Vydavatel Federal Laboratory Consortium
Datum vydání před téměř 10 roky
Shrnutí
Popis
FUNCTION: The system generates superior quality mass spectrometry (MS) and tandem mass spectrometry (MS/MS) data from both atmospheric pressure ionization (API) and matrix-assisted laser desorption ionization (MALDI) techniques. DESCRIPTION: The QSTAR ® XL Hybrid LC/MS/MS System is a high-performance, hybrid quadrupole time-of-flight mass spectrometer designed for protein identification and characterization and drug metabolism studies. The unique flexibility to switch between the standard API NanoSpray ™ source and the new oMALDI ™ 2 ion source makes the QSTAR ® XL System the preferred choice for proteomics. Specific scan modes such as precursor ion scanning, enabled by the patented LINAC ™ Pulsar collision cell technology, identify the type and location of post-translational modifications or drug metabolites with outstanding specificity and sensitivity. FEATURES: Enhanced ion optics for highest sensitivity and reliability. Excellent mass accuracy and stability yield unequivocal molecular weight and high-quality structural information. Unique, patented LINAC ™ Pulsar collision cell technology enables the most sensitive product ion and precursor ion scan capabilities for metabolite, protein and peptide, and post-translational modification determination. Maximum flexibility with a comprehensive selection of interchangeable, application-specific ion sources; new oMALDI ™ 2 source for increased sensitivity. Sensitive and rugged IonSpray ™ , TurboIonSpray ® , and atmospheric pressure chemical ionization (APCI) ion sources for routine low-level drug metabolism identification and characterization. New NanoSpray ™ ion source for capillary liquid chromatography (LC) provides increased sensitivity and throughput for protein and peptide identification and characterization. New PhotoSpray ™ source for analysis of low-molecular- weight, highly polar compounds via atmospheric pressure photoionization. Extended MS and MS/MS mass range (6,000 and 40,000 m/z) expands scope of protein and peptide