<p><strong>Join us for a fascinating conversation with Dr. Subhoja Chakraborty from the University of Central Florida, whose cutting-edge research targets the global challenge of malaria drug resistance. Dr. Chakraborty shares her journey from structure-based drug design during her PhD to her recent collaborative work repurposing human kinase inhibitors as rapid, selective antimalarials against drug-resistant Plasmodium falciparum strains.</strong></p><h4><strong>In this episode, you'll learn:</strong></h4><ul><li>How structure-guided approaches reveal potential drug targets, including cysteine proteases like falcipain-2, and kinases implicated in malaria's complex life cycle.</li><li>The power of repurposing kinase inhibitors originally developed for cancer and other diseases, focusing on compound 12, which blocks hemozoin formation and protein kinase 6—key steps in parasite survival.</li><li>Lab techniques such as affinity, gel filtration, and size exclusion chromatography for recombinant protein purification—and how troubleshooting is crucial for high-yield, stable complexes.</li><li>Advances in mass spectrometry for characterizing protein interactions, validating drug targets, and mapping molecular pathways pivotal to malaria therapeutics.</li><li>Tips and lessons for new researchers facing the challenges of sample preparation, complex protocols, and working as part of a collaborative team.</li></ul><p>Dr. Chakraborty’s insights bridge the gap between basic science and translational drug discovery, offering hope for more effective, targeted malaria treatments in a world where resistance to frontline therapies threatens millions.</p><h4><strong>Referenced Papers:</strong></h4><ul><li>"Plasmodium falciparum protein kinase 6 and hemozoin formation are inhibited by a type II human kinase inhibitor exhibiting antimalarial activity" (Cell Chemical Biology, 2025)</li><li>"New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain" (BBRC, 2022)</li><li>"Structure-Based Optimization of Protease−Inhibitor Interactions to Enhance Specificity of Human Stefin‑A against Falcipain‑2 from the Plasmodium falciparum 3D7 Strain" (Biochemistry, 2023)</li></ul><p>If you’re a student, scientist, or simply passionate about advances in infectious disease research, this episode offers actionable insights, inspiring advice, and a front-row seat to innovation in combating malaria.</p><h3><strong>Video Transcription</strong></h3><h4><strong>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</strong></h4><h5><strong>Introduction</strong></h5><p>In this discussion, Subhoja shares insights into her research journey, focusing on malaria drug discovery and the role of modern analytical techniques in biological and biomedical research. The conversation is aimed primarily at undergraduate students and early-career researchers interested in chemistry, biotechnology, and life sciences.</p><h5><strong>Research Focus: Malaria Drug Discovery and Kinase Targets</strong></h5><p>Subhoja is currently involved in malaria drug discovery research at the University of Central Florida, where she has been working since beginning her postdoctoral position two years ago. Her earlier PhD research focused on structure-based drug design in malaria, using a combination of in silico approaches, recombinant protein expression, and X-ray crystallography to determine precise three-dimensional structures of target proteins and their inhibitors.</p><p>This structural perspective provided a foundation for her current work, which centers on drug discovery through compound screening and repurposing. A recent publication from her laboratory explores the use of repurposed mammalian CDK-like kinase inhibitors as potential antimalarial agents. While such kinase inhibitors are well known in cancer and cardiovascular research, their application to malaria targets represents a novel and promising approach.</p><p>Kinases are attractive drug targets because of their central role in cell signaling and growth pathways. By targeting specific kinases involved in different stages of the malaria parasite life cycle—whether asexual growth, gametocytogenesis, or differentiation—it may be possible to significantly inhibit parasite growth and progression.</p><h5><strong>Chromatography in Protein Expression and Purification Workflows</strong></h5><p>Chromatography plays a critical role throughout Subhoja’s research. Her experience spans from basic chromatography techniques during her early training to advanced protein purification workflows using affinity chromatography, gel filtration (size exclusion chromatography), and ion exchange chromatography.</p><p>Recombinant proteins are routinely purified using affinity resins such as nickel or cobalt, followed by further purification to remove contaminants. Fast Protein Liquid Chromatography (FPLC) enables compact, stepwise purification workflows suitable for producing proteins for in vitro assays.</p><p>A recurring challenge in this process is the expression of high-molecular-weight proteins, which often accumulate in insoluble fractions or inclusion bodies. Careful selection of expression vectors, host systems, and induction conditions is therefore essential to maximize yield and solubility.</p><h5><strong>Integrating Size Exclusion Chromatography into the Workflow</strong></h5><p>Size exclusion chromatography (SEC) is typically used after affinity purification to further improve protein purity. Following elution with imidazole or glutathione, desalting is required to prevent buffer components from interfering with downstream assays. This is often achieved using desalting columns such as G-25 or PD-10.</p><p>To remove lower-molecular-weight contaminants, finer SEC media—such as Superdex or Sephacryl columns—are employed. Concentration steps using molecular-weight cut-off filters are then applied to obtain the desired protein concentration for functional studies.</p><p>These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.</p><h5><strong>The Role of Mass Spectrometry in Biomolecular Characterization</strong></h5><p>Mass spectrometry is a key analytical tool in Subhoja’s research pipeline, particularly for target identification and validation. In both malaria and cancer research, MS is used alongside chromatography, immunoprecipitation, and pull-down assays to study protein interactions and molecular recognition events.</p><p>Affinity-based mass spectrometry enables the identification of binding partners and interactors, whether studying proteins, long non-coding RNAs, or protein complexes. Techniques such as native MS, tandem affinity purification, and proximity labeling (e.g., TurboID-based workflows) provide deeper insights into molecular networks and signaling pathways.</p><p>These approaches are essential for understanding how candidate drug targets function within complex biological systems.</p><h5><strong>Sample Preparation Challenges in Biological Research</strong></h5><p>Sample preparation remains one of the most challenging aspects of biological experimentation. Whole-cell lysates contain proteases, nucleases, and other components that can rapidly degrade target molecules. Preventing degradation requires minimizing preparation time, maintaining low temperatures, and using appropriate inhibitor cocktails.</p><p>Reproducibility is also critical: biological experiments require multiple replicates, and variability is often unavoidable. Careful handling, protocol optimization, and continuous troubleshooting are essential to ensure reliable results, whether preparing samples for chromatography, mass spectrometry, sequencing, or immunoprecipitation.</p><h5><strong>Advances in Chromatography and MS for Malaria Research</strong></h5><p>Modern advances in chromatography and mass spectrometry significantly enhance malaria research by enabling precise target identification, quantification, and functional characterization. Drug discovery workflows begin with construct design and recombinant expression, followed by purification and interaction studies.</p><p>In malaria research, stage-specific parasite biology requires careful extraction and analysis of proteins from different life cycle stages. Tandem affinity MS, immunoprecipitation, and in vivo validation studies help confirm target relevance and therapeutic potential.</p><p>Recent work on repurposed kinase inhibitors has shown promising results, including inhibition of hemozoin formation—a key detoxification pathway for the malaria parasite—highlighting the potential of such compounds for further development.</p><h5><strong>Malaria, Drug Resistance, and Global Impact</strong></h5><p>Malaria remains a major global health burden, with over 600,000 deaths annually and widespread drug resistance complicating treatment. Artemisinin resistance, particularly associated with mutations in the K13 propeller domain, has driven the search for new targets and therapies.</p><p>During her PhD, Subhoja focused on falcipain-2, a cysteine protease involved in hemoglobin degradation within the parasite. This pathway is critical for parasite survival and has emerged as a promising drug target. Her work revealed that falcipain-2 operates within a larger protein complex responsible for hemoglobin processing and amino acid release.</p><p>Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.</p><h5><strong>Advice for Early-Career Researchers</strong></h5><p>For researchers just starting out, Subhoja emphasizes the importance of hands-on experience. Working directly with cells, lysates, and analytical tools is essential for truly understanding experimental systems. Failure is an inherent part of research, and perseverance is key.</p><p>Motivation, teamwork, careful sample handling, and thorough preparation all contribute to long-term success. Reading extensively, critically evaluating one’s own work, and appreciating incremental progress are vital aspects of a sustainable research career.</p><p>Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.</p><h5><strong>Closing Remarks</strong></h5><p>The discussion highlights how interdisciplinary approaches combining chromatography, mass spectrometry, structural biology, and biochemistry are driving advances in malaria drug discovery. Through careful experimental design, analytical rigor, and collaborative teamwork, researchers can address complex biological challenges and contribute to global health solutions.</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>

Affinity, Gel Filtration, Size Exclusion Chromatography: Repurposing Kinase Inhibitors for Malaria

<p><strong>In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 000 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</strong></h5><ul><li>Tu, 10.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5807">Registration</a></li></ul><p>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.</p><h5><strong>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</strong></h5><ul><li>We, 11.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5793">Registration</a></li></ul><p>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.</p><h5><strong>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</strong></h5><ul><li>We, 11.2.2026 15:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5816">Registration</a></li></ul><p>Get a practical overview of PFAS in food and food contact materials, including EU and US regulations, key analytical challenges, and reliable PFAS testing strategies.</p><h5><strong>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</strong></h5><ul><li>We, 11.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5720">Registration</a></li></ul><p>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.</p><h5><strong>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</strong></h5><ul><li>We, 11.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5772">Registration</a></li></ul><p>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.</p><h5><strong>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</strong></h5><ul><li>Th, 12.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5834">Registration</a></li></ul><p>Discover how PAT HPLC enables near-real-time monitoring of critical quality attributes in bioprocessing, with a case study on charge-variant control by cation-exchange chromatography.</p><h5><strong>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</strong></h5><ul><li>Th, 12.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5889">Registration</a></li></ul><p>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.</p><h5><strong>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</strong></h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5833">Registration</a></li></ul><p>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.</p><h5><strong>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</strong></h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5814">Registration</a></li></ul><p>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.</p><h5><strong>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</strong></h5><ul><li>Th, 12.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/2104">Registration</a></li></ul><p>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.</p><h5><strong>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</strong></h5><ul><li>Fr, 13.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5787">Registration</a></li></ul><p>Discover why LC method transfer between legacy and modern systems is challenging, which hidden parameters affect retention and peak shape, and how to achieve robust, reliable results.</p>

Webinars LabRulezLCMS Week 07/2026

<p><strong>Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.</strong></p><p>DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771"><strong>Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</strong></a></h4><p>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*</p><p>Anal. Chem. 2025, 97, 49, 27057–27063</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><p>Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T<sub>4</sub>) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.</p><p>Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a></p><p>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and <i>m</i>/<i>z</i> of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping <i>m</i>/<i>z</i> values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a></p><p>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (<i>m</i>/<i>z</i> × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.</p><h4><strong>Experimental Section</strong></h4><h5><strong>Data Collection</strong></h5><p>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560"><strong>Thermo Scientific Q-Exactive UHMR</strong></a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.</p><h4><strong>Results and Discussion</strong></h4><p>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and <i>m</i>/<i>z</i> for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 <i>m</i>/<i>z</i>). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T<sub>4</sub> bound states of both WT- and CT-TTR tetramers, where &lt;3900 <i>m</i>/<i>z</i> has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T<sub>4</sub>- and 1 T<sub>4</sub>-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na<sup>+</sup>, K<sup>+</sup>, and Zn<sup>2+</sup>) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this <i>m</i>/<i>z</i> overlap to resolve and quantify hybrid tetramer formation and T<sub>4</sub> binding.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"></p><h5><strong>Thyroxine Binding to TTR Homotetramers</strong></h5><p>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T<sub>4</sub> into T<sub>3</sub> (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T<sub>4</sub> at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T<sub>4</sub>) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T<sub>4</sub>.</p><p>DMT was further applied to quantify T<sub>4</sub> binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T<sub>4</sub>. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 <i>m</i>/<i>z</i> range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with <i>m</i>/<i>z</i> by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 <i>m</i>/<i>z</i>. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in <i>m</i>/<i>z</i> yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"></p><h4><strong>Conclusion</strong></h4><p>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T<sub>4</sub> binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.</p><p>Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of <i>m</i>/<i>z</i> domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 <i>m</i>/<i>z</i> range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a></p>

Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology

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Waters ACQUITY QDa II Mass Detector

The ACQUITY™ QDa™ II Mass Detector enhances efficiency and productivity in separations workflows with advanced technology.

<h3><strong>Advancing the Power of Mass Detection</strong></h3><ul><li><strong>Identify Everything in Your Sample with Complete Confidence&nbsp;</strong></li></ul><h5><strong>Information-rich mass spectral data starts here&nbsp;</strong></h5><p><strong>Built on a solid foundation of groundbreaking technology, the ACQUITY™ QDa™ II Mass Detector provides even more efficiency and productivity of separations workflows, providing information-rich mass spectral data, ensuring compliance, and regulatory certainty.</strong></p><h4><strong>SEE MORE COMPOUNDS</strong></h4><p>Greater compound coverage from an extended mass range to support small molecules, large molecules and new modalities. A complementary technique to analog detection for chemicals with no chromophores, ACQUITY QDa II Mass Detector enables you to confirm the identity and purity of more compounds with the power of mass detection.</p><h4><strong>ANALYZE MORE SAMPLES</strong></h4><p>Robust, reliable and requiring no sample-specific adjustment. Simply power on to make informed decisions with the full picture of what’s in your sample. Minimal maintenance along with system performance monitoring ensures maximum uptime.&nbsp;</p><h4><strong>HAVE MORE CONFIDENCE IN THE ROBUSTNESS OF YOUR SEPARATIONS</strong></h4><p>The addition of mass detection to your method development workflow enables fast peak tracking and greater confidence in peak purity, for more robust separations. Combined with industry-leading AQbD method development software, your lab can achieve unprecedented MS peak tracking functionality with the ACQUITY QDa II Mass Detector.</p><h4><strong>STRIVE FOR MORE SUSTAINABILITY</strong></h4><p>Achieve up to a 70% reduction in energy consumption and heat output compared to other vendor’s MS systems. The ACT Environmental Impact Factor Label<strong>*</strong> -- available and published by My Green Lab – provides clear, third-party verified information about the environmental impact of laboratory products, enabling you to make the most sustainable decisions for your organization.</p><p><strong>* </strong>ACT - About (<a target="_blank" rel="noopener noreferrer" href="https://www.mygreenlab.org/">mygreenlab.org</a>)</p><h3><strong>Continuing to Separate Beyond Question</strong></h3><ul><li><strong>Ensure your laboratory is prepared for the future</strong></li></ul><h4><strong>MORE PERFORMANCE</strong></h4><p>Plug and play performance with its intuitive design, complementary to optical detection with the robustness to handle all of your analyses. Working in harmony with your chromatography, it’s pre-optimized to work with your samples, without the sample-specific or user adjustments typical of traditional mass spectrometers.</p><h4><strong>MORE EFFICIENCY</strong></h4><p>The intuitive design of the ACQUITY QDa II Mass Detector provides additional data without cost or complexity. The most information you can get out of your separation for complete characterization. In synergy with optical detection, you can significantly reduce the chance that a sample component will go undetected helping to mitigate risk and ensuring a sound return on your investment.</p><h4><strong>MORE SUSTAINABILITY</strong></h4><p>Purposeful innovation, a stackable mass detector that seamlessly integrates into existing workflows resulting in less bench space and more energy efficient. Minimal cleaning and routine maintenance ensuring maximum uptime. Compatible with green solvents ensuring reduced environmental impact.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_3_f98f84c080.jpg" alt="Waters ACQUITY QDa II Mass Detector." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_3_f98f84c080.jpg 234w," sizes="100vw" width="1024" height="682"></p><ul><li>Simply power on, and you’re ready to go</li><li>Zero user set-up optimization, calibration, or adjustment</li><li>Run your analyses − it just works</li><li>When you’re done, just power-off</li></ul><h3><strong>The Perfect Partner</strong></h3><h4><strong>Designed for compatibility with your chromatography&nbsp;</strong></h4><p>Meet all your chromatography requirements with Waters chromatography systems, including our dependability and flexibility ranges of HPLC systems, performance range of UPLC systems, and our purification and specialty systems.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_The_Perfect_Partner_Designed_for_compatibility_with_your_chromatography_1042adecb0.jpg" alt="Waters ACQUITY QDa II Mass Detector: The Perfect Partner. Designed for compatibility with your chromatography." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_The_Perfect_Partner_Designed_for_compatibility_with_your_chromatography_1042adecb0.jpg 189w," sizes="100vw" width="1299" height="1074"></p><h3><strong>Effortless Integration</strong></h3><h4><strong>Achieve more with flexible software solutions</strong></h4><p>Process, Interpret, visualize, and compare the most complex data, and turn it into meaningful information quickly and simply. With integrated optical and mass detector data processing workflows, you can also analyze mass spectral data in the same way as you do photo diode array (PDA) data.</p><p>The ACQUITY QDa II Mass Detector is fully compatible with Masslynx™ Software and its suite of data processing application managers. Empower™ Software, our industry-leading chromatography data software platform is also fully compatible providing the ultimate flexibility.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_Effortless_Integration_Achieve_more_with_flexible_software_solutions_4fd6e9f0d8.jpg" alt="Waters ACQUITY QDa II Mass Detector: Effortless Integration. Achieve more with flexible software solutions." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_Effortless_Integration_Achieve_more_with_flexible_software_solutions_4fd6e9f0d8.jpg 245w," sizes="100vw" width="1397" height="422"></p><h4><strong>EMPOWER CHROMATOGRAPHY DATA SYSTEM (CDS)</strong></h4><p>Simplifying the way you collect, manage, and report chromatography test results is critical to your lab efficiency. With a suite of flexible functionalities that grows to meet your changing quality, business, and laboratory needs, Empower CDS has been purposefully designed to help you address your most demanding chromatographic, regulatory, and networking challenges.</p><h4><strong>EMPOWER LAB MANAGEMENT SYSTEM (LMS)</strong></h4><p>Automating your lab workflow, from sample creation to data archival, is critical for maintaining data integrity and enhancing productivity. Manage your data all from a single, simple dashboard for an integrated approach to your product lifecycle management so you can reduce transcription errors, increase efficiency, and maximize data durability.</p><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1544"><strong>waters_connect™</strong></a><strong> SYSTEM MONITORING</strong></h4><p>Monitor all Empower Software-controlled chromatography systems remotely, at any time, from anywhere. Dynamically plan laboratory activities, monitor the status of your laboratory and maximize productivity. Troubleshoot and respond to errors faster, increasing system uptime.</p><h3><strong>Identify More in Released Glycan Analysis</strong></h3><h4><strong>Unlock the full potential of your QC glycan testing</strong></h4><p>While non-MS methods offer routine QC capabilities, they fall short in delivering the detailed characterization, crucial for biopharmaceutical development. The ACQUITY QDa II Mass Detector with extended mass range revolutionizes routine analysis, offering accurate QC monitoring of N-glycan species with speed and precision. Coupled with Waters chromatography systems, enjoy enhanced MS response with uniform charge state for accurate quantitation, enabling scrutiny of released N-glycan profiles in under 40 minutes per sample. Complement fluorescence (FLR) detection and embrace reproducible, quantitative separation for rapid decision-making.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_Selected_Ion_Recording_SIR_chromatogram_of_doubly_charged_components_of_a_glycan_sample_Highlighted_additional_components_identified_s_a_result_of_the_extended_mass_range_ac0160e74d.jpg" alt="Waters ACQUITY QDa II Mass Detector: Selected Ion Recording (SIR) chromatogram of doubly charged components of a glycan sample. Highlighted additional components identified s a result of the extended mass range." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_Selected_Ion_Recording_SIR_chromatogram_of_doubly_charged_components_of_a_glycan_sample_Highlighted_additional_components_identified_s_a_result_of_the_extended_mass_range_ac0160e74d.jpg 238w," sizes="100vw" width="1347" height="883"></p><h3><strong>Unparalleled Robustness for More Qualitative and Quantitative Performance</strong></h3><h4><strong>Reduce the risk of genotoxic impurities formation in drug manufacturing</strong></h4><p data-start="0" data-end="296">Support risk assessment through routine monitoring of excipients and raw materials in drug manufacturing. Accessible, regulatory compliant-ready LC-MS solutions provide an efficient and cost-effective approach in mitigating the risk of impurity formation during the manufacture of drug product.</p><p data-start="298" data-end="768">Nitrite, a critical risk factor in N-Nitrosamine formation, presents as an impurity in pharmaceutical excipients, often in parts per million (ppm). The ACQUITY QDa II Mass Detector is a robust and reliable solution for routine analysis of nitrite in excipients. With automated resolution, tuning, and calibration during start-up, the ACQUITY QDa II Mass Detector eliminates the need for analyst intervention, ensuring seamless operation and precise results every time.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_Over_29_days_of_rigorous_testing_it_flawlessly_executed_approximately_6000_injections_with_minimal_downtime_02a496f422.jpg" alt="Waters ACQUITY QDa II Mass Detector: Over 29 days of rigorous testing, it flawlessly executed approximately 6000 injections with minimal downtime." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_Over_29_days_of_rigorous_testing_it_flawlessly_executed_approximately_6000_injections_with_minimal_downtime_02a496f422.jpg 245w," sizes="100vw" width="1185" height="529"></p><p data-start="770" data-end="1012" data-is-last-node="" data-is-only-node="">Empower CDS reporting functionality offers simple reviewing of excipient nitrite concentration within a sample batch. This allows for fast and comprehensive decision making, while ensuring compliance and data integrity within your laboratory.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_Example_of_Empower_CDS_generated_data_report_for_nitrite_content_in_a_maize_starch_sample_2f106193ee.jpg" alt="Waters ACQUITY QDa II Mass Detector: Example of Empower CDS generated data report for nitrite content in a maize starch sample." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_Example_of_Empower_CDS_generated_data_report_for_nitrite_content_in_a_maize_starch_sample_2f106193ee.jpg 245w," sizes="100vw" width="937" height="585"></p><h3><strong data-start="0" data-end="62">Improving Efficiency with a More Sustainable Mass Detector</strong></h3><h4><strong>Low operational costs and environmental footprint</strong></h4><p data-start="123" data-end="346"><strong>As a leading technology innovator in chromatography, mass spectrometry, and thermal analysis instruments and software, Waters shares a common mission with our customers: to leave the world a better place than we found it.</strong></p><p data-start="348" data-end="674" data-is-last-node="" data-is-only-node="">Many of our customers are actively working to address environmental sustainability in balance with the need to continually reduce operational costs. Waters has addressed these challenges by providing an instrument with low electricity consumption and BTU/hr output – lessening the need for air conditioning and lowering costs.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_ACQUITY_Q_Da_II_Mass_Detector_Improving_Efficiency_with_a_More_Sustainable_Mass_Detector_Low_operational_costs_and_environmental_footprint_a9e182ea1f.jpg" alt="Waters ACQUITY QDa II Mass Detector: Improving Efficiency with a More Sustainable Mass Detector. Low operational costs and environmental footprint." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_ACQUITY_Q_Da_II_Mass_Detector_Improving_Efficiency_with_a_More_Sustainable_Mass_Detector_Low_operational_costs_and_environmental_footprint_a9e182ea1f.jpg 245w," sizes="100vw" width="1124" height="389"></p><p><strong>*</strong>From competitor A Specification Sheet.</p><p><strong>**</strong>From competitor B Site Preparation Checklist</p><h3><strong>Unrivaled Support</strong></h3><h3><strong>Ensure your success with world-renowned services</strong></h3><p data-start="77" data-end="464" data-is-last-node="" data-is-only-node="">Waters Service and Support helps maintain peak system performance, minimize downtime, address scientific challenges, and meet compliance requirements.&nbsp;</p><p>Waters award-winning consistent quality support, professional services, and education ensure your success wherever your laboratory is located in the world. With Waters service and support offerings<strong>*</strong> for your ACQUITY QDa II Mass Detector, you can</p><h4><strong data-start="0" data-end="30">GET UP AND RUNNING QUICKLY</strong></h4><p data-start="0" data-end="235">Get the onsite training and consultation you need to integrate the ACQUITY QDa II Mass Detector into your laboratory and assist with data migration and method transfer needs with Waters Professional Services.</p><h4><strong data-start="237" data-end="276">MEET YOUR LAB’S UNIQUE REQUIREMENTS</strong></h4><p data-start="237" data-end="460">Protect your instrument investment with the comprehensive portfolio of service plans from Waters FlexCHOICE™, which provides access to the most in-depth and up-to-date knowledge of the advanced science and technologies within Waters systems.</p><h4><strong data-start="462" data-end="487">FACILITATE COMPLIANCE</strong></h4><p data-start="462" data-end="635">Simplify the process of qualification, and record-keeping so that your business can focus on delivering products to market with Waters Compliance Services – so you can meet the regulations in your industry and in the countries where you conduct business.</p><h4><strong data-start="637" data-end="671">REDUCE TOTAL COST OF OWNERSHIP</strong></h4><p data-start="637" data-end="864">FlexCAPITAL™ <strong>**</strong> is designed to support continuous laboratory operation while satisfying the budgeting challenges of a constantly shifting landscape. Minimize total cost of ownership while optimizing instrument performance and protecting your organization from security risks associated with outdated software platforms.</p><h4><strong data-start="866" data-end="903">LEVERAGE YOUR EXISTING TECHNOLOGY</strong></h4><p data-start="866" data-end="1104" data-is-last-node="" data-is-only-node="">With the FlexUP™ Technology renewal program, you can upgrade your older single quadrupole mass spectrometry system to the ACQUITY QDa II Mass Detector -- improving performance, results, and productivity while controlling costs and mitigating compliance risk.</p><p><strong>*</strong> Availability of offerings varies by country. Contact Waters or your local Waters representative for details<br><strong>**</strong> FlexCAPITAL payment plan options and availability may vary by country. Other restrictions may apply.</p>

Waters RADIAN ASAP Direct Mass Detector

Combining flexibility, ease of operation, and speed without the need for complex sample preparation, separation or extensive MS experience, the RADIAN ASAP helps you and your laboratory achieve more.

<div><div id="title-a9e634f6cb" data-locator="title-with-text"><h3><strong>The power of knowing now</strong></h3></div></div><div><div id="text-c687cac6aa" data-locator="text"><p><strong>Whether you are looking to improve your drug discovery cycle, expand your client services, or simply become more competitive in your turnaround times, integrating direct mass spectrometry (MS) analysis can drive multiple system-wide efficiencies helping to achieve your operational goals.</strong></p><p>Combining flexibility, ease of operation, and speed without the need for complex sample preparation, separation or extensive MS experience, the RADIAN ASAP helps you and your laboratory achieve more.</p><ul><li>Simple operation and data interpretation</li><li>Minimal sample preparation</li><li>No separation required</li><li>Real-time results and classification</li></ul><figure class="image"><img style="aspect-ratio:454/321;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_RADIAN_ASAP_7cfe24b23d/Waters-RADIAN-ASAP_s.webp" alt="Waters RADIAN ASAP Direct Mass Detector" width="454" height="321"></figure><h3><strong>Overview</strong></h3><div data-locator="section-container-body"><div><div><div data-locator="layoutcontainer-"><div><div id="text-6b896f6da4" data-locator="text"><ul><li>Ensure users get up and running quickly with RADIAN ASAP’s easy to learn and fully automated set up, streamlined workflow, and minimal training requirements</li><li>Minimize sample prep with direct sampling onto glass probe</li><li>Minimize the need for solvent use and disposal with no chromatography</li><li>Save time with 30 second analysis and real-time sample classification</li></ul></div></div><div><div id="text-161a2a5c01" data-locator="text"><h4><strong>Recommended Use</strong></h4><p>For rapid, easy, and low-cost analysis of liquids and solids.</p><div><div id="text-4973311325" data-locator="text"><h3 data-locator="modal-title"><strong>Compact without compromise</strong></h3><p>The RADIAN ASAP is a novel, dedicated direct analysis system specifically designed for rapid, easy and low-cost analysis of liquids and solids. Engineered using proven and robust single quadrupole mass spectrometry technology combined with the Atmospheric Pressure Solids Analysis Probe (<a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/nextgen/us/en/services/instrument-services/instrument-upgrades/mass-spectrometry-ms-upgrades/atmospheric-solids-analysis-probe.html" data-di-id="di-id-70d78c77-7e033f9d">ASAP</a>), the RADIAN ASAP delivers quality and ease of use in a compact footprint.&nbsp;</p><p>This single quadrupole mass detector provides high quality mass spectral data, without the need for any special training or expertise, eliminating any need to contract out and wait for results from specialist analytical service laboratories.</p></div></div><div><div id="text-08366f2c0d" data-locator="text"><h3 data-locator="modal-title"><strong>Flexible workflow solutions in 4 simple steps</strong></h3><p>Operation of the RADIAN ASAP is simple and intuitive, allowing users to generate results with minimal or no sample preparation, making it an ideal tool for laboratories to make informed decisions. Capable of ionizing molecules directly from a liquid or solid makes the system available to a wide range of applications and workflows.</p><h4><strong>Generate results in 4 simple steps:</strong></h4><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_RADIAN_ASAP_analyza_ve_4_jednoduchych_krocich_a997bfddda/Waters-RADIAN-ASAP-analyza-ve-4-jednoduchych-krocich.jpg" alt="Waters RADIAN ASAP Direct Mass Detector: Flexible workflow solutions in 4 simple steps" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_RADIAN_ASAP_analyza_ve_4_jednoduchych_krocich_a997bfddda/thumbnail_Waters-RADIAN-ASAP-analyza-ve-4-jednoduchych-krocich.jpg 245w," sizes="100vw" width="1683" height="490"></p><h3><strong>Ideal for numerous application requirements</strong></h3><p><a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/nav.htm?cid=135078611" data-di-id="di-id-7f758d90-ccee23de"><strong>Rapid triage of seized drug materials for Forensics</strong></a><i>&nbsp;<strong>—</strong>&nbsp;</i>RADIAN ASAP and LiveID ensure crime labs can quickly screen samples against a library of known compounds for rapid, confident identification of illicit drugs. The sensitivity and selectivity of mass spectrometry provides confidence in detecting drugs with an easy, efficient triage workflow.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/nav.htm?cid=134528742" data-di-id="di-id-3a3c46e4-ccee23de"><strong>Assess food integrity for Food &amp; Environmental</strong></a>&nbsp;<strong>—</strong> The threat posed by food fraud has created additional demands on both the food industry and regulators to protect food consumers and maintain brand reputation. RADIAN ASAP and LiveID offer a powerful combination of mass spectrometry and chemometric modeling, allowing users to easily and efficiently screen samples and make quicker decisions.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.tainstruments.com/radian-asap-direct-mass-detector/" data-di-id="di-id-2fac456-44144a9d"><strong>Fast chemical analysis for improved formulation testing in Chemical and Materials</strong></a><i>&nbsp;<strong>—</strong>&nbsp;</i>RADIAN ASAP and IonLynx supports quality control (QC) and development labs in the chemical industry to reduce costs and increase efficiencies. Streamline workflows like fast chemical analysis for improved formulation testing or&nbsp;material release testing. Features including thermal gradient analysis are ideal for the complex samples in the chemical industry.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/nav.htm?cid=134751395" data-di-id="di-id-76921eaa-ccee23de"><strong>Discovery reaction monitoring&nbsp;for Pharma</strong></a>&nbsp;<strong>—</strong> The demand to accelerate the drug discovery and development process has never been higher.&nbsp;RADIAN ASAP provides synthetic chemists easy access to mass spectral data for near-instantaneous assessment of reaction progress and identification of purification fractions, increasing lab efficiency.</p><div><div><div><div id="text-8b0fa56c8c" data-locator="text"><p><a target="_blank" rel="noopener noreferrer" href="https://www.waters.com/waters/nav.htm?cid=134971387" data-di-id="di-id-10e51f17-ccee23de"><strong>Undergraduate teaching&nbsp;and method development&nbsp;in Academia</strong></a><strong> —&nbsp;</strong>Simplicity and ease of use makes RADIAN ASAP the ideal tool for busy academic laboratories that need a robust and reliable solution.</p><figure class="image"><img style="aspect-ratio:474/308;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_RADIAN_ASAP_2_87ddc46f15/Waters-RADIAN-ASAP-2_s.webp" alt="Waters RADIAN ASAP Direct Mass Detector" width="474" height="308"></figure><div><div id="text-a5e5e26910" data-locator="text"><h3 data-locator="modal-title"><strong>Software solutions for your data requirements</strong></h3><p><strong>RADIAN ASAP</strong> is compatible with software solutions for rapid interpretation and classification as well as automated data processing and reporting.</p><p>For customers investigating the authenticity, adulteration, and quality of food or raw materials, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=5&amp;search=liveid"><strong>LiveID</strong></a> uses statistical models to classify samples. First, authentic or verified samples are used to create and validate a statistical model. The validated model can then be used with test samples and generate live classifications with a simple yes/no answer output. LiveID can also do real time <strong>library</strong> matching workflows, where the software matches all compounds in the library against each sample analyzed, giving a score out of <strong>1000</strong>, where values close to 1000 indicate the compound of interest is likely in the sample and lower scores indicate unlikely presence in the sample.</p><p><strong>OpenLynx</strong> processing provides user customizable processing capabilities to generate automated mass confirmation reports in either pdf, printed or browser format.&nbsp;</p><p><strong>IonLynx</strong> allows users to determine levels and relative ratios of analytes of interest in complex samples to aid decision making in QC and formulation monitoring. IonLynx provides automated processing and reporting of non-chromatographic data sets, such as those generated by RADIAN ASAP.</p></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div>

Products from category Single quadrupoles distributed by Waters Corporation (Europe) - page 1

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