<p><strong>Ask any analytical chemist which hyphenated technique has become indispensable over the past decade, and the answer will almost certainly be the same: tandem chromatography–mass spectrometry. Whether it is </strong><a target="_blank" rel="noopener noreferrer" href="https://www.organomation.com/preparing-samples-for-lc-ms/ms-analysis"><strong>LC–MS/MS</strong></a><strong> quantifying a novel biologic’s metabolic fate, or </strong><a target="_blank" rel="noopener noreferrer" href="https://www.organomation.com/preparing-samples-for-gc-ms/ms-analysis"><strong>GC–MS/MS</strong></a><strong> chasing per- and polyfluoroalkyl substances (PFAS) down to sub-part-per-trillion levels in municipal water, the combination of chromatographic separation with the specificity of tandem mass detection has become the analytical workhorse of choice across virtually every regulated sector.</strong></p><p>Below we examine the key forces propelling this expansion, from biopharma pipeline dynamics and PFAS regulatory mandates to AI-driven automation and reshoring of pharmaceutical manufacturing—and explore what each trend means for laboratories managing sample preparation and analytical workflows.</p><h3><strong>Biopharma: The Engine Room of LC–MS/MS Demand</strong></h3><h4><strong>GLP-1 Agonists and the Metabolomics Gold Rush</strong></h4><p>The explosive commercial and scientific interest in GLP-1 receptor agonists—<a target="_blank" rel="noopener noreferrer" href="https://www.sepscience.com/advancing-glp-1-peptide-analysis-chromatography-challenges-and-innovations-12163"><strong>semaglutide and related peptide therapeutics </strong></a>for diabetes and obesity—has dramatically expanded the analytical demands placed on tandem MS platforms. Discovery programs require precise quantification of peptide drug candidates and endogenous biomarkers across complex biological matrices. These workflows rely on high-sensitivity LC–MS/MS for pharmacokinetic profiling, receptor occupancy studies, and metabolomics characterization. Metabolomics is, in fact, projected to be the fastest-growing application segment in mass spectrometry, driven in part by its growing role in cancer screening, biomarker discovery, and metabolic disease research.</p><p>I have been spending more time learning about GLP-1s because this is the hot topic that people want to discuss on the Concentrating on <a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL?si=n9GLz9zjSCOrVfXPxFPhng&amp;nd=1&amp;dlsi=52868e027aad4d22"><strong>Chromatography podcast</strong></a>. With that said, I was astounded looking at CNBC.com during breakfast this morning to see that <a target="_blank" rel="noopener noreferrer" href="https://www.cnbc.com/2026/03/21/glp-1-diets-restaurants-protein-fiber-weight-loss-drugs.html"><strong>one in eight Americans are currently taking one of these drugs such as Ozempic</strong></a>.</p><h4><strong>Antibody–Drug Conjugates and Gene Therapy: Complexity at Every Step</strong></h4><p>The ascent of antibody–drug conjugates (ADCs) and gene therapies has introduced a new level of analytical complexity. ADCs blend the target specificity of monoclonal antibodies with the cytotoxic potency of small-molecule payloads—and characterizing the linker chemistry, drug-to-antibody ratio (DAR), and conjugate stability demands high-resolution LC–MS/MS at every stage from discovery through QC release testing. Gene therapy vectors require equally rigorous characterization of impurities, aggregates, and empty/full capsid ratios.</p><p>This translates into a direct need for low-evaporation, high-recovery concentration methods that preserve labile protein structures and maintain sample integrity prior to LC–MS/MS injection. <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/article/5392"><strong>Nitrogen evaporation workflows</strong></a> that minimize oxidative stress and maintain sample temperature are increasingly critical in these pipelines.</p><h4><strong>Precision Medicine and Multi-Omics Integration</strong></h4><p>The shift toward precision medicine has accelerated adoption of high-throughput, multi-analyte MS platforms. Proteomics, metabolomics, and lipidomics workflows are converging on a single analytical platform—tandem MS—and generating datasets of a scale and complexity that were unimaginable ten years ago.</p><p>Make no mistake: the triple quadrupole serves an irreplaceable role in quantitative targeted analysis. At the same time, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=134&amp;manufacturerItems=3"><strong>Orbitrap </strong></a>and <strong>Q–TOF</strong> hybrid platforms are growing rapidly as researchers demand full-scan accurate mass for untargeted discovery.</p><h3><strong>Environmental Mandates: PFAS Testing Drives Adoption</strong></h3><p>Environmental testing is something that every person, chemist or not, can understand the importance of. Mounting mandates from the U.S. Environmental Protection Agency and European regulators regarding PFAS—the “forever chemicals” whose extraordinary environmental persistence is matched only by the analytical challenge of detecting them at trace levels—have created immediate, compliance-driven investment in LC–MS/MS infrastructure.</p><h4><strong>The Regulatory Framework Chemists Need to Know</strong></h4><p>The EPA has codified a suite of LC–MS/MS-based methods as the analytical standard for PFAS in water and solid matrices:</p><ul><li><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><strong>:</strong> Weak anion exchange SPE combined with LC–MS/MS; covers 25 PFAS including short-chain compounds in drinking water.</li><li><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/sample-concentration-epa-method-537-pfas-determination"><strong>EPA Method 537.1</strong></a><strong>: </strong>Reversed-phase SPE followed by LC–MS/MS; covers 18 PFAS including the GenX compound, with method detection limits in the low ng/L range.</li><li><a target="_blank" rel="noopener noreferrer" href="https://www.agilent.com/en/solutions/environmental/water-testing/pfas-in-water/us-epa-method-8327?srsltid=AfmBOooCY1pcavj7B1PH-75d3HO4BGDglNlhmyTyrpDY3zvUksMO1dlg"><strong>EPA Method 8327</strong></a><strong>: </strong>LC–MS/MS for selected PFAS in prepared extracts of aqueous and solid matrices.</li><li><a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/preparing-diverse-sample-matrices-for-epa-method-1633"><strong>EPA Draft Method 1633</strong></a><strong>: </strong>The emerging benchmark for PFAS in non-aqueous matrices—aqueous, solid, biosolids, and tissue—quantifying up to 40 PFAS.</li></ul><p>All of these methods designate LC–MS/MS, specifically LC coupled to triple quadrupole or tandem-in-time platforms operating in negative electrospray ionization mode with multiple reaction monitoring (MRM), as the required or recommended analytical technique. PFAS analysis is, at its core, an LC–MS/MS problem.</p><h4><strong>The Sample Preparation Bottleneck</strong></h4><p>Chemists who have worked with PFAS methods understand the particular demands they place on sample preparation. The ubiquity of<a target="_blank" rel="noopener noreferrer" href="https://blog.organomation.com/blog/tackling-pfas-contamination-practical-insights-from-epa-537.1-method-development"><strong> PFAS in laboratory materials</strong></a>—PTFE tubing, some SPE sorbents, standard bench supplies—means that blank contamination control is as analytically demanding as the detection itself. EPA 537.1 requires that sample volumes of approximately 250 mL be extracted and reconstituted in as little as 1 mL, creating a 250:1 concentration factor that can expose even trace contamination in the sample processing chain. The installation of a delay column between the LC pump and autosampler to prevent instrument background interference is now standard practice.</p><p>This is precisely where robust, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/article/5385"><strong>inert nitrogen evaporation </strong></a>systems earn their keep. PFAS workflows that use nitrogen-assisted evaporation to concentrate extracts prior to reconstitution benefit from materials that avoid PTFE and other fluoropolymers that can leach PFAS background—a consideration Organomation addresses in its concentration system designs.</p><p>The analytical community is also moving beyond targeted PFAS analysis. High-resolution accurate mass (HRAM) spectrometry via Orbitrap technology, paired with non-targeted screening workflows, is gaining traction for the identification of the more than 5,000 currently catalogued PFAS compounds and the novel structures that continue to emerge. LC–MS/MS remains the quantitative gold standard; HRAM provides the discovery layer.</p><h3><strong>Technological Trends Reshaping the LC–MS/MS Workflow</strong></h3><h4><strong>Artificial Intelligence and Automated Data Interpretation</strong></h4><p>The datasets generated by modern tandem MS platforms—particularly in omics applications—are too large and too complex for conventional manual review. AI-driven spectral deconvolution, automated peak integration, and AI-assisted hypothesis generation are now embedded in the software suites accompanying leading instruments. <a target="_blank" rel="noopener noreferrer" href="https://www.agilent.com/about/newsroom/presrel/2022/17feb-gp22004.html?srsltid=AfmBOop3warRIaEojXM2YyMML6RXfMIDzE-Wm0h-SiKkkocBeeET2m7u"><strong>Agilent’s acquisition of Virtual Control’s ACIES </strong></a>software specifically to automate LC–MS and GC–MS data analysis is emblematic of this direction.</p><p>For laboratory managers, AI integration means smaller specialized teams can operate high-throughput multi-analyte workflows—but it also means that the front-end sample preparation must be even more reproducible, since algorithmic interpretation amplifies inconsistencies introduced upstream.</p><h4><strong>Online SPE Coupling and “Chromatography Without Walls”</strong></h4><p>A significant trend is the integration of solid-phase extraction directly into the HPLC flow path—so-called online SPE–HPLC coupling. Systems that combine extraction and chromatographic separation in a single analytical instrument reduce manual transfer steps, minimize the risk of sample loss or contamination, and dramatically increase throughput. For analytes at very low concentrations, online SPE provides the on-column concentration capability that traditional offline preparation achieves with manual evaporation steps.</p><p>That said, offline sample preparation—including <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/article/5392"><strong>nitrogen-assisted evaporation</strong></a> under controlled conditions, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/2407"><strong>liquid–liquid extraction</strong></a>, and protein precipitation—retains significant advantages in flexibility, matrix handling, and the ability to process sample volumes that exceed online system capacity. The two approaches are increasingly complementary rather than competitive in well-designed analytical laboratories.</p><h4><strong>High-Purity Solvents and Reference Materials</strong></h4><p>As detection limits push further into the femtogram range and regulatory methods demand demonstrable blank performance, the quality of analytical consumables—mobile phase solvents, derivatization reagents, reference standards—has moved from background consideration to front-of-mind. Method validation in regulated environments now routinely requires vendor certification of solvent purity at a level that directly interfaces with instrument performance.</p><h3><strong>The Ever-Present Need for Sample Evaporation</strong></h3><p>As LC–MS/MS methods push detection limits lower, the analytical burden shifts increasingly upstream. The quality of the concentration, cleanup, and reconstitution steps preceding injection determines whether the instrument’s theoretical sensitivity is achievable in practice.</p><p><strong>Several specific developments are particularly relevant:</strong></p><ul><li><strong>ADC and gene therapy characterization workflows</strong> require gentle, low-temperature evaporation that preserves protein structure and prevents aggregation prior to LC–MS/MS. Nitrogen evaporation under controlled conditions is the preferred approach.</li><li><strong>PFAS trace analysis</strong> demands evaporation systems constructed from PFAS-inert materials, with rigorous attention to avoiding fluoropolymer surfaces throughout the sample path.</li><li><strong>High-throughput pharmaceutical QC</strong> driven by reshoring demands parallel processing capability—multi-position evaporators that maintain consistent flow and temperature across all positions simultaneously.</li><li><strong>Multi-omics and metabolomics workflows</strong> generate large sample batches that benefit from automated, walk-away evaporation with programmable endpoints to ensure reproducible final volumes across a cohort.</li></ul><p>Tandem chromatography–mass spectrometry is not merely growing; it is becoming structurally embedded in the analytical workflows of every major regulated industry. The convergence of biopharma complexity, PFAS regulatory mandates, AI-enabled data analysis, and pharmaceutical reshoring is creating a multi-year demand cycle that will require laboratories to invest not only in instruments, but in the entire sample preparation ecosystem that makes those instruments perform.</p><p>For analytical chemists, the practical takeaway is this: as mass spectrometry sensitivity continues to advance, the sample preparation step becomes the binding constraint on method performance. Whether you are developing a new PFAS method to meet EPA 1633, characterizing an ADC’s drug-to-antibody ratio, or running a 500-sample metabolomics cohort overnight, the reliability and cleanliness of your concentration and cleanup workflow determines the quality of every data point that follows.&nbsp;</p>

The Continued Rise of Tandem Chromatography–Mass Spectrometry

News from LabRulezLCMS Library - Week 27, 2026

<p><strong>🎤Dr. Christopher Reid (Professor of Chemistry and Biochemistry at Bryant University in Rhode Island)</strong></p><p><strong>In this episode of Concentrating on Chromatography, host Dave Oliva sits down with Chris Reid to explore how chemical biology and LC-MS are being used to tackle one of the most urgent global challenges: antimicrobial resistance.</strong></p><p>As antibiotic resistance continues to rise—and new drug development struggles to keep pace—researchers are looking beyond traditional approaches. Instead of targeting how bacteria build their cell walls, Chris’s work focuses on how they break them down, opening the door to entirely new antimicrobial strategies.</p><h4><strong>What You’ll Learn in This Episode:</strong></h4><ul><li>Why antimicrobial resistance is accelerating globally</li><li>What peptidoglycan is and why it’s essential to bacterial survival</li><li>How targeting cell wall degradation differs from traditional antibiotics</li><li>The strategy behind designing small molecule probes and inhibitors</li><li>How LC-MS is used to analyze peptidoglycan fragments and enzyme activity</li><li>Key analytical challenges: complex mixtures, low-abundance species, and structural similarity</li><li>The importance of sample preparation and reproducibility in LC-MS workflows</li><li>How this research could lead to new antibiotic targets</li></ul><h3><strong>Video Transcription</strong></h3><h4><strong>The Growing Challenge of Antibiotic Resistance</strong></h4><p>According to Reid, antibiotic resistance is increasing across a broad spectrum of bacterial pathogens that were once readily treated with existing therapies. In some cases, clinicians must now rely on only a handful of last-line antibiotics, while resistance is also rising in diseases such as tuberculosis.</p><p>One of the major obstacles is the limited commercial incentive to develop entirely new antibiotics. Because bacterial resistance can emerge relatively quickly after a drug reaches the market, pharmaceutical companies often favor modifying existing antibiotics or combining them with resistance-modifying agents rather than investing in completely new drug classes. As a result, genuinely novel antibacterial targets remain urgently needed.</p><h4><strong>Why the Bacterial Cell Wall Remains an Attractive Target</strong></h4><p>The bacterial cell wall consists primarily of <strong>peptidoglycan</strong>, a highly cross-linked polymer that provides structural integrity, maintains cell shape, and enables bacterial growth and division.</p><p>Many widely used antibiotics—including the β-lactam antibiotics such as penicillins—target enzymes responsible for synthesizing or cross-linking peptidoglycan. These pathways have proven highly successful therapeutic targets because peptidoglycan is unique to bacteria and absent from human cells, minimizing unwanted effects on the host.</p><p>However, most existing antibiotics target only specific stages of peptidoglycan biosynthesis. Reid's research explores another part of this complex pathway: enzymes responsible for degrading the carbohydrate backbone of peptidoglycan during normal bacterial growth and remodeling. These enzymes may represent an underexplored class of antimicrobial targets capable of overcoming existing resistance mechanisms.</p><h4><strong>Targeting the Glycan Backbone</strong></h4><p>A key advantage of focusing on the carbohydrate backbone is its remarkable conservation across both Gram-positive and Gram-negative bacteria.</p><p>Whereas the peptide components of peptidoglycan vary considerably between bacterial species—and frequently acquire mutations associated with antibiotic resistance—the glycan backbone remains highly conserved and tolerates relatively few structural modifications.</p><p>This biological constraint makes enzymes acting on the glycan backbone particularly attractive targets. Reid's group developed a series of <strong>small-molecule probes and inhibitors</strong> designed to recognize enzymes known as <strong>N-acetylglucosaminidases</strong>, which cleave glycosidic bonds within peptidoglycan and generate soluble degradation products.</p><p>Rather than beginning with purified enzymes, the researchers adopted a <strong>top-down phenotypic screening strategy</strong>. Candidate compounds were first evaluated for their ability to inhibit bacterial growth before progressively narrowing the list of potential molecular targets through genetic studies, microscopy, enzyme assays, and biochemical characterization. This iterative workflow ultimately identified compounds capable of inhibiting the desired enzyme class while simultaneously providing valuable chemical probes for studying bacterial cell wall biology.</p><h4><strong>LC-MS as a Central Analytical Tool</strong></h4><p>Liquid chromatography coupled with mass spectrometry plays a central role throughout the project by enabling detailed characterization of structural changes occurring within peptidoglycan after bacterial cells are treated with candidate inhibitors.</p><p>Because intact peptidoglycan is an insoluble polymer, sample preparation begins with isolation of the bacterial cell wall through detergent extraction and differential centrifugation. Additional purification steps remove proteins, nucleic acids, and teichoic acids before enzymatic digestion converts the insoluble material into soluble fragments suitable for chromatographic analysis.</p><p>The resulting digest is analyzed by LC-MS to examine changes in the distribution of peptidoglycan fragments. Chromatographic retention times provide an immediate indication of changes in cross-linking, with larger oligomers such as trimers and tetramers generally eluting later than monomeric fragments. Mass spectrometry then confirms the identity of these fragments by measuring their intact molecular masses, while tandem MS experiments can provide further structural information when required.</p><h4><strong>Sample Preparation Determines Data Quality</strong></h4><p>Reid emphasized that sample preparation represents one of the most critical—and challenging—stages of the entire workflow.</p><p>Because peptidoglycan analysis involves multiple purification, digestion, and reduction steps, even minor procedural differences between samples can introduce analytical artifacts that complicate biological interpretation.</p><p>Maintaining strict consistency throughout sample preparation is therefore essential. Appropriate controls must accompany every experiment, ensuring that observed chromatographic and mass spectrometric differences truly reflect biological responses rather than experimental variability. The complexity of bacterial cell wall composition further increases the analytical challenge, as subtle differences in amino acid substitutions and low-abundance cross-linked species can complicate LC-MS data interpretation.</p><h4><strong>Chemical Biology for Future Antibiotic Discovery</strong></h4><p>Although the identified compounds may eventually serve as starting points for antibiotic development, Reid views them primarily as <strong>chemical biology tools</strong>.</p><p>By selectively inhibiting individual enzymes, these probes allow researchers to investigate previously unexplored aspects of bacterial cell wall remodeling that cannot easily be studied using classical genetic approaches alone.</p><p>The research team is now expanding this strategy by combining their probes with <strong>proximity-labeling proteomics and mass spectrometry</strong>, aiming to map protein interaction networks associated with bacterial cell wall degradation. Such studies may reveal entirely new antibacterial targets and provide deeper insight into the biological processes governing bacterial growth and division.</p><p>Ultimately, the work illustrates how integrating synthetic chemistry, microbiology, molecular biology, and advanced LC-MS can accelerate the search for innovative therapeutic strategies against antimicrobial resistance. As existing antibiotics become progressively less effective, multidisciplinary approaches such as these may play an increasingly important role in identifying the next generation of antibacterial targets.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

 Fighting Antibiotic Resistance with LC-MS: Targeting Bacterial Cell Walls

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Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

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Waters Xevo MRT QTof Mass Spectrometer

Achieve exceptional science with the Xevo™ MRT Mass Spectrometer—100K resolution at 100 Hz, sub-ppm accuracy, and confident identification for greater lab productivity.

<h3><strong>Delivering Performance and SPEED</strong></h3><ul><li><strong>Resolution AND Speed Without Compromise</strong></li></ul><p><strong>Whether you’re in academia or industry achieve exceptional science - 100% of the time with the Xevo™ MRT Mass Spectrometer. This state-of-the art QTof delivers 100K resolution at 100 Hz with sub ppm mass accuracy for confident identification and greater productivity in your lab.</strong></p><h4><strong>Delivering performance at speed</strong></h4><p>The high resolution and mass accuracy of the Xevo MRT Mass Spectrometer are independent of acquisition rate. Working at maximum resolution ensures you can resolve analytes in complex matrices, providing comprehensive, high accurate mass data for scientific interpretation.</p><h4><strong>Increase compound identification confidence</strong></h4><p>Probe deeper at biologically relevant concentrations with high levels of mass accuracy. Search tolerances can be minimized resulting in efficient data review, improving turnaround times for increased lab productivity.</p><h4><strong>Connected solutions</strong></h4><p>A complete workflow for metabolomics, lipidomics, and metabolite identification through market leading chemistry and cutting-edge, informatics ensures your lab is operating with maximum efficiency – reducing the time to result.</p><h4><strong>Exceptional science - every day</strong></h4><p>System performance is critical. From instrument stability and robustness for extended studies to precision measurements in every injection, innovative multi reflecting time-of-flight technology delivers high quality experimental outcomes for every lab, every day.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_1_63e746d310.jpg" alt="Waters Xevo MRT Mass Spectrometer" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_1_63e746d310.jpg 244w," sizes="100vw" width="1119" height="715"></p><h3><strong>Extraordinary Performance</strong></h3><h4><strong>Without compromises</strong></h4><h5><strong>Exceptional science for every lab, scientist, problem, question, and sample… Solved</strong></h5><p>The exceptional combination of high mass resolving power of 100,000 FWHM and mass accuracy of &lt;500 part per billion (ppb) of the Xevo MRT Mass Spectrometer are achieved independent of acquisition rates, up to 100Hz. Maximum performance, matched to throughput levels that matter for complex and challenging analyses, increases statistical power and confidence in results.</p><h5><strong>Feeling trapped?</strong></h5><p>Unlike other high-resolution MS technologies, multi-reflecting time-of-flight delivers mass resolution consistent over a broad m/z range independent of scan speed, even at the fastest acquisition rates for MS and MS/MS data, ensuring confident identification of analytes across a range of samples and matrices – an ideal solution for metabolite profiling and discovery.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Mass_Spectrometer_Extraordinary_Performance_d8879eda23.jpg" alt="Waters Xevo MRT Mass Spectrometer: Extraordinary Performance." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Mass_Spectrometer_Extraordinary_Performance_d8879eda23.jpg 245w," sizes="100vw" width="1309" height="774"></p><h3><strong>Connected Solutions</strong></h3><h4><strong>From advanced chemistry to flexible informatics</strong></h4><p>Make meaningful scientific discoveries more efficient with dedicated workflows combining column chemistries, separations, and informatics with the exceptional data quality of the Xevo MRT Mass Spectrometer. The waters_connect™ platform allows you to process and report your data in the way that you want. Whether using a Waters supported solution or exporting data via mzML to custom scripted workflows, we have you covered.</p><h4><strong>The Xevo MRT mass spectrometer readily integrates with your existing pipeline and workflow strategy</strong></h4><p>Waters has partnered with Mass Analytica™ (mass-analytica.com) and their market leading metabolomic, lipidomic, and metabolite identification software packages, MARS, Lipostar2, and MassMetaSite, respectively. Through either the waters_connect Application Programming Interface (API) or via mzML*, there is the option for you to transfer your data into the relevant software package for statistical interpretation and identification of analytes.</p><p>The DATA Convert Application within the waters_connect Platform enables you to convert to and export mzML file formats, ensuring a seamless integration of technology and informatics for every lab.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_6_d0fc257136.jpg" alt="Waters Xevo MRT Mass Spectrometer: Connected Solutions." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_6_d0fc257136.jpg 236w," sizes="100vw" width="1212" height="802"></p><p>The waters_connect platform provides flexible data processing options, either using third-party applications via the waters_connect API or conversion of data sets to mzML file format via DATA Convert.&nbsp;</p><h3><strong>Unlocking a New Level of Confidence&nbsp;</strong></h3><h4><strong>By bringing an analytical powerhouse to every lab</strong>&nbsp;</h4><p>To meet the most challenging analytical problems that you experience head on, Waters has taken cutting edge technology that was pioneered in the SELECT SERIES™ MRT, scaling the raw power and resolution at speed into a compact flexible, benchtop platform.</p><h4><strong>The MRT Xevolution</strong></h4><p>The Xevo MRT Mass Spectrometer has been engineered to deliver high-end technology into a benchtop platform to solve your most challenging problems. 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>

Analysis of Synthetic Peptide Hormones (Bioanalytic)

We offer highly specific and sensitive quantitative analysis of peptides by LC-MS/MS technique (LOQ < 1 ng/ml).

<h4><strong>Synthetic peptide hormones - a study of the purity of formulations and composition of dietary supplements.</strong></h4><p>In sports doping, small synthetic peptide hormones represent an increasingly attractive class of supplements for improving physical performance in amateur and professional athletes. Their use, depending on the type of peptide, is aimed primarily at building muscle tissue while intensifying fat reduction processes combined with the induction of the body's regenerative processes.</p><p>Do you want to be sure that the peptide you are using is in the product in the amount declared by the manufacturer? Or do you have doubts that the supplement you are using is contaminated with these compounds? If you are troubled by these or similar questions - feel free to contact us. We perform tests in cooperation with <a target="_blank" rel="noopener noreferrer" href="http://www.lab4tox.pl"><strong>Lab4Tox</strong></a>. We offer highly specific and sensitive quantitative analysis of peptides by LC-MS/MS technique (LOQ &lt; 1 ng/ml). At the moment, we analyze the following peptides:</p><ul><li><span class="ts-list-li-content">GHRP-2</span></li><li><span class="ts-list-li-content">GHRP-6</span></li><li><span class="ts-list-li-content">BPC-157</span></li><li><span class="ts-list-li-content">Melanotan-2</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 Synthetic Peptide Hormones. We perform tests in cooperation withLab4Tox." 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>

Determination of nitrosamine content (Bioanalytic)

Our offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products. We perform the work according to the criteria and needs of the client based on the EMA note.

<p><strong>Determination of nitrosamines is one of the pharmaceutical industry's top priorities. After the presence of N-nitrosodimethylamine (NDMA) was first reported in an active pharmaceutical ingredient (API), the U.S. Food and Drug Administration (FDA) and the European Medicines Agency (EMA) mandated the identification and control of all APIs and finished products in which there is a risk of nitrosamines.</strong></p><p>The content of nitrosamines in drug products can be controlled primarily by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) analysis. More than that, a reliable analysis result in our offer consists of a well-chosen sample preparation procedure, a selective and sensitive analytical method, and the experience of the analyst, who selects the best method parameters at the optimization stage.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg 234w," sizes="100vw" width="1536" height="1024"></p><p><strong>We have gained experience working with leading pharmaceutical companies.</strong> As part of our ongoing work, we have developed analytical methods for small-molecule nitrosamines of 70-150 g/mol. These compounds are mainly formed during manufacturing processes and depend on the presence and type of excipients (e.g. NDBA - N-nitroso-dibutylamine). We have also developed methods for determining molecules with higher nitrosamine drug substance related impurities (NDSRIs). In our work, we focus on achieving the highest possible sensitivity, selectivity and precision. To this end, we individually select the parameters of the methods depending on the composition of the drug and the expected nitrosamines. Due to the above criteria and the required detection limits, we perform nitrosamine impurity determinations using LC-MS/MS kits based on <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+5500%2B"><strong>QTRAP 5500+</strong></a> and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+6500%2B"><strong>QTRAP 6500+</strong></a> mass spectrometers (<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=55"><strong>SCIEX</strong></a>).</p><blockquote><p><span style="font-size:22px;"><strong>Our offer</strong></span></p><p><strong>Our offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products.</strong> <strong>We perform the work according to the criteria and needs of the client based on the EMA note.</strong></p><p>At the stage of sample preparation, we focus on:</p><ul><li>obtaining the <strong>highest possible recovery</strong> of nitrosamines (matrix purification);</li><li><strong>limiting additional synthesis</strong> of impurities (selection of appropriate equipment and reagents);</li><li><strong>ensuring the stability</strong> of the sample prepared for LC-MS/MS analysis.</li></ul><p>During the optimization of the LC-MS/MS method, we solve such problems as:</p><ul><li>selection of an <strong>appropriate internal standard</strong>;</li><li><strong>separation of the impurity from the API</strong>;</li><li>obtaining the expected <strong>sensitivity of the analytical method</strong>.</li></ul><p><strong>Quantitative analysis of nitrosamines requires sensitivity, precision and accuracy, which we provide to our customers.</strong></p></blockquote><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg 103w," sizes="100vw" width="1130" height="1710"></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 Development of LC-MS/MS method

We take an individual and factual approach to developing a new method and performing analyses.

<h4><strong>An experienced partner in the LC-MS/MS analysis industry</strong></h4><p>If you are interested in performing quantitative, qualitative or mixed analysis using LC-MS/MS analytical methods but lack such capabilities due to lack of equipment, “know-how” or are looking for a team to perform analysis for a project - you have come to the right place. We work on <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/companies/315"><strong>equipment</strong></a> with high sensitivity, speed and specificity. Our team is a group of specialists with comprehensive experience in the industry. The LabExperts <a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/zespol/">team</a> has participated in many scientific projects, R&amp;D and commercial implementations. We take an individual and factual approach to developing a new method and performing analyses:</p><ul><li>In the first stage, we get to know your requirements - to align expectations with capabilities;</li><li>Next, we will form and approve the framework for cooperation, ensuring the observance of confidentiality by signing a non-disclosure agreement (NDA);</li><li>We will plan together and, for our part, meet the deadlines for the completion of the set tasks;</li><li>We will perform preliminary studies, after which we will decide together whether and to what extent we continue to develop the methods;</li><li>We will handle the development of the sample preparation procedure;</li><li>We will select the best parameters for the LC-MS/MS analytical method;</li><li>The analytical method along with the sample preparation procedure will be validated according to generally accepted guidelines and standards, or we will establish the required acceptance criteria and ranges for your needs;</li><li>We will perform LC-MS/MS analyses of a series of samples;</li><li>We will provide results in the form of easy-to-read reports at each required stage;</li><li>We will evaluate the feasibility and assist in the transfer of the method to your laboratory.</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Development_of_LC_MS_MS_method_2594c9fd54.jpg" alt="Bioanalytic: Bioanalytic Development of LC-MS-MS method." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Development_of_LC_MS_MS_method_2594c9fd54.jpg 234w," sizes="100vw" width="1536" height="1024"></p><p>Pricing and the framework for cooperation are always determined individually depending on the scope of the study. This is influenced by the amount of work and the complexity of the development of the sample preparation procedure and analytical method and routine analytics. As a rule, the final price consists of three separately priced elements: the cost of preliminary studies, method validation, and the cost of analysis of one sample within a series of analyses.</p><p>Don't beat your head against the wall - we will help you achieve your goal!</p><p>We look forward to working with you!</p>

Products focused on LC/MS/MS - page 3

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