4.0.27.10 (Thermo Fisher Scientific). The native electrospray platform is coupled to a three-tiered tandem MS process. First, the analysis of the intact nucleosome (MS1) provides the total complex mass (reported as a deconvoluted neutral average mass value).13 (link) In stage two, the nucleosome is activated by collisions with nitrogen gas to eject histones (MS2). In stage three, further vibrational activation of the ejected histones via collisions with nitrogen gas yields backbone fragmentation products from each monomer (MS3) that are recorded at isotopic resolution (120,000 resolving power at m/z 400). These fragments can be mapped onto the primary sequence of the histones in order to localize posttranslational modifications. A step-by-step protocol for Nuc-MS data acquisition and analysis is available on the Nature Protocol Exchange repository (DOI 10.21203/rs.3.pex-1288/v1) and in the Supplemental Information.34
+ Open protocol
+ Expand
6

Native Mass Spectrometry of Nucleosomes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Nucleosomes samples at a concentration of 2 μM and desalted into 150 mM ammonium acetate using 30 kDa MWCO 0.5 mL spin filters (Millipore-Sigma). Samples were analyzed using a Q Exactive HF mass spectrometer with Extended Mass Range (QE-EMR) and a Q Exactive HF Ultra-High Mass Range (QE-UHMR), both by Thermo Fisher Scientific. Data were collected using XCalibur QualBrowser 4.0.27.10 (Thermo Fisher Scientific). The native electrospray platform is coupled to a three-tiered tandem MS process. First, the analysis of the intact nucleosome (MS1) provides the total complex mass (reported as a deconvoluted neutral average mass value).13 (link) In stage two, the nucleosome is activated by collisions with nitrogen gas to eject histones (MS2). In stage three, further vibrational activation of the ejected histones via collisions with nitrogen gas yields backbone fragmentation products from each monomer (MS3) that are recorded at isotopic resolution (120,000 resolving power at m/z 400). These fragments can be mapped onto the primary sequence of the histones in order to localize posttranslational modifications. A step-by-step protocol for Nuc-MS data acquisition and analysis is available on the Nature Protocol Exchange repository (DOI 10.21203/rs.3.pex-1288/v1) and in the Supplemental Information.34
+ Open protocol
+ Expand
7

Native Mass Spectrometry Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein samples were measured at a concentration of 2 μM and desalted into 150 mM ammonium acetate using 10–30 kDa MWCO 0.5 mL spin filters (Millipore-Sigma). Samples were analyzed using a Q Exactive HF mass spectrometer with Extended Mass Range (QE-EMR) by Thermo Fisher Scientific. Data were collected using XCalibur Qual Browser 4.0.27.10 (Thermo Fisher Scientific). The native electrospray platform was coupled to a three-tiered tandem MS process. First, the analysis of the intact complex (MS1) provides the total complex mass (reported as a deconvoluted neutral average mass value).21 (link) In stage two, the complex is activated by collisions with nitrogen gas to eject subunits (MS2). In stage three, further vibrational activation of the ejected subunits via collisions with nitrogen gas yields backbone fragmentation products from each monomer (MS3) that are recorded at isotopic resolution (120,000 resolving power at m/z 400). These fragments can be mapped onto the primary sequence of the subunits in order to localize PTMs.
+ 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?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!