TripleTOF 5600
The TripleTOF 5600 is a high-resolution mass spectrometer designed for advanced analytical applications. It combines a triple quadrupole front-end with a time-of-flight (TOF) mass analyzer, providing high sensitivity and accurate mass measurements. The instrument is capable of performing various modes of operation, including full-scan acquisition, targeted data-dependent acquisition, and independent data acquisition.
Lab products found in correlation
455 protocols using TripleTOF 5600
Comprehensive Peptide Analysis by MS
Polypeptide Characterization by Triple TOF LC-MS
Quantitative ALA Analysis by LC-MS/MS
Antioxidant Evaluation of Bioactive Compounds
Shotgun Proteomics by Information-Dependent Acquisition
ESI-LC-MS/MS Analysis of Protein Samples
Tear Proteome Analysis by SWATH-MS
Porcine Proteome Identification and Quantitation
The *.group results files (1 per experiment) were exported as Peptide Summaries.
Plasma Metabolomics Analysis of Breast Cancer
Flow Injection Analysis (FIA) was performed using isocratic elution with Methanol/Water (90/10) with 5.0 mM of ammonium formate. Flow rate and injection volumes were 0.025 mL/min and 50 μL respectively.
No ion source or declustering potential (50 V and −40 V) optimization was performed. The following ionization parameters were applied: CUR = 20 psi, GS1 = 20 psi, GS2 = 15 psi, Temp = 250oC, IS = 5000 V (–4000V). MS scan ranging from m/z 100 to 1200 with accumulation time of 0.25 s and product ion scan from m/z 100 to 1200 and accumulation time of 0.03 s were the adopted parameters during survey and dependent scans respectively.
Trypsin Digestion and LC-MS/MS Analysis
Briefly, gel slices were reduced with DTT, alkylated with iodoacetamide and digested with 20 ng/μl of Trypsin (Promega, Madison, USA) overnight at 37 °C. Digestion was stopped with 10% trifluoroacetic acid (TFA) to a final concentration of 0.1%, and the supernatants were filtered through a 0.22 μm filter and dried by centrifugation in a vacuum. Pellets were re-suspended in 6 μl of 5% acetonitrile, 0.1% TFA, and 5 μl of every sample was loaded onto a trap column (Nano LC Column, 3 μ C18-CL, 350 μm × 0.5 mm, Eksigent) and desalted with 0.1% TFA at a flow rate of 3 μl/min for 5 min. The peptides were then loaded onto an analytical column (LC Column, 3 μ C18-CL, 75 μm × 25 cm, Eksigent) and equilibrated in 5% acetonitrile (ACN) and 0.1% formic acid (FA). Elution was carried out with a linear gradient of 5–40% B (B: ACN, 0.1% FA) in A (A: 0.1% FA) for 30 min at a flow rate of 300 nl/min. Eluted peptides were analysed in a nanoESI qQTOF mass spectrometer (5600TripleTOF, ABSCIEX, Ontario, Canada) in IDA mode performing 0.25-s TOF MS scans from 350 to 1250 m/z, followed by 0.05-s product ion scans from 100 to 1500 m/z on the 50 most intense 2–5 charged ions.
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