🎤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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SIELC Alltesta Power Tower for HPLC Alltesta

The Alltesta™ Power Tower acts as a power supply and chromatography data acquisition device, connecting, controlling, and streaming your Alltesta™ devices to our free cloud software at hplc.cloud.

The Alltesta™ Power Tower acts as a power supply and chromatography data acquisition device, connecting, controlling, and streaming your Alltesta™ devices to our free <a href="https://lcms.labrulez.com/products/1250">cloud software</a> at <a href="https://hplc.cloud/">hplc.cloud</a>. It serves as a bridge between your laboratory and a centralized data storage hub. With the Power Tower and your free HPLC.cloud subscription, you can access your equipment and experiment results from anywhere, on any device, at any time, using any interface!
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SIELC has developed the first and only HPLC software that is accessible via the cloud.

<h5>Each <a href="https://lcms.labrulez.com/products?instrumentationItems=27&amp;search=SIELC">instrument</a> is connected directly to our secure cloud server via an Ethernet line.</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_1_441d304d5d.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
<h5>All instrument parameters are visible and adjustable on the fly from any internet-enabled device. Instrument settings are stored as methods, which can be retrieved and used for specific compounds.</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_2_f626a8f395.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
<h5>Multiple samples can be organized in a sequence with various methods. Results can be compared and quantitated:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_3_6eb75a29c9.jpg" alt="SIELC: SIELC Software – HPLC.cloud."/>
Please see an online example of the separation results <a href="https://chrom.app/share/#/samples/11972/injection/21307/?t=a992fefcdd3647b19f6bed81e182d3d8">here</a>.
<h5>With your Alltesta and HPLC.cloud free subscription, you can analyze almost any compound from the palm of your hand. For example, you can analyze the dyes that are in your favorite purple sports drink:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_4_b8e9abd33a.jpg" alt="SIELC: Separation of Blue 1 and Red 40 dyes in Gatorade Zero – Grape."/>
<h5>Alternatively, you can analyze the caffeine content in your morning coffee:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_5_f39557543e.jpg" alt="SIELC: Retention of Caffeine."/>
<h5>Another option is to separate and analyze the vitamin content in your daily multi-vitamin:</h5>
<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/SIELC_SIELC_Software_HPLC_cloud_6_bbf8e002a3.jpg" alt="SIELC: Separation of Vitamin C and Vitamin B2."/>

Waters/Wyatt microViscoStar viscometer

The Waters microViscoStar incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for UHPLC. 

<h4>Highly Sensitive</h4>A highly sensitive, on-line differential viscometer used with SEC-MALS-IV to determine the size and conformation of polymers, proteins and peptides separated by UHPLC.<h4>Multiple Novel Technologies</h4>The microViscoStar™ incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for UHPLC. Its ease-of-use and serviceability make it the perfect companion for Wyatt's microDAWN™ light scattering and microOptilab™ refractive index detectors for UHPLC.<h4>Another path to polymer and protein characterization: SEC-MALS-IV</h4>When coupled with size-exclusion chromatography and a concentration detector such as the Optilab™ , the microViscoStar derives the intrinsic viscosity (IV) of polymers. An inherently valuable physico-chemical property in itself, IV is best utilized together with molar mass information from multi-angle light scattering (SEC-MALS-IV) to derive the hydrodynamic radius, conformation, and branching ratio of a macromolecule in solution.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg" alt="Waters microViscoStar: Patented pulse compensation technology in the microViscoStar eliminates pump fluctuations. At the hardware level, the bridge is impedance-matched for dynamic balance, greatly reducing the effect of pump pulses. An additional layer of software filtering eliminates residual pump pulses." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg 233w," sizes="100vw" width="348" height="233"><h5>Key benefits of the ViscoStar</h5><ul><li>High sensitivity, equivalent to 5 ng of 100 kDa polystyrene in THF at 1.0 mL/min injected onto a standard GPC column</li><li>High dynamic range of over 135,000:1. The full measurement range corresponds to over 13 mg/mL of 100 kDa polystyrene in THF</li><li>Extended solvent compatibility with all-316 stainless steel transducers</li><li>Temperature range from 4 °C to 70 °C for polymers or proteins that require a range of temperatures</li><li>Minimal band broadening thanks to fast pressure transducers</li><li>Pump pulse suppression to below 4 Pa (hardware alone) or 1 Pa (hardware + software) without loss of chromatographic resolution</li><li>Automated capillary bridge tuning with no moving parts, to guarantee a perfectly balanced bridge, every run</li><li>Enhanced thermal stability with drift of &lt;1.25 Pa/hour</li></ul><h4>SEC-IV without MALS?</h4>Yes, as much as we love MALS for optimal polymer analysis, it's true that there are occasions when it just won't fit the bill.Universal calibration is a parallel technique to SEC-MALS for determining molecular weight, commonly used to characterize linear polymers. While universal calibration overcomes some of the problematic issues associated with column calibration by reference molecules, it does not account for non-ideal column behavior caused by chemical solute-column interactions or hyperbranching.Universal calibration is particularly-well suited to replace MALS for:<ul><li>Strongly fluorescent polymers</li><li>Weakly-scattering polymer/solvent systems with very low dn/dc values</li></ul>The Mark-Houwink-Sakurada relationship makes use of empirical relationships between intrinsic viscosity and molar mass, specific to each polymer and solvent, to estimate molar mass from SEC-IV measurements. Of course, the best way to determine MHS coefficients is to measure them using SEC-MALS-IV and ASTRA™<h4>Specifications</h4><h5>Measurement Capabilities – Differential Viscosity</h5><ul><li>Sensitivity: Detects as little as 5 ng of 100 kDa polystyrene in THF at 1 mL/min under typical UHPLC-SEC conditions.</li><li>Differential Pressure Performance:<ul><li>Noise: &lt; 0.05 Pa</li><li>Range: Up to 6.9 kPa, with overpressure protection</li><li>Drift: &lt; 1.25 Pa/hr</li><li>Linearity: Within 0.5% of full scale</li><li>Dynamic Range: 135,000:1</li></ul></li><li>Capillary Bridge Autobalance: Thermal, leak-free mechanism ensures stable baseline performance.</li><li>Sample Shear Rate: Up to 15,000 Hz with water at 1 mL/min for high-resolution viscosity profiling.</li></ul><h5>Fluidics and Compatibility</h5><ul><li>Maximum Flow Rate: Aqueous and THF: up to 1 mL/min (Note: Using an inline UV detector may reduce allowable flow rate.)</li><li>Delay Volume: 5.4 mL</li><li>Maximum Inlet-to-Outlet Pressure: 3000 kPa (435 psi)</li><li>Wetted Materials: 316 stainless steel, PTFE, zirconium silicate, Kalrez®, Inconel, 26-1 stainless steel, and nickel</li></ul><blockquote>Note: Due to the location of wetted components, this instrument is primarily recommended for use with organic solvents. High-ionic-strength buffers may cause corrosion.</blockquote><h5>Temperature Control</h5><ul><li>Operating Range: 4 °C to 70 °C</li><li>Stability: Maintains temperature within &lt; 0.005 °C</li><li>Ambient Conditions: 0 °C to 40 °C; 20% to 70% relative humidity</li></ul><h5>Electronics and Connectivity</h5><ul><li>Digital Output: 20-bit resolution at 10 Hz</li><li>Auxiliary I/O:<ul><li>Inputs: Autoinject contact closure, Alarm In, and 2 analog inputs (16-bit, ±10 V)</li><li>Outputs: Autoinject retransmit, Alarm Out, Recycle Out</li></ul></li><li>Communication Interface: Ethernet</li></ul><h5>User Interface</h5><ul><li>Front Panel Display: 7” (178 mm) high-resolution, capacitive multi-touch screen for real-time monitoring, configuration, and diagnostics</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 60 cm (L) × 36 cm (W) × 17 cm (H)</li></ul><h4>Other Viscometers</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1117">ViscoStar™</a> - A highly sensitive, on-line differential viscometer used in conjunction with SEC-MALS to determine the size and conformation of all types of biopolymers, synthetic polymers and even proteins and peptides.</li><li>The ViscoStar incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for GPC. Its ease-of-use and serviceability make it the perfect companion for Wyatt's DAWN® light scattering and Optilab® refractive index detectors. Temperature-controlled from 4 °C to 70 °C .</li></ul>

Waters/Wyatt Optilab On-line Differential Refractometer

The Waters Optilab is a unique dRI detector for standard HPLC/GPC with 256 times the detection power and 50 times the dynamic range of every other RI detector for chromatography in existence today, making it a valuable addition to any MALS setup.

<h4>Independent of Chromaphores</h4>Independent of chromaphores or fluorophores, differential Refractive Index (dRI) detectors serve as accurate and versatile concentration detectors in all types of solvents. dRI is part of standard instrumentation for a variety of macromolecular characterization techniques including standard chromatography, SEC-MALS, FFF-MALS and CG-MALS.<h4>Unique dRI Detector</h4>The Optilab is a unique dRI detector for standard HPLC/GPC with 256 times the detection power and 50 times the dynamic range of every other RI detector for chromatography in existence today, making it a valuable addition to any MALS setup.<h4>Product Description</h4>Using a combination of cutting-edge semiconductor photodiode technology and proprietary computer algorithms, the Optilab achieves an unprecedented combination of sensitivity and range. These features mean that it addresses both standard chromatographic applications and some challenges unique to light scattering measurements such as high concentrations, determination of sample refractive increments (dn/dc) and solvent refractive index.<h5>Key Benefits</h5><ul><li>Extraordinary dRI measurement range, -0.0047 to +0.0047 RIU (comparable to 25 mg/mL protein in PBS)</li><li>Highly sensitive, ±7.5 x 10 -10 &nbsp;RIU across the entire measurement range</li><li>Measures solvent absolute refractive index, required for MALS calculations</li><li>Measures at the same wavelength as the MALS detector, for maximum accuracy in MALS calculations</li><li>Band broadening &lt; 20 µL preserves SEC resolution</li><li>Temperature range 4 °C to 65 °C for proteins and polymers that require a range of temperatures</li><li>High-resolution, touch-screen front panel displays data graphs and diagnostics, even with the host computer turned off</li></ul><h5>Unparalleled Features</h5>Even though the Optilab offers a dRI measurement range orders of magnitude beyond that of other dRI detectors, unlike other detectors there are no range or gain settings in the Optilab. The full range of instrument detection is always present, and the full sensitivity exists over the entire range.The Optilab can also do something no other on-line refractive index detector can: it can measure the absolute refractive index of a solution. In addition, it can measure the dn/dc of a solvent at the same wavelength of light as the light scattering instrument. And just to make sure it can't be matched, you can replace the light source in the Optilab for other wavelengths (e.g., 690, 633, 488, etc.) in just minutes!The Optilab can go below ambient temperatures as easily as above ambient. No hassle temperature control can be programmed from 4 °C to 65 °C. Compatible with all HPLC systems.<h4>Specifications</h4><h5>Measurement Capabilities – Differential Refractive Index</h5>Standard Optilab Configuration<ul><li>Measurement Range: –0.0047 to +0.0047 RIU</li><li>Peak-to-Peak Noise: ±7.5 × 10⁻¹⁰ RIU (Measured per ASTM-E1303-95 at 25 °C)</li></ul>High Concentration (HC) Option<ul><li>Measurement Range: –0.0026 to +0.034 RIU</li><li>Peak-to-Peak Noise: ±1.5 × 10⁻⁹ RIU (Optimized for higher concentration samples)</li><li>Response Time: User-selectable from 0.1 to 5 seconds</li><li>Absolute Refractive Index Measurement Range: 1.2 to 1.8 RIU</li><li>Absolute RI Sensitivity: ±0.002 RIU</li></ul>Fluidics and Flow Properties<ul><li>Band Broadening: &lt;12 µL</li><li>Fill Volume (Inlet Tubing + Flow Cell): 51.4 µL</li><li>Outlet Tubing Volume (0.030" ID): 370 µL</li></ul>Pressure Ratings<ul><li>Inlet Back Pressure (0.5 mL/min H₂O @ 20 °C): &lt;22 psi (1.5 bar)</li><li>Max Outlet Back Pressure: 30 psi (2 bar)</li></ul>Temperature Control<ul><li>Sample Temperature Control Range: 4 °C to 65 °C</li><li>Regulation Stability: ±0.005 °C</li></ul>Light Source Options<ul><li>Standard: 660 nm</li><li>HC Model (Optional): 488 nm, 785 nm, or 940 nm</li></ul>Safety Features<ul><li>Built-in vapor and liquid leak sensors for enhanced lab safety</li></ul>Electronics and Connectivity<ul><li>Digital Output: 22+ bit resolution @ 10 Hz</li><li>Analog Output: ±10 V or ±1 V, 18-bit resolution</li><li>Computer Interface: Ethernet</li></ul>Auxiliary I/O Ports<ul><li>Inputs:<ul><li>Analog In (16-bit, ±10 V A/D)</li><li>Zero dRI</li><li>Purge</li><li>Recycle In</li><li>Autoinject In</li><li>Alarm In</li></ul></li><li>Outputs:<ul><li>Autoinject Retransmit</li><li>Alarm Out</li><li>Recycle Out (controls Orbit™ valve switching)</li></ul></li></ul>User Interface<ul><li>Front Panel Display: 7” (178 mm) high-resolution multi-touch screen for viewing signals, diagnostics, and adjusting instrument settings</li></ul>Instrument Dimensions<ul><li>Size: 58 cm (L) × 36 cm (W) × 18 cm (H)</li></ul><h4>Other Refractive Index Detectors</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1269">microOptilab™</a> - The first RI detector specifically designed for use with all UHPLC systems.</li></ul>

Waters/Wyatt microOptilab On-line Differential Refractometer

The Waters microOptilab brings the universal detection capabilities, unsurpassed concentration range, and superb sensitivity and linearity

<h4>Independent of Chromaphores</h4>Independent of chromaphores or fluorophores, differential Refractive Index (dRI) detectors measure concentrations of all types of samples in almost all solvents. The microOptilab brings the universal detection capabilities, unsurpassed concentration range, and superb sensitivity and linearity – familiar from the Optilab™ – to the domain of UHPLC.<h4>SEC-MALS with UHPLC</h4>Like standard SEC, UHPLC-SEC analysis relying on column calibration with molecular standards is unreliable when the standards do not accurately reflect your samples in terms of conformation, non-ideal (e.g., hydrophobic) column interactions or reversible association. SEC-MALS employs a microDAWN™ MALS detector downstream of the SEC column and UV detector, to determine molar mass / molecular weight distributions of macromolecules independently of column calibration.Refractive index detection is an important component of any SEC-MALS system, and necessary for analyzing conjugated proteins or polymers devoid of chromaphores. The microOptilab connects with the microDAWN MALS detector for a complete UHP-SEC-MALS setup that transfers the many benefits of SEC-MALS analysis to the realm of UHPLC.<h5>Key benefits</h5><ul><li>Very low band broadening, &lt; 4 µL, to maintain the resolution of very narrow UHPLC peaks</li><li>Extraordinary dRI measurement range, -4.7 x 10 -3 &nbsp;to +4.7 x 10 -3 &nbsp;RIU (comparable to 25 mg/mL protein in PBS)</li><li>Highly sensitive, ± 1.5 x 10 -9 &nbsp;RIU across the entire measurement range</li><li>Measures solvent refractive index, require for MALS calculations</li><li>Measures at the same wavelength as the MALS detector, for maximum accuracy in MALS calculations</li><li>Temperature range 4 °C to 65 °C for proteins and polymers that require a range of temperatures</li><li>High-resolution, touch-screen front panel displays data graphs and instrument diagnostics, even with the host computer turned off</li></ul><h5>Unparalleled features</h5><ul><li>Considering the extremely small peak volumes of UHPLC, band broadening in the microOptilab is kept to the absolute minimum, at less than 4 µL, as compared to 20 - 40 µL or more for standard RI detectors. As a result, the superior resolution from UHPLC columns and instruments will not be compromised with the microOptilab RI detector.</li><li>Even though the microOptilab offers a dRI measurement range orders of magnitude beyond that of other UHPLC dRI detectors, unlike other detectors there are no range or gain settings in the microOptilab. The full range of instrument detection is always present, and the full sensitivity exists over the entire range. The small flow cell and proprietary temperature regulation enable stable RI baselines and signals which further enhance the detector's sensitivity.</li><li>Unlike all other dRI detectors, the microOptilab also measures absolute refractive index in order to determine solvent RI, necessary in light scattering calculations and useful in assessing the accuracy of mixing of solvent gradients.</li><li>The microOptilab can be operated below ambient temperatures as easily as above ambient. No hassle temperature control can be programmed down to 4 °C or as high as 65 °C.</li><li>The microOptilab is compatible with all UHPLC systems.</li></ul><h4>Specifications</h4><h5>Measurement Capabilities – Differential Refractive Index</h5><ul><li>Differential RI Measurement Range: –0.0047 to +0.0047 RIU</li><li>Peak-to-Peak Noise: ±1.5 × 10⁻⁹ RIU (Measured per ASTM-E1303-95 at 25 °C with a 0.5 sec collection interval)</li><li>Response Time: User-selectable from 0.04 to 5 seconds</li><li>Absolute Refractive Index Range: 1.2 to 1.8 RIU</li><li>Absolute RI Sensitivity: ±0.002 RIU</li></ul>Fluidics and Flow Properties<ul><li>Band Broadening: &lt;4 µL (at 0.3 mL/min)</li><li>Fill Volume (Inlet Tubing + Flow Cell): 13.7 µL</li><li>Outlet Tubing Volume (0.030” ID): 228 µL</li></ul>Pressure Ratings<ul><li>Inlet Back Pressure (0.5 mL/min H₂O @ 20 °C): &lt;320 psi (22 bar)</li><li>Maximum Permissible Outlet Pressure: 30 psi (2 bar)</li></ul>Temperature Control<ul><li>Control Range: 4 °C to 65 °C</li><li>Stability: ±0.005 °C for precise thermal regulation</li></ul>Optical Source and Safety<ul><li>Light Source: 660 nm wavelength</li><li>Safety Sensors: Integrated vapor and liquid leak detection</li></ul>Electronics and Connectivity<ul><li>Digital Output Rate: 25 Hz</li><li>Analog Output: ±10 V or ±1 V, 18-bit resolution</li><li>Computer Interface: Ethernet for seamless data connectivity</li></ul>Auxiliary I/O Ports<ul><li>Inputs:<ul><li>Analog In (16-bit, ±10 V A/D)</li><li>Zero dRI</li><li>Purge</li><li>Recycle In</li><li>Autoinject In</li><li>Alarm In</li></ul></li><li>Outputs:<ul><li>Autoinject Retransmit</li><li>Alarm Out</li><li>Recycle Out (Orbit™ valve switching)</li></ul></li></ul>User Interface<ul><li>Display: 7” (178 mm) high-resolution multi-touch screen for viewing live signals, diagnostics, and configuring instrument settings</li></ul>Instrument Dimensions<ul><li>Size: 58 cm (L) × 36 cm (W) × 18 cm (H)</li></ul><h4>Other Refractive Index Detectors</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1268">Optilab™</a> - A unique on-line differential refractometer for measuring concentration of any macromolecule, regardless of chromophores. Temperature controlled from 4 °C to 65 °C. The high-concentration option accommodates protein concentration up to 180 mg/mL.</li></ul>

Watrex SCI-AQUA ROWAPUR BASIC Water Purification System

Fully automatic system for the preparation of pure water based on reverse osmosis. Reverse osmosis membrane is protected by three-stage pre-filtration consisting of sediment filter and two carbon adsorption filters.

Fully automatic system for the preparation of pure water based on reverse osmosis. Reverse osmosis membrane is protected by three-stage pre-filtration consisting of sediment filter and two carbon adsorption filters.<a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/water-purification/reverse-osmosis-systems/sci-aqua-basic/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex SCI-AQUA BASIC</a> is driven by water pressure from water distribution network, it does not require electric power. It prepares water free of mechanical impurities, chlorine, 95-99% of all dissolved substances are removed.&nbsp;Depending on input water composition and supply pressure the output water has a specific conductivity in the range of 10-20 µS/cm.Price: <bdi>384&nbsp;€</bdi> ex. VAT<h4>Features</h4><ul><li>Removes 95 – 99% of dissolved substances</li><li>Typical specific conductivity of produced water 10 – 20 µS/cm</li><li>6 to 12 months filters lifetime</li><li>2 – 5 years RO membrane lifetime</li><li>No electricity is required for operation</li><li>Supplied from water distribution network</li></ul><h4>Technical specification</h4><ul><li>Daily production capacity: 50 – 70 liters</li><li>Input water pressure: 0,3 – 0,7 MPa</li><li>Input water temperature: &lt; 35 °C</li><li>Maximum input water TDS: 1200 mg/l</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Water_purification_systems_8810a2c48a.jpg" alt="Watrex: Water purification systems" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Water_purification_systems_8810a2c48a.jpg 245w," sizes="100vw" width="2286" height="1130">Basic requirements for laboratory operations include the easy availability of pure laboratory water in the necessary quantity and quality. Distillation, a popular technique for producing purified water in the past, has virtually completely supplanted by less energy-intensive and operationally dependable alternatives today. Reverse osmosis is the foundation of the majority of contemporary systems for producing purified water; in reality, this principle is supplemented with adsorption, ion exchange, filtration, ultrafiltration, and other physical-chemical techniques.

Watrex SCI-AQUA ROWAPUR DEMI 90 Water Purification System

Fully automatic system for the preparation of clean water based on reverse osmosis combined with purification by a mixed ion exchanger.

Fully automatic system for the preparation of clean water based on reverse osmosis combined with purification by a mixed ion exchanger. Reverse osmosis membrane is protected by two-stage pre-filtration consisting of sediment and carbon filter.<a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/water-purification/reverse-osmosis-systems/rowapur-demi-90/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex ROWAPUR DEMI</a> is driven by water pressure from water distribution network, it does not require electric power.The output water has a specific conductivity less than &lt;1 µS/cm. The system includes a conductivity tester with optical indication of output water quality.Price: <bdi>761 €</bdi> ex. VAT<h4>Features</h4><ul><li>Specific conductivity of produced water &lt;1 µS/cm</li><li>6 to 12 months filters lifetime</li><li>2 – 5 years RO membrane lifetime</li><li>1000 – 2000 liters polishing filter capacity</li><li>No electricity is required for operation</li><li>Supplied from water distribution network</li></ul><h4>Technical specification</h4><ul><li>Specific conductivity of produced water: &lt; 1 µS/cm</li><li>Daily production capacity:&nbsp;up to 90 liters</li><li>Input water pressure:&nbsp;0,3 – 0,7 MPa</li><li>Input water temperature:&nbsp;&lt; 35 °C</li><li>Maximum input water TDS:&nbsp;1200 mg/l</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Water_purification_systems_8810a2c48a.jpg" alt="Watrex: Water purification systems" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Water_purification_systems_8810a2c48a.jpg 245w," sizes="100vw" width="2286" height="1130">Basic requirements for laboratory operations include the easy availability of pure laboratory water in the necessary quantity and quality. Distillation, a popular technique for producing purified water in the past, has virtually completely supplanted by less energy-intensive and operationally dependable alternatives today. Reverse osmosis is the foundation of the majority of contemporary systems for producing purified water; in reality, this principle is supplemented with adsorption, ion exchange, filtration, ultrafiltration, and other physical-chemical techniques.

Watrex SCI-AQUA ROWAPUR DEMI 180 Water Purification System

Fully automatic system for the preparation of clean water based on reverse osmosis combined with purification by a mixed ion exchanger. Reverse osmosis membrane is protected by two-stage pre-filtration consisting of sediment and carbon filter.<a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/water-purification/reverse-osmosis-systems/rowapur-demi-180/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex ROWAPUR DEMI</a> is driven by water pressure from water distribution network, it does not require electric power.The output water has a specific conductivity less than &lt;1 µS/cm. The system includes a conductivity tester with optical indication of output water quality.Price: 833<bdi> €</bdi> ex. VAT<h4>Features</h4><ul><li>Specific conductivity of produced water &lt;1 µS/cm</li><li>6 to 12 months filters lifetime</li><li>2 – 5 years RO membrane lifetime</li><li>1000 – 2000 liters polishing filter capacity</li><li>No electricity is required for operation</li><li>Supplied from water distribution network</li></ul><h4>Technical specification</h4><ul><li>Specific conductivity of produced water: &lt; 1 µS/cm</li><li>Daily production capacity:&nbsp;up to 180 liters</li><li>Input water pressure:&nbsp;0,3 – 0,7 MPa</li><li>Input water temperature:&nbsp;&lt; 35 °C</li><li>Maximum input water TDS:&nbsp;1200 mg/l</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Water_purification_systems_8810a2c48a.jpg" alt="Watrex: Water purification systems" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Water_purification_systems_8810a2c48a.jpg 245w," sizes="100vw" width="2286" height="1130">Basic requirements for laboratory operations include the easy availability of pure laboratory water in the necessary quantity and quality. Distillation, a popular technique for producing purified water in the past, has virtually completely supplanted by less energy-intensive and operationally dependable alternatives today. Reverse osmosis is the foundation of the majority of contemporary systems for producing purified water; in reality, this principle is supplemented with adsorption, ion exchange, filtration, ultrafiltration, and other physical-chemical techniques.

Watrex SCI-AQUA ROWAPUR 090 Water Purification System

Fully automatic system for the preparation of pure water based on reverse osmosis.

Fully automatic system for the preparation of pure water based on reverse osmosis. Reverse osmosis membrane is protected by three-stage pre-filtration consisting of sediment filter and two carbon adsorption filters.<a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/water-purification/reverse-osmosis-systems/rowapur-90/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex ROWAPUR</a> is driven by water pressure from water distribution network, it does not require electric power.It prepares water free of mechanical impurities, chlorine, 95-99% of all dissolved substances are removed. Depending on input water composition and supply pressure the output water has a specific conductivity in the range of 10-20 µS/cm.Price: 500<bdi>&nbsp;€</bdi> ex. VAT<h4>Features</h4><ul><li>Removes 95 – 99% of dissolved substances</li><li>Typical specific conductivity of produced water 10 – 20 µS/cm</li><li>6 to 12 months filters lifetime</li><li>2 – 5 years RO membrane lifetime</li><li>No electricity is required for operation</li><li>Supplied from water distribution network</li></ul><h4>Technical specification</h4><ul><li>Daily production capacity:&nbsp;up to 90 liters</li><li>Input water pressure:&nbsp;0,3 – 0,7 MPa</li><li>Input water temperature:&nbsp;&lt; 35 °C</li><li>Maximum input water TDS: 1200 mg/l</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Water_purification_systems_8810a2c48a.jpg" alt="Watrex: Water purification systems" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Water_purification_systems_8810a2c48a.jpg 245w," sizes="100vw" width="2286" height="1130">Basic requirements for laboratory operations include the easy availability of pure laboratory water in the necessary quantity and quality. Distillation, a popular technique for producing purified water in the past, has virtually completely supplanted by less energy-intensive and operationally dependable alternatives today. Reverse osmosis is the foundation of the majority of contemporary systems for producing purified water; in reality, this principle is supplemented with adsorption, ion exchange, filtration, ultrafiltration, and other physical-chemical techniques.

Watrex SCI-AQUA ROWAPUR 180 Water Purification System

Fully automatic system for the preparation of pure water based on reverse osmosis. Reverse osmosis membrane is protected by three-stage pre-filtration consisting of sediment filter and two carbon adsorption filters.<a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/water-purification/reverse-osmosis-systems/rowapur-180-reverse-osmosis-system/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex ROWAPUR</a> is driven by water pressure from water distribution network, it does not require electric power.It prepares water free of mechanical impurities, chlorine, 95-99% of all dissolved substances are removed. Depending on input water composition and supply pressure the output water has a specific conductivity in the range of 10-20 µS/cm.Price: 541<bdi>&nbsp;€</bdi> ex. VAT<h4>Features</h4><ul><li>Removes 95 – 99% of dissolved substances</li><li>Typical specific conductivity of produced water 10 – 20 µS/cm</li><li>6 to 12 months filters lifetime</li><li>2 – 5 years RO membrane lifetime</li><li>No electricity is required for operation</li><li>Supplied from water distribution network</li></ul><h4>Technical specification</h4><ul><li>Daily production capacity:&nbsp;up to 180 liters</li><li>Input water pressure:&nbsp;0,3 – 0,7 MPa</li><li>Input water temperature:&nbsp;&lt; 35 °C</li><li>Maximum input water TDS: 1200 mg/l</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Water_purification_systems_8810a2c48a.jpg" alt="Watrex: Water purification systems" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Water_purification_systems_8810a2c48a.jpg 245w," sizes="100vw" width="2286" height="1130">Basic requirements for laboratory operations include the easy availability of pure laboratory water in the necessary quantity and quality. Distillation, a popular technique for producing purified water in the past, has virtually completely supplanted by less energy-intensive and operationally dependable alternatives today. Reverse osmosis is the foundation of the majority of contemporary systems for producing purified water; in reality, this principle is supplemented with adsorption, ion exchange, filtration, ultrafiltration, and other physical-chemical techniques.

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