<p><strong>When I think about what it takes to keep a high-performing MS laboratory running—especially those dealing with tight timelines, strict regulations, and ever-expanding datasets—I’m reminded that the software we rely on isn’t just a tool. It’s the backbone of our workflows, our decisions, and ultimately, our results.</strong></p><p>Whether you’re in pharma, environmental testing, or food safety, managing the complexity of targeted mass spectrometry workflows while maintaining accuracy, compliance, and efficiency requires a lot of work.</p><p>That’s where a purpose-built solution makes a difference. I’ve worked closely with labs that are navigating these challenges—and from the many conversations and experiences, I put together five main capabilities you should look for in your software when it comes to targeted MS quantitation:</p><h3><strong>1. Simplified data and workflow management</strong></h3><p>Too many labs are still relying on disconnected systems or folder-based setups that can lead to inconsistent methods and reports. When utilizing modern software solutions, everything—methods, templates, data, reports—can be centrally managed, reducing errors and training time while ensuring everyone is working from the same validated workflows.</p><p>It’s a big plus if the software also supports multi-consensus reporting, making it easy to compare results across sequences and analyses for greater confidence in the data. By packaging complete workflows and setting predefined views, labs can streamline routine operations and ensure method repeatability, so anyone can run the analysis reliably and consistently.</p><h3><strong>2. Controlled access in and out of the lab</strong></h3><p>Many labs are still tied to legacy setups that make remote work challenging. Researchers often rely on standalone workstations that store data locally, making it hard to access critical results when off-site. Transferring data via USB drives or external hard disks not only adds inefficiency, but it can also raise serious security concerns. These outdated practices slow down collaboration and increase the risk of data loss or breaches.</p><p>Hybrid work is here to stay. With the ability to control and access instruments and data, users can securely set up runs, review results, and manage workflows from anywhere. You’re no longer tied to a specific bench, workstation, or even building. Productivity doesn’t have to stop when you step out of the lab.</p><p><i>“Managing all our instruments and work with data remotely via a centralized server means we don’t need to be in the laboratory to access our data.” – Dr. Kayleigh Arthur, Owlstone Medical Ltd.</i></p><h3><strong>3. It’s built for MS workflows</strong></h3><p>Whether you’re running triple quads, high-res accurate mass, or both—life’s much easier when working with software solutions that give you native instrument control and deep integration for targeted workflows. That includes support for MSⁿ, intact mass deconvolution, spectral libraries, and high-throughput quantitation.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_5_Things_to_Consider_When_Selecting_Software_for_Targeted_MS_Quantitation_9e5e9dc842.jpg" alt="Thermo Fisher Scientific: 5 Things to Consider When Selecting Software for Targeted MS Quantitation." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_5_Things_to_Consider_When_Selecting_Software_for_Targeted_MS_Quantitation_9e5e9dc842.jpg 245w," sizes="100vw" width="1536" height="411"></p><p>Just as important is what happens after data acquisition. Integrated, built-in reporting capabilities—paired with customizable reporting options—should make it easy to flag results and automate the necessary calculations, all within the software. You need a powerful combination that can streamline review and ensures consistency across analyses.</p><h3><strong>4. Scalability</strong></h3><p>From small bioanalytical teams to global enterprises, can it be scaled up or down without the need for reinstallation or manual data transfer? It should be built to handle complex, multi-site deployments with ease.</p><p>Add to that network resilience, automated data protection, and centralized updates—and you’ll get a system designed to grow with your organization.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_5_Things_to_Consider_When_Selecting_Software_for_Targeted_MS_Quantitation_2_8ec325678b.jpg" alt="Thermo Fisher Scientific: 5 Things to Consider When Selecting Software for Targeted MS Quantitation." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_5_Things_to_Consider_When_Selecting_Software_for_Targeted_MS_Quantitation_2_8ec325678b.jpg 245w," sizes="100vw" width="1200" height="660"></p><article><div><h3><strong>5. Stress-free compliance</strong></h3><p>Let’s face it, if you have to do it, compliance is non-negotiable, but it can be time-consuming. The system should include built-in features that support GxP, 21 CFR Part 11, and audit readiness—like audit trails, version control, and detailed user management.</p><p>The ability to query and interrogate data within the system would ensure that data integrity requirements are met, delivering full traceability, and verification of data throughout its lifecycle. Your QA team will be very pleased!</p><h3><strong>Conclusion</strong></h3><p>Managing targeted MS quantitation shouldn’t feel like assembling a puzzle with missing pieces. A modern software should bring together everything you need—scalable infrastructure, powerful MS data tools, and built-in compliance features—into one cohesive solution. It must support your science, your team, and your business goals.</p><p>If you’re ready to rethink how your lab handles MS data, this is the right time to explore what’s possible.</p><blockquote><p>Join our <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5232"><strong>upcoming webinar</strong></a> to learn about networked software for MS labs.</p><p><strong>Visit us on&nbsp;</strong><a target="_blank" rel="noopener noreferrer" href="https://www.linkedin.com/showcase/72003132/admin/dashboard/"><strong>LinkedIn:</strong></a>&nbsp;#targetedquantitation #compliance #massspectrometry #control</p></blockquote></div></article><section><blockquote><h4><strong>Laercio Fernandes</strong></h4><p>Laércio Fernandes is a Product Marketing Manager for software at Thermo Fisher Scientific. With a background rooted in analytical chemistry, Laércio has over 20 years of experience in the analytical field with a focus on chromatography instrumentation, enterprise software and compliance. His background in sales and support has enabled him to have a good overview and understanding of different processes and challenges that laboratories may face, which has allowed him to better support our customers in order to improve their workflows and productivity.</p></blockquote></section>

5 Things to Consider When Selecting Software for Targeted MS Quantitation

<p><strong>Our Library never stops expanding. What are the most recent contributions to LabRulezLCMS Library in the week of 7th July 2025? Check out new documents from the field of liquid phase, especially HPLC and LC/MS techniques!</strong></p><blockquote><p><span style="font-size:20px;">👉 </span><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library"><span style="font-size:20px;"><strong>SEARCH THE LARGEST REPOSITORY OF DOCUMENTS ABOUT LCMS AND RELATED TECHNIQUES</strong></span></a></p></blockquote><blockquote><p><strong>👉 Need info about different analytical techniques?</strong> Peek into <a target="_blank" rel="noopener noreferrer" href="https://gcms.labrulez.com/library"><strong>LabRulezGCMS</strong></a> or <a target="_blank" rel="noopener noreferrer" href="https://icpms.labrulez.com/library"><strong>LabRulezICPMS</strong></a> libraries.</p></blockquote><p>This week we bring you application note by <strong>Agilent Technologies </strong>and posters by<strong> Shimadzu / ASMS, Thermo Fisher Scientific / ASMS </strong>and<strong> Waters Corporation / ASMS!</strong></p><h3><strong>1. Agilent Technologies: Rapid and Sensitive Analysis of Antifungal Agents in Human Serum Using the Agilent 6475 LC/TQ</strong></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/an_antifungal_human_serum_5994_8338en_agilent_89f89cb4dc.pdf"><strong>Full PDF for download</strong></a></li></ul><p>In addition to minimizing drug-related toxicity, TDM has been hailed as a key step to prevent the emergence of drug resistance. The growing number of invasive fungal infections creates a ripple effect on the rapid advancement of TDM for antifungal agents. Increasing evidence confirms the critical role of TDM in preventing and treating antifungal infections.1 The RECIPE ClinMass TDM kit system for antimycotics in serum (Munich, Germany) was used on a 6475 LC/TQ for the analysis of eight antifungal agents. This application note demonstrates the evaluation and validation of the RECIPE TDM kit, covering sensitivity, linearity, and robustness across five consecutive days (n =&nbsp;5). Quick and simple sample preparation was implemented, providing high-throughput monitoring of antifungal agents in biological&nbsp;samples.</p><h4><strong>Experimental</strong></h4><h5><strong>Instrumentation</strong></h5><ul><li><strong>Liquid Chromatography System&nbsp;</strong><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=1&amp;search=Agilent+1290+Infinity+II"><strong>Agilent 1290 Infinity II</strong></a> High-Speed Pump&nbsp;</li><li>Agilent 1290 Infinity II Multisampler&nbsp;</li><li>Agilent 1290 Infinity II Multicolumn Thermostat&nbsp;</li></ul></li><li><strong>Mass Spectrometry System&nbsp;</strong><ul><li>Agilent <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=1&amp;search=6475+LC%2FTQ"><strong>6475 LC/TQ &nbsp;</strong></a></li><li>Agilent Jet Stream Technology Ion Source (AJS)</li></ul></li></ul><h5><strong>Method&nbsp;</strong></h5><p>The optimization of multiple reaction monitoring (MRM) transitions for analytes and ISTDs was carried out using Auto MRM Optimizer in the Agilent MassHunter acquisition software to provide optimal sensitivity and selectivity. Data were processed using the Agilent <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=1&amp;search=MassHunter+Qualitative+Analysis+software"><strong>MassHunter Qualitative Analysis software</strong></a>, version B.12, and Agilent <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=1&amp;search=MassHunter+Quantitative+Analysis+software"><strong>MassHunter Quantitative Analysis software</strong></a>, version B.12.</p><h4><strong>Results and discussion&nbsp;</strong></h4><p>Figure 2 shows the chromatograms of quantifier MRM transitions for the eight antifungal agents at the lowest calibration level. Six out of eight antifungal agents had good chromatographic separation across the run time. The retention times of two antifungals, posaconazole and hydroxy-itraconazole, were slightly overlapped. Despite this overlap, measurement integrity can still be maintained due to MRM selectivity.</p><h4><strong>Conclusion&nbsp;</strong></h4><p>A fast and sensitive analysis of eight antifungal agents in serum was validated on an Agilent 6475 triple quadrupole LC/MS. By employing a ready-to-use RECIPE ClinMass TDM kit, this method demonstrates accurate and precise quantitation of antifungal agents in biological samples. Additionally, the streamlined sample preparation method allows high throughput analysis of up to 350 samples per day.</p><h3><strong>2. Shimadzu / ASMS: Robustness Evaluation of PFAS Analysis in Soil Using LC-MS/MS</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/ASMS_25_WP_137_e932b391c7.pdf"><strong>Full PDF for download</strong></a></li></ul><p>Per- and polyfluoroalkyl substances (PFAS) are widely used in various fields and industries. However, due to their structural stability and resistance to degradation, they accumulate in the environment and are suspected of being harmful to humans. PFAS in soil can accumulate in the human body via agricultural products, thus it is essential to develop sensitive and robust analytical methods for the detection of PFAS in soil with complex matrices.1 This study shows a robustness evaluation by adding 30 PFAS to a soil matrix and using the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=3&amp;search=LCMS-8060RX"><strong>LCMS-8060RX</strong></a> to measure these PFAS in the soil matrix 500 consecutive times.</p><h4><strong>Methods&nbsp;</strong></h4><p>For this analysis, LC-MS/MS equipped with a newly designed ESI source was used, and a delay column was installed between the mixer and the autosampler to inhibit the effects of PFAS contamination from the LC system. Six points calibration curves were built, and each calibration point was measured 3 times. A soil sample was prepared referring to part of the soil preparation procedures published by the National Agricultural and Food Research Organization. 2 Thirty PFAS compounds were spiked to the soil sample at 0.1 μg/L after pretreatment and 500 soil sample analyses were performed for the robustness evaluation. This sample contains more than 90% soil matrix. QC samples were also analyzed after every 20 injections of the soil samples.</p><h4><strong>Conclusion</strong></h4><p>The <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=3&amp;search=LCMS-8060RX"><strong>LCMS-8060RX</strong></a> performed 500 consecutive measurements of 30 PFAS spiked to a soil matrix sample. The results showed good peak area repeatability, good peak shapes, and good recovery. The newly designed ESI source showed excellent robustness, and stable analysis was achieved over a long period, even for samples with complex matrices.</p><h3><strong>3. Thermo Fisher Scientific / ASMS: Evaluation of a modified Orbitrap Astral Mass Spectrometer for label-free quantitation of proteomic samples</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/PO_439_ms_ASMS_25_Astral_Zoom_LFQ_po439_na_en_c1a0b2a11e.pdf"><strong>Full PDF for download</strong></a></li></ul><p>The demand for high-throughput proteomics analysis of complex samples is continually increasing, focusing on greater analysis depth and improved precision and accuracy in quantitation. Label-free quantitation of very complex proteomic samples poses significant challenges for mass spectrometers, requiring faster and more efficient processing of eluting peptide ions and their fragments. The new Orbitrap Astral Zoom mass spectrometer addresses these challenges, offering a higher acquisition rate by improved ion optics switching times and faster ion transfer, higher sensitivity due to ion pre-accumulation, and enhanced spectral processing, leading to deeper coverage with higher confidence.</p><h4><strong>Materials and methods</strong></h4><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/398"><strong>Vanquish Neo</strong></a><strong>: Direct injection mode using 25cm x 75 μm ID Aurora Ultimate TS column (IonOpticks)&nbsp;</strong></h5><ul><li>High loads: 37min gradient; 4-45%B and injection-to-injection time 48min (30SPD)&nbsp;</li><li>Low loads: 20min gradient; 1-40%B and injection-to-injection time 28min (50SPD)&nbsp;</li></ul><h5><strong>Mass Spectrometer: </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/836"><strong>Orbitrap Astra</strong></a><strong>l and </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1959"><strong>Orbitrap Astral Zoom&nbsp;</strong></a></h5><ul><li>Orbitrap (MS1) and Astral (MS2) detectors&nbsp;</li><li>Orbitrap: 240K; m/z range 380-980; AGC 500%; max IT 5ms&nbsp;</li><li>NCE 25; Thermo Scientific FAIMS Pro Duo (low loads): -48V; gas 3.5 L/min</li><li>Astral: DIA; window size depending on loads (in the tables below); m/z 150-2000; AGC 800% (low loads) or 100% (high loads); max IT depending on load; cycle time: 0.6s&nbsp;</li></ul><h5><strong>Data Processing&nbsp;</strong></h5><ul><li>Spectronaut® v19.5 Direct DIA, 6 files (2 x 3 replicates) processed together for each load; all other settings were default&nbsp;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1782"><strong>Thermo Scientific Proteome Discoverer software </strong></a>3.3.0.54, CHIMERYS 4.0.21</li><li>Human, E.coli, and Yeast FASTA (all w/o isoforms) from UniProt; normalization by Human FASTA</li></ul><h4><strong>Results (High Loads)</strong></h4><p>The new Orbitrap Astral Zoom mass spectrometer takes advantage of ion preaccumulation in the bent trap, increasing the effective MS2 injection time. Its reduced ion transfer overheads result in a higher MS2 acquisition rate of up to 270 scans per second. Additionally, an enhanced spectral processing algorithm was implemented to deconvolute overlapping spectral features in MS2, for better handling spectra with increased spectrum density.&nbsp;</p><p>Using Orbitrap Astral Zoom MS and Spectronaut® 19.5 software, there was a 12-17% increase in IDs at the precursor level, 10-15% at the peptide level (stripped sequence), and 4-9% at the protein groups level. With Proteome Discoverer software, the gain was 12-19% at the DIA precursor level, 12-17% at the peptide level, and 4-7% at the protein group level. The increase in identifications was primarily observed for low-abundant species. Orbitrap Astral Zoom mass spectrometer also yielded, on average, a 15% higher median number of MS2 data points per peak, while maintaining consistently high quantitation precision and accuracy at the MS2 level.</p><h4><strong>Conclusions</strong></h4><p>The novel Orbitrap Astral Zoom mass spectrometer demonstrates improved performance for qualitative and quantitative analysis of complex proteomics samples over a wide range of sample loads spanning four orders of magnitude, from 100 pg to 1µg.</p><h3><strong>4. Waters Corporation / ASMS: Investigating Fire Fighter and E-waste Handlers Exposure to PFAS Using Liquid Chromatography and Cyclic Ion Mobility Mass Spectrometry</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/720008883_21620a6293.pdf"><strong>Full PDF for download</strong></a></li></ul><p>PFAS are persistent environmental pollutants linked to health risks, including cancer. Monitoring their levels in human biofluids provides insight into exposure pathways. However, the analysis of PFAS isomers is technically challenging due to their structural similarity. To overcome this, the study employs <strong>LC coupled with cyclic ion mobility mass spectrometry (LC-cIM-MS)</strong> using the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/202"><strong>Waters SELECT SERIES Cyclic IMS</strong></a>, which adds a new separation dimension for better specificity.</p><h4><strong>Methods</strong></h4><p>Serum samples from Ghanaian firefighters and E-waste workers were prepared using <strong>solid-phase extraction (SPE)</strong> on 96-well µElution plates. A <strong>22-minute reversed-phase LC gradient</strong> was used for separation. The <strong>Cyclic IMS system</strong>, with ion mobility resolution R~65 and 145, enabled non-targeted PFAS analysis, including the generation of <strong>collision cross section (CCS)</strong> values to support compound identification.</p><h4><strong>Results</strong></h4><ul><li>PFAS compounds such as <strong>PFOS, PFHxS, PFHpS, PFNA</strong>, and <strong>6:2 FTS</strong> were identified in real serum samples.</li><li>The <strong>cyclic IMS</strong> allowed for the separation of coeluting isobaric compounds, such as <strong>PFOS isomers</strong> and <strong>cholic acid biomarkers</strong>, minimizing false identifications (Figure 3).</li><li><strong>Figure 4</strong> lists CCS values and other parameters for PFAS standards and identified analytes from a firefighter serum sample.</li><li><strong>Figure 5</strong> shows ion mobility conformeric profiles for <strong>PFNA</strong>, enabling reliable identification even at low signal intensities.</li></ul><h4><strong>Conclusion</strong></h4><p>The LC-cIM-MS method:</p><ul><li>Significantly improves specificity in PFAS identification.</li><li>Enables both <strong>targeted and untargeted detection</strong> of known and unknown PFAS in complex human samples.</li><li>Can be a key part of future occupational and environmental exposure assessments.</li></ul>

News from LabRulezLCMS Library - Week 28, 2025

News from LabRulezLCMS Library - Week 32, 2025

<p><strong>In a recent blog post we discussed how </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/article/5073"><strong>centralized data management</strong></a><strong> enhances security and control in analytical laboratories. But beyond security, networked environments offer other architectural advantages that fundamentally change how data flows through the lab.</strong></p><p>One key benefit is the separation of data acquisition from processing and review—a structural shift that brings measurable improvements in performance, uptime, and compliance.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Decoupling_Acquisition_From_Data_Review_Unlocking_Flexibility_and_Efficiency_in_Chromatography_and_Mass_Spectrometry_Workflows_a982d7ba0d.jpeg" alt="Thermo Fisher Scientific Decoupling Acquisition From Data Review Unlocking Flexibility and Efficiency in Chromatography and Mass Spectrometry Workflows" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Decoupling_Acquisition_From_Data_Review_Unlocking_Flexibility_and_Efficiency_in_Chromatography_and_Mass_Spectrometry_Workflows_a982d7ba0d.jpeg 245w," sizes="100vw" width="1024" height="512"></p><h3><strong>Maximizing instrument uptime</strong></h3><p>In many labs, data acquisition and review occur on the same computer, which tends to be placed next to the instrument. This ties up the acquisition workstation long after a run is complete, especially when processing tasks—such as baseline correction, peak integration, or spectral deconvolution—are resource-intensive.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Decoupling_Acquisition_From_Data_Review_Unlocking_Flexibility_and_Efficiency_in_Chromatography_and_Mass_Spectrometry_Workflows_304df97f03.jpg" alt="Thermo Fisher Scientific Decoupling Acquisition From Data Review Unlocking Flexibility and Efficiency in Chromatography and Mass Spectrometry Workflows" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Decoupling_Acquisition_From_Data_Review_Unlocking_Flexibility_and_Efficiency_in_Chromatography_and_Mass_Spectrometry_Workflows_304df97f03.jpg 245w," sizes="100vw" width="1024" height="428"></p><article><div><p>Separating these tasks means the acquisition PC can be dedicated solely to capturing raw data, while automated transfer and processing occur on a separate system. &nbsp;If processing is the biggest bottleneck in your workflow, this has clear advantages.</p><h3><strong>Enabling remote review and flexible access</strong></h3><p>When data is stored centrally and accessed over the network, analysts can log in from remote locations or satellite labs to perform review and approval workflows.</p><p>Central data storage also moves away from flat file sharing into a secure, user-controlled, archived storage location, which offers enhanced security and controlled access to archived data</p><p>Decoupling supports hybrid work environments and multi-user labs while supporting traceability through system audit trails and role-based access control.</p><h3><strong>Scaling processing power independently</strong></h3><p>Mass spectrometry data analysis—especially when using techniques like data-independent acquisition (DIA), MSⁿ workflows, or top-down proteomics—demands significant computational resources. These tasks benefit from multithreading, GPU acceleration, or distributed computing environments.</p><p>By shifting processing to centralized servers or virtual machines, labs can scale compute resources as needed without overloading acquisition systems, risking&nbsp;data loss or even sample loss from crashes during data collection.</p><h3><strong>Supporting collaborative review and shared methods</strong></h3><p>Decoupled environments allow multiple users to access and process the same dataset simultaneously, without file duplication or manual data transfer. Analysts can apply shared processing templates, compare runs side-by-side, and annotate results in a common workspace.</p><p>This is especially valuable for QA/QC teams performing multi-batch comparisons, method validation, or deviation investigations.</p><p>Enhancing compliance and traceability.</p><p>From a compliance standpoint, separating acquisition and processing improves data governance. Centralized environments can enforce version control, restrict unauthorized edits, and capture complete audit trails for every action taken—critical for GxP labs and 21 CFR Part 11 compliance. Review workflows can also be digitally signed and locked, ensuring that once approved, the data and metadata are still immutable</p><h3><strong>Conclusion</strong></h3><p>Decoupling acquisition from processing is a foundational change in how modern analytical labs operate. It reduces bottlenecks, increases system uptime, availability and enables advanced processing workflows to run on purpose-built infrastructure—without compromising compliance or productivity.</p><blockquote><p>You can see how Thermo Fisher Scientific is solving these challenges in <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/digital-solutions/ardia-platform/proteomics.html"><strong>Proteomics software solution</strong></a>.</p></blockquote><blockquote><p><strong>Visit us on&nbsp;</strong><a target="_blank" rel="noopener noreferrer" href="https://www.linkedin.com/showcase/72003132/admin/dashboard/"><strong>LinkedIn:</strong></a><strong>&nbsp;</strong>#Ardia #ChromatographyDataSystemSoftware, #DataManagement</p></blockquote></div></article><section><blockquote><h4><strong>Chris Knowles</strong></h4><p>Chris Knowles began his career with a PhD in mammalian cell line engineering and over a decade as a Principal Scientist and applications specialist in biopharma and bioprocessing. With deep expertise in software solutions for LC-MS, MS/MS, and advanced mass spectrometry techniques, he focuses on biologics production and analytics, including emerging areas like gene therapy, oligonucleotide therapeutics, and viral vectors. Now, as a Product Marketing Manager for BioPharma Software at Thermo Fisher Scientific, Chris is dedicated to helping customers overcome analytical challenges by delivering powerful, compliant, and user-friendly software solutions.</p></blockquote></section>

Decoupling Acquisition From Data Review: Unlocking Flexibility and Efficiency in Chromatography and Mass Spectrometry Workflows

<p><strong>Modern proteomics research produces vast quantities of complex data — and managing it all manually slows you down. Imagine transforming your work with a seamless, automated solution that not only accelerates data acquisition but also automates analysis and provides secure data management. Thermo Fisher Scientific are supporting researchers with a Proteomics Software Solution that delivers the future of proteomics, with innovation meeting automation to elevate your research to new heights. By leveraging the solution, featuring </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1782"><strong>Thermo Scientific Proteome Discoverer software</strong></a><strong> and </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1821"><strong>Thermo Scientific Ardia Platform</strong></a><strong>, you get a secure, connected environment that automates repetitive tasks, streamlines workflows, and accelerates analysis — whether you’re in the lab or working remotely.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Accelerate_Proteomics_Research_with_Smart_Automation_ef4e885127.jpg" alt="Thermo Fisher Scientific: Accelerate Proteomics Research with Smart Automation" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Accelerate_Proteomics_Research_with_Smart_Automation_ef4e885127.jpg 245w," sizes="100vw" width="1536" height="576"></p><h4><strong>What is the Proteomics software solution?</strong></h4><p>At its core, the solution combines powerful mass spectrometry data analysis with centralized data management and processing. This integrated setup means your data flows directly from the instrument to the secure, central storage where automated processes immediately launch data processing and securely store the results — no manual steps needed.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Thermo_Fisher_Scientific_Ardia_proteomics_process_a62402dd81.jpg" alt="Thermo Fisher Scientific: Ardia proteomics process" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Thermo_Fisher_Scientific_Ardia_proteomics_process_a62402dd81.jpg 245w," sizes="100vw" width="1200" height="363"></p><p>Because data storage and compute resources are co-located within the <strong>Ardia Platform</strong>, you <strong>eliminate time-consuming transfers</strong>, <strong>reduce risk of data loss</strong>, and <strong>keep high-throughput workflows moving</strong>. Remote access means researchers no longer need to be physically present at the system; they can connect remotely and monitor the acquisition and processing of their data in real time and quickly address any potential issues.</p><p>Designed as an <strong>open platform</strong>, the solution can <strong>support multiple instruments simultaneously</strong>, making it ideal for complex proteomics workflows and large-scale studies. It also makes it easy to work with a growing list of software tools and third-party applications, for data processing.</p><p>The <strong>Ardia Platform</strong> <strong>data</strong>-sync allows automated, bi-directional data transfer to other software packages — helping eliminate silos, avoiding manual data handling, and keeping your workflows flexible – meaning you can harness the power of an integrated environment while still working with your preferred applications.</p><h4><strong>What are the benefits?</strong></h4><h5><strong>Streamlined data management</strong></h5><ul><li>Automated data transfer. Store data and results in one secure, centralized environment with robust backup and archiving — minimizing the risk of data loss or manual error.</li></ul><h5><strong>Faster processing, fewer bottlenecks</strong></h5><ul><li>Co-localization of data storage and processing capabilities means each injection’s processing can begin immediately after acquisition. This is essential for high-throughput proteomics or labs running large-cohort or multiplexed studies where data volumes can be huge.</li></ul><h5><strong>Remote access &amp; real-time monitoring</strong></h5><ul><li>Researchers can monitor runs, check processing status, and collaborate from anywhere — ideal for collaborative research environments where multiple researchers need access to the same data. Plus, user access controls enable secure collaboration without moving files outside your organization.</li></ul><h5><strong>Powerful, automated analysis tools</strong></h5><ul><li>The Proteomics Software Solution offers advanced workflows including Thermo Scientific TMT (Tandem Mass Tag) quantification, cross-linking analysis for protein–protein interactions, and deep learning-powered algorithms like CHIMERYS and INFERYS to increase the number of identified peptides and proteins. The comprehensive suite of analytical tools supports various quantification methods, including label-free and SILAC, providing researchers with the flexibility to automate their analyses to specific experimental needs.</li></ul><h5><strong>Cost efficiency &amp; CHIMERYS on-premise</strong></h5><ul><li>CHIMERYS is delivered locally, saving on manual upload/download time, recurring license fees and improving performance compared to cloud service</li></ul><h5><strong>Flexible integration</strong></h5><ul><li>Export your results easily to other analytical tools for further interpretation, quantification, or visualization. This flexibility supports open science, collaboration, and customized data analysis that fit your lab’s needs.</li></ul><h4><strong>The future of proteomics is connected and automated</strong></h4><p>As proteomics research continues to evolve, you need proteomics software that stands at the forefront of innovation. The Proteomics Software Solution provides an integrated, automated environment, replacing fragmented, manual workflows with a secure solution designed to handle today’s high-throughput demands. The result? Faster insights, easier collaboration, streamlined data management, and the confidence to push your research further.</p><p><strong>See what’s possible </strong>– Explore the <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/cz/en/home/digital-solutions/ardia-platform/proteomics.html"><strong>Proteomics Software Solution</strong></a> or watch our recent webinar: <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5684"><strong>Facilitating High-Throughput, Large Cohort Proteomic Analyses Using an Integrated Software Solution</strong></a>, to learn more</p><blockquote><p><strong>Visit us on LinkedIn:</strong> #Proteomics #ProteomicsSoftwareSolution #ArdiaPlatform #Automation</p><p><strong>Zoe Julian</strong></p><p>Zoe Julian is a Product Marketing Manager for Chromatography and Mass Spectrometry software at Thermo Fisher Scientific. With over 12 years' experience of working with chromatography and mass spectrometry techniques with a background in GC and GC-MS(/MS) organic environmental analysis, she has helped many laboratories and industries improve their workflows through a unique understanding of their challenges. Transitioning to a focus on Chromeleon CDS she has shown customers how software solutions can improve their productivity and support their day-to-day operations.</p></blockquote>

Accelerate Proteomics Research with Smart Automation

<p><strong>Our Library never stops expanding. What are the most recent contributions to LabRulezLCMS Library in the week of 1st December 2025? Check out new documents from the field of liquid phase, especially HPLC and LC/MS techniques!</strong></p><blockquote><p><span style="font-size:20px;">👉 </span><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library"><span style="font-size:20px;"><strong>SEARCH THE LARGEST REPOSITORY OF DOCUMENTS ABOUT LCMS AND RELATED TECHNIQUES</strong></span></a></p></blockquote><blockquote><p><strong>👉 Need info about different analytical techniques?</strong> Peek into <a target="_blank" rel="noopener noreferrer" href="https://gcms.labrulez.com/library"><strong>LabRulezGCMS</strong></a> or <a target="_blank" rel="noopener noreferrer" href="https://icpms.labrulez.com/library"><strong>LabRulezICPMS</strong></a> libraries.</p></blockquote><p>This week we bring you application notes by <strong>Agilent Technologies,</strong> <strong>Shimadzu </strong>and<strong> Waters Corporation</strong> and poster by <strong>Thermo Fisher Scientific / HPLC!</strong></p><h3><strong>1. Agilent Technologies: Quantitative Bioanalysis of Oligonucleotides Using a 6495D Triple Quadrupole LC/MS System Combined with an Automated SPE Workstation</strong></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/an_bioanalysis_oligonucleotides_6495d_qqq_lcms_spe_5994_8339en_agilent_82610a68ca.pdf"><strong>Full PDF for download</strong></a></li></ul><p>In drug development, the quantitative analysis of oligonucleotides in biological samples is crucial for pharmacokinetics (PK), pharmacodynamics (PD), and toxicological safety evaluations. Due to the associated structural complexity of oligonucleotides and the unique nature of biological matrices, the corresponding sample preparation techniques are often complex. Liquid-liquid extraction (LLE) and solid-phase extraction (SPE) are commonly used sample preparation methods, with SPE being more suitable to meet lower limit of quantitation (LLOQ) requirements and complex matrices.2 However, traditional manual SPE methods are time consuming and prone to human error.&nbsp;</p><p>Liquid chromatography/tandem mass spectrometry (LC/MS/MS) is widely used in oligonucleotide bioanalysis due to its high sensitivity, low detection limits, high selectivity, and specificity. Methods using LC/MS/MS enable the rapid and accurate detection and quantification of low-concentration target compounds in complex matrices without the need for special reagents and probes.3&nbsp;</p><p>To address the challenges in sample preparation, Agilent developed an automated SPE workstation based on the Bravo liquid handling platform, combined with the next‑generation triple quadrupole LC/MS/MS system, the 6495D triple quadrupole LC/MS system, providing a complete solution from sample preparation to data analysis. The 6495D triple quadrupole LC/MS system excels in high sensitivity quantification and low detection limits from complex matrices, while the automated SPE workstation significantly reduces manual intervention time and improves operational consistency and reliability. This complete automated SPE bioanalysis workflow significantly enhances the efficiency and reliability of quantitative oligonucleotide&nbsp;bioanalysis.&nbsp;</p><h4><strong>Experimental&nbsp;</strong></h4><h5><strong>Instruments&nbsp;</strong></h5><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?search=1290+Infinity+III+Bio+LC+"><strong>Agilent 1290 Infinity III Bio LC&nbsp;</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=6495D"><strong>Agilent 6495D triple quadrupole LC/MS system&nbsp;</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=Automated+SPE+workstation"><strong>Agilent Automated SPE workstation</strong></a>, including Bravo, BenchCel and MiniHub</li></ul><h4><strong>Conclusion&nbsp;</strong></h4><p>This study verified the use of the automated Agilent SPE workstation combined with the Agilent 6495D triple quadrupole LC/MS system for oligonucleotide bioanalysis studies through the quantitative analysis of mipomersen in pig plasma. The experimental results showed that the system exhibited excellent linearity (R²=0.999) within the dynamic range of 2 to 1,000 ng/mL. The reproducibility and accuracy of the QC samples were within acceptable ranges, with most RSD values below 5%, QC low points below 10%, and back‑calculated concentration accuracy between 85 and 115%. Additionally, in the three-day repeatability experiment, the inter-batch reproducibility of the QC samples was good, with RSD values all below 10%. The back-calculated accuracies for QC samples at high, medium, and low concentration levels, as well as the LLOQ (2 ng/mL), remained stable between 80 and 120%.&nbsp;</p><p>By reducing manual intervention and improving operational consistency, the automated SPE workstation significantly enhances the efficiency and reliability of sample preparation. Combined with the high sensitivity and low detection limits of the 6495D triple quadrupole LC/MS system, this solution achieves efficient and accurate detection of low‑concentration oligonucleotides in complex matrices. Overall, this automated solution has broad application prospects in high-throughput oligonucleotide bioanalysis and meets the high requirements for quantitative analysis in drug&nbsp;development.</p><h3><strong>2. Shimadzu: Determination of N-Nitroso-Nebivolol in Nebivolol Drug Substance by </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=1&amp;search=LCMS-2050"><strong>LCMS-2050</strong></a></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/an_03_lcms_055_en_8d77db9fd3.pdf"><strong>Full PDF for download</strong></a></li></ul><h4><strong>User Benefits</strong></h4><ul><li>A new method for the determination of NDSRI impurity in nebivolol raw material was established using LCMS-2050.</li><li>The method has high sensitivity, short analysis time and high accuracy, which can fully meet the FDA's AI limit for N-Nitrosonebivolol.</li></ul><p>On September 4, 2024, the FDA issued the final guidance on the control of nitrosamine impurities in human drugs (Nitrosamine Guidance Version 2). The revised guidance describes two categories of nitrosamines: small-molecule nitrosamines and nitrosamine drug substance-related impurities (NDSRIs). Unlike small-molecule nitrosamine impurities that are structurally dissimilar to the active pharmaceutical ingredient (API), NDSRIs generally exhibit structural similarity to the API and may form through interactions between the API and nitrosating agents, such as nitrite impurities present in drug excipients.&nbsp;</p><p>Nebivolol is a potent and selective third-generation β-blocker clinically used for the treatment of patients with moderate-tosevere hypertension, as well as angina pectoris and congestive heart failure, with a recommended daily dose of 5 mg. Due to its structural characteristics, the synthesis of nebivolol may involve nitrosation reactions, leading to the introduction of the NDSRI impurity N-nitroso-nebivolol. According to the FDA's nitrosamine guidance, based on the Carcinogenic Potency Categorization Approach (CPCA), the acceptable intake (AI) limit for N-nitroso-nebivolol, a potential NDSRI in nebivolol, is set at 1500 ng/day.&nbsp;</p><p>This study established an LC-MS (<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=1&amp;search=LCMS-2050"><strong>LCMS-2050</strong></a>) method for the determination of N-nitroso-nebivolol in nebivolol drug substance. The method demonstrates high sensitivity, short analysis time, and accurate results, providing a reference for the detection of related nitrosamine impurities.</p><h4><strong>Separation Evaluation&nbsp;</strong></h4><p>To ensure high sensitivity in impurity analysis and prevent contamination of the mass spectrometer by high-concentration active pharmaceutical ingredient (API) components, flow path switching technology was employed. This method diverts the main nebivolol peak to waste, allowing only impurities to enter the mass spectrometer for detection. Under the optimized chromatographic conditions, The retention times of nebivolol and N-nitroso-nebivolol were 1.952 min and 3.408 min, respectively, so the mass spectrometry acquisition was initiated after 2.8 min, ensuring selective detection of the target impurity. This approach effectively enabled accurate and interferencefree analysis of trace-level impurities.</p><h4><strong>Conclusion</strong></h4><p>A novel method for determining the content of N-nitrosonebivolol in nebivolol drug substance was established by using the LCMS-2050. Within the concentration range of 1 - 180 ng/mL, the correlation coefficients of the N-nitroso-nebivolol was 0.9999. When the spiked concentration of 0.03 μg/mg and 0.3 μg/mg, the recovery rate of N-nitroso-nebivolol was 100.4 and 100.2, respectively, and the recovery rate was good and met the requirements of pharmacopoeia. The method has high sensitivity, linearity, precision and recovery rate can meet the detection requirements, and which can be used for the detection of nitrosamine impurity N-nitroso-nebivolol in nebivolol drug substance.</p><h3><strong>3. Thermo Fisher Scientific / HPLC: At the intersection between chromatographic performance, ESI efficiency and instrument productivity: nano to capillary flow LC/MS on long μPAC Columns</strong></h3><ul><li>Poster</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/po_intersection_between_chromatographic_performance_po_en_1a1d6f722b.pdf"><strong>Full PDF for download</strong></a></li></ul><p>LC-MS-based proteomics commonly employs low-flow liquid chromatography (LC) to separate tryptic peptides, which helps reduce sample complexity before MS/MS detection and protein identification. This technique benefits from minimal dilution on miniaturized columns and increased ionization efficiency via nanoflow electrospray ionization (ESI). As mass spectrometry (MS) devices become more sensitive and faster, there is an increasing need to boost throughput. The challenge lies in maintaining or increasing proteome coverage while simultaneously reducing analysis time. Typically, higher flow rates improve instrument productivity but may compromise sensitivity. In this study, the impact of eluting flow rates was assessed across various throughput ranges to identify the optimal balance between productivity and proteome coverage. Additionally, the transition to a dual-column single emitter configuration was evaluated to determine its effects on productivity and coverage. This approach aims to enhance LC-MS performance, ensuring high throughput without sacrificing the depth of proteome analysis.</p><h4><strong>Methods</strong></h4><p>HeLa cell digests were resuspended in 0.1% TFA and 1% ACN to create a 200 ng/µL stock solution, sonicated, diluted in 0.1% TFA, and vortexed. A <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/398"><strong>Thermo Scientific Vanquish Neo UHPLC instrument</strong></a> was configured for either a single analytical column in a trap-and-elute setup or two columns in tandem. For single column experiments, a Thermo Scientific PepMap Neo trap cartridge and a 110 cm µPAC Neo Plus column on a Thermo Scientific EASY-Spray source were used. LC methods with flow rates from 200 to 1000 nL/min were tested for throughputs ranging from 16 to 50 samples per day. The column was positioned in an external heating device mounted directly onto the ionization source and connected to an ESI emitter via a 20 µm ID voltage spacer. For tandem column experiments, two 110 cm µPAC Neo Plus columns were placed in the Vanquish Neo UHPLC column compartment between two low-dispersion 6-port switching valves. A 20 µm ID nanoViper line connected the eluents to an ESI emitter with an integrated liquid junction in an EASY-Spray source. Data were acquired using a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/402"><strong>Thermo Scientific Orbitrap Exploris 240</strong></a>/<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/401"><strong>480 mass spectrometer</strong></a> in data-independent acquisition mode.</p><h4><strong>Data Analysis&nbsp;</strong></h4><p>LC-MS data were analyzed either using a trial version of <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1782"><strong>Thermo Scientific Proteome Discoverer 3.3 software</strong></a> with Chimerys or with Spectronaut® 19. Results shown have been filtered to a 1% FDR</p><h4><strong>Conclusions&nbsp;</strong></h4><ul><li>Increasing the flow rate to 1 µL/min significantly increases instrument productivity. For gradient times below 30 minutes, 1 µL/min performs slightly better than lower flow methods, identifying up to 6679 protein groups at 50 SPD.&nbsp;</li><li>For gradient lengths over 50 minutes, a 200 nL/min flow rate provides superior chromatographic metrics and proteome coverage, resulting into a maximum of 8556 protein groups identified at 16 SPD.&nbsp;</li><li>The negative impact of a low-dispersion 6-port valve's impact scales inversely with flow rate. At 1 µL/min, peak width increases by 40%, yielding 5% lower proteome coverage but 26% higher productivity.&nbsp;</li><li>Optimized dual column single-emitter methods identified up to 6947 protein groups at 50 SPD with 3-6% CVs for the same column and 4-8% between columns (n=6).&nbsp;</li><li>Column reproducibility was shown across 5 columns, with an ID rate variation of 0.7% for HeLa digests and a median RT CV of 0.99% for spiked-in PRTC peptides.</li></ul><h3><strong>4. Waters Corporation: Improving Sample Throughput of HPLC Methods Using CORTECS 5 μm Columns</strong></h3><ul><li>Application note</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/720009072_en_1203625d4f.pdf"><strong>Full PDF for download</strong></a></li></ul><h5><strong>Benefits&nbsp;</strong></h5><ul><li>Comparable chromatographic performance for abacavir impurities was achieved using a shorter CORTECS Premier C18 5 µm Column in place of a column packed with fully porous 5 µm particles</li><li>33% reduction in solvent usage and analysis time using a CORTECS Premier C18 5 µm Column compared to a fully porous 5 µm column</li><li>33% reduction in analytical method greenness score indicating improved sustainability for the new method</li></ul><p>Improving validated HPLC methods can be challenging. Two of the approaches to increase analytical throughput, increasing mobile phase flow rate or using shorter columns, have drawbacks in higher pressures or reduced chromatographic performance. Typically, using a shorter column also requires decreasing the particle size to maintain a constant length to particle size (L/dp) ratio to ensure similar column efficiency. However, columns packed with smaller particles generate higher back pressures. Some labs may be able to migrate methods to shorter columns packed with smaller particles by transferring to a HPLC system capable of operating at higher pressures. However, if a laboratory lacks access to such systems, then their options may be limited. In those situations, finding appropriate columns to use to improve a method is not only a matter of chromatographic performance but also system compatibility, particularly from a pressure standpoint. Older HPLC systems are limited to lower pressures compared to more modern systems.&nbsp;</p><p>This application brief examines the improvement of a method for testing abacavir impurities by migrating the original method from a 4.6 x 150 mm 5 µm fully porous C18 column to a CORTECS Premier C18 4.6 x 100 mm 5 µm Column. Additionally, a fully porous 3.5 µm C18 column in 4.6 x 100 mm hardware was evaluated to determine if moving to a smaller particle size would have as much of a benefit as that provided by using a CORTECS Column. The separation conditions for method migration were obtained using the Waters Column Calculator. Along with examining throughput, solvent savings were calculated as well as analytical method greenness scores for each column tested.</p><h4><strong>Experimental</strong></h4><h5><strong>Method Conditions&nbsp;</strong></h5><ul><li><strong>LC system:</strong> <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/210"><strong>Alliance™ HPLC System</strong></a> with 2489 UV/Visible (UV/Vis) Detector</li></ul><h5><strong>Data Management&nbsp;</strong></h5><ul><li><strong>Chromatography software: </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/627"><strong>Empower™ Chromatography Data System (CDS)</strong></a></li></ul><h4><strong>Results and Discussion&nbsp;</strong></h4><p>Previously, the impurity method for abacavir was migrated to a 2.7 µm CORTECS Column.1 While that work showed the benefits of scaling to a smaller particle size, not all laboratories are comfortable moving to such a small particle size. In those instances, moving from a 5 µm to a 3.5 µm particle column is a good first step. However, depending on the method, this migration might not be appropriate and could result not only in elevated system pressure but also performance loss. Figure 1 shows the chromatograms for abacavir impurities using the original method column, a 3.5 µm C18 column, and the CORTECS Premier C18 5 µm Column.</p><h4><strong>Conclusion&nbsp;</strong></h4><p>CORTECS Premier 5 µm Columns are suitable alternatives for fully porous 5 µm columns for improving validated HPLC methods. Using a CORTECS solid-core stationary phase can allow for a shorter column to be used because of their higher efficiency per unit length. To highlight this, the impurity method for abacavir was migrated from the original fully porous 5 µm, 4.6 x 150 mm column to a CORTECS Premier C18 5 µm, 4.6 x 100 mm Column, as well as a 4.6 x 100 mm 3.5 µm fully porous column. The use of the CORTECS Column achieved comparable separation performance as the original while also exhibiting a shorter analysis time, lower solvent usage, and a better AMGS value.</p>

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News from LabRulezLCMS Library - Week 49, 2025

Accelerate Proteomics Research with Smart Automation

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