🎤Alex BrodyIn this episode of Concentrating on Chromatography, we sit down with Alex Brody, an organic chemist at Aqua America, to discuss the rigorous analytical methods required for regulated drinking water testing.Alex walks us through the multi-step PFAS detection process using EPA Method 537.1, including extraction, nitrogen blowdown concentration, and LC-MS analysis. He explains why sample preparation and quality control are critical for achieving trace-level detection—and why these methods can't be rushed or simplified, even with new technologies available.We also explore taste and odor investigations, disinfection byproducts, and volatile organic compounds, plus the surprising reality of why regulated labs move slowly when adopting new instrumentation. You'll learn about the quality control checkpoints, peer review processes, and the misconceptions surrounding analytical turnaround times in compliance labs.<h5>Topics Covered:</h5><ul><li>Role of organic chemistry in regulated drinking water labs</li><li>EPA compliance requirements and regulatory bodies (EPA, PA-DEP)</li><li>PFAS detection using Method 537.1 and LC-MS</li><li>The critical importance of nitrogen blowdown sample concentration</li><li>Taste and odor analysis: MIB, Geosmin, and unknown compound identification</li><li>Why regulated methods evolve slowly (validation timelines, approval processes)</li><li>Quality control procedures: calibration checks, matrix spikes, surrogate standards, internal standards</li><li>Automated sample preparation and lab efficiency</li><li>Future PFAS regulations and Method 533 expansion</li></ul><h5>Ideal For:</h5><ul><li>Analytical chemists and environmental lab professionals</li><li>Water utilities and compliance officers</li><li>Chromatography practitioners interested in regulated workflows</li><li>Anyone curious about how drinking water safety is ensured</li></ul><h2>Video Transcription</h2><h3>Ensuring Safe Drinking Water Through Advanced Analytical Chemistry</h3><h4>Insights from a Regulated Water Testing Laboratory</h4>Analytical laboratories responsible for regulated drinking water testing operate under strict compliance frameworks to ensure the delivery of safe and reliable water supplies. In this interview, Alex, an organic chemist at Aqua America, outlines the scope of analytical work conducted in a modern water quality laboratory. The team primarily focuses on the determination of taste- and odor-causing compounds, disinfection byproducts, volatile organic compounds (VOCs), and per- and polyfluoroalkyl substances (PFAS). These analyses rely heavily on GC-MS and LC-MS instrumentation, supported by rigorous maintenance programs to ensure continuous operational performance and data reliability.<h4>Regulatory Compliance and Quality Control in Drinking Water Analysis</h4>Operating as a regulated drinking water laboratory requires adherence to stringent requirements established by agencies such as the U.S. Environmental Protection Agency (EPA) and state-level regulatory bodies. Compliance is driven by extensive quality control protocols integrated into every analytical batch. Typical workflows include calibration verification, matrix spike recovery assessments, internal standard monitoring, and surrogate performance checks. Notably, analytical batches are often limited in sample number to accommodate a substantial proportion of quality control samples, reflecting the critical importance of data defensibility in regulatory reporting.One common misconception is the perceived speed at which results can be delivered. In reality, comprehensive sample preparation, including extraction procedures and validation steps, can extend turnaround times to a full working day or longer. Additionally, validated regulatory workflows impose limitations on the rapid adoption of new analytical technologies, as method modifications must undergo formal evaluation and approval before implementation.<h4>Analytical Strategies for Taste and Odor Investigations</h4>Taste and odor events represent a significant operational challenge for water utilities. Standard targeted methods are routinely applied for compounds such as 2-methylisoborneol (MIB) and geosmin, which are commonly associated with earthy or musty sensory characteristics. When targeted analysis does not reveal the source, laboratories employ broad-scan GC-MS screening combined with spectral library interpretation to identify potential causative compounds. In some cases, sensory evaluation panels complement instrumental analysis, providing preliminary insight into potential treatment-related or environmental influences affecting water quality.<h4>PFAS Monitoring: Methodological Complexity and Trace-Level Sensitivity</h4>PFAS determination represents a rapidly evolving priority in drinking water monitoring. The laboratory currently applies EPA Method 537.1, with efforts underway to expand capabilities through certification for Method 533, thereby broadening analyte coverage. Analytical workflows typically involve solid-phase extraction followed by solvent evaporation using nitrogen-assisted blow-down techniques to achieve the trace-level sensitivity required for regulatory compliance. This concentration step is essential because PFAS compounds remain non-volatile under controlled evaporation conditions, enabling enhanced detection performance upon reconstitution and LC-MS analysis.<h4>Future Directions in Drinking Water Analytics</h4>Looking ahead, the primary technological driver in regulated water analysis is the demand for increasingly lower detection limits and expanded compound coverage. While regulatory frameworks can slow methodological innovation, laboratories continue to pursue efficiency improvements, such as automated sample preparation systems and optimized analytical workflows. These advances support the growing need to process high sample volumes while maintaining the stringent data quality standards required for public health protection.Ultimately, the work performed in regulated drinking water laboratories represents a critical intersection of analytical chemistry, environmental monitoring, and public safety. Continuous methodological refinement, coupled with advances in mass spectrometry and sample preparation technologies, will play a central role in addressing emerging contaminants and ensuring long-term water quality assurance.<blockquote>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.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>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!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

Regulated Drinking Water Testing: PFAS Detection, Sample Prep & Real Lab Insights

This study investigates how ionization polarity influences the gas-phase stability of native-like proteins analyzed by ion mobility spectrometry–mass spectrometry. While proteins generally retain folded structures in both positive and negative electrospray ionization modes, significant differences in unfolding behavior were observed.Proteins exhibited greater gas-phase stability when analyzed in the ionization polarity corresponding to their solution-phase charge, requiring higher energy for unfolding. These findings emphasize the importance of considering protein isoelectric points and ionization polarity in native IMS-MS experiments to ensure accurate structural characterization.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295">Investigating the Effect of Isoelectric Points on the Gas-Phase Stability of Native-like Proteins Analyzed in Positive- versus Negative-Ion Mode by IMS-MS</a></h4>Alexis N. Edwards, Madeline G. Bannon, Michael S. Cordes, and Elyssia S. Gallagher*Anal. Chem. 2026, 98, 6, 4518–4527<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c04295">https://doi.org/10.1021/acs.analchem.5c04295</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.<div>In native mass spectrometry (nMS), the native-like structures of proteins are maintained in the gas phase by preserving the secondary, tertiary, and quaternary structures. <a href="javascript:void(0);">(1−7)</a> The preservation of native-like protein structures is primarily accomplished via the use of electrospray ionization (ESI), a soft ionization method that forms a distribution of multiply charged protein ions. These multiply charged ions can then be investigated to characterize stoichiometry, oligomeric composition, and ligand binding. <a href="javascript:void(0);">(8−10)</a>During ESI, a potential is applied to the sample-containing solution. In an aqueous spray solvent, H3O+ and OH– are produced in positive-ion mode (+ESI) and negative-ion mode (−ESI), respectively. <a href="javascript:void(0);">(11)</a> The buildup of like-charges within the solution results in the formation of a Taylor Cone at the capillary tip, which ejects charged droplets that travel toward the inlet of the mass spectrometer. Droplets undergo evaporation and fission until complete analyte desolvation, leading to the release of folded, gas-phase protein ions. As the droplets shrink, H3O+ or OH– can become concentrated, causing the pH of the droplet to decrease or increase, respectively. Shifts in pH can denature proteins. Therefore, to maintain native-like protein structures, nMS is conducted with solutions containing volatile salts, usually ammonium acetate, that provide ionic strength and minimize pH changes compared to spraying from pure water. <a href="javascript:void(0);">(11,12)</a> Droplet pH in ESI is influenced by flow rate, solvent composition, and applied voltage, <a href="javascript:void(0);">(13)</a> but often approaches values near the pKa of acetate (4.76) or ammonium (9.25) in +ESI or −ESI, <a href="javascript:void(0);">(12,14)</a> respectively. During ESI, changes in overall protein charge take place via proton transfer at chargeable amino acid residues, resulting in the formation of protonated or deprotonated protein ions with the charged sites being dependent on the relative proton affinities of ammonium, acetate, and chargeable amino acids as proteins near complete desolvation. <a href="javascript:void(0);">(15−19)</a>Ion mobility spectrometry (IMS) measures an ion’s mobility through an inert gas under the influence of an electric field. Thus, mobility is directly influenced by the ion’s size, shape, and charge. <a href="javascript:void(0);">(20)</a> A protein’s mobility can be used to estimate its structure by calculating an average momentum-transfer collisional cross section (CCS). In addition to structural characterization, IMS-MS can investigate the gas-phase stability of protein complexes when paired with collision-induced unfolding (CIU). Specifically, in CIU experiments, protein ions are accelerated into a cell filled with inert gas molecules and undergo multiple collisions with higher frequency and energy relative to IMS. This converts kinetic energy to internal, vibrational energy, disrupting noncovalent interactions and inducing unfolding of the protein ions. <a href="javascript:void(0);">(21)</a> Unfolding alters the protein structure, which can then be quantified by monitoring the protein’s mobility during subsequent IMS-MS measurement. <a href="javascript:void(0);">(22)</a> Prior work with mutant proteins has shown that proteins with similar intramolecular interactions have similar CIU fingerprints, while proteins with different intramolecular interactions have different CIU fingerprints. <a href="javascript:void(0);">(23)</a> Therefore, gas-phase protein stability is correlated with intramolecular interactions.Past native IMS-MS work has primarily been conducted in +ESI given that -ESI has the reputation of being unreliable for native-like protein analysis due to the occurrence of corona discharge, <a href="javascript:void(0);">(24)</a> and charge-state distributions that may not be representative of folded proteins. <a href="javascript:void(0);">(25)</a> In recent years, −ESI has been increasingly used in CIU and IMS-MS, with recent work demonstrating that −ESI-MS is capable of discerning denatured and native-like protein structures. <a href="javascript:void(0);">(26,27)</a> Prior work showed that charge manipulation of folded proteins, such as charge reduction, to achieve similar absolute charge states in both ion modes, results in CCS values of protein cations that are comparable to their anion counterparts. <a href="javascript:void(0);">(26,28)</a> This suggests that gas-phase structures are weakly dependent on protein charge and ionization polarity. <a href="javascript:void(0);">(23,26,28)</a> Yet, Hong et al. showed that, in the absence of charge reduction, the gas-phase stability of two proteins (avidin and β-lactoglobulin) is sensitive to ionization polarity, highlighting that gas-phase stability is not consistent between +ESI and −ESI. <a href="javascript:void(0);">(29)</a><h4>Materials and Methods</h4><h5>Native IMS-MS Analysis</h5>Glass capillaries were pulled using a P-1000 micropipette puller (Sutter Instrument Company, Novato, CA). Samples and calibrants were sprayed from pulled capillaries (inner diameter ∼1 μm) and analyzed with a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/152">Synapt G2-S High-Definition MS </a>(Waters Corporation, Milford, MA). The trap and transfer cells contained Ar, the helium cell contained He, and the IMS cell contained N2. IMS wave velocity was 350 m/s, while IMS wave height was either 7 or 9 V, depending on the protein size (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Table S2</a>). Proteins with larger mass required a wave height of 9 V to ensure that all the ions migrated out of the IMS cell prior to the next ion injection. Mass spectra were collected and signal averaged over 30 s. Additional instrument details can be found in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Table S2</a>).To limit systematic error due to repositioning of the ESI tip between runs, <a href="javascript:void(0);">(48)</a> the XYZ-stage position was optimized and kept consistent for all replicates. Approximately 5 μL of sample was loaded into a glass capillary, which was then mounted on the XYZ-stage. Electric potential was delivered to the sample by a platinum wire inserted into the capillary and placed in contact with the solution. The voltage applied to the tip holder ranged from 0.60 to 1.2 kV for native samples, and 0.80 to 1.40 kV for denatured samples. Nine replicates in each ion mode were collected for all proteins with measurements spread across 8 days over 3 weeks. These replicates were conducted in pairs by collecting data in both ion modes consecutively. To accomplish this, a CIU experiment was collected in +ESI before the instrument polarity was changed to −ESI. A second CIU experiment was performed, beginning with −ESI to counteract any changes in protein stability due to pH changes during ESI. <a href="javascript:void(0);">(14)</a> This allowed for use of the same capillary, at the same position in relation to the instrument inlet, for each +ESI/–ESI replicate pair. A new tip was used for each +ESI/–ESI replicate pair. CIU experiments were accomplished by increasing collision voltage (CV) to the trap cell in 5 V steps, from 0 V to a maximum of 120 V.<h4>Results and Discussion</h4>Ten proteins were chosen for analysis in +ESI and −ESI in this work (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl1">Table 1</a>). These proteins can be broken into three groups depending on the net-charge in solution at pH 7: net-negative (with pI &lt; 6.5), net-neutral (with 6.5 ≤ pI ≤ 7.5), and net-positive (with pI &gt; 7.5). Five of the ten proteins have a net-negative charge at pH 7, though four of these proteins (con A, β-lactoglobulin, ovalbumin, and α-lactalbumin) are routinely analyzed via +ESI-IMS-MS. <a href="javascript:void(0);">(18,28)</a> Additionally, each protein had charge-state distributions in +ESI and −ESI that resulted in at least one overlapping charge state (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#fig1">Figure 1</a>), allowing for direct comparison of TWCCSN2→He and CIU50 in both ion modes.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2026_98_6_4518_4527_Figure_1_Representative_mass_spectra_in_ESI_top_and_ESI_bottom_cb81976247.jpg" alt="Anal. Chem. 2026, 98, 6, 4518–4527: Figure 1. Representative mass spectra in +ESI (top) and −ESI (bottom) for (A) ovalbumin, (B) GNA, (C) β-lactoglobulin, (D) α-lactalbumin, (E) con A, (F) streptavidin, (G) ubiquitin, (H) WGA, (I) cytochrome c, and (J) lysozyme. Proteins that have blue or red charge states indicate additional oligomeric states that were detected. Outlines in red boxes are overlapping charge states that are compared herein. *Indicates contaminant peaks." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2026_98_6_4518_4527_Figure_1_Representative_mass_spectra_in_ESI_top_and_ESI_bottom_cb81976247.jpg 245w," sizes="100vw" width="1600" height="865"><h5>Proteins with Disulfide Bridges are Stable in Both Polarities</h5>For both lysozyme and α-lactalbumin, the average TWCCSN2→He were within experimental uncertainty in +ESI and −ESI for both the initial, folded structures and the final, extended structures (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl2">Table 2</a>). However, the 6+ and 6- ions of lysozyme and α-lactalbumin showed a high resistance to unfolding with &gt;90% of the ions retaining their folded TWCCSN2→He values even at high CV (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#fig2">Figure 2</a>). Replicate data showed similar trends (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S2</a>). While CCS values provide a description of gas-phase structures, CIU experiments provide information on the stability of the gas-phase protein structures. Furthermore, the number and pattern of disulfide bridges present in antibodies has been characterized by CIU. <a href="javascript:void(0);">(63)</a> Lysozyme and α-lactalbumin both contain the glycosyl hydrolases family 22 (GH22) domain, which has four disulfide bridges that span ∼94% and ∼93% of the amino acid sequence, respectively (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S3</a>). Thus, we hypothesize that rather than effects from protein pI and ionization polarity, the unfolding behavior of these proteins is controlled to a greater extent by the presence of stabilizing disulfide bridges that prevent routine unfolding during collisional activation.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2026_98_6_4518_4527_Figure_2_Representative_mobiligrams_showing_arrival_times_for_lysozyme_A_C_and_a_lactalbumin_B_D_0f3d23c3c1.jpg" alt="Anal. Chem. 2026, 98, 6, 4518–4527 - Figure 2. Representative mobiligrams showing arrival times for lysozyme (A, C) and α-lactalbumin (B, D) at low and high CV (blue solid and orange dashed lines, respectively) for +ESI (A, B) and −ESI (C, D). For lysozyme, different values were chosen for the high CV (e.g., 540 eV in +ESI and 480 eV in −ESI) because these were the last analyzed CV where the signal-to-noise ratio (S/N) for the 6 ± ions was greater than 3." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2026_98_6_4518_4527_Figure_2_Representative_mobiligrams_showing_arrival_times_for_lysozyme_A_C_and_a_lactalbumin_B_D_0f3d23c3c1.jpg 212w," sizes="100vw" width="1600" height="1178">To characterize the stabilizing effect of disulfides, MD simulations were conducted that heat denatured 6+ ions of lysozyme and α-lactalbumin with disulfide bridges either present or removed with the resulting cysteine residues being protonated prior to heating (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S4</a>). Structural changes associated with heat denaturation were characterized by taking the root-mean-square deviation (RMSD) of the heated structures relative to initial, crystal structures. Over ten trials, lysozyme ions possessed an average RMSD of (1.6 ± 0.2) nm when disulfides were present which increased to (3.5 ± 0.5) nm when disulfides were removed. Similarly, the RMSD of α-lactalbumin ions increased from (1.8 ± 0.1) nm when disulfides were present to (3.7 ± 0.3) nm when disulfides were removed, suggesting that the disulfides serve as a barrier to unfolding. This is visually represented in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S4C,D</a> where simulated structures of heated lysozyme and α-lactalbumin ions with intact disulfides adopt more condensed configurations relative to those with disulfides removed. In essence, the disulfides “tie” disparate regions of protein together, which serves as a barrier to more thorough unfolding even at a maximum simulated temperature of 900 K, explaining the similarity of TWCCSN2→He values in +ESI versus −ESI as well as the limited percentage of ions that undergo a change in TWCCSN2→He upon additional collisional activation.WGA has 16 disulfide bridges per monomeric subunit (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl1">Table 1</a>). On average, these disulfides encompass seven amino acids each, with ∼78% the total amino acids in WGA being encompassed by at least one disulfide bridge (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c04295/suppl_file/ac5c04295_si_001.pdf">Figure S3</a>). Compared to lysozyme and α-lactalbumin, the presence of disulfide bridges across small numbers of amino acids enables WGA to unfold with ΔCCS of (370 ± 60) Å2 and (390 ± 120) Å2 in +ESI and −ESI, respectively (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295#tbl2">Table 2</a>). However, in comparison to the other lectins, GNA and con A, we hypothesize that these disulfide bridges in WGA limit the extent of unfolding, resulting in the extended, TWCCSN2→He values being within experimental uncertainty in both ion modes.To summarize, lysozyme and α-lactalbumin exhibit similar gas-phase behavior in both +ESI and −ESI, with most ions retaining folded structures even under high CV. We hypothesize this resistance to unfolding is largely attributed to their four disulfide bridges, which span over 90% of their sequences and act as stabilizing constraints. MD simulations confirm that removing these disulfides significantly increases structural deviation during heat denaturation, indicating their critical role in maintaining compact configurations. Consequently, the presence of disulfide bridges explains the minimal changes in TWCCSN2→He and the proteins’ high stability under activation.<h4>Conclusions</h4>IMS-MS allows for detailed analysis of the structure and stability of native-like proteins in the gas phase. The structure of a protein is dictated by its amino acid sequence and the resulting noncovalent interactions that form the secondary, tertiary, and quaternary structures. Chargeable amino acid residues that are solvent exposed can carry charges leading to the protein having a net-positive, net-negative, or net-neutral charge in solution at physiological pH. Yet, most native IMS-MS analysis is conducted in +ESI, leading to proteins that are net-negative in solution experiencing large swings in their net-charge during the ESI process.This work highlights that gas-phase stability of native-like proteins varies with ionization polarity. While CCS values for folded structures are generally comparable between +ESI and −ESI, unfolding energetics differ─net-negative proteins are more stable in −ESI, whereas net-positive proteins are more stable in +ESI. We hypothesize that these differences are due to changes in the intramolecular interactions within cationic and anionic proteins. Therefore, proteins analyzed in the mode opposite to their solution-phase charge may have different gas-phase structures compared to biological systems. For example, proteins that are net-negatively charged in physiological environments (pI &lt; 6.5) are more likely to represent their biological counterparts as gas-phase anions when analyzed in −ESI compared to +ESI, enabling nMS experiments to more closely characterize the structures present in biological systems.</div>

Investigating the Effect of Isoelectric Points on the Gas-Phase Stability of Native-like Proteins Analyzed in Positive- versus Negative-Ion Mode by IMS-MS

In the week of March 30, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 500 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. Bruker: MALDI Imaging Becomes IR-resistible: Going Multimodal for Advanced Biomedical Insights</h5><ul><li>Mo, 30.3.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5971">Registration</a></li></ul>Explore advanced multimodal imaging with MALDI, QCL-based IR, and fluorescence microscopy to achieve ROI-focused molecular insights in complex tissues.<h5>2. Shimadzu Corporation: Environmental PFAS Testing: Introducing Next-Generation Mass Spectrometry Solutions</h5><ul><li>Tu, 31.3.2026 09:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6026">Registration</a></li></ul>Explore advanced PFAS analysis strategies combining LC-MS/MS and MALDI-TOF screening to improve sensitivity, efficiency, and regulatory readiness in environmental testing.<h5>3. Tosoh Bioscience: Tosoh Tuesday - Scaling Up from Process Development to GMP Production with Pre-packed Columns</h5><ul><li>Tu, 31.3.2026 15:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6089">Registration</a></li></ul>This webinar will introduce SkillPak™ MAX pre-packed columns and present performance data using TOYOPEARL® Super A, a novel Protein A resin.<h5>4. Phenomenex: Recipe for Separation: Crafting Your Perfect HPLC Method</h5><ul><li>We, 1.4.2026 10:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6091">Registration</a></li></ul>Discover how to properly use and maintain your column to maximize its performance and lifespan.

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Discover how fermentation-driven innovation and advanced formulation science are shaping the next generation of functional food ingredients, with insights from leading R&amp;D and applications experts.Attendees will learn practical ways to use fermentation-derived ingredients while optimising flavour, functionality and stability. The panel will explore emerging trends, strategies for clean-label formulations, and tips for navigating the complexity of bio-crafted ingredients while meeting quality and sustainability goals.<h4>Key learning points:&nbsp;</h4><ul><li>Fermentation as a driver of next-generation ingredient innovation<ul><li>new sensory, functional, and nutritional possibilities</li></ul></li><li>Understanding ingredient performance through analytical and sensory science<ul><li>The role of advanced characterisation techniques in assessing flavour, stability, functionality and batch consistency, and how data improves formulation decisions for complex and novel ingredients.</li></ul></li><li>Applying fermentation-derived ingredients in real-world formulations<ul><li>practical tips for yeast extracts, bio-crafted ingredients, and clean-label solutions</li></ul></li></ul><blockquote>Presenter: Professor William Chen (Nanyang Technological University)William Chen is the Michael Fam Endowed Professor and Director of Food Science &amp; Technology Programme at Nanyang Technological University Singapore. He is concurrently Director of Singapore Future Ready Food Safety Hub (FRESH). He is also Director of Singapore Agri-food Innovation Lab (SAIL).Professor Chen is active in securing and leading large competitive research grants from major government agencies as well as leading international food companies. Findings from his food research have been published in npj Science of Food, EMBO Reports, Trends in Food Science &amp; Technology, Comprehensive Reviews in Food Science &amp; Food Safety, Critical Reviews in Food Science and Nutrition, Current Opinion in Food Science, Food Chemistry, Journal of Functional Foods, Journal of Agricultural and Food Chemistry, among others.His food technology innovations have been extensively attracting global attention, and a number of these innovations have been translated into consumer products. His views on food tech innovations, food safety and food security have been regularly covered by major local and international media outlets (Asahi Shimbun, AFP, BBC, Bloomberg News, CGTN, CNBC, CNN, Los Angeles Times, Mainishi Shimbun, People’s Daily, The Washington Post, and The Wall Street Journal). He is also consultant to overseas universities, Singapore government agencies (ESG, NEA, and SFA), food industry, and international organizations (ADB, FAO, WEF, WHO among others).Presenter: Katia Merten-Lentz (Founder and Managing Partner of Food Law Science &amp; Partners)Katia Merten-Lentz is the Founder and Managing Partner of the law firm Food Law Science &amp; Partners. For more than 25 years, she has been a leading lawyer in European food and feed law. She is ranked first tier in the category Agro/Food — Europe-wide by Chambers and The Legal 500, and was nominated Best Food Lawyer by the European Legal Awards in 2024.Her practice also extends to agri-tech/food-tech and environmental law.She is one of the few lawyers assisting clients end to end in the food and feed sector, including obtaining European authorisations for new additives, enzymes, and novel foods, and advising on related matters ranging from marketing (labelling and claims) to the management of food crises.Her main focus is innovation, supported by strong in-house scientific expertise. She is therefore regularly asked to mentor start-ups and participates in incubator programmes.She holds degrees in EU competition law and corporate/business law, and speaks fluent French and English.Presenter: Dr. Ramkumar Nair (Founder and CEO of SMAQO)Dr Ramkumar Nair is a Sweden-based biotechnology researcher and entrepreneur, best known as the founder of Mycorena AB, a food-tech company pioneering the development of sustainable fungi-based mycoprotein ingredients. Building on his scientific background, he founded Mycorena in 2017 to commercialise mycoprotein technology and led the development of Promyc, a low-impact alternative protein now used by global food companies.Under his leadership, Mycorena has secured major investments, scaled industrial production in Sweden, and formed strategic collaborations with leading industry partners, positioning the company as a key player in the alternative protein and circular-economy space.In addition to his entrepreneurial work, Dr Nair has published numerous scientific papers, serves as a start-up mentor, and is widely recognised as a prominent Indian-origin innovator in Europe. He is currently the Founder and CEO of SMAQO, Europe’s first fungi-based consumer brand, with a focus on hybrid meat–fungi products for consumer applications.Presenter: Peter Kalkowsky (Co-Founder and CEO of Shocken Foods)Peter Kalkowsky is Co-Founder and CEO of Shocken Foods, a UK-based food tech company developing next-generation plant-based meats. He leads strategy, partnerships, and commercial translation of fermentation-derived ingredients into real-world food applications. Shocken Foods is a multi award-winning producer of gourmet vegan charcuterie and pizza toppings, working at the intersection of fermentation, formulation, and clean-label innovation. Peter is also an Industry Collaborations Adviser at the Cambridge Alt Protein Project.</blockquote>

New Food Magazine: The science of next-gen ingredients: fermentation, formulation and function

The science of next-gen ingredients: fermentation, formulation and function

Discover practical strategies for formulating with fermentation-derived ingredients, improving flavour, functionality & stability.

Next-gen ingredients: fermentation, formulation & function

Accurate mass fundamentals breaks down the barriers of complexity, demystifies misconceptions, and provides helpful tips on how to improve your data quality.Whether you already use accurate mass spectrometry and are looking to grow your knowledge or are currently working with nominal mass spectrometry and are thinking about making the switch, this webinar series will show you how accurate mass can simplify your workflow, clarify your data, and give you greater confidence in every result.Sign up today to discover the practical advantages of accurate mass spectrometry.<h4>Session 3: Interpreting and applying your data</h4><ul><li>Explore ways to expand beyond quantitation methods</li><li>See how to confirm compound identity and report with confidence</li><li>Troubleshoot data and expand your quantitation strategies for more reliable reporting</li></ul>

Accurate mass fundamentals - Interpreting and applying your data

Learn how to interpret accurate mass data in practice. Session 3 covers identity confirmation, advanced quantitation strategies, and troubleshooting.

Accurate mass fundamentals - Interpreting data

<h5>Key Learning Points</h5><ul><li>Learn to optimize preparative loading capacity to maximize resolution and yield.</li><li>Scale an existing analytical method up to preparative level.</li><li>Identify the capabilities and limitations of preparative HPLC columns.</li></ul><h5>Who Should Attend</h5><ul><li>Any chemists who primarily work in small-molecule pharma, biopharma, or academia.</li></ul><blockquote>Speaker: Zach Woodward (Senior Technical Specialist, Phenomenex)Zachary Woodward is a Senior Technical Specialist with Phenomenex, Inc, assisting laboratories with method development in the bio-pharma, GMP pharma, and environmental industries. Zachary spent his formative years developing HPLC and GC methods with a pharmaceutical lab in Albany, NY, after which he developed HPLC and SPE methods in a clinical setting here in Southern California. Zachary received his B.Sci. in Chemistry from the College of William and Mary, was awarded his Master’s in Chemistry at San Diego State University, and is happy to speak with you today!</blockquote>

Phenomenex: Big Scale, Big Wins: Prep Chromatography Explained

Big Scale, Big Wins: Prep Chromatography Explained

Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharma applications.

Prep Chromatography Explained

Developing next‑generation energy storage systems demands a deeper, more precise understanding of electrochemical behavior, including how to optimize electrode composition and ensure chemical homogeneity throughout the electrode structure. Combining electrochemistry with Infrared and Raman spectroscopy offers a powerful approach for achieving these goals. Pairing these techniques with microscopy further enables micrometer-scale insights into chemical composition and distribution.This 20-minute TechTalk will explore how these capabilities come together with four key instruments that make this integrated approach possible: INVENIO, RAMANtouch, HYPERION II and VERTEX NEO R.Join Dr. Sergey Shilov, Senior Application Scientist, Bruker Optics, as he shares his 40+ years of FTIR and Raman knowledge to inspire and accelerate your research in batteries, fuel cells, and advanced energy materials.<h4>Key learning objectives:</h4><ul><li>Understand spectroelectrochemical tools and workflows for probing reactions at electrodes and within electrolytes.</li><li>Learn how to optimize instrument setup and integration, including effective communication between potentiostats and spectrometers.</li><li>Understand how to apply fast chemical imaging techniques to visualize electrode surfaces and reaction dynamics.</li><li>Explore real‑world electrochemical case studies such as metal–organic complex oxidation, polymer distribution mapping, electrode degradation analysis, and SEI characterization in lithium metal batteries.</li></ul><h4>Who should attend?</h4><ul><li>Chemists, battery engineers, and scientists who are developing new materials for energy storage.</li></ul><h4>Certificate of attendance</h4><ul><li>If you attend the live TechTalk, you will automatically receive a certificate of attendance, including a learning outcomes summary, for continuing education purposes.</li><li>If you view the on-demand TechTalk, you can request a certificate of attendance by emailing editor@selectscience.net.</li></ul><blockquote>Presenter: Dr. Sergey Shilov (Senior Application Scientist, Bruker Optics)Dr. Sergey V. Shilov is a Senior Application Scientist and &nbsp;Product Manager for North America at Bruker Optics. Dr. Shilov is responsible for the support and development of new applications for the Bruker research FTIR systems. He received his Ph.D. in 1992 from the Russian Academy of Sciences in Polymer Physics. He has published 37 papers in peer-reviewed journals and his research interests include time-resolved FTIR spectroscopy, surface science, polymer, and life science applications.&nbsp;</blockquote>

SelectScience: Advancing energy storage with spectroelectrochemistry

Advancing energy storage with spectroelectrochemistry

How electrochemistry, FTIR, Raman spectroscopy, and microscopy enable advanced chemical insight into electrodes for next-generation energy storage systems.

<div>High-concentration antibody formulations provide patients with the flexibility of self-administered subcutaneous dosing. However, achieving stability and manufacturability of these solutions can lead to increasingly complex formulation development. With expansive libraries of protein variants and formulation conditions to evaluate, researchers need smarter, faster, and more comprehensive analytical tools to ensure chemical stability and optimal delivery characteristics.Join Dr. Sophia Kenrick of Waters | Wyatt Technology and Dr. Christine Nervig of TA Instruments as they present complementary approaches to stability characterization, leveraging high-throughput technologies:<ol><li>High-throughput dynamic and static light scattering (DLS/SLS): These techniques provide rapid, sensitive indicators of aggregation and colloidal stability across a wide range of conditions.</li><li>Rapid screening-differential scanning calorimetry (RS-DSC): This next-generation DSC platform enables simultaneous, low-volume measurements to assess protein unfolding and conformational stability with exceptional throughput.</li></ol>Discover how these complementary methods offer a high-resolution, high-throughput solution for evaluating &nbsp;thermal, colloidal, and long-term stability, to empower scientists to make faster, data-driven decisions in the development of stable, effective biologics.<h4>Key learning objectives:</h4><ul><li>Understand how protein stability influences candidate and formulation selection during biotherapeutic development.</li><li>Recognize the benefits of high-throughput analysis for accelerating workflows in the biopharmaceutical industry.</li><li>Learn how DLS/SLS and DSC can be applied to comprehensively assess thermal, colloidal, and long-term stability.</li></ul><h4>Who should attend?</h4><ul><li>Formulation scientists and protein engineers involved in developing high-concentration biologics.</li><li>Analytical and biophysical characterization teams responsible for evaluating aggregation, conformational, and conformation stability.</li><li>Biopharmaceutical R&amp;D leaders and project managers overseeing biologics development pipeline looking for orthogonal approaches that streamline collection and decision making.</li></ul><h4>Certificate of attendance</h4><ul><li>If you attend the live webinar, you will automatically receive a certificate of attendance, including a learning outcomes summary, for continuing education purposes.</li><li>If you view the on-demand webinar, you can request a certificate of attendance by emailing editor@selectscience.net.</li></ul><blockquote>Presenter: Dr. Sophia Kenrick (Director, Analytical Services, Waters | Wyatt Technology)Dr. Sophia Kenrick received her Ph.D. in Chemical Engineering from the University of California, Santa Barbara. She joined Wyatt in 2010 and now acts as Director of Analytical Services, where she supports emerging applications for light scattering instrumentation and the development of new solutions to address customer applications. These include the development of platform LC-MALS, CG-MALS, and DLS methods for biophysical characterizations of proteins, excipients, and other biotherapeutics.Presenter: Dr. Christine Nervig (R&amp;D Applications Scientist, TA Instruments)Dr. Christine Nervig is a Senior R&amp;D Applications Scientist at TA Instruments, based in Lindon, Utah. She is a biological chemist with an extensive background in the development and evaluation of antibody, protein, and peptide conjugates for the targeted delivery of small molecule therapeutics. At TA Instruments, Dr. Nervig specializes in biophysical characterization of biologic drug products, supporting the development of cutting-edge biophysical characterization instrumentation.Moderator: Olivia Long (Editorial Team, SelectScience)</blockquote></div>

SelectScience: High-throughput stability screening strategies for antibody formulation

High-throughput stability screening strategies for antibody formulation

How high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations

Stability screening strategies for antibody formulation

Per- and polyfluoroalkyl substances (PFAS) remain at the center of global food safety discussions, driven by rapidly evolving regulations and growing consumer concern. Food producers, retailers and packaging suppliers are under increasing pressure to understand where PFAS may occur in their supply chains and how to monitor them reliably.In this webinar, ALS experts will provide a clear and practical overview of PFAS in food and food contact materials, combining regulatory insight with technical know-how and real-world examples. Participants will learn how to navigate current requirements in key markets, what makes PFAS analysis so challenging, and how robust testing strategies can support compliance and brand protection.<h4>Key topics will include:</h4><h5>Regulatory landscape (EU, US, global)</h5><ul><li>Current and emerging PFAS regulations impacting food and food contact materials</li><li>Differences and commonalities between EU, US and other major markets</li><li>Implications for manufacturers, importers and retailers</li></ul><h5>Technical challenges in PFAS detection</h5><ul><li>Why PFAS are difficult to analyze (ultra-trace levels, complex matrices, background contamination)</li><li>Methodological considerations: sampling, sample preparation and instrumental analysis</li><li>Data quality, detection limits and interpretation of results</li></ul><h5>Reliable PFAS testing, from sampling to defensible results</h5><ul><li>Overview of ALS PFAS testing services for food and food contact material</li><li>Analytical platforms, method development and validation approach</li><li>Quality assurance, accreditation and global laboratory network</li></ul>This session is designed for quality, regulatory, R&amp;D and procurement professionals across the food, beverage and packaging industries who want to strengthen their understanding of PFAS and build a reliable testing strategy together with a trusted laboratory partner.<blockquote>Speaker: Stefania Donda (Laboratory Supervisor, ALS Italia S.r.l.)Speaker: Buddhi Dias (Global Food Technical Manager Chemistry, ALS Laboratories (UK) Ltd)</blockquote>

ALS: PFAS in Food & Food Contact Material

PFAS in Food & Food Contact Material

Get a practical overview of EU and US regulations, key analytical challenges, and reliable PFAS testing strategies from ALS experts.

<h3>Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution</h3>Join us for an insightful two-part webinar series exploring high-resolution LC/MS screening and unlocking instrument capabilities.In these sessions, we’ll address common misconceptions about HRMS screening and provide practical guidance to help you achieve confident, efficient screening in complex analytical workflows. Discover strategies, best practices, and expert insights that will empower you to streamline your processes and maximize the value of your instrumentation.<h4>Part 2: How to Set-Up for Success</h4>In this session we demystify instrument capabilities, highlighting key performance metrics and practical considerations for reliable results. Complementing this, we present personal experiences when assessing and improving screening workflows, emphasizing that overly selective sample preparation can bias screening outcomes. The guidelines include technical specifications, essential software tools, operator competencies, and validation strategies, enabling laboratories to benchmark their processes. Together, these insights provide a roadmap for achieving confident, streamlined screening in complex analytical environments.<h5>Who should attend?</h5>Scientists already using HRMS who need insights about their methods, results, or workflows and scientists considering moving to HRMS screening and looking for clarity on what it can and can’t deliver.<blockquote>Presenter: Shaun Reeksting (Field Application Specialist LC/MS, Agilent Technologies)Shaun has a passion for bridging the gap between complex science and practical solutions. With over a decade of experience in mass spectrometry—from hands-on method development in academic and commercial labs to supporting cutting-edge analytical workflows, he thrives on helping customers discover the fascinating world of multi-molecule analyses and unlocking insights from their data.Presenter:&nbsp;Dr Christian Klein (Biopharma Application Specialist, Agilent Technologies)With an education in Chemistry, Chris Klein received his PhD in 2005 at the Max-Planck-Institute for Biochemistry in Martinsried, Germany. After a PostDoc and 3 years as demo chemist and product specialist with Bruker Daltonics in California, Chris joint Agilent Technologies’ LC/Q-TOF R&amp;D team in 2010 and took in 2018 the role as LC/Q-TOF and IM-QTOF Product Manager. In 2025 he returned to Germany as Biopharma Application Specialist in Waldbronn.Presenter:&nbsp;Dr Susanne Soelter (Field Application Specialist LC/MS, Agilent Technologies)Susanne Soelter started her career as a product specialist for LC/MS 2004. She has remained loyal to LC/MS since then. In her current position as a Field Application Specialist, she develops new methods in the Agilent laboratory in Waldbronn and supports customers on site.Susanne studied chemistry in Hamburg and received a doctorate degree in organic chemistry from the University of Hamburg.</blockquote>

Agilent Technologies: Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution

Screening Demystified: Practical Guidelines for Getting It Right with High-Resolution Part 2: How to Set-Up for Success

Guidelines for setting up HRMS LC/MS screening. Learn LC/QTOF performance metrics, workflow design, validation, and software tools for reliable HRMS results.

Screening Demystified: How to Set-Up for Success

Monitoring and control of biotech processes is non-trivial. Most unit operations are complex and have non-linear dynamics, which makes it difficult to model, monitor, and control.HPLC has been the gold standard of biopharmaceutical analysis for decades. However, typical HPLC analysis takes anywhere from 30 to 90 minutes, making the technique suitable for Quality Control applications but suboptimal for process analysis on the manufacturing floor.This talk will aim to elucidate how recently launched Agilent PAT HPLC can facilitate near-real time monitoring of CQAs during bioprocessing.A case study involving the monitoring and control of charge variants in a process cation exchange chromatography column will be used to demonstrate this.<h4>Who must attend?</h4><ol><li>Scientists working or keen to explore LC as a PAT Tool.</li><li>Biopharmaceutical R&amp;D, Quality &amp; Process Scientists.</li><li>Scientists who are keen to learn more about the PAT tool in the API and Chemicals industry.</li></ol>Learn more from the expert on Process Analytical Techniques (PAT) and Quality by Design (QbD), Dr. Anurag Rathod. Register now for this webinar &amp; explore hidden possibilities of LC as a PAT Tool.<blockquote>Presenter: Anurag S. Rathore, Ph.D. (Professor, Department of Chemical Engineering, Indian Institute of Technology, Delhi)ANURAG S. RATHORE is Professor and Head at the Department of Chemical Engineering, Indian Institute of Technology, Delhi, India. He is also the Coordinator for the DBT COE for Biopharmaceutical Technology. He is presently serving as the Editor in Chief for The AAPS Journal. His previous roles included management positions at Amgen Inc., Thousand Oaks, California and Pharmacia Corp., St. Louis, Missouri. His areas of interest include process development, scale-up, technology transfer, process validation, biosimilars, continuous processing, formulation, biopharmaceutics, PAT and QbD. He has authored more than 800 publications and presentations in these areas. He has a Ph.D. in Chemical Engineering from Yale University.Presenter:&nbsp;Dr. Sebastian Weinig-Berger (Technical Product Manager, Agilent Technologies Germany GmbH)Dr. Sebastian has studied “Molecular Biotechnology” at the Technical University in Munich. His Master's Thesis was characterized by Proteomic Profiling of NSCLC (Non-Small Cell Lung Cancer) samples and the concurrent Kinase profiling. In particular, he joined Prof. Küster’s Lab in Freising-Weihenstephan. Next, he joined the Steen Lab at Harvard Medical School in Boston, MA. This lab was in particular adjacent to the Boston Children’s Hospital. His Ph.D. thesis focused on Proteome Biomarker Profiling in the context of Concussion. The ultimate goal was to develop a fast-screening urine test. During this time, he also established the published and still cited method for “Urinome” profiling: MS tern Blot - https://pubmed.ncbi.nlm.nih.gov/26223766/. After his Ph.D., he moved back to Germany and joined Agilent Technologies as an Application Test Lead and progressed to Marketing and his current role as Product Manager since January 2022.</blockquote>

Agilent Technologies: Process Analytical Techniques: Online HPLC for Real Time Monitoring and Control of Bioprocesses

Process Analytical Techniques: Online HPLC for Real Time Monitoring and Control of Bioprocesses

Learn how PAT HPLC supports real-time bioprocess monitoring and control of CQAs, bridging LC analysis with Quality by Design in biopharmaceutical manufacturing.

Online HPLC for Real Time Monitoring and Control

The presentation introduces the new Thermo Scientific Orbitrap Exploris Pro, highlighting its expanded capabilities for biopharmaceutical and protein therapeutic characterization. Building on the robustness and flexibility of earlier Orbitrap systems, the new instrument adds electron transfer dissociation (ETD) with optional supplemental activation (EThcD) and an extended mass range up to 12,000 m/z, enabling improved intact protein analysis and detection of large aggregates at low abundance. These enhancements support deeper sequence coverage, confident PTM identification, isobaric amino acid differentiation, and disulfide bond mapping. Additional improvements include a new ion source to reduce source fragmentation, higher scan speeds, increased throughput, and advanced workflows such as hybrid DIA and adaptive retention time correction. The biopharma edition is particularly suited for complex modalities such as ADCs, bispecific antibodies, and long peptides, providing high sensitivity, accuracy, and confidence for critical analytical decisions in biologics characterization.<h4>Learning points:</h4><ul><li>Orbitrap Exploris Pro advances biopharma analysis: Added ETD/EThcD and an extended mass range (up to 12,000 m/z) enable better characterization of complex biologics, including low-level aggregates and variants</li><li>ETD delivers higher confidence results: ETD/EThcD improves sequence coverage, PTM localization, disulfide mapping, and differentiation of isobaric amino acids</li><li>Improved performance and workflows: Reduced source fragmentation, higher speed and throughput, and new workflows (hybrid DIA, adaptive RT) enhance sensitivity and data quality across applications</li></ul><h4>Who should attend?</h4><ul><li>Biopharma and protein therapeutics scientists: Researchers working on monoclonal antibodies, bispecifics, ADCs, and complex biologics who need confident structural characterization and PTM analysis</li><li>Mass spectrometry and proteomics experts: Users focused on advanced MS/MS strategies, ETD-based workflows, and high-sensitivity peptide and protein analysis</li><li>Analytical development and characterization teams: Scientists responsible for method development, comparability, and quality-relevant characterization in biopharmaceutical pipelines</li></ul>This webinar is a recording from the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5672">Omics innovations for the biopharmaceutical industry</a> seminar on December 11, 2025 in Strasbourg.Cannot attend on February 12? Please register anyway to automatically receive the link to the recording.<blockquote>Presenter: Claire Dauly (Senior Manager, Product Management, Thermo Fisher Scientific)</blockquote>

Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS

Introducing the Orbitrap Excedion Pro Hybrid MS

Learn how Orbitrap Exploris Pro advances biopharma analysis with ETD/EThcD, mass range to 12,000 m/z, and high-confidence protein characterization workflows.

Join us for an engaging on-demand webinar exploring advanced solutions and workflows designed to address today’s most pressing challenges in environmental testing. Hear directly from our Environment and Food Safety specialists and leading industry experts as they share cutting-edge approaches to meet the evolving demands of testing and compliance. This session features a spotlight presentation by Allen Martin from the North Carolina Department of Environmental Quality, titled “Integrated PFAS Analysis: Targeted Methods and Non-Targeted Discovery in North Carolina."<h4>Who should attend?</h4>This event is tailored for professionals committed to tackling environmental challenges, including:<ul><li>Laboratory managers and technicians</li><li>Quality assurance and regulatory specialists</li><li>Environmental scientists and researchers</li><li>Industry consultants and advisors</li><li>Policy makers and regulators</li><li>Academic researchers</li></ul><h4>What will you learn?</h4><ul><li>Master detection techniques for PFAS: Equip yourself with the latest tools to identify and quantify these persistent contaminants.</li><li>Leverage automation: Discover how automation can streamline your lab processes, enhancing accuracy and efficiency.</li><li>Navigate regulatory landscapes: Stay compliant with current and future regulations across the Americas</li><li>Adopt innovative workflows: Implement new methodologies to boost lab performance.</li><li>Gain expert insights: Learn from leading specialists through in-depth discussions and real-world case studies.</li></ul><blockquote>Presenter: Allen Martin (Public Health Scientist, North Carolina Department of Environmental Quality)Allen Martin is a public health scientist and PFAS Unit Supervisor at NCDEQ, leading the analytical lab focused on PFAS detection and method development. He holds degrees in biochemistry, organic chemistry, and an MBA from UNC Wilmington, and has 18+ years’ experience in PFAS analysis, environmental testing, and statewide monitoring.Presenter:&nbsp;Richard Cochran, PhD (Senior Application Scientist for LSMS Thermo Fisher Scientific)Richard Cochran is a Senior Application Scientist for LSMS at Thermo Fisher Scientific with 18+ years of mass spectrometry experience. He holds a PhD in Analytical Chemistry and he currently focuses on advancing mass spectrometry solutions that help scientists around the world improve the global environment and our quality of life.Presenter:&nbsp;Michael Ebitson (Product Manager, Thermo Fisher Scientific)Michael Ebitson is an analytical sciences professional with extensive experience in environmental labs and global sample preparation. He has led GC/LC workflows, collaborated with the EPA on method development, and now manages Thermo Fisher’s sample prep product lines, specializing in PFAS and POPs.Presenter:&nbsp;Ed George (Global EFS Regulatory Strategy and KOL Manager Thermo Fisher Scientific)Ed George holds a BS in Chemistry from the University of Notre Dame. He spent 15 years in the environmental lab industry developing soil and water methods using GC- and LC-MS/MS and collaborating with the US EPA. Since joining Thermo Fisher in 2014, he has developed workflows for pesticides, veterinary drugs, and PFAS and now serves as EFS Global KOL and Regulatory Affairs Manager.Moderator: Maggie Ostrowski, PhD (Sr. Environmental Food &amp; Safety Business Development Manager, Thermo Fisher Scientific)Maggie A. Ostrowski, PhD, is Senior Manager of Business Development for Environmental and Food Safety at Thermo Fisher Scientific. With 25+ years in product management, marketing, business development, and R&amp;D, she has a strong record of commercializing analytical technologies, including GC/MS and LC/MS, across both the applied and life science markets.</blockquote>

Thermo Fisher Scientific: PFAS in the environment: New workflow solutions and industry perspectives

PFAS in the environment: New workflow solutions and industry perspectives

Join us to explore advanced solutions and workflows designed to address today’s most pressing challenges in environmental testing.

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