<p><strong>Taťána Gazárková is currently a&nbsp;postdoctoral fellow in the Laboratory of Antibiotic Resistance and Microbial Metabolomics. During her doctoral studies, she focused on chromatography and mass spectrometry. Recently, she was awarded second place in the “Sanofi Prize for Pharmacy 2026” competition.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/MBU_AV_CR_Lukas_Biba_Rozhovor_Cim_zaujala_analyticka_chemie_postdoktorandku_Tatanu_Gazarkovou_7450c646fa.jpg" alt="MBÚ/Lukas Biba:&nbsp;Sanofi Prize for Pharmacy 2026" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_MBU_AV_CR_Lukas_Biba_Rozhovor_Cim_zaujala_analyticka_chemie_postdoktorandku_Tatanu_Gazarkovou_7450c646fa.jpg 234w," sizes="100vw" width="1024" height="683"></p><p><strong>Taťána Gazárková </strong>is currently a&nbsp;postdoctoral fellow in the <strong>Laboratory of Antibiotic Resistance and Microbial Metabolomics</strong>. During her doctoral studies, she focused on chromatography and mass spectrometry. Recently, she was awarded second place in the <strong>“Sanofi Prize for Pharmacy 2026” </strong>competition, which is awarded by the<strong> French Embassy in the Czech Republic</strong> for her dissertation – Steroid Analysis Using Modern Chromatographic and Mass Spectrometry Techniques: From Fundamental Studies to Targeted Bioanalytical Applications (supervisor: <strong>Lucie Nováková, Charles University</strong>).&nbsp;</p><h5><strong>What makes this field particularly exciting or unique in your view?</strong></h5><p>What I&nbsp;enjoy about analytical chemistry is that, to a&nbsp;certain extent, it is a&nbsp;kind of detective work. You are often looking for ways to “make the invisible visible”. In other words, extract the information you are interested in from a&nbsp;complex sample and then interpret it correctly. What also appeals to me about bioanalytical chemistry is its interdisciplinary nature. It brings together analytical chemistry, biochemistry, biology and medicine, which means that you need to be able not only to translate a&nbsp;biological or clinical question into a&nbsp;measurable analytical experiment, but also to place the resulting data back into a&nbsp;broader biological context. This combination of different perspectives is probably what I&nbsp;enjoy most about the field. At the same time, there is still plenty of room for fundamental research, ranging from studying analytical techniques themselves and improving them to developing new methodological approaches.</p><h5><strong>How did you end up at the </strong><a target="_blank" rel="noopener noreferrer" href="https://mbu.cas.cz/en/research/laboratory-of-antibiotic-resistance-and-microbial-metabolomics"><strong>Laboratory of Antibiotic Resistance and Microbial Metabolomics</strong></a><strong>, and what project are you currently working on?</strong></h5><p>I came to the Institute of Microbiology through a&nbsp;joint project between<strong> Dr Zdeněk Kameník and Assoc. Prof. Jan Bobek from the First Faculty of Medicine, Charles University</strong>. For me, it was also an opportunity to move from targeted analysis and the study of chromatographic techniques towards untargeted metabolomics and new biological questions.</p><p>In the project, we are trying to identify new biologically active compounds that would be effective, particularly against pathogenic fungi. As a&nbsp;potential source of such compounds, we study streptomycetes, bacteria known for their ability to produce a&nbsp;wide range of biologically active compounds, including many antibiotics that are currently in clinical use. We focus on less-explored host-associated streptomycetes, in which we had already observed antifungal activity in previous experiments. We are especially interested in strains active against Candida albicans whose activity cannot be explained by the presence of a&nbsp;known bioactive compound. These strains may represent an interesting source of novel compounds. We then integrate the results of untargeted metabolomic analyses with genomic analyses, which allows us to obtain a&nbsp;more comprehensive view of the biosynthetic potential of selected strains.</p><h5><strong>You also took part in this year’s Vědafest, a&nbsp;science outreach event for the public. What was it like?</strong></h5><p>I already had some experience with science outreach through events such as Researchers’ Night and the Science Fair at my previous institution, but this year’s Vědafest was still new to me in some ways. This time, I&nbsp;was presenting a&nbsp;field that I&nbsp;myself had entered only relatively recently. It was therefore more challenging to find the right analogies and explain the essence of the topic in a&nbsp;way that was simple, yet precise and scientifically accurate. At the same time, that was exactly what made it inspiring. It forces you to look at your own work from a&nbsp;different perspective. What I&nbsp;enjoyed most was the spontaneity and curiosity of the children, who often came up with questions that would never even occur to an adult.</p><h5><strong>What are the biggest challenges you face on your scientific journey, and what helps you overcome them?</strong></h5><p>One of the greatest, but at the same time most interesting, challenges is, in my view, the uncertainty that is inseparably linked to research. For a&nbsp;long time, you often do not know whether you have taken the right direction in addressing a&nbsp;particular question or whether you will ultimately manage to find that figurative final piece of the puzzle. At the same time, this uncertainty is precisely what makes science exciting for me.</p><p>Another major challenge, particularly in interdisciplinary projects, is communication. It is important from the very formulation of a&nbsp;hypothesis and the planning of experiments through to the interpretation of results, including negative ones, and placing them in a&nbsp;broader context. To some extent, every field has its own language, and finding a&nbsp;common understanding is not always straightforward. Personally, I&nbsp;find it very helpful to be able to discuss problems with colleagues on an ongoing basis, whether individually or during regular laboratory seminars. One of the major strengths of our current group is its interdisciplinary nature, which allows me to look at the same problem from several different perspectives. It is also important for me not to lose my curiosity, because that is ultimately what leads us to ask further questions.</p><h5><strong>What are your plans after completing your PhD?</strong></h5><p>After finishing my PhD, I&nbsp;decided that I&nbsp;do not need to have everything that comes next precisely mapped out straight away. I&nbsp;would like to keep different options open for a&nbsp;while and continue building on my experience in analytical chemistry, while at the same time connecting it with other areas that have a&nbsp;biological or medical relevance. I&nbsp;believe that we can keep learning throughout our lives, so I&nbsp;am quite curious to see where the next stage of my journey will take me.</p><p><i>Thank you for the interview!</i></p>

Interview: What Drew Postdoc Taťána Gazárková to Analytical Chemistry

<p><strong>Per- and polyfluoroalkyl substances (PFAS) have earned the moniker "forever chemicals" due to their extreme persistence in the environment. Their detection is crucial for protecting public health and the environment as these synthetic compounds continue to pose significant challenges worldwide. This comprehensive exploration examines why PFAS detection matters, current detection methods, and future directions in addressing PFAS contamination.</strong></p><h3><strong>Understanding PFAS and Their Health Impacts</strong></h3><p>PFAS are a class of synthetic organic compounds with diverse structures, properties, and uses. Despite their diversity, all PFAS contain perfluoroalkyl moieties that are extremely resistant to environmental and metabolic degradation [1]. This high persistence is a defining characteristic that makes PFAS management particularly challenging.</p><h3><strong>Documented Health Effects</strong></h3><p>Current scientific research has linked PFAS exposure to numerous adverse health outcomes:</p><ul><li>Reproductive effects including decreased fertility and increased high blood pressure in pregnant women [8]</li><li>Developmental effects in children such as low birth weight, accelerated puberty, and behavioral changes [8]</li><li>Reduced immune system function, including decreased vaccine response</li><li>Interference with natural hormones and endocrine disruption</li><li>Increased cholesterol levels and obesity risk</li><li>Increased risk of several cancers, including prostate, kidney, testicular, oral cavity/pharynx, brain, and endocrine cancers [3]</li></ul><p>A 2023 study linked PFAS-contaminated water with up to a <strong>33% increase in cancer incidence</strong> in affected areas [3]. The study compared regions with elevated PFAS levels to cancer data from the National Cancer Institute, finding higher incidences of various cancers after controlling for factors like smoking and obesity.</p><h3><strong>Environmental Persistence and Contamination</strong></h3><p>The extreme persistence of PFAS represents a fundamental concern for environmental management. PFAS are considered the most environmentally persistent substances among organic chemicals [7]. This persistence means that even if all PFAS uses were immediately phased out, existing contamination would continue to affect ecosystems and water supplies for generations.</p><p>A 2023 study at a military fire training site estimated that PFAS contamination will persist for centuries without remediation [7]. The research found that terminal PFAS still exceed regulatory limits by 2000-fold decades after aqueous film-forming foam (AFFF) use ceased, with precursors accounting for around half of the extractable organofluorine across years.</p><h3><strong>Current Detection Methods</strong></h3><h4><strong>EPA Standardized Methods</strong></h4><p>The<strong> Environmental Protection Agency (EPA</strong>) has developed several standardized methods for PFAS detection, each with specific applications and capabilities:</p><h5><strong>EPA Method 533</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/epa-533-drying-down-pfas-samples-after-spe"><strong>EPA Method 533</strong></a> focuses on "short chain" PFAS with carbon chain lengths of<strong> C4 to C12</strong>. Released in December 2019, this method complements Method 537.1 and includes several key features:</p><ul><li>Uses isotope dilution quantification approach with extracted internal standards, which reduces overall analytical uncertainty</li><li>Employs weak anion exchange solid phase extraction cartridges as opposed to polystyrene divinylbenzene used in 537.1</li><li>Can analyze 25 PFAS compounds, including additional short-chain PFAS that were not apart of Method 537.1</li><li>Allows for longer holding times: 28 days to extraction and 28 days to analyze (compared to 14 days to extraction in Method 537.1)</li><li>Uses ammonium acetate as a preservative (versus Trisma in Method 537.1) [1]</li></ul><h5><strong>EPA Method 537/537.1</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/sample-concentration-epa-method-537-pfas-determination"><strong>EPA Method 537 </strong></a>was first published in 2009 for the determination of 14 PFAS in drinking water [6]. It was later updated to Method 537.1 in 2018 (with editorial updates in 2020) to expand its capabilities:</p><ul><li>Uses<a target="_blank" rel="noopener noreferrer" href="https://www.organomation.com/what-is-solid-phase-extraction-spe"><strong> solid phase extraction (SPE) </strong></a>and<a target="_blank" rel="noopener noreferrer" href="https://www.organomation.com/preparing-samples-for-lc-ms/ms-analysis"><strong> liquid chromatography/tandem mass spectrometry (LC-MS/MS)</strong></a></li><li>Method 537.1 expanded detection to 18 PFAS compounds, including HFPO-DA (one component of GenX technology)</li><li>Utilizes styrene-divinylbenzene (SDVB) media for extraction</li><li>Requires samples to be extracted within 14 days and analyzed within 28 days</li><li>Methanol is used to elute the extracts. This should then be reconstituted with a 96:4 methanol:water mixture [1]</li></ul><p>Together, Methods 533 and 537.1 can detect a total of <strong>29 unique PFAS compounds in drinking water </strong>and are approved for monitoring under the fifth Unregulated Contaminant Monitoring Rule (UCMR 5) and the PFAS National Primary Drinking Water Regulation [1] [3].</p><h5><strong>EPA Method 1633</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/preparing-diverse-sample-matrices-for-epa-method-1633"><strong>EPA Method 1633</strong></a>, released in 2024, represents a significant advancement in PFAS analysis:</p><ul><li>Developed for the analysis of <strong>40 PFAS compounds </strong>in various matrices, including surface water, groundwater, wastewater, soil, biosolids, sediment, landfill leachate, and fish tissue</li><li>Expands beyond the drinking water focus of Methods 533 and 537.1</li><li>Provides a standardized approach that may replace modified drinking water methods (i.e., modified EPA 537) that were previously used for non-drinking water matrices [1]</li></ul><h4><strong>Conventional Analytical Techniques</strong></h4><p>The gold standard for PFAS analysis involves chromatographic techniques coupled with mass spectrometry:</p><ul><li>Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) is the most widely used method for PFAS analysis, offering high sensitivity and specificity [1]</li><li>High-Resolution Mass Spectrometry (HRMS) allows for rapid detection and identification of PFAS species at very low concentrations [5]</li></ul><p>These techniques can detect PFAS at parts per trillion (ppt) levels, which is essential given the low concentrations at which PFAS can cause health effects [1]. However, these methods require sophisticated equipment, specialized training, and significant financial resources, making them inaccessible in many regions, particularly in developing countries.</p><h4><strong>Emerging Detection Technologies</strong></h4><p>Several innovative approaches are being developed to address the limitations of conventional methods:</p><ul><li>Electrochemical biosensors using modified electrodes have shown promise for selective PFAS detection with low detection limits [2]</li><li>Surface-Enhanced Raman Spectroscopy (SERS) uses metallic nanoparticles and can be made into a portable method for on-site testing [1]</li><li>Molecular imprinted polymers (MIPs) offer thermal and physical stability, reusability, and low-cost synthesis for PFAS detection [6]</li></ul><p>These emerging technologies aim to provide more accessible, field-deployable, and cost-effective alternatives to traditional laboratory-based methods.</p><h3><strong>Challenges in PFAS Detection</strong></h3><h4><strong>Analytical Challenges</strong></h4><p>Detecting PFAS presents several technical challenges:</p><ul><li>The ubiquity of PFAS in laboratory equipment and accessories can lead to background contamination when measuring at parts-per-trillion levels [1]</li><li>Many components in liquid chromatographs, mass spectrometers, and solid-phase extraction systems contain materials that can leach PFAS compounds [9]</li><li>The vast number of PFAS (thousands of compounds) makes comprehensive detection difficult, as analytical standards are only available for a small subset [1]</li><li>Complex matrices like food and environmental samples require sophisticated sample preparation techniques</li></ul><h4><strong>Global Disparities in Detection Capabilities</strong></h4><p>Access to PFAS detection technology varies significantly worldwide:</p><ul><li>Many developing regions, particularly in Africa, lack adequately equipped laboratories with the necessary instrumentation to detect and measure PFAS</li><li>There is often a scarcity of qualified professionals with experience in PFAS analysis in these regions</li><li>The high cost of acquiring and maintaining sophisticated analytical instruments presents a substantial obstacle to conducting extensive PFAS investigations in resource-limited settings [1]</li><li>Competing priorities such as infectious diseases, poverty, and food security often divert attention and resources from environmental pollutants like PFAS</li></ul><h4><strong>Regulatory Landscape and Compliance</strong></h4><p>The regulatory framework for PFAS is evolving rapidly worldwide:</p><ul><li>The EPA finalized Section 8(a)(7) of the Toxic Substances Control Act in September 2024, requiring manufacturers and importers to report on their use of PFAS since 2011 [10]</li><li>Electronic reporting for PFAS will open on July 11, 2025, with final reporting deadlines in 2026</li><li>Companies must report detailed information including chemical identity, production volumes, industrial and consumer products, worker exposure, and disposal methods [10]</li></ul><p>These regulations are driving demand for more effective and accessible PFAS detection methods to ensure compliance and protect public health.</p><h3><strong>Future Directions in PFAS Detection</strong></h3><h4><strong>Technological Advancements</strong></h4><p>The future of PFAS detection lies in developing more accessible, sensitive, and comprehensive methods:</p><ul><li>Non-targeted screening methods that can identify unknown PFAS compounds without requiring analytical standards for each specific compound</li><li>Total fluorine analysis techniques like Adsorbable Organic Fluorine and Total Oxidizable Precursor Assay that can quantify the presence of fluorine atoms within a sample [1]</li><li>Portable sensors and field-deployable technologies that enable on-site monitoring and rapid response to contamination events</li><li>AI-driven solutions that can improve data analysis and interpretation for complex PFAS mixtures</li></ul><h4><strong>Collaborative Approaches</strong></h4><p>Addressing the global challenge of PFAS detection requires coordinated efforts:</p><ul><li>International partnerships between researchers in developed and developing regions to enhance expertise and capacity building</li><li>Standardization of analytical methods to ensure consistency and comparability of results across different laboratories and regions</li><li>Open data sharing and collaboration across countries to leverage collective knowledge and resources</li><li>Integration of PFAS monitoring into broader environmental and public health surveillance systems</li></ul><h3><strong>Conclusion</strong></h3><p>The detection of PFAS is not merely a technical challenge but a critical public health and environmental imperative [1]. As these "forever chemicals" continue to persist in our environment, developing effective, accessible, and comprehensive detection methods becomes increasingly important. By advancing detection technologies, strengthening regulatory frameworks, and fostering global collaboration, we can better understand, monitor, and ultimately mitigate the impacts of PFAS contamination.</p><p>The EPA's standardized methods (533, 537.1, and 1633) provide crucial tools for monitoring PFAS in various environmental matrices, but continued innovation is needed to address the full spectrum of PFAS compounds and to make detection more accessible globally [1] [6]. The path forward requires sustained investment in research and development, capacity building in resource-limited settings, and a commitment to environmental justice that ensures all communities have access to the tools and information needed to protect themselves from PFAS exposure. Only through such comprehensive approaches can we hope to address the complex challenges posed by these persistent pollutants.</p><p><span>Be sure to check out our other installments of our&nbsp;</span><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/introducing-our-environmental-contaminants-series-making-sense-of-the-alphabet-soup"><span>Environmental Contaminant Series</span></a><span>&nbsp;covering&nbsp;</span><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/the-importance-of-detecting-persistent-organic-pollutants-pops"><span>Persistent Organic Pollutants (POPs)</span></a><span>,&nbsp;</span><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/the-importance-of-detecting-polycyclic-aromatic-hydrocarbons-pahs"><span>Polycyclic Aromatic Hydrocarbons (PAHs)</span></a><span>,&nbsp;</span><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/the-importance-of-detecting-semi-volatile-organic-compounds-svocs"><span>Semi-Volatile Organic Compounds (SVOCs)</span></a><span>, and </span><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/the-importance-of-detecting-polychlorinated-biphenyls-pcbs"><span>Polychlorinated Biphenyls (PCBs)</span></a><span>.</span></p>

The Importance of Detecting Per- and Polyfluoroalkyl Substances (PFAS)

News from LabRulezLCMS Library - Week 36, 2026

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The Czech Academy of Sciences (CAS) was established by Act No. 283/1992 Coll. as the Czech successor of the former Czechoslovak Academy of Sciences. It is set up as a complex of 54 public research institutions.

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Waters Xevo MRT QTof Mass Spectrometer

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The novel acquisition system, with dual gain analogue-to-digital converter, delivers long term system stability over a high dynamic range, ensuring exceptional quality data with consistent robustness and reproducibility.</p><p>The 4 m flight path with a total of 8 reflections within the MRT mass analyzer, achieves 100,000 FWHM resolution at scan rates of up to 100 Hz - for ultimate MS/MS performance.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_Schema_2448b0bc8d.jpg" alt="Waters Xevo MRT Mass Spectrometer: The Xevo MRT Mass Spectrometer schematic. ​" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_Schema_2448b0bc8d.jpg 236w," sizes="100vw" width="1199" height="794"></p>

Thermo Scientific Stellar Mass Spectrometer

Move biomarker candidates from discovery to validation more efficiently, confidently, and at lower cost with breakthroughs in extended scale, massive throughput, higher sensitivity, greater specificity, and unrivaled productivity.

<div><div id="container-a1c36dfacf"><div><div><div id="text-913638046"><p><strong>A new paradigm for targeted quantitation.&nbsp;Move biomarker candidates from discovery to validation more efficiently, confidently, and at lower cost with breakthroughs in extended scale, massive throughput, higher sensitivity, greater specificity, and unrivaled productivity.</strong></p><p>The Thermo Scientific Stellar Mass Spectrometer introduces revolutionary technology combining robust quantitation with the specificity of rapid full scan MS<sup>n</sup>&nbsp;acquisition creating unrivaled improvements in laboratory productivity.</p><div><div id="text-801893275"><h3><strong>Expanded experimental capabilities to meet the most challenging biomarker verification</strong></h3></div></div><div><div id="container-1e8e478f3a"><div><div><div id="text-1204752335"><p>The Thermo Scientific Stellar Mass Spectrometer offers an array of data acquisition capabilities to deliver robust and reproducible quantitation for a wide range of analytes across an extended dynamic range.</p></div></div></div></div></div><h4><strong>System highlights</strong></h4><div><div id="container-a89a56f063"><div><div><div id="text-451891225"><h5><strong>Improve ionization efficiency for more compounds at higher LC flow rates&nbsp;</strong></h5></div></div><div><div id="text-1671602085"><p>For a wider range of compounds separated using liquid chromatography operated at analytical flow rates, the Stellar Mass Spectrometer comes equipped with the Thermo Scientific OptaMax Plus Ion Source, which can deliver higher vaporizer temperatures to improve desolvation and ionization potentials.</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/725;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_Opta_Max_c303cf500a.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys OptaMax" width="1290" height="725"></figure><div><div id="container-d79c3b2946"><div><div><div id="text-251514658"><h5><strong>Spend less time on instrument set-up and focus on the science</strong></h5></div></div><div><div id="text-989104128"><p>Trigger on-demand or scheduled system calibrations remotely and without disruption to your LC-MS system with the integrated Auto-Ready ion source.</p></div></div></div></div></div><div><div id="container-81dd07c9bb"><div><div><div id="text-1289282711"><h5><strong>Improve ion utilization by extending the capabilities of the new collision cell</strong></h5></div></div><div><div id="text-1641484825"><p>The ion concentrating routing multipole (ICRM) is a curved collision cell performing both beam-type fragmentation (HCD) and precursor/product ion accumulation capabilities as controlled by dynamic automatic gain control (AGC) with synchronized ion packet release to the high-pressure linear ion trap for downstream manipulation or detection.</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/725;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_ICRM_3b2326f3af.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys ICRM" width="1290" height="725"></figure><div><div id="container-dbf5a6cdd9"><div><div><div id="text-813962034"><h5><strong>Efficiently manage ion populations for fast and sensitive analysis</strong></h5></div></div><div><div id="text-2033771024"><p>The&nbsp;hyper-fast dual-pressure linear ion trap mass analyzer expands analytical capabilities while maximizing fast, high-quality data acquisition.</p><p>The differential neutral pressures maintained in the high- and low-pressure linear ion traps prepares ions for higher-order manipulation or fast and sensitive ion ejection at scan rates up to 220 kDa/S, but typically operates at 125 kDa/S for robust data acquisition.</p></div></div></div></div></div><div><div id="container-9a523f34e0"><div><div><div id="text-1491120095"><h5><strong>Extended analytical capabilities to increase laboratory productivity</strong></h5></div></div><div><div id="text-328051555"><p>The high-pressure linear ion trap maximizes ion packet manipulation enabling multi-notch RF excitation for dissociation or ejection for SIM, higher order MS<sup>n</sup>, SPS MS<sup>3</sup>, or data-independent acquisition (DIA) to address the most challenging quantitative experiments.&nbsp;</p><div><div id="container-82e5907416"><div><div><div id="text-693866740"><h5><strong>Leverage single ion detection sensitivity to address the most challenging quantitation demands</strong></h5></div></div><div><div id="text-737565098"><p>Efficient and sensitive ion detection drives improved quantitative performance at scale. The dual conversion dynode configuration coupled to the photomultiplier tube detects ca. 84% of trapped ions for single ion sensitivity.</p></div></div></div></div></div></div></div></div></div></div><figure class="image"><img style="aspect-ratio:2048/1152;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_hmotnostni_spektrometr_SF_Sys_Extended_Scale_750dc20128.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys Extended Scale" width="2048" height="1152"></figure><div><div id="text-1993749933"><h5><strong>Automated intelligence manages tMSn acquisition</strong></h5></div></div><div><div id="text-1206797739"><p>Streamline tMSn method creation and data acquisition management. PRM Conductor software effectively and efficiently creates robust targeted quantitative methods and manages reproducible data acquisition and processing.</p></div></div><div><div id="container-b03b606507"><div><div><div id="text-2005266584"><h5><strong>Maximize data completeness with the Adaptive RT routine</strong></h5></div></div><div><div id="text-671832198"><p>Eliminate the cost and time of optimizing RT kits to the study samples to boost timed/scheduled data acquisition performance using the Adaptive RT routine.</p><p>The method leverages a novel real-time mapping routine to dynamically adjust timed/scheduled data acquisition windows at narrower time intervals to eliminate missing values that compromise data quality.&nbsp;</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/654;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_PRM_Conductor_5b596e7e4c.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys PRM Conductor" width="1290" height="654"></figure><div><div id="container-a192ba4b83"><div><div><div id="container-38d4c699d2"><div><div><div id="text-1578189934"><h5><strong>Industry-leading polarity switching speeds increase laboratory productivity</strong></h5></div></div><div><div id="text-1173595596"><p>Reduce the time, cost, and challenges associated with creating and implementing highly multiplexed quantitative metabolite analysis. Fast polarity switching speeds enable comprehensive compound interrogation in +ESI and -ESI at all MS<sup>n</sup> levels on an LC timescale.</p><div><div id="container-b5fb525888"><div><div><div id="text-18006314"><h5><strong>Environmentally friendly dry pumps decrease energy usage and maintenance</strong></h5></div></div><div><div id="text-1704557304"><p>Changing from two oil-based fore pumps to a single dry pump reduces heat output by 22% and decreases maintenance.</p><p>The use of a single dry pump also eliminates oil vapors and the need for oil checks and changes.</p><h3><strong>Solutions for additional research support</strong></h3><div><h4><strong>Translational proteomics</strong></h4><p>The Stellar Mass Spectrometer offers new possibilities for translational proteomics with improved specificity for greater quantitative performance at scale.</p><h4><strong>Quantitative proteomics</strong></h4><p>Accurate and precise quantitation for label-free and TMT multiplexing sample analysis strategies with the Stellar Mass Spectrometer.</p><div><h4><strong>Metabolomics and Lipidomics</strong></h4><p>Extended analytical capabilities quantify more metabolites and lipids with greater specificity using faster liquid chromatography gradients to increase laboratory productivity.</p></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div>

Quantitative analysis of proteins (Bioanalytic) 

In our laboratory, proteomic analyses, including quantitative analysis of proteins, are performed by HPLC-MS or HPLC-MS/MS methods on a ZenoTOF 7600 high-resolution mass spectrometer (SCIEX).

<p><strong>Quantitative analysis of proteins is important in many industries and applications. Proteins include a diverse group of compounds that participate in virtually every biological process. Proteins are building blocks, hormones, transport molecules, cell receptors, cell growth and differentiation factors. Because of this, the analysis of protein interactions is crucial in drug design and production.</strong></p><p>Proteins are macromolecules - the basis of their structure are polypeptide chains containing from 100 to more than 10000 amino acids (10 - 100 kDa). Proteins are found in simple and complex forms. Complex proteins contain a non-protein component (sugar, lipids, metal ions or dyes) in their structure.</p><p>In our laboratory, proteomic analyses, including quantitative analysis of proteins, are performed by HPLC-MS or HPLC-MS/MS methods on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=ZenoTOF+7600"><strong>ZenoTOF 7600</strong></a> high-resolution mass spectrometer (SCIEX). We process the obtained results using Sciex OS, Spectronaut, Skyline software.</p><h4><strong>MS vs MS/MS</strong></h4><p>Quantitative analysis of intact protein (whole protein in intact form) leads to the concentration (determined from a prepared curve from a standard (with or without matrix) and confirmation of the identification by superimposing (on a mirrored basis) the MS spectrum of the protein determined in the sample to the MS spectrum of the standard. For your needs, we can generate a list of protein-structured compounds (impurities) that were identified in the sample and determine the ratio of their signal area to the signal area of the analyzed protein.</p><p>The result of proteomic quantitative peptide analysis allows precise and much more sensitive determination of protein concentration. The analysis is based on MS/MS data obtained for peptides obtained by digestion with proteolytic enzymes. The reported result consists of the concentration of the protein under study and confirmation of its presence based on the determined amino acid sequence. For such analyses, it is recommended to add standards internal standards.</p><blockquote><p><span style="font-size:22px;"><strong>Our offer:</strong></span></p><ul><li>For proteins and peptides with low masses - intact analysis with MS detection;</li><li>Proteins with masses &gt;20kDa require optimization of the digestion method and MS/MS detection. This results in specific signals from the analyzed protein in the mixture/matrix;</li><li>From complex matrices (including serum, cell culture, fungal suspension), sample analysis involves several steps:&nbsp;<ul><li>Sample purification;</li><li>Digestion to obtain unique peptides to distinguish the analyzed proteins from other proteins in the sample;</li><li>Sample preparation requires appropriate method optimization and validation (let's set validation criteria individually);</li></ul></li><li>Reported quantitative result includes confirmation of the presence of the protein in native form or a peptide derived from it (usually confirmation includes at least two peptide sequences);</li><li>Statistical analysis using tools: MarkerView (PCA), GraphPad Prism, Trends, Sciex OS.</li></ul><p><i>To optimize and validate the method, it is necessary to provide a standard, in the case of proteins with high masses - it is recommended to add an internal standard.</i></p><p>See also:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/"><strong>Protein identification</strong></a><strong>,</strong></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296"><strong>Analysis and characterization of monoclonal antibodies</strong></a><strong>.</strong></li></ul></blockquote><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Quantitative_analysis_of_proteins_1_de494646f2.jpg" alt="Bioanalytic: Quantitative analysis of proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Quantitative_analysis_of_proteins_1_de494646f2.jpg 200w," sizes="100vw" width="777" height="606"></p>

Identification of the substance – what is in your sample? (Bioanalytic)

We are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.

<h4><strong>Substance Identification - Looking for answers to what's in your sample? - we can help you.</strong></h4><p>Substance identification based on LC-MS/MS techniques can involve single compounds or mixtures of substances. In our analyses, we rely primarily on the knowledge and skills we have acquired after many years of work. For analysis, we use full laboratory facilities for sample preparation and high-resolution mass spectrometry (<a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/o-nas/">equipment</a>).</p><p>We use different work algorithms depending on the material we are dealing with and the analytical task to be solved. We use DDA (IDA) or DIA (SWATH) methods or targeted approaches (e.g. MRMhr) if we know what to expect. Thus, we are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg 245w," sizes="100vw" width="1881" height="1156"></p><h4><strong>COST OF SERVICE</strong></h4><p>We determine the cost of the service individually. The final cost is influenced by many factors related to the nature of the sample itself and the client's expectations. Thus, the price depends, among other things, on the complexity of the sample preparation procedure, the scope and number of analyses, etc.</p><p><strong>The service includes (depending on individual arrangements):</strong></p><h5><strong>Development of sample preparation procedure</strong></h5><ul><li>Depending on the matrix and test substances.</li></ul><h5><strong>Development of analytical methods</strong></h5><ul><li>Application of high-resolution LC-MS/MS analyses using DDA (IDA) or DIA (SWATH) experiments and software to support the development of targeted screening methods.</li></ul><h5><strong>Analysis of results includes:</strong></h5><ul><li>finding and identifying the substances of interest, interpreting MS/MS spectra and proposing a structural formula.</li><li>Comparative analysis of sample series, e.g. PCA,</li><li>profiling of analytes in sample series</li></ul><h5><strong>Reporting of results</strong></h5><ul><li>Compile results into easy-to-read reports.</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg 245w," sizes="100vw" width="1919" height="1208"></p>

Characteristics of monoclonal antibodies (Bioanalytic)

At LabExperts, proteomic analyses are performed on a ZenoTOF 7600 high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation.

<p><strong>Antibodies are molecules made up of 4 polypeptide chains: two heavy (H - high-chain) linked to each other by a specific type of chemical bond - a disulfide bridge, and two light (L - light-chain) linked by an identical bond to the heavy chains. Monoclonal antibodies (mABs) are used in various forms - as free molecules, in the form of a drug-antibody combination, and in the form of an immunoconjugate, a drug-antibody-biopolymer combination.</strong></p><p>Their main use is in highly specific targeted therapy for cancer, cardiovascular, autoimmune and nervous system diseases. They are also used in the treatment of osteoporosis, Alzheimer's disease or transplantation. The range of applications of monoclonal antibodies is systematically expanded. The introduction of a new antibody to the market requires complex product characterization, which involves numerous proteomic analyses, which are performed by LC-MS/MS techniques, among others.</p><h4><strong>LC-MS/MS</strong></h4><p>The characterization of monoclonal antibodies involves many aspects, including, but not limited to, a suite of analyses related to confirmation of the structure, chain sequence and degree of modification of the antibody. Post-translational modifications (PTMs) are chemical changes that occur after the translation process. These changes generally result in an increase in the immunogenicity of the drug. For this reason, it is essential to monitor modifications as critical quality attributes (CQAs) during both the production and storage of the drug. To ensure monitoring of CQA points, the primary structure of the protein is characterized based on peptide mapping (peptide mapping) analysis. The protein under study is subjected to proteolytic digestion using enzymes such as trypsin, chymotrypsin, Lys-C, Glu-C. As a result of various proteolytic enzymes, a wide range of peptides is obtained. Ultimately, coverage of the entire sequence of the protein under study is obtained.</p><figure class="image"><img style="aspect-ratio:1536/947;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg" alt="Bioanalytic: Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg 245w," sizes="100vw" width="1536" height="947"></figure><p>At LabExperts, proteomic analyses are performed on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=ZenoTOF+7600"><strong>ZenoTOF 7600</strong></a> high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation. This provides us with data for unambiguous identification of protein-building amino acids. We process the results using Sciex OS, Skyline and Spectronaut software.</p><blockquote><p><span style="font-size:22px;"><strong>We perform:</strong></span></p><ul><li>Whole protein analyses - Intact - to determine the exact mass and confirm the theoretical mass;</li><li>N-glycosylation profile determination (based on MS spectrum reconstruction):<ul><li>Glycosylated form;</li><li>Deglycosylated;</li><li>Glycosylated with reduced disulfide bridges;</li><li>Deglycosylated with reduced disulfide bridges.</li></ul></li><li>Peptide maps:<ul><li>Protein digestion with various proteases so that sequence coverage is close to 100%<ul><li>Analysis of PTMs:</li><li>Location of modifications</li></ul></li><li>[%] of modifications compared to the unmodified sequence</li></ul></li><li>TiPOS testing - (technical proof of similarity) - technical confirmation of the similarity of the protein synthesized by the customer (from several LOTs) with the target protein (provided as a template).</li></ul><p>In order to maintain the highest possible analytical standards, we perform monoclonal antibody analyses under the regime of an internally developed and implemented laboratory quality system based on GLP principles.</p><p>See also our other proteomics services: <a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/"><strong>Protein identification</strong></a>, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294"><strong>Protein quantitative analysis</strong></a></p></blockquote><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg 245w," sizes="100vw" width="1536" height="908"></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg 245w," sizes="100vw" width="1536" height="858"></p>

Analysis of Anabolic steroids (Bioanalytic)

We offer a highly specific and sensitive qualitative analysis of a wide profile of anabolics by LC-HR-MS/MS technique (detection limits range from 0.01 to 5 ng/ml, depending on the substance).

<h4><strong>Anabolic substances in urine</strong></h4><p>The effect of anabolic steroids (<a target="_blank" rel="noopener noreferrer" href="https://en.wikipedia.org/wiki/Anabolic_steroid"><strong>more information</strong></a>) is to stimulate the growth of muscle mass and sometimes also bone mass by stimulating protein synthesis or altering calcium metabolism. This effect is often used in sports doping. However, anabolic steroids also have many side effects, as they strongly affect the body's overall hormonal balance.</p><p>Anabolic steroids used by purely recreational athletes are still not banned in most countries, including Poland. Nevertheless, their amateur use during adolescence often results in the inability to continue a professional sports career into adulthood or leads to hormonal imbalances in the body.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_1_46fa2f41ca.jpg" alt="Bioanalytic: Analysis of Anabolic steroids." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_1_46fa2f41ca.jpg 245w," sizes="100vw" width="1200" height="740"></p><p>If you want to know whether and which anabolic substances are present in the samples of athletes, or you want to exclude doping in this area - use the offer carried out by us together with the company <a target="_blank" rel="noopener noreferrer" href="http://www.lab4tox.pl/"><strong>Lab4Tox</strong></a>. We offer a highly specific and sensitive qualitative analysis of a wide profile of anabolics by LC-HR-MS/MS technique (detection limits range from 0.01 to 5 ng/ml, depending on the substance). The use of high-resolution mass spectrometry (HR-MS and HR-MS/MS) in the analysis of anabolic steroids makes it possible to unequivocally confirm or exclude the presence of a given compound. The list of compounds at present includes:</p><ul><li><span class="ts-list-li-content">Boldenone undecylenate</span></li><li><span class="ts-list-li-content">Turinabol</span></li><li><span class="ts-list-li-content">Drostanolone enanthate</span></li><li><span class="ts-list-li-content">Drostanolone propionate</span></li><li><span class="ts-list-li-content">Methandienone</span></li><li><span class="ts-list-li-content">Methenolone acetate</span></li><li><span class="ts-list-li-content">Methenolone enanthate</span></li><li><span class="ts-list-li-content">Nandrolone phenylpropionate</span></li><li><span class="ts-list-li-content">Oxandrolone</span></li><li><span class="ts-list-li-content">Oxymetholone</span></li><li><span class="ts-list-li-content">Stanozolol</span></li><li><span class="ts-list-li-content">5-alpha-DHT</span></li><li><span class="ts-list-li-content">6-beta-hydroxymethandienone</span></li><li><span class="ts-list-li-content">19-norandrosterone</span></li><li><span class="ts-list-li-content">3'-hydroxystanazolol</span></li><li><span class="ts-list-li-content">4-beta-hydrozystanazolol</span></li><li><span class="ts-list-li-content">17-alpha-trenbolone</span></li><li><span class="ts-list-li-content">Testosterone caproate</span></li><li><span class="ts-list-li-content">Testosterone cypionate</span></li><li><span class="ts-list-li-content">Testosterone decanoate</span></li><li><span class="ts-list-li-content">Testosterone enanthate</span></li><li><span class="ts-list-li-content">Testosterone isocaproate</span></li><li><span class="ts-list-li-content">Testosterone phenylpropionate</span></li><li><span class="ts-list-li-content">Testosterone propionate</span></li><li><span class="ts-list-li-content">Testosterone undecanoate</span></li><li><span class="ts-list-li-content">Trenbolone acetate</span></li><li><span class="ts-list-li-content">Testosterone</span></li><li><span class="ts-list-li-content">Epitestosterone</span></li></ul><p><span class="ts-list-li-content">The list of compounds is not complete and will be systematically expanded according to customer needs.</span></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg" alt="Bioanalytic: Analysis of Anabolic steroids is carried out by us together with the company Lab4Tox." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg 245w," sizes="100vw" width="625" height="100"></p><p><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=54&amp;distributorItems=315"><span class="ts-list-li-content"><strong>Other analytical methods we offer</strong></span></a><span class="ts-list-li-content">.</span></p>

Identification of the proteins (Bioanalytic)

We perform proteomic analyses on a state-of-the-art high-resolution ZenoTOF 7600 (SCIEX), in which the Zeno ion trap and EAD (Electron-Activated Dissociation) technology together make a powerful combination.

<p><strong>Protein identification is based on experimental measurement of peptide molecular weights and matching the amino acid sequence of the protein under study with protein sequences deposited in libraries (databases). Two approaches are most commonly used in proteomic studies: top-down and bottom-up. The top-down method involves analyzing full protein sequences. Bottom-up analyses, on the other hand, use digestion of proteins with proteolytic enzymes. The peptides obtained by digestion are analyzed using a mass spectrometer. Each analysis leads to a comparison of experimental data with data obtained by theoretical digestion of proteins described in the database.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg 245w," sizes="100vw" width="1536" height="766"></p><h4><strong>LC-MS/MS</strong></h4><p>Tandem mass spectrometers are commonly used to determine protein sequences. They allow ion selection of pseudomolecular peptides and then fragmentation and measurement of the masses of the resulting fragments. Fragmentation using <i>collision induced dissociation</i>(CID ) is an invaluable tool in targeted and untargeted MS/MS analysis of small molecules. It is important to note that in proteomic analysis, data obtained using the aforementioned fragmentation method may leave gaps. For example, spectra obtained by CID fragmentation do not allow unambiguous differentiation of some amino acids: leucine from isoleucine (identical molar masses and CID fragmentation) and lysine from glutamine (very similar masses). For this reason, we perform proteomic analyses on a state-of-the-art high-resolution <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=+ZenoTOF+7600"><strong>ZenoTOF 7600</strong></a> (SCIEX), in which the Zeno ion trap and EAD (<i>Electron-Activated Dissociation</i>) technology together make a powerful combination. It enables the creation of unique fragments to differentiate problematic amino acids and increase the sensitivity and specificity of the analysis.</p><blockquote><p><span style="font-size:22px;"><strong>We perform analyses of:</strong></span></p><ul><li>samples from solution;</li><li>samples from a gel;</li><li>samples from a complex matrix (by prior arrangement);</li><li>samples from lyophilizer;</li><li>samples previously prepared by the client.</li></ul><p>Qualitative analysis of proteins includes:</p><ul><li>To confirm the presence of a protein, the sample is subjected to digestion and the result obtained from experimental data is compared with theoretical data;</li><li>Comparison of experimental data on the masses of peptides included in the analyzed protein with the protein sequences described in the database;</li><li>Analysis and identification of the protein mixture;</li><li>Identification of post translational modifications (PTMs) (we use the tools: Skyline, Spectronaut).</li><li>Reporting of the result including, but not limited to, confirmation of the coverage of the protein sequence obtained in the test sample with the theoretical protein and the list of modified peptides, location and % of modifications.</li></ul><p><span style="font-size:22px;"><strong>Comparative analyses include:</strong></span></p><ul><li>Determining the composition of mixtures;</li><li>Comparison and profiling of sample series - protein identification and trend analysis.</li></ul><p><span style="font-size:22px;"><strong>Our offer also includes</strong>:</span></p><ul><li>Support in the planning and execution of studies (the scope is determined individually);</li><li>Assistance in the development of extraction methods from complex matrices - biological fluids, plant tissue, animal tissues (the scope is determined individually);</li><li>Statistical analysis using tools: MarkerView (PCA), GraphPad Prism, Trends, Sciex OS;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294"><strong>Quantitative analysis of proteins</strong></a>;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296"><strong>Analysis and characterization of monoclonal antibodies</strong></a>.</li></ul></blockquote><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg 117w," sizes="100vw" width="1500" height="2000"></p>

Bioanalytic QTOF quantitative and qualitative analysis training

The purpose of the training is to introduce users to the capabilities of the LC-HR-MS/MS (QTOF) system in quantitative and qualitative analysis.

<h4><strong>BASIC INFORMATION</strong></h4><ul><li>TITLE:&nbsp;<strong> QTOF quantitative and qualitative analysis training</strong></li><li>CATEGORY: <strong>LC-MS/MS training</strong></li><li>LOCATION: <strong>Lodz, PL</strong></li><li>TRAINING TIME: <strong>3 days</strong></li><li>NUMBER OF PARTICIPANTS: <strong>up to 5 people</strong></li><li>EQUIPMENT:<strong> SCIEX</strong><span class="ts-pf-details-content"><strong> </strong></span><strong>QTOF LC-MS/MS</strong></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_QTOF_quantitative_and_qualitative_analysis_training_af1620ae8c.jpg" alt="Bioanalytic: Bioanalytic QTOF quantitative and qualitative analysis training." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_QTOF_quantitative_and_qualitative_analysis_training_af1620ae8c.jpg 221w," sizes="100vw" width="1000" height="707"></p><h4><strong>TRAINING COURSE DESCRIPTION</strong></h4><p><strong>Qualitative and quantitative analysis of QTOF</strong> - the training is designed for laboratory personnel using <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?instrumentationItems=30&amp;mainauthorItems=55"><strong>high-resolution (HR) LC-MS/MS</strong></a> systems for qualitative and quantitative analysis. The following topics are covered during the training:</p><ul><li><strong>QTOF spectrometer calibration</strong></li><li><strong>Targeted and untargeted methods</strong></li><li><strong>Quantitative analysis (TOF MS, MRMhr)</strong></li><li><strong>Qualitative and quantitative analysis - DDA (IDA) vs DIA (SWATH) methodology</strong></li><li><strong>Software and its use in high-resolution data analysis</strong></li><li><strong>Reporting of results</strong></li></ul><p>The purpose of the training is to introduce users to the capabilities of the LC-HR-MS/MS (QTOF) system in quantitative and qualitative analysis. To point out the advantages of high resolution in identifying or confirming the presence of substances in a sample and also the strengths of modern QTOF systems in parallel quantitative analysis.</p><h3><strong>Training program</strong></h3><h4><span style="font-size:20px;"><strong>Day I</strong></span></h4><h5><strong>Theoretical part</strong></h5><ul><li>The principle of operation and capabilities of the QTOF system</li><li>Comparison of typical analytical procedures and their application</li><li>Targeted and quantitative analysis (TOF MS vs MRMhr)</li><li>DDA (IDA) vs DIA (SWATH) methodology.</li><li>Supporting software - Molecule Profiler, ACD Labs, MarkerView</li><li>General principles of compound fragmentation</li></ul><h4><span style="font-size:20px;"><strong>Day II</strong></span></h4><p><strong>Objective</strong> - to develop methods for quantitative analysis, confirmation or search for metabolites of a known substance, general characterization of the sample.</p><h5><strong>Practical part:</strong></h5><ul><li>Creation and optimization of the MRMhr targeted method</li><li>Creation and optimization of a non-targeted method IDA</li><li>Creation and optimization of the non-targeted method SWATH</li><li>Data acquisition (overnight)</li></ul><h4><span style="font-size:20px;"><strong>Day III</strong></span></h4><p><strong>Objective</strong> - quantitative analysis, confirmation of the presence or identification of metabolites of a known substance, general characterization of the sample (identification of compounds present in the sample), profiling.</p><h5><strong>Practical part:</strong></h5><ul><li>Quantitative analysis - TOF MS vs MRMhr</li><li>Methods for searching and analyzing data</li><li>IDA vs SWATH data</li><li>Manual search and identification</li><li>Automated search and identification - SciexOS, databases</li><li>Molecule Profiler, MarkerView</li><li>Summary and discussion</li></ul>

Thermo Scientific Orbitrap Exploris MX Mass Detector

Accelerate biopharmaceutical late-stage development, commercialization, manufacturing, and quality control (QC) by easily and reliably obtaining compliance-ready, high-quality mass information. 

<p><strong>Accelerate biopharmaceutical late-stage development, commercialization, manufacturing, and quality control (QC) by easily and reliably obtaining compliance-ready, high-quality mass information.&nbsp;</strong></p><p>The <strong>Thermo Scientific Orbitrap Exploris MX mass detector</strong> is the perfect fit for deploying routine mass monitoring.</p><p>In addition to high-resolution mass detection provided by Thermo Scientific Orbitrap mass analyzers, this fit for purpose system is simple to operate and compliance ready with <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/cz/en/home/industrial/chromatography/chromatography-learning-center/chromeleon-cds-information/cds-mass-spectrometry-software.html">Thermo Scientific Chromeleon chromatography data system (CDS) software</a>. Consistent performance between the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/402">Thermo Scientific Orbitrap Exploris 240 mass spectrometer</a> and Orbitrap Exploris MX detector ensures seamless method transfer from development to QC.</p><h4><strong>High-resolution accurate-mass (HRAM) data provide utmost confidence for:</strong></h4><ul><li>Sequence confirmation</li><li>Peptide monitoring</li><li>Intact protein analysis (from small to large molecules, reduced mAbs, and intact mAbs under native and denaturing conditions)</li><li>Glycan profiling</li><li>Oligonucleotide and oligonucleotide impurity mass confirmation</li></ul><h3><strong>Highlights of Orbitrap Exploris MX mass detector&nbsp;</strong></h3><div colctrl-id="5-1"><div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><h4><strong>Simplicity for scientists and technicians</strong></h4><p>Simplify tasks and reduce errors for more ‘right first time’ analyses with Chromeleon CDS, with built in methods, control, data processing, and management. The suite of smart tools makes your work faster and easier, while ensuring reproducible, high-quality mass monitoring.</p></div></div></div><div><div container-id="cq-colctrl-lt0" comp-id="B1"><div><h4><strong>Accelerate productivity</strong></h4><p>High uptime boosts productivity. Rapid “set and forget” calibration procedures provide consistent mass stability for at least four weeks at prescribed conditions. Instrument status monitoring and optimized pressure control alert users when maintenance is needed, avoiding unnecessary downtime and repeat analyses.</p></div></div></div></div><div colctrl-id="6-1"><div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><h4><strong>Compliance for competitive advantage</strong></h4><p>Designed for data integrity, data security, and compliance, fully scalable Chromeleon CDS provides comprehensive technical controls to give you a competitive edge in meeting global regulatory requirements.</p></div></div></div><div><div container-id="cq-colctrl-lt0" comp-id="B1"><div><h4><strong>Consistent results deliver confidence</strong></h4><p>Robust and reliable performance from system to system and site to site ensure confidence in results used to make critical decisions. Industry-proven Orbitrap technology, now purposely designed for mass monitoring in future-proof lab operations.</p></div></div></div></div><div colctrl-id="7-1"><div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><h4><strong>Seamless method transfer to MAM</strong></h4><p>Easy transfer of sophisticated Multi-Attribute Method (MAM) assays from development to manufacturing bridges the gap between development and QC.</p></div></div></div><div><div container-id="cq-colctrl-lt0" comp-id="B1"><div><h4><strong>Dedicated, global support team</strong></h4><p>The dedicated, global Thermo Scientific MAM team maximizes your productivity and confidence with installation, training, and fast service and support. Standardized system performance evaluation test (SET) and installation qualification/operational qualification (IQ/OA) thoroughly assess system performance with comprehensive installation and post-maintenance acceptance criteria.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Scientific_Orbitrap_Exploris_MX_Mass_Detector_4_2ad72d9b21.jpg" alt="Orbitrap Exploris MX mass stability: mass deviation relative to first observed mass in parts-per-million for 9 BSA tryptic peptides monitored over a period of 6 weeks using the new internal recalibration option. Each data point is an average of 19 individual injections." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Scientific_Orbitrap_Exploris_MX_Mass_Detector_4_2ad72d9b21.jpg 184w," sizes="100vw" width="1240" height="1052"></p><h3><strong>Accelerate MAM deployment&nbsp;</strong></h3><h4><strong>Seamless knowledge and method transfer</strong></h4><p>Benefit from the end-to-end Thermo Scientific MAM 2.0 workflow approach to comprehensive characterization and monitoring of biotherapeutics from development to commercialization. <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/402">Orbitrap Exploris 240</a> mass spectrometer methods, established during development, seamlessly transfer to the Orbitrap Exploris MX detector in manufacturing or by contract partners. In addition to full integration into the high-resolution MAM 2.0 workflow, the usability and low cost of the Orbitrap Exploris MX detector make it the perfect fit for high-throughput QC and contract labs.</p><p>Users can identify and evaluate relevant product quality attributes (PQAs) via high-throughput analytics provided by Thermo Scientific BioPharma Finder software. Connected labs can access data from development through QC using MAM 2.0 powered by Thermo Scientific Ardia Platform. And, PQAs can be monitored throughout the entire drug development process using the MAM target peptide workbook built from the list of identified peptides upon incorporation into a Chromeleon processing method. The processing method along with the instrument method, injection sequence, view setting and report template can be stored into a MAM eWorkflow for easy and direct transfer to QC via Chromeleon CDS Enterprise software.</p><div><h5><strong>MAM 2.0 offers:</strong></h5><ul><li>Fast decision making based on high-confidence PQAs obtained using industry-leading HRAM Orbitrap technology</li><li>Seamless knowledge and method transfer across instruments, departments, and sites using compliance-ready, Chromeleon CDS enterprise software, and Ardia Platform</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Scientific_Orbitrap_Exploris_MX_Mass_Detector_cd7474e7ed.jpg" alt="Thermo Scientific Orbitrap Exploris MX Mass Detector" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Scientific_Orbitrap_Exploris_MX_Mass_Detector_cd7474e7ed.jpg 245w," sizes="100vw" width="1170" height="504"></p><blockquote><p><strong>Thermo Scientific MAM 2.0</strong></p><p>The end-to-end MAM solution for a fully connected, compliance-ready platform. MAM 2.0 includes everything you need to bring your next biotherapeutic candidate straight through to breakthrough.</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/cz/en/home/industrial/pharma-biopharma/biopharmaceutical-analytical-testing/multi-attribute-method.html"><strong>Learn more</strong></a></li></ul></blockquote></div></div></div></div></div>

Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer

Be ready for tomorrow’s most challenging demands. Exceed experimental expectation with the MultiOmics, Structural Biology, and BioPharma Editions of the Thermo Scientific Orbitrap Ascend Editions Tribrid Mass Spectrometer.

<p><strong>Exceed experimental expectation with the MultiOmics, Structural Biology, and BioPharma Editions of the Thermo Scientific Orbitrap Ascend Editions Tribrid Mass Spectrometer.</strong></p><p><strong>With new capabilities for multiplexed quantitative proteomics, native protein characterization, and deep biopharmaceutical analyses, the three new Editions deliver ultimate experimental throughput, versatility, and ease-of-use for your specific needs.</strong></p><p>Detect and characterize the most difficult protein complexes and native samples without losing low <i>m/z</i> instrument performance and flexibility with the new Native MS option, including world class Orbitrap detection up to <i>m/z</i> 16,000 and ion isolation in the ion trap and quadrupole up to <i>m/z</i> 8,000, with isolation widths down to <i>m/z</i> 100 and <i>m/z</i> 5, respectively.</p><figure class="image"><img style="aspect-ratio:1937/796;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Scientific_Orbitrap_Ascend_Tribrid_hmotnostni_spektrometr_3_03576fcf9a/Thermo-Scientific-Orbitrap-Ascend-Tribrid-hmotnostni-spektrometr_3.jpg" alt="Thermo Fisher Scientific: Key innovations for Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer" width="1937" height="796"></figure><h3><strong>Orbitrap Ascend Editions Tribrid MS</strong></h3><div><ul><li><strong>Orbitrap Ascend MultiOmics Tribrid MS: </strong>Discover more from comprehensive metabolomics to proteomics.</li><li><strong>Orbitrap Ascend Structural Biology Tribrid MS:</strong> Take advantage of ultimate versatility for native protein characterization.</li><li><strong>Orbitrap Ascend BioPharma Tribrid MS: </strong>Successfully characterize your most complex biotherapeutics.</li></ul><div><h3><strong>Introducing the Orbitrap Ascend Editions Tribrid MS</strong></h3></div><div><div><div id="container-deb530bb93"><div><div><div id="container-fffbeb2334"><div><div><div id="text-1451003751"><p>Eliminate the guesswork from your purchase decision with the MultiOmics, BioPharma, and Structural Biology Editions of the Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer.&nbsp;Simplify your decisions and streamline your research with a tailored configuration for your unique application space.</p><p>Employ cutting edge native structural and biopharmaceutical analyses with multiple fragmentation and ion manipulation techniques. With the new Native MS option, detect protein complexes up to <i>m/z</i> 16,000 in the Orbitrap mass analyzer and isolate proteoforms&nbsp;up to <i>m/z</i> 8,000 with an isolation width as low as <i>m/z</i> 5 in the quadrupole.</p><p>Quantify more peptides, identify more proteins, confidently assign more labile-PTMs, and discover more previously undetectable protein complexes. Characterize proteoforms and modified compounds with more precision than ever before.&nbsp;</p></div></div></div></div></div></div></div></div></div><h3><strong>System highlights</strong></h3><h5><strong>Spend less time on instrument set-up and focus on your science</strong></h5><p>With the integrated Auto-Ready ion source, trigger on-demand or scheduled system calibrations remotely and without disruption to your LC-MS system.</p><h5><strong>Gain increased characterization from lipids to intact proteins to oligonucleotides with orthogonal fragmentation &nbsp;</strong></h5><p>The Orbitrap Ascend Editions mass spectrometers have multiple fragmentation techniques that provide complementary information.</p><ul><li>Standard collision-induced dissociation (CID) and higher-energy collisional dissociation (HCD) can be used for multiple analytes.</li><li>Optional electron transfer dissociation (ETD) increases coverage for proteins and glycopeptide experiments, and ultraviolet photodissociation (UVPD) benefits protein, oligonucleotide, and lipid analysis.</li></ul><h5><strong>Study the largest protein complexes using native MS techniques, all on the same system as bottom-up proteomics techniques</strong></h5><p>The Native MS option comprises the extension of the Orbitrap mass range to m/z 16,000, ion trap ion isolation up to 8,000 with MSn capabilities, and more sensitive and selective extended quadrupole isolation up to m/z 8,000. With the Native MS option, you can detect large protein complexes and characterize the subunits by multiple fragmentation techniques.</p><h5><strong>Environmentally friendly dry pumps decrease energy usage and maintenance</strong></h5><p>By changing the fore pumps from oil-based to a dry pump, we reduce the heat output by 22%. They also eliminate the production of oil vapors and the need for oil checks and changes, lowering maintenance.</p><p>The Orbitrap Ascend Editions mass spectrometers have also received the ACT label, the standard for determining the environmental impact of laboratory products to help labs make informed, sustainable purchasing decisions.</p><h5><strong>Software solutions for your application</strong></h5><p>Streamlined instrument control software across all next-generation Thermo Scientific platforms for ease-of-use through different systems. Edition-specific application templates are ready to use and built into the method editor so you can get meaningful results faster.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Thermo_Scientific_Orbitrap_Ascend_Tribrid_Mass_Spectrometer_The_most_versatile_platform_for_deep_untargeted_and_accurate_targeted_metabolomics_336c0b833d.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer - The most versatile platform for deep untargeted and accurate targeted metabolomics" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Thermo_Scientific_Orbitrap_Ascend_Tribrid_Mass_Spectrometer_The_most_versatile_platform_for_deep_untargeted_and_accurate_targeted_metabolomics_336c0b833d.jpg 245w," sizes="100vw" width="2349" height="1165"></p><h4><strong>Orbitrap Ascend MultiOmics Tribrid MS</strong></h4><p>Benefit from experimental throughput, versatility, and ease-of-use. With industry leading capabilities, the Thermo Scientific Orbitrap Ascend MultiOmics Tribrid Mass Spectrometer delivers ultimate data quality. Quantify more samples at lower concentrations using intelligent acquisition and faster Real-Time Search.</p><h5><strong>Applications</strong></h5><ul><li>The most versatile platform for deep untargeted and accurate targeted metabolomics</li><li>The most versatile platform for deep untargeted and accurate targeted metabolomics</li><li>The most versatile platform for deep untargeted and accurate targeted metabolomics</li><li>The most versatile platform for deep untargeted and accurate targeted metabolomics</li><li>The most versatile platform for deep untargeted and accurate targeted metabolomics</li><li>Lipidomics experiments benefit from AqcuireX software and alternative fragmentation capabilities</li></ul><h4><strong>Orbitrap Ascend Structural Biology Tribrid MS</strong></h4><div><div id="container-26e6c6fa34"><div><div><div id="text-872767366"><p>Be prepared for tomorrow's challenges in structural analysis with this powerful solution. Achieve greater coverage and explore different ion manipulation options with an expanded <i>m/z</i> range and multiple fragmentation options.</p><ul><li>Characterize complex molecules (Native MS option) with a recommended mass range up to <i>m/z</i> 16,000 and an extended quadrupole isolation range of up to <i>m/z</i> 8,000.</li><li>Take advantage of multiple fragmentation options (ETD, EThcD, UVPD) and Proton-Transfer Charge Reduction to achieve comprehensive sequence coverage of your protein target.</li></ul><h5><strong>Applications</strong></h5><ul><li>Native MS option facilitates the identification of membrane proteins by top-down MS&nbsp;</li><li>Utilizing PTCR for complex mixture analysis enables more identification across the <i>m/z</i> range &nbsp;</li><li>Crosslinking experimentation is aided by Real-Time Library Search available on the Orbitrap Ascend Structural Biology MS&nbsp;&nbsp;</li><li>Comprehensive disulfide bond mapping analysis using FAIMS and EThcD</li><li>Characterize larger proteoforms by top-down proteomics</li><li>Characterize larger proteoforms by top-down proteomics</li><li>Native MS option extends ion detection of large protein complexes</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Thermo_Scientific_Orbitrap_Ascend_Tribrid_Mass_Spectrometer_Lipidomics_experiments_benefit_from_Aqcuire_X_software_and_alternative_fragmentation_capabilities_da54862143.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Orbitrap Ascend Tribrid Mass Spectrometer - Lipidomics experiments benefit from AqcuireX software and alternative fragmentation capabilities" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Thermo_Scientific_Orbitrap_Ascend_Tribrid_Mass_Spectrometer_Lipidomics_experiments_benefit_from_Aqcuire_X_software_and_alternative_fragmentation_capabilities_da54862143.jpg 245w," sizes="100vw" width="3257" height="850"></p><h4><strong>Orbitrap Ascend BioPharma Tribrid MS</strong></h4></div></div></div></div></div><p>Elevate your analytical capabilities and successfully characterize your most complex products from peptides to native protein characterization with the Thermo Scientific Orbitrap Ascend BioPharma Tribrid Mass Spectrometer.&nbsp; Achieve greater coverage for oligonucleotide sequences and analyze even the largest and most complex molecules.</p><ul><li>Recommended alternate fragmentation techniques enable detailed structural elucidation.</li><li>Automated Auto-Ready ion source and application-specific pre-built method templates streamline instrument setup.</li></ul><h5><strong>Applications</strong></h5><ul><li>Comprehensive native analysis of complex therapeutic proteins using Native MS option and PTCR</li><li>Comprehensively characterize antibody-drug conjugates combining orthogonal fragmentation techniques</li><li>Enhanced speed and sensitivity for high sequence coverage and low abundant PTM identifications in peptide mapping experiments</li><li>Improved sensitivity allows highly confident identification of ppb Host Cell Proteins at analytical flow rates</li><li>Characterize intact sgRNA up to 100 base pairs using low-q CID fragmentation</li><li>Unparalleled characterization of low-abundant modifications in oligonucleotides</li></ul><p>&nbsp;</p></div>

Products focused on LC/HRMS - page 2

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