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Life Sciences Mass Spectrometry
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Welcome to the 50th issue of Critical Mass! We'd like to thank our readers for your continued interest in our monthly e-newsletter. This month, we've enabled two new features to make it more interactive:
Thank you for your support,
Critical Mass Team
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Tip of the Month: Metabolism and Selectivity
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Many researchers think that with multiple metabolites, many compensation voltages are required. When using high-Field Asymmetric waveform Ion Mobility Spectrometry (FAIMS) for selectivity, most small molecules emerge in a tight band between -13 and -17V. Drugs and their metabolites emerge together!
» Learn More About FAIMS Today!
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Proteomics: Analysis of Sialylated Glycans with the MALDI LTQ Orbitrap Mass Spectrometer using DHB/N,N-Dimethylaniline Matrix
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Alterations in glycan structures can have great biological significance. Of particular interest are sialylated glycans due to their involvement in biological phenomena, such as cell-cell adhesion and cell-pathogen interaction. This note discusses a technique that is a fast, simple, and reliable workflow for profiling N-linked glycans. It combines the benefits of the Thermo Scientific MALDI LTQ Orbitrap mass spectrometer with the homogeneity of sample distribution provided by a DHB/DMA matrix. The high mass accuracy and mass resolution provided by the Thermo Scientific Orbitrap detector enables confident structural discrimination without the aid of tandem MS. The ability to profile both sialylated and asialylated glycans with a single ionization mode in MALDI experiments makes the workflow especially practical. This ability is useful in determining the degree of silaylation relative to overall glycan composition.
This application note describes the use of MALDI on a Thermo Scientific LTQ Orbitrap hybrid mass spectrometer, and a unique MALDI matrix, to improve analysis of N-linked sialylated glycans.
» Download Complete Application Note [PDF 649 kB]
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Proteomics: Streamlining the Process of Biomarker Verification using Pinpoint Software
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Interest in targeted protein quantitation has increased significantly over the past two years. The focus of proteomics research has started to shift from pure shotgun experiments, in which the goal was to detect all possible proteins and peptides in a biological sample, to a more targeted approach for monitoring specific proteins or pathways. This shift in research focus requires an integrated workflow to simultaneously and reproducibly measure protein abundance across many targets. The primary approach to targeted protein quantitation studies incorporates selected-reaction monitoring (SRM) using a triple quadrupole mass spectrometer. The two stages of mass filtering in the triple quadruple mass spectrometer yield superior sensitivity and selectivity by reducing background interferences while maintaining fast cycle times. The novel Thermo Scientific Pinpoint software facilitates the transition from qualitative proteomics to targeted protein quantitation.
» Download Complete Application Note [PDF 1.8 MB]
Attending the European Bioanalysis Forum in Barcelona December 2-4, 2009? See our presentation on this application.
» Download Pinpoint Software Today!
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| On-Demand Webinar: Increase Mass Spectrometry Throughput up to 400% |
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Today’s budget-limited LC/MS customers are looking for ways to increase throughput and flexibility of their mass spectrometers without sacrificing data quality or reliability. Multiplexing is a proven technology that can produce these results. Though there are different approaches to multiplexing, not all are created equal. This webinar discusses the following:
- Existing technologies to increase mass spectrometry throughput
- Industry-leading multiplexing solution: allowing increased throughput, flexibility, multiple methods, data quality
- A sneak peek into a new LC software technology to improve quality and results
» Register to View This On-Demand Webinar [53 minutes]
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Clinical: A Quantitative Test for Multiple Classes of Illicit Drugs and Their Primary Metabolites in Human Biological Fluids by LC-MS/MS for Forensic Use
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Currently, GC/MS is the method of choice for quantifying drugs of abuse. In recent years, however, many forensic labs have been switching to LC-MS/MS methods, which do not require time-consuming derivatization or extensive sample cleanup necessary in GC/MS analyses. Yet, many of the LC-MS/MS methods described in the literature either assay a limited number of illicit drug classes or do not include their primary metabolites of these illicit drugs.
This application note describes a method to assay multiple drugs of abuse including opiates, stimulants, depressants, and the primary metabolites of these illicit drugs.
» Download Complete Application Note [PDF 360 kB]
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| Food Safety: LC-MS/MS Analysis of Malachite Green, Leucomalachite Green, Ciprofloxacin, and Tetracycline in Food Samples Using a TurboFlow Method |
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Accurate monitoring of chemical residue levels in food and agriculture products is essential to assure the safety of the food supply and manage global health risks. The analysis of chemical residues requires techniques sensitive enough to detect and quantify contaminants at or below the maximum residue limit (MRL) of the compound in a given sample matrix. In addition, because of increased food safety regulations and the growing numbers of samples to be analyzed, it is critical that the analytical techniques provide high sample throughput.
This application note demonstrates a solution that combines the Thermo Scientific Aria TLX system utilizing TurboFlow™ technology with a Thermo Scientific TSQ Quantum Access mass spectrometer. Compared to traditional offline extraction methods, this solution provides fast and reliable sample analysis of chemical residues in food by online sample extraction followed by LC-MS/MS.
» Register to Download Complete Application Note [PDF 770 kB]
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Upcoming Events
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Resolving Complexity
Visit the Thermo Scientific booths at these events for more information about products and workflows to meet your challenges.
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Biodistribution: Experimental Strategies for Determining the Distribution of Erlotinib in Pancreatic Tumors by MALDI Using an LTQ Linear Ion Trap Mass Spectrometer
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Imaging Mass Spectrometry (IMS) using matrix-assisted laser desorption ionization (MALDI) is being investigated using a linear ion trap with the overall goal of analyzing the distribution of various targeted therapies within patients' tumors. The drug chosen for evaluation is erlotinib which targets the epidermal growth factor receptor (EGFR), a type I receptor tyrosine kinase (TK) involved in cellular differentiation and proliferation, by binding to the ATP pocket and inhibiting the autophosphorylation of the receptor. Erlotinib has demonstrated clinical activity in non-small cell lung cancer, head and neck cancer, and ovarian cancer in Phase II studies. The sensitivity and MS/MS capabilities of the Thermo Scientific LTQ XL are exploited for the unambiguous determination of the distribution of this drug within human pancreatic tumors.
» Download Complete Application Note [PDF 991 kB]
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| Trap Talk: Comparison of a Dual-Cell Linear Ion Trap with a Four-Fold Symmetric Stretch Versus a Two-Fold Symmetric Stretch |
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A dual-cell linear ion trap (LIT) quadrupole mass spectrometer has been developed with enhanced performance over single-cell LITs in terms of improved scanning rate, resolution, MS/MS efficiency, and trapping efficiency. In commercially available LITs, the X-rods are displaced from the nominal quadrupolar r0 in order to compensate for field distortions created by slots cut into the X-rods for ion ejection. The Y-rods do not include these slots nor the corresponding rod displacement, therefore resulting in a two-fold symmetric stretch (2FSS). In contrast, the dual-cell configuration incorporates four identical electrodes, where the r0 is the same for both X and Y rods, resulting in a four-fold symmetric stretch (4FSS). This work investigates some fundamental differences between these LIT geometries.
» Download Poster [PDF 622 kB]
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