<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

<p><strong>Eurachem and CITAC welcome analysts interested in the evaluation of chemical analysis uncertainty and in how to use this information in results interpretation. The Eurachem Week 2026 will begin with a training course on “Evaluation of the measurement uncertainty from in-house precision and recovery data” scheduled for Sunday, 10 May 2026. A two-days workshop on “Quality in Analytical Measurements: Uncertainty Evaluation and Results Interpretation” open to all interested participants will take place from 11 to 12 May 2026. On 13 May 2026, the Eurachem Working Groups will convene, followed by the Eurachem General Assembly, which will bring together the Executive and national delegates on 14 and 15 May. Both Working Group Meetings and the General Assembly are restricted to their members.</strong></p><p>The results of qualitative and quantitative chemical analyses should have an acceptable uncertainty, which should ideally be reported and considered in results interpretation.</p><p>For many analytical applications, simplified uncertainty evaluations can determine uncertainty values that meet the defined requirements for this parameter. The workshop will focus on the key technical challenges involved in practical evaluations of measurement uncertainty based on precision and recovery data gathered during in-house method validation and quality control. There will be a discussion of how to model the variation of the measurement uncertainty within the analytical range and how to handle divergent recovery values from the analysis of various reference materials. A session on the use of measurement uncertainty in conformity assessment will explore how the risk of false conformity decisions can be managed.</p><blockquote><h5><strong>New Eurachem guidance on using in-house precision and recovery data will be discussed at the workshop.</strong></h5></blockquote><p>Topics will also include the validation and uncertainty evaluation for qualitative analyses with particular attention to current accreditation requirements for these types of analysis. The last session of the workshop will be dedicated to the evaluation of measurement uncertainty arising from sampling and using it to judge the fitness for purpose, and hence validation, of measurement procedures that include sampling. Four sessions of the workshop will include engaging breakout sessions where participants will have the chance to share their views about challenging aspects of the analytical work. Participants are invited to propose posters and oral communications on session topics or any other relevant topic for analytical chemists or stakeholders of the analytical work.</p><h3><strong>Registration</strong></h3><blockquote><p class="cke-user_style-important"><strong>👉</strong><a target="_blank" rel="noopener noreferrer" href="https://conferences.chemistry.pt/register/eurachem2026"><strong>Register here for the workshop</strong></a></p></blockquote><h4><strong>Registration Fees</strong></h4><h5><strong>Early bird (EUR) - Until April 15th</strong></h5><ul><li><strong>Workshop: Regular participant (11 &amp; 12 May 2026): </strong>400 EUR</li><li><strong>Workshop: Student (11 &amp; 12 May 2026): </strong>250 EUR</li><li><strong>Eurachem Working Group<sup>1</sup> (13 May 2026):</strong> 75</li><li><strong>General Assembly<sup>2</sup> (14 &amp; 15 May 2026): </strong>250</li><li><strong>Training On Uncertainty Evaluation<sup>3</sup> (10 May 2026):</strong> 150</li></ul><h5><strong>After April 15th</strong></h5><ul><li><strong>Workshop: Regular participant (11 &amp; 12 May 2026): </strong>450 EUR</li><li><strong>Workshop: Student (11 &amp; 12 May 2026):</strong> 300 EUR</li><li><strong>Eurachem Working Group<sup>1</sup> (13 May 2026): </strong>100</li><li><strong>General Assembly<sup>2</sup> (14 &amp; 15 May 2026):</strong> 300</li><li><strong>Training On Uncertainty Evaluation<sup>3</sup> (10 May 2026): </strong>200</li></ul><blockquote><p>§ - <strong>50 EUR reduction for members of Eurachem</strong>, CITAC, SPQ, RELACRE, ForMEQ and SPMet at the workshop.</p><p>10% reduction for organisations that registered more than one participant.</p><p><sup>1 </sup>- Working group members</p><p><sup>2</sup> - Eurachem members</p><p><sup>3</sup> - 50% reduction for workshop participants</p></blockquote><h3><strong>Workshop</strong></h3><h4><strong>Eurachem/CITAC Workshop on Quality in Analytical Measurements:</strong></h4><h5><strong>Uncertainty Evaluation and Results Interpretation</strong></h5><p>The results of qualitative and quantitative chemical analyses should have an acceptable uncertainty, which should ideally be reported and considered in results interpretation. For many analytical applications, simplified uncertainty evaluations can determine uncertainty values meeting defined requirements for this parameter. The workshop will focus on the key technical challenges involved in practical evaluations of measurement uncertainty based on precision and recovery data gathered during in-house method validation. It will be discussed how to model the variation of the measurement uncertainty within the analytical range and how to handle divergent recovery values from the analysis of various reference materials. A session on the use of measurement uncertainty in conformity assessment will explore how the risk of false conformity decisions can be managed.</p><p>Topics will also include the validation and uncertainty evaluation of qualitative analyses with particular attention to current accreditation requirements for these types of analysis. The last session of the workshop will be dedicated to the evaluation of measurement uncertainty arising from sampling and using it to judge the fitness for purpose, and hence validation, of measurement procedures that include sampling.</p><p>Four sessions of the workshop will include engaging breakout sessions where participants will have the chance to share their views about challenging aspects of the analytical work. Participants are invited to propose posters and oral communications on session topics or any other relevant topic for analytical chemists or stakeholders of the analytical work.</p><h3><strong>Training Course</strong></h3><h4><strong>Evaluation of the measurement uncertainty from in-house precision and recovery data</strong></h4><ul><li>10 May 2026</li></ul><p>A course on the fundamentals of the evaluation of the measurement uncertainty from in-house precision and recovery data will be held on Sunday, 10 May 2026. This training is targeted for analysts with a basic understanding of the measurement uncertainty concept, how uncertainty components propagate, and how the combined uncertainty is expanded. Following the morning presentation of the theory of uncertainty evaluation, the afternoon will be dedicated to applying the theory to real-world cases. Trainees should have basic skills in using Microsoft Excel spreadsheets and bring a laptop with Microsoft Excel to complete the exercises. The interaction between trainers and trainees will be promoted to guarantee learning efficiency.</p><h5><strong>Trainers:</strong></h5><ul><li>Ricardo Bettencourt da Silva, Faculdade de Ciências da Universidade de Lisboa, Portugal (rjsilva@ciencias.ulisboa.pt)</li><li>Stephen L. R. Ellison - UK National Measurement Laboratory (NML) hosted at LGC, United Kingdom</li><li>Vicki Barwick - UK National Measurement Laboratory (NML) hosted at LGC, United Kingdom</li></ul><h4><strong>Agenda</strong></h4><h5><strong>8:00 Registration</strong></h5><h5><strong>9:00 Opening</strong></h5><h5><strong>9:05 Identifying, combining, and expanding uncertainty components: Theory and examples</strong></h5><h5><strong>9:45 Precision uncertainty: Theory and examples</strong></h5><h5><strong>10:30 </strong>Coffee break</h5><h5><strong>10:50 Trueness-related uncertainty: Theory and examples</strong></h5><h5><strong>12:00 Additional questions and discussion</strong></h5><h5><strong>12:30 </strong>Lunch</h5><h5><strong>13:30 Application example 1</strong></h5><h5><strong>15:30 </strong>Coffee break</h5><h5><strong>15:50 Application example 2</strong></h5><h5><strong>17:00 Additional questions and discussion</strong></h5><h5><strong>17:30 Closing</strong></h5><h3><strong>Venue</strong></h3><p>The series of Eurachem events will be held in:</p><ul><li>Meliã Lisboa Aeroporto ****</li><li>Rua C,2 1749-125 Lisboa, Portugal&nbsp;</li></ul>

Eurachem/CITAC Workshop on Quality in Analytical Measurements 2026

Article

Events

Webinars

Scientific article

Science and research

Eurachem is a European network promoting international traceability of chemical measurements and good analytical practice. It provides expert guidance, supports method validation, uncertainty evaluation, proficiency testing, and facilitates discussion on technical and policy issues in analytical quality.

Eurachem

Everything from the world of analytical chemistry in one place. We connect people in solving their problems. At Labrulez you will find all the necessary information easily, quickly and clearly. Stop searching and start finding.

LabRulez

New Food magazine

Agilent Technologies

Bruker

Thermo Fisher Scientific

SelectScience

Waters Corporation

<p><strong>Reversed-phase high-performance liquid chromatography (RP-HPLC) is a cornerstone technique for peptide analysis due to its exceptional resolving power. In this webinar, we will explore how to optimize RP-HPLC parameters for effective separation of peptides derived from protein digests and analysis of PTMs analysis. Key topics include the role of stationary phase chemistry in influencing selectivity, and how column physical characteristics affect separation performance. We will also examine how mobile phase modifiers—such as trifluoroacetic acid (TFA), formic acid, and pH—impact chromatographic outcomes and compatibility with mass spectrometry (MS). Attendees will gain practical insights into method development strategies that enhance both resolution and detection sensitivity.</strong></p><blockquote><p><strong>Presenter: </strong>Mohit Patel (Application Engineer, Agilent Technologies, Inc.)</p><p>Mohit Patel is part of the CSD Online AE Team. His primary focus is to support SMLC, Bio-Columns, and consumables.</p><p>Before joining Agilent, Mohit was an Assistant Professor of Chemistry at Temple University. Mohit developed his passion for science through his experiences as a faculty researcher and a mentor. Mohit actively taught, developed curriculum, and served as senior personnel, with a leadership position, on funded grants, mentored research projects, and co-coordinator of STEAM related outreach services.</p><p>Mohit has earned a Doctorate degree in Chemistry from Temple University in 2016.</p></blockquote>

Agilent Technologies: Advanced RP-HPLC Techniques for Peptide Analysis: From Column Chemistry to Mobile Phase Modifiers

Advanced RP-HPLC Techniques for Peptide Analysis: From Column Chemistry to Mobile Phase Modifiers

We will explore how to optimize RP-HPLC parameters for effective separation of peptides derived from protein digests and analysis of PTMs analysis.

Advanced RP-HPLC Techniques for Peptide Analysis

<p><strong>Discover how modern Listeria monitoring solutions can support faster, more reliable food and environmental testing, and help elevate your laboratory’s efficiency and confidence in results.</strong></p><p>Listeria remains one of the most challenging pathogens for the food industry due to its ability to persist in production environments and survive under conditions that inhibit many other bacteria, including refrigeration and high-salt processing. Its association with severe illness and food recalls places ongoing pressure on manufacturers and laboratories to detect contamination quickly and reliably across both food and environmental samples.</p><p>This webinar will explore how Listeria monitoring solutions are evolving to meet these demands, particularly for laboratories balancing speed, cost and operational complexity. Traditional culture methods can delay critical decisions, while PCR and ELISA often require significant capital investment, infrastructure changes and specialist training, creating barriers for low to medium-throughput operations.</p><p>Using <strong>Solus NanoFast™</strong> Listeria as a practical example, the session will demonstrate how alternatives to culture, <strong>PCR, and ELISA</strong> can support next-day detection through simplified workflows that reduce training requirements and infrastructure changes. The discussion will also highlight how automated result interpretation and digital data management can improve consistency, traceability and audit readiness.</p><h4><strong>During the session, you will learn how to:</strong></h4><ul><li>Address common challenges in food and environmental Listeria monitoring</li><li>Evaluate cost-effective alternatives to culture, PCR, and ELISA for low to medium-throughput testing (up to ~50 samples/day)</li><li>Improve turnaround times without increasing workflow complexity</li><li>Support audit readiness through objective results and digital traceability</li><li>Align Listeria testing strategies with operational and regulatory requirements</li></ul><p>Whether you’re overseeing environmental monitoring or finished product testing, this session will deliver practical insights to optimise Listeria testing workflows for efficiency, consistency and confidence in results. Don’t miss this opportunity to streamline your approach to food and environmental Listeria monitoring.</p><blockquote><p><strong>Presenter:</strong> Nathan Welch, Product Manager at PerkinElmer (Solus)</p><p>Nathan Welch brings over 25 years of expertise in food safety and quality assurance to the stage. His career spans diverse roles that have shaped his deep understanding of the industry. Starting with two years in a food testing contract laboratory, Nathan advanced into nine years specializing in culture media testing at Oxoid/Thermo Fisher, where he honed his technical and analytical skills.</p><p>He later transitioned into technical support at Thermo Fisher, providing critical guidance to clients and teams, before moving into product management, a role he has been in for the past 13 years, including nine years at Thermo Fisher and four years at Solus.</p><p><strong>Presenter: </strong>Jean-Paul Anthony, Application Scientist at PerkinElmer (Solus)</p><p>J-P Anthony is the Applications Scientist for Solus/PerkinElmer contributing to training in the techniques and equipment for food pathogen testing. Prior to this he was a Senior Developmental Scientist and created many aspects of the enzyme and luminescent-based immunoassays including bacterial broth development from the time of the company’s inception in 2009. He trained in Immunology and Pharmacology at the University of Strathclyde before obtaining a PhD in novel drug discovery to combat protozoan parasitical infections at Queen Margaret University, Edinburgh.&nbsp;</p></blockquote>

New Food Magazine: Rethinking Listeria monitoring: faster, simpler solutions for food safety & environmental testing

Rethinking Listeria monitoring: faster, simpler solutions for food safety & environmental testing

How Listeria monitoring solutions are evolving to meet these demands, particularly for laboratories balancing speed, cost and operational complexity.

Listeria monitoring for food safety & environmental testing

<p><strong>In recent years, glucagon-like peptide-1 receptor (GLP-1R) agonists have gained significant attention because of their effectiveness to treat obesity and type 2 diabetes. The global market for GLP-1 analogues is projected to grow rapidly, reaching $260 billion by 2034. Developing sensitive bioanalytical assays to determine pharmacokinetics and toxicokinetics is crucial for advancing these medications.&nbsp;</strong></p><p>Traditionally, the plasma concentration of GLP-1 analogs was measured by ligand binding assay, which requires time to develop antibody and lack selectivity and specificity. Liquid chromatography-mass spectrometry (LC/MS), which is used for sequence identification of GLP-1 receptor agonists, has emerged as an alternative methodology to precise quantify these molecules in biological matrix because of its superior sensitivity, wide dynamic range, and high specificity. Here we present an automated workflow, which combines automation and LC/MS technologies, to quantify GLP-1 analog drug in human plasma by using an Agilent 1290 Infinity II Bio LC and an Agilent 6495D triple quadrupole system (Figure 1). Our results indicate that this automated LC/MS workflow can enhance assay sensitivity by five times compared to traditional organic solvent precipitation.&nbsp;</p><p>This workflow can be used for quantitative analysis of GLP-1 therapeutics without the need to have specific antibody while providing excellent sensitivity, high specificity and fast method development, which will play a crucial role in drug discovery and development.</p><blockquote><p><strong>Presenter: </strong>Xi Qiu, PhD (LC-MS Application Scientist, Agilent Technologies, Inc.)</p><p>Xi Qiu is application scientist at Agilent, he has extensive experience using LC-MS for large molecules analysis including protein, protein conjugates, peptide, and oligos. He earned his Ph.D. degree from the department of Pharmacognosy and Medicinal Chemistry at University of Illinois at Chicago focusing on benefits and safety of botanical dietary supplements and herbal-drug interactions. After graduation, he did his postdoc training at Pfizer and Bristol Myers Squibb where he worked on drug transporters protein expression analysis in tissues as well as drug induced liver injury mechanism. He then worked for two major contract research organizations leading their large molecule LC-MS group performing protein, protein conjugates, peptide, and oligos pharmacokinetics/toxicokinetics analysis under GLP/regulated environment. Prior to joining Agilent, he worked at Johnson and Johnson where he focused on large molecule quantification using LC-MS at intact and peptide level.</p></blockquote>

Thermo Fisher Scientific: Comprehensive workflow for Automated Sample Cleanup and Sensitive Quantitation of Glucagon-like peptide-1 (GLP-1) Analogs from Plasma

Comprehensive workflow for Automated Sample Cleanup and Sensitive Quantitation of Glucagon-like peptide-1 (GLP-1) Analogs from Plasma

Discover automated LC/MS approach for GLP-1 bioanalysis with Agilent, delivering higher sensitivity, specificity, and assay development without antibodies.

Automated Sample Cleanup & Sensitive Quantitation of GLP-1

<div><p><strong>Lipid nanoparticles (LNPs) and liposomal drug products present unique analytical challenges due to their structural complexity and sensitivity to formulation and processing conditions.</strong></p><p>Regulatory guidance from the FDA, EMA, and USP highlights critical quality attributes (CQAs) such as particle size, surface charge, morphology, and encapsulation efficiency as essential for ensuring product quality, consistency, and performance.</p><p>This webinar introduces field-flow fractionation coupled with multi-angle light scattering (FFF-MALS) as a powerful platform for comprehensive LNP and liposome characterization. We will review the fundamental principles of FFF-MALS and demonstrate how the technique enables size-resolved measurement of key CQAs while preserving native particle structure. Practical guidance on method development, implementation, and best practices will be shared to help achieve robust, reproducible, and regulatory-relevant results.</p><h4><strong>Top 3 Key Takeaways:</strong></h4><ul><li>Review recent and upcoming regulatory changes affecting LNP and liposomal drug CQAs</li><li>Learn how FFF‑MALS can address critical quality attributes</li><li>Discover resources and practical tips for implementation</li></ul><h4><strong>Who should attend?</strong></h4><p>This webinar is designed for you if you are a scientist, analyst, or lab manager working on vaccine, LNP, or liposome characterization, or if you are part of a CDMO, CRO, or testing organization looking to expand analytical capabilities.</p><blockquote><p><strong>Presenter:</strong> Nemal Gobalasingham, Ph.D. (Product Manager, Waters | Wyatt Technology)</p><p>Nemal Gobalasingham is a Product Manager for the Eclipse FFF system and DAWN MALS instrument line. He joined Wyatt Technology in 2018 as an Application Scientist and works closely with customers across a broad range of fields to provide application support and training. Nemal also serves as the Global Training Manager, overseeing and developing Wyatt’s field staff training programs. He earned a B.S. in Chemistry from Syracuse University and a Ph.D. in Chemistry from the University of Southern California, where his research focused on semiconducting polymers and materials science.</p><p><strong>Presenter:</strong> Udayabagya (Bud) Halim (Sr. Marketing Analyst, Waters | Wyatt Technology)</p><p>Bud Halimis a senior marketing analyst at Waters | Wyatt Technology with a PhD in physical chemistry from UCLA. He began his career teaching biochemistry and chemistry and contributing to laboratory manuals before transitioning into the scientific instrumentation industry as an applications scientist. At Waters, he supports researchers in the characterization of peptides, biologics, lipid nanoparticles (LNPs), and viral vectors.</p></blockquote></div>

Waters Corporation: Navigating Regulatory Guidance for LNP and Liposomal Drug Characterization Using FFF-MALS

Navigating Regulatory Guidance for LNP and Liposomal Drug Characterization Using FFF-MALS

Discover how FFF-MALS supports regulatory-ready characterization of LNPs and liposomes by resolving key CQAs like particle size, structure, and consistency.

Regulatory Guidance for LNP and Liposomal Drug By FFF-MALS

<h4><strong>Designing Robust Metabolomics Studies: From Biological Questions to Analytical Success</strong></h4><p><strong>Designing a robust metabolomics study requires balancing biological questions with analytical constraints. This webinar guides researchers through the critical decisions that shape successful outcomes - from sample collection and experimental design to choosing targeted or untargeted methods and the right analytical platforms.</strong></p><p>Attendees will learn practical strategies to minimize bias, enhance data quality, and align methodological choices with study goals. Ideal for scientists seeking clearer pathways through the complexity of metabolomics workflows.</p><h4><strong>Who should attend?</strong></h4><p>This webinar is tailored for professionals who want to strengthen their metabolomics study design, including:</p><ul><li>Academic researchers in biomedical sciences, exposomics, nutrition, and food research</li><li>Pharmaceutical scientists involved in early discovery and translational research</li><li>Anyone seeking practical strategies to reduce bias, improve data quality, and navigate complex metabolomics workflows</li></ul><h4><strong>Key Learning Objectives</strong></h4><ul><li>Understand the core components of metabolomics study design, including biological question definition, cohort selection, and strategies to reduce variability.</li><li>Learn how to choose between targeted, untargeted, and hybrid metabolomics approaches, and know when each method is most appropriate.</li><li>Identify best practices for sample collection, preparation, and QC workflows to ensure high-quality, reproducible data.</li><li>Recognize common pitfalls in metabolomics studies and apply practical strategies to improve robustness, interpretation, and downstream analysis.</li></ul><p><i>Ready to elevate your metabolomics research? Register now to secure your spot!</i></p><blockquote><p><strong>Presenter: </strong>Dr. Elizabeth Want (Associate Professor in Clinical Mass Spectrometry, Imperial College London)</p><p>Dr. Elizabeth Want is a Senior Lecturer in the Department of Metabolism, Digestion and Reproduction. She joined Imperial College in 2006 after working as a postdoctoral researcher at the Scripps Research Institute in La Jolla, CA. Prior to that, Elizabeth obtained her PhD in Clinical Biochemistry from King’s College London. At Imperial College, she became a Lecturer in 2007, Senior Lecturer in 2014 and Head of the Section of Bioanalytical Chemistry in 2022. She is also the Director of the Imperial International Phenome Training Centre which runs several hands-on courses in Metabolomics every year.</p><p>Elizabeth has &gt;25 yrs of experience in mass spectrometry and chromatographic techniques and has spent the past 20 years working in the field of mass spectrometry-based metabolite profiling. Her research focuses primarily on the development and application of novel mass spectrometry (MS) assays for metabolic profiling and on the fusion of mass spectrometric methods with chemometric analysis.</p><p>Her research at Imperial College has involved the development, optimisation and application of UPLC-MS methodologies for the analysis of biological samples. She applies these methods to biomedical research areas including cardiovascular disease, glioblastoma, neurodegenerative disorders and burn injury.</p><p><strong>Presenter:&nbsp;</strong>David Heywood (Senior Manager Biomedical Research Marketing, Waters Corporation)</p><p>David has more than 28 years of experience in the mass spectrometry business and has performed many roles - both in the UK and the Americas,including technical hardware and software support, sales, marketing and business development.</p><p>Now based at Waters’ Mass Spectrometry Head Quarters in Wilmslow UK,David has helped commercialize many of Waters successful high-resolution mass spectrometrybasedsolutions for discovery omics and is now responsible for global marketing strategies of these platforms.</p></blockquote>

Navigating Metabolomics Study Design and Method Choices

Learn how to design robust metabolomics studies—from defining biological questions to selecting targeted or untargeted methods

<div><p><strong>Discover new perspectives on the complexity of high‑grade serous ovarian cancer in our upcoming webinar, where cutting‑edge spatial multiomics meets real clinical impact. Learn how MALDI Imaging, combined with LMD‑based proteomics, spatial transcriptomics, and MALDI HiPLEX-IHC, is revealing previously unseen cellular subpopulations linked to treatment response and patient survival. This integrated strategy uncovers critical interactions between tumor and microenvironment that may drive chemoresistance and could pave the way for improved patient stratification and more personalized therapy. Join us to explore these groundbreaking results and see how spatial biology is transforming the future of cancer research.</strong></p><h4><strong>Key Learning Objectives</strong></h4><ul><li>Learn how combining multimodal technologies can accelerate advanced biomarker discovery in oncology research</li><li>Understand how MALDI Imaging adds valuable, untargeted spatial context to existing transcriptomics, proteomics, or imaging workflows</li><li>Identify molecular subtypes and chemoresistance‑related interactions using spatial multiomics</li></ul><h4><strong>Who Should Attend</strong></h4><ul><li>Researchers in oncology, spatial biology, and multiomics</li><li>Clinical and translational scientists seeking new approaches for biomarker discovery and therapy prediction.</li><li>Pharma and biotech professionals developing targeted therapies or exploring tumor–microenvironment interactions.</li><li>Biologists working with transcriptomics, single‑cell, or microscopy methods who want to expand their capabilities into spatial and discover what MALDI Imaging can add</li><li>Anyone interested in cutting‑edge imaging mass spectrometry and its applications in cancer research</li></ul><blockquote><p><strong>Presenter:</strong> Dr. Oliver Klein, Group Leader, Berlin Institute of Health at Charité, Berlin, Germany</p><p>Dr. Oliver Klein received his master degree in Pharmaceutical/Chemical Engineering at the Beuth University of Applied Sciences and was subsequently focusing on the expression of protein domains to structure elucidation via NMR and mass spectrometry at the Leibniz Institute for Molecular Pharmacology (FMP) Berlin. Since 2007 he is working at the Charité, leading the Proteomics Unit at Berlin-Brandenburg Center for Regenerative Therapies (today BIH Center for Regenerative Therapies) since 2009. 2015 Dr. Klein earned his doctorate in the field of regenerative medicine, focusing on the detection of pathophysiological processes in tissue following cell therapy using Imaging MS and LC MS. From 2022 until today Dr. Oliver Klein leads the “Imaging mass spectrometry Unit at BIH” and is involved in several clinically driven projects including BMBFTR, DFG, EU and industry cooperations.</p></blockquote></div>

Bruker: Making the Invisible Visible: Unlocking the Potential of Imaging Mass Spectrometry in Ovarian Carcinoma and Beyond

Making the Invisible Visible: Unlocking the Potential of Imaging Mass Spectrometry in Ovarian Carcinoma and Beyond

Spatial multiomics in ovarian cancer showing how MALDI Imaging uncovers tumor heterogeneity, chemoresistance mechanisms, and clinically relevant biomarkers.

Imaging Mass Spectrometry in Ovarian Carcinoma

<p><strong>The microbiology laboratory plays a vital role in selecting antimicrobial susceptibility testing (AST) methods to guide treatment of severe infections in critically ill patients. Delayed or inaccurate results, especially in multi-drug-resistant cases, can lead to poor outcomes and higher mortality.</strong></p><p>In this SelectScience webinar Dr. James A. McKinnell, M.D. an infectious disease specialist, will describe how accurate minimum inhibitory concentration (MIC) data can improve turnaround times, optimize therapeutic decisions, and support the use of new treatments. The session will explore how reliable broth microdilution-based MICs for novel antibiotics enhance patient outcomes while reducing length of stay, adverse effects, and costs.</p><p>Join the webinar to learn how antimicrobial stewardship efforts are most effective when supported by timely diagnostics and collaboration among microbiologists, clinicians, stewardship teams, and policymakers, helping to address the global challenge of antibiotic resistance in the post-Covid era.</p><h4><strong>Key learning objectives:</strong></h4><ul><li>Describe the role of the microbiology laboratory in guiding AST for critically ill patients.</li><li>Recognize the value of accurate MIC data in improving turnaround times, optimizing therapy, and supporting new antibiotic use.</li><li>Identify how antimicrobial stewardship programs rely on timely diagnostic data and collaboration to improve patient outcomes.</li><li>Discuss the importance of multidisciplinary collaboration among microbiologists, clinicians, stewardship teams, and policymakers to combat antibiotic resistance in a post-Covid world.</li></ul><h4><strong>Who should attend?</strong></h4><ul><li>Clinical microbiologists, laboratory technicians, lab managers, lab directors, infectious disease specialists, and infectious disease clinicians.</li></ul><h4><strong>Accreditation statement</strong></h4><p>SelectScience® is approved as a provider of continuing education programs in the clinical laboratory sciences by the ASCLS P.A.C.E.® Program. Attendees of these webinars may be entitled to 1.0 ACCENT Continuing Education Credits from the ADLM. This activity was planned in accordance with ACCENT® Standards and Policies. Verification of Participation certificates are provided to registered participants based on completion of the activity, in its entirety, and the activity evaluation. For questions regarding continuing education, please email education@myadlm.org.</p><blockquote><p><strong>Presenter: </strong>Dr. James A. McKinnell (M.D. and Infectious Disease Specialist, Milefchik-Rand Medical Group, Torrance and Memorial Medical Center, Torrance CA)</p><p>Dr. James A. McKinnell is an infectious disease specialist whose research focuses on healthcare-associated infections, particularly VRE, MRSA, and carbapenem-resistant organisms. He has authored over 40 publications on antibiotic optimization and antimicrobial resistance. Dr. McKinnell works closely with skilled nursing facilities in Los Angeles and Orange County (USA) to develop practical infection prevention and stewardship strategies. He also contributes as an invited speaker for the Infectious Disease Association of California and as a committee member for Los Angeles County’s HAI and antimicrobial resistance initiatives.</p><p><strong>Moderator: </strong>Sarah Thomas (Associate Editor, SelectScience)</p></blockquote>

SelectScience: Critical antimicrobial susceptibility testing results for critical patients: A 2025 perspective

Critical antimicrobial susceptibility testing results for critical patients: A 2025 perspective

Antimicrobial susceptibility testing highlighting role of accurate MIC data in optimizing therapy, stewardship, patient outcomes in critical infections.

Antimicrobial susceptibility testing results

<div><h4><strong>Advanced Analytics for Next‑Generation Protein Therapeutics</strong></h4><p><strong>Proteins like monoclonal antibodies (mAbs) and protein conjugates promise higher efficacy and novel targets compared to traditional therapies. Given their biotherapeutic structural complexity, these molecules pose significant analytical challenges, with quality attributes like composition, aggregation, purity, and conformation affecting efficacy and toxicity.&nbsp;</strong></p><p>This webinar explores the comprehensive analysis of Antibody Oligonucleotide Conjugates (AOCs) using Liquid Chromatography-Mass Spectrometry (LC-MS) and Liquid Chromatography-Multi-Angle Light Scattering (LC-MALS). &nbsp;</p><h5><strong>The value you’ll get from attending</strong></h5><ul><li>Discover methodologies for accurate pairing of technology and attribute across the product lifecycle&nbsp;</li><li>Learn about recent advances, with insights into adopting advanced analytics</li><li>Ensure novel and robust analytical capability for the analysis of bioconjugates&nbsp;</li></ul><h5><strong>Who should attend?</strong></h5><p>This webinar is designed for you if you are a scientist, lab manager, director, or analyst involved in protein development, process development, or quality control of AOCs, ADCs, or other protein therapeutics.</p><p><i>Don't miss it!</i></p><blockquote><p><strong>Presenter:</strong> Samantha Ippoliti (Principal Scientist, Biologics Business, Waters Corporation)</p><p>Samantha (Sam) joined Waters (Milford, MA) in 2018 and has worked on a variety of applications for LC-MS based biopharmaceutical characterization, including peptide mapping &amp; intact/subunit analysis, and most recently antibody-oligonucleotide conjugates (AOCs).</p><p>Sam has experience with LC-MS analysis using BioAccord, Xevo series, Synapt XS, and Cyclic IMS LC-MS instruments.</p><p>Prior to joining Waters, she was part of the LC-MS characterization group supporting a biopharmaceutical developability assessment group at Novartis in Cambridge, MA. Sam acquired a BS-MS in Chemistry from Northeastern University in 2012.</p><p><strong>Presenter: </strong>Nick Pittman (Sr. Marketing Manager, Global Biopharma Business, Waters Corporation)</p></blockquote></div>

From Raw Materials to Conjugation Sites: Advanced LC, MS and MALS Strategies for AOC Characterization and Monitoring

This webinar explores the comprehensive analysis of Antibody Oligonucleotide Conjugates (AOCs) using LC-MS and LC-MALS.  

LC, MS and MALS for AOC Characterization and Monitoring

<div><h4><strong>Navigating Challenges and Opportunities for Environmental Testing Labs Under the Revised EU Water Framework Directive</strong></h4><p><strong>The European Commission’s proposed updates to the Water Framework, Groundwater, and Environmental Quality Standards Directives are bringing new responsibilities and opportunities for environmental testing labs. With expanded pollutant lists - including PFAS, pharmaceuticals, and pesticide metabolites - and stricter monitoring and reporting requirements, the landscape of water analysis is rapidly evolving.</strong></p><p>Join the 4th Waters Environmental Webinar Series to explore how your lab can navigate these challenges and turn regulatory change into opportunity.</p><p>Register for free and partner with us to shape the future of European water quality.</p><h5><strong>Why Attend</strong></h5><p>Stay ahead of new EU regulatory demands with insights from leading experts. Gain practical guidance, share experiences with peers, and prepare your lab for the next generation of water quality standards.</p><h5><strong>Highlights</strong></h5><ul><li>New pollutant categories and analytical challenges</li><li>Updates to monitoring protocols and reporting</li><li>Innovative methods to meet revised Environmental Quality Standards</li><li>Strategic guidance for compliance and adaptation</li></ul><p><strong>Lead the change in water analysis—stay ahead, stay compliant, and make a real impact.</strong></p><h4><strong>EPISODE 2: PFAS in the Environment: A Deep Dive into Analysis, Regulation, and Real-World Data</strong></h4><blockquote><p><strong>Presenter:</strong> Tessa Grefenstette (Associate Director, Search &amp; Evolution)</p><p>Tessa Grefenstete is helping the health tech sector integrate and grow within the continuously shifting landscape.</p><p><strong>Presenter: </strong>Jason Moore (Director of Engineering)</p><p>Jason leads the genetics team and is a past chair of the Bioengineering Department at Chatham University.</p></blockquote></div>

PFAS in the Environment: A Deep Dive into Analysis, Regulation, and Real-World Data

Explore PFAS analysis, regulation, and real-world data under the revised EU Water Framework Directive in Episode 2 of the Waters Environmental Webinar Series.

PFAS in Environment: Analysis, Regulation

<div><p><strong>Smarter Bioanalysis: Driving Consistency and Efficiency in Today’s Labs Discovery and regulated bioanalysis labs strive for simplicity, consistency, robustness and operational efficiency to maximize impact and resource utilization. Optimizing every step of the bioanalytical workflow is key to developing assays that perform consistently over time. As therapeutic modalities continue to evolve, so do the needs of bioanalytical laboratories.</strong></p><p>In this webinar, Dr. Basile Khara from Alderley Analytical (now a part of Synexa Life Sciences) shares his experiences on how out-of-the-box performance of detergent-free OligoWorks™ SPE Microplate Kit, combined with a robust analytical platform like the Xevo TQ Absolute XR Mass Spectrometer and waters_connect for quantitation software simplifies bioanalytical workflows.</p><h4><strong>What you’ll walk away with</strong></h4><ul><li>How OligoWorks™ SPE Microplate Kit simplifies oligonucleotide sample preparation</li><li>The implications of having a robust analytical platform that shows consistent performance even after 30,000 injections or protein precipitated plasma</li><li>A simplified, compliant ready informatics platform can streamline data review and help you get to decisions faster</li></ul><h4><strong>Who should attend?</strong></h4><p>This webinar is designed for you if you are a Research Associate, Scientist, Director, or Lab Manager in pharma, biopharma, biotech, or CROs involved in bioanalysis.</p><p>Don't miss it.</p><blockquote><p><strong>Presenter:</strong> Dr. Basile Khara (Principal Scientist, Alderly Analytical (Part of Synexa Life Sciences))</p><p>Basile Khara is currently the Principal Scientist in the method development team at Alderley Analytical situated in Macclesfield U.K, part of Synexa Life Science Ltd. His leading role focuses on the design and validation of novel LC-MS bioanalysis methods that specifically target chemical entities such as oligonucleotides, proteins and conjugated peptides.</p><p>Overall, he has accumulated over ten years’ worth of LC-MS quantification and characterization experience in pre-clinical drug discovery and clinical bioanalysis, along with a Ph.D. in chemistry from the University of Manchester.</p></blockquote></div>

Bioanalysis simplified – A case study with Basile Khara

How OligoWorks™ SPE Microplate Kit simplifies oligonucleotide sample preparation.

Related content

Eurachem/CITAC Workshop on Quality in Analytical Measurements 2026

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

Webinars LabRulezLCMS Week 07/2026