🎤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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Eaton 9E2000I UPS

Reliable 2000 VA / 1600 W online UPS with double-conversion technology, ensuring continuous power protection, stable output, and easy integration for IT systems and analytical equipment.

The Eaton 9E2000I is a reliable double-conversion (online) UPS designed to provide continuous power protection for critical equipment. With a capacity of 2000 VA / 1600 W, it ensures stable voltage and frequency output, making it ideal for servers, networking devices, and laboratory or analytical instruments.The compact tower design allows easy integration into various environments, while the intuitive LCD interface provides clear status monitoring and control. High efficiency operation (up to 97.5% in eco mode) helps reduce energy consumption and operating costs.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E2000_I_UPS_3_af8342a083.jpg" alt="Eaton 9E2000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E2000_I_UPS_3_af8342a083.jpg 176w," sizes="100vw" width="1000" height="887"><h3>Key features</h3><ul><li>True online double-conversion topology for maximum protection</li><li>2000 VA / 1600 W output power</li><li>Wide input voltage range reduces battery usage</li><li>LCD display for real-time monitoring (load, battery, alarms)</li><li>Automatic voltage regulation and frequency stabilization</li><li>Cold start capability (startup without mains power)</li><li>Compatible with external battery packs for extended runtime</li><li>Communication ports (USB, RS232) for system integration</li><li>Compact tower form factor</li><li>High efficiency up to 97.5% (eco mode)</li><li>Automatic battery testing and deep discharge protection</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E2000_I_UPS_4_7c6bf8b875.jpg" alt="Eaton 9E2000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E2000_I_UPS_4_7c6bf8b875.jpg 178w," sizes="100vw" width="1000" height="878"><h3>Technical specifications</h3><ul><li>Power rating: 2000 VA / 1600 W</li><li>Topology: Online (double conversion)</li><li>Input connection: IEC C14</li><li>Output connections: 6 × IEC C13</li><li>Form factor: Tower</li><li>Battery type: Sealed lead-acid (internal)</li><li>Display: LCD</li><li>Communication: USB, RS232</li><li>Input voltage range: 176–300 V (without battery use)</li><li>Input frequency range: 40–70 Hz</li><li>Output voltage: 230 V (configurable 220/230/240 V)</li><li>Output waveform: Pure sine wave</li><li>Runtime: up to ~16 minutes at 50% load (typical)</li><li>Battery configuration: 6 × 12 V / 7 Ah</li><li>Software compatibility: Eaton Intelligent Power Manager, Intelligent Power Protector</li><li>Applications: Servers, IT infrastructure, analytical instruments, laboratory systems</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E2000_I_UPS_6_47619799ff.jpg" alt="Eaton 9E2000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E2000_I_UPS_6_47619799ff.jpg 179w," sizes="100vw" width="1000" height="872">

Eaton 9E3000I UPS

Reliable 3000 VA / 2400 W online UPS with double-conversion technology, delivering continuous power protection, stable output, and flexible integration for IT infrastructure and critical equipment.

The Eaton 9E3000I is a reliable double-conversion (online) UPS designed to provide continuous power protection for critical equipment. With a power rating of 3000 VA / 2400 W, it ensures stable voltage and frequency output, making it ideal for servers, networking infrastructure, and laboratory or analytical instruments.The compact tower design allows easy integration into various environments, while the intuitive LCD display provides clear real-time system monitoring.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E3000_I_UPS_3_21e5358d03.jpg" alt="Eaton 9E3000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E3000_I_UPS_3_21e5358d03.jpg 179w," sizes="100vw" width="1000" height="874"><h3>Key features</h3><ul><li>True online double-conversion topology for maximum protection</li><li>3000 VA / 2400 W output power</li><li>Pure sine wave output</li><li>Wide input voltage range (176–300 V)</li><li>LCD display for real-time monitoring (load, battery, alarms)</li><li>Voltage and frequency stabilization</li><li>Cold start capability (startup without mains power)</li><li>Compatible with external battery packs</li><li>USB, RS232 and communication card slot</li><li>Compatible with Eaton Intelligent Power Manager and Intelligent Power Protector software</li><li>Compact tower design</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E3000_I_UPS_5_94dcd6f68b.jpg" alt="Eaton 9E3000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E3000_I_UPS_5_94dcd6f68b.jpg 180w," sizes="100vw" width="1000" height="870"><h3>Technical specifications</h3><ul><li>Power rating: 3000 VA / 2400 W</li><li>Topology: Online (double conversion)</li><li>Input: IEC C20</li><li>Outputs: 6 × IEC C13, 1 × IEC C19</li><li>Phase: Single-phase input / output</li><li>Dimensions (W × H × D): 39.9 × 33 × 19 cm</li><li>Weight: 24.2 kg</li><li>Display: LCD</li><li>Communication:<ul><li>USB port (HID compatible)</li><li>Serial port (RS232)</li><li>Communication card slot</li></ul></li><li>Software: Eaton Intelligent Power Manager, Eaton Intelligent Power Protector</li><li>Battery:<ul><li>Maintenance-free sealed lead-acid (VRLA), 6 × 12 V / 9 Ah</li><li>Automatic battery test</li><li>Deep discharge protection</li></ul></li><li>Efficiency: up to 98% (eco mode)</li><li>Noise level: &lt;37 dB (at 1 m)</li><li>Operating temperature: 0 to 40 °C</li><li>Color: Black</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eaton_9_E3000_I_UPS_2_aecae50e52.jpg" alt="Eaton 9E3000I UPS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eaton_9_E3000_I_UPS_2_aecae50e52.jpg 181w," sizes="100vw" width="1000" height="865">

Products from category UPS Backup Power - page 1

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