The maXis Impact™ Mass Spectrometer Identifies >1600 Proteins In A Single LC-MS/MS Experiment

The analysis of complex proteomic samples is one of the most demanding tasks in proteomics studies. The sample complexity requires the utmost speed, dynamic range and sensitivity from an analytical system to be used effectively. To address the speed issue, Bruker has implemented a new dynamic adaptation feature for MS/MS acquisition speed into its QTOF instrument control software. This new feature leads to a significant increase in acquisition speed. When combined with the excellent sensitivity and advanced data analysis capabilities of Bruker's ProteinScape™ software, a very powerful tool for demanding proteomic analysis is empowered.

Analysis of a tryptic digest of a human tumor cell line HT29 was performed using a Bruker maXis impact™ high resolution QTOF mass spectrometer. One µg of the tryptic peptide mixture was analyzed using a Dionex Ultimate 3000 nanoRSLC system equipped with a Dionex PepMap C18 column (250mmx75µm). Separation was performed with a 180 min water/ acetonitrile gradient. Database searching was performed using MASCOT against Swissprot. Taxonomy was restricted to human. Carbamidomethylation was considered as fixed modification and various variable modifications were investigated. For positive ID at least 1 peptide above identity threshold was required. All results were stored and further analyzed using Bruker's ProteinScape 2.1 software.