Detection was carried out with a QTRAP 6500+ mass spectrometry system (Sciex, Darmstadt, Germany) equipped with an ESI IonDrive™ Turbo V Source using scheduled MRM mode for the detection of different dipeptides, parameters are listed in Table 3 . Compound-specific details on MRM transitions, potentials and retention times are listed in Table 1 . Analyst® 1.7 (Sciex) was used as system operation software. Evaluation and analysis of data was performed using SciexOS® software (Sciex, Version 1.4.0.18067) and AutoPeak algorithm. Quantification parameters can be found in Supplementary Table S1 .
Qtrap 6500 mass
Manufactured by AB Sciex
Sourced in Germany, United States
The QTRAP 6500+ mass spectrometer is a high-performance analytical instrument designed for advanced quantitative and qualitative analysis. It combines the capabilities of a triple quadrupole and a linear ion trap to provide enhanced sensitivity, resolution, and versatility for a wide range of applications.
Automatically generated - may contain errors
Lab products found in correlation
5 protocols using qtrap 6500 mass
1
Targeted Dipeptide Detection via QTRAP 6500+
2
Rat Plasma LC-MS/MS Bioanalysis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
A qualified method was used in a specialized bioanalytical laboratory. Rat blood plasma samples (50 µl) were extracted by protein precipitation. Extracts (20 µl) were injected into the analytical column (YMC Triart C18, 3 mm; 2.1´50 mm) and analyzed using liquid chromatography coupled to tandem mass spectrometry. Separation was performed using gradient elution from 30−95% mobile phase B in 2.5 min at a flow of 0.8 ml/min, where mobile phase A was 20 mm ammonium-acetate and mobile phase B was acetonitrile. Multiple reaction monitoring was conducted on a Sciex QTrap 6500+ mass spectrometer using MRM transitions.
3
Quantifying H3.3K27M Peptide in DIPG Cells
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The HLA-A∗02:01-positive DIPG cell line eluates were spiked with the H3.3K27M26–35 heavy peptide. Samples were assessed for the presence of peptide by MRM using SCIEX QTRAP 6500+ mass spectrometer, equipped with an on-line Ekspert nanoLC 415 (Eksigent) autosampler using Analyst 1.6 (SCIEX) software, as previously described.27 (link) The eluates of peptide pulsed T2 cells, SU DIPG 21 cells, and SU DIPG 36 cells were spiked with the H3.3K27M26–35 heavy peptide and assessed for the presence of endogenous peptide by MRM-HR28 (link) using SCIEX 7600 mass spectrometer. MRM and MRM-HR data were visualized on Skyline software 64-bit v4.1.0 (MacCoss Laboratory).
4
Quantifying Cellular Cholesterol Levels
5
Quantitative Peptide Detection by MRM-MS
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The detection of peptides was carried out by the method of Multiple Reaction Monitoring (MRM) on a Q-TRAP 6500 mass spectrometer (AB Sciex, Framingham, MA, USA) combined with an high-performance liquid chromatograph Infinity 1290 (Agilent, Canta Clara, CA, USA).
Chromatographic separation was carried out on a column Titan C18, 1,9 µm, 10 cm × 2.1 mm (Supelco, Bellefonte, PA, USA) in several stages: 0–40 min–from 2% to 23% of phase B, 40–43 min–from 23% to 45%, 43–43.5 min–from 45% to 80%, 43.5–45.5 min–80% of phase B, 45.5–46 min–from 80% to 2%, 46–50 min 2% of phase B. Mobile phase A: 99.9%–water, 0.1%–formic acid; phase B: 99.9%–acetonitrile, 0.1%–formic acid. The flow rate was 0.4 mL/min, the separation temperature is 45 °C. Positively charged ions obtained by electrospray ionization in the Turbo Spray IonDrive source were detected. The source temperature was 400 °C, the capillary voltage was 4 kV, the curtain gas pressure was 40 psi, the gas pressure was40 psi, and the decasterization potential was 40 V.
Calibration curves were constructed and protein concentrations were determined using the MultiQuant 3.0.2 program (AB Sciex, Framingham, MA, USA) based on the area of peaks of MRM transitions specific to each studied peptide.
Chromatographic separation was carried out on a column Titan C18, 1,9 µm, 10 cm × 2.1 mm (Supelco, Bellefonte, PA, USA) in several stages: 0–40 min–from 2% to 23% of phase B, 40–43 min–from 23% to 45%, 43–43.5 min–from 45% to 80%, 43.5–45.5 min–80% of phase B, 45.5–46 min–from 80% to 2%, 46–50 min 2% of phase B. Mobile phase A: 99.9%–water, 0.1%–formic acid; phase B: 99.9%–acetonitrile, 0.1%–formic acid. The flow rate was 0.4 mL/min, the separation temperature is 45 °C. Positively charged ions obtained by electrospray ionization in the Turbo Spray IonDrive source were detected. The source temperature was 400 °C, the capillary voltage was 4 kV, the curtain gas pressure was 40 psi, the gas pressure was40 psi, and the decasterization potential was 40 V.
Calibration curves were constructed and protein concentrations were determined using the MultiQuant 3.0.2 program (AB Sciex, Framingham, MA, USA) based on the area of peaks of MRM transitions specific to each studied peptide.
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
Revolutionizing how scientists
search and build protocols!