<p><strong>🎤Alex Brody</strong></p><p><strong>In 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.</strong></p><p>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.</p><p>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.</p><h5><strong>Topics Covered:</strong></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><strong>Ideal For:</strong></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><strong>Video Transcription</strong></h2><h3><strong>Ensuring Safe Drinking Water Through Advanced Analytical Chemistry</strong></h3><h4><strong>Insights from a Regulated Water Testing Laboratory</strong></h4><p>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 <strong>GC-MS and LC-MS instrumentation</strong>, supported by rigorous maintenance programs to ensure continuous operational performance and data reliability.</p><h4><strong>Regulatory Compliance and Quality Control in Drinking Water Analysis</strong></h4><p>Operating as a regulated drinking water laboratory requires adherence to stringent requirements established by agencies such as the <strong>U.S. Environmental Protection Agency (EPA)</strong> 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.</p><p>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.</p><h4><strong>Analytical Strategies for Taste and Odor Investigations</strong></h4><p>Taste and odor events represent a significant operational challenge for water utilities. Standard targeted methods are routinely applied for compounds such as <strong>2-methylisoborneol (MIB)</strong> and <strong>geosmin</strong>, which are commonly associated with earthy or musty sensory characteristics. When targeted analysis does not reveal the source, laboratories employ <strong>broad-scan GC-MS screening</strong> 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.</p><h4><strong>PFAS Monitoring: Methodological Complexity and Trace-Level Sensitivity</strong></h4><p>PFAS determination represents a rapidly evolving priority in drinking water monitoring. The laboratory currently applies <strong>EPA Method 537.1</strong>, with efforts underway to expand capabilities through certification for <strong>Method 533</strong>, 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.</p><h4><strong>Future Directions in Drinking Water Analytics</strong></h4><p>Looking ahead, the primary technological driver in regulated water analysis is the demand for <strong>increasingly lower detection limits</strong> 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.</p><p>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.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

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

<p><strong>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.</strong></p><p>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.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c04295"><strong>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</strong></a></h4><p>Alexis N. Edwards, Madeline G. Bannon, Michael S. Cordes, and Elyssia S. Gallagher*</p><p>Anal. Chem. 2026, 98, 6, 4518–4527</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c04295">https://doi.org/10.1021/acs.analchem.5c04295</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><div><p>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></p><p>During ESI, a potential is applied to the sample-containing solution. In an aqueous spray solvent, H<sub>3</sub>O<sup>+</sup> and OH<sup>–</sup> 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, H<sub>3</sub>O<sup>+</sup> or OH<sup>–</sup> 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 p<i>K</i><sub>a</sub> 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></p><p>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.</p><p>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></p><h4><strong>Materials and Methods</strong></h4><h5><strong>Native IMS-MS Analysis</strong></h5><p>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"><strong>Synapt G2-S High-Definition MS </strong></a>(Waters Corporation, Milford, MA). The trap and transfer cells contained Ar, the helium cell contained He, and the IMS cell contained N<sub>2</sub>. 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>).</p><p>To limit systematic error due to repositioning of the ESI tip between runs, <a href="javascript:void(0);">(48)</a> the <i>XYZ</i>-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 <i>XYZ</i>-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.</p><h4><strong>Results and Discussion</strong></h4><p>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 <sup>TW</sup>CCS<sub>N2→He</sub> and CIU50 in both ion modes.</p><p><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"></p><h5><strong>Proteins with Disulfide Bridges are Stable in Both Polarities</strong></h5><p>For both lysozyme and α-lactalbumin, the average <sup>TW</sup>CCS<sub>N2→He</sub> 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 <sup>TW</sup>CCS<sub>N2→He</sub> 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.</p><p><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"></p><p>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 <sup>TW</sup>CCS<sub>N2→He</sub> values in +ESI versus −ESI as well as the limited percentage of ions that undergo a change in <sup>TW</sup>CCS<sub>N2→He</sub> upon additional collisional activation.</p><p>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) Å<sup>2</sup> and (390 ± 120) Å<sup>2</sup> 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, <sup>TW</sup>CCS<sub>N2→He</sub> values being within experimental uncertainty in both ion modes.</p><p>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 <sup>TW</sup>CCS<sub>N2→He</sub> and the proteins’ high stability under activation.</p><h4><strong>Conclusions</strong></h4><p>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.</p><p>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.</p></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

<p><strong>Anna Vanluchene&nbsp;from UCT Prague’s&nbsp;Department of Chemical Engineering has received a&nbsp;prestigious start-up grant from the Dagmar Procházková Fund. However, she did not receive funding right away. In this interview, she describes how she developed ten versions of her&nbsp;</strong><i><strong>Illuminating Flow</strong></i><strong>&nbsp;project idea (combining photocatalysis with flow reactors for pharmaceutical synthesis). She explains why she considers perseverance to be crucial when applying for grants, how international experience has influenced her approach to team management, and how her research can reduce the chemical industry’s&nbsp;dependence on fossil fuels and imports from China.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_2_5b7d63b8e9.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_2_5b7d63b8e9.jpg 127w," sizes="100vw" width="1128" height="1387"></p><h5><strong>What did the Dagmar Procházková Fund grant mean to you?</strong></h5><p>I&nbsp;consider it to be a&nbsp;great success. It is the first injection of funding that will allow me to ensure full independence for my research endeavour, to start my own research group, and to fund students so I&nbsp;can get started properly.</p><h5><strong>What have been your previous experiences with grants?</strong></h5><p>During my doctorate, a <i>cotutelle</i> (international doctorate under dual supervision), I&nbsp;was funded by a&nbsp;grant from the French government. Then I&nbsp;worked at the Academy of Sciences of the Czech Republic (CAS) and received a&nbsp;Marie Skłodowska-Curie Action (MSCA) Postdoctoral Fellowship to go abroad. The idea for my now-funded project was developed about two years ago and, since then, I&nbsp;have gradually developed and adapted the idea for various grant calls. I&nbsp;submitted about ten different versions of the proposal. I&nbsp;did not receive a&nbsp;grant from the Dagmar Procházková Fund last year, but this year, my application was successful.</p><h5><strong>This probably requires a&nbsp;great deal of patience and perseverance.</strong></h5><p>Certainly, because the success rates for most grants have been declining for some time. But as a&nbsp;motivational example, I&nbsp;will tell the story of Timothy Noel, a&nbsp;Belgian professor of chemistry living in the Netherlands. He applied for the prestigious European Research Council (ERC) grant, which is among the most sought-after in Europe, seven times. But no failure deterred him and eventually he succeeded and opened the door to potentially massive grant funding. He was already one of the world’s&nbsp;top scientists in the field at that time and openly described his journey on his blog <a target="_blank" rel="noopener noreferrer" href="https://www.noelresearchgroup.com/2022/03/17/my-personal-story-to-obtain-an-erc-grant-7-submissions-4-interviews-and-6-heartbreaks/"><strong>blog</strong></a>.</p><h5><strong>What advice does this convey to other grant applicants and early career researchers?</strong></h5><p>Start early, read a&nbsp;lot, don’t&nbsp;give up, and—most importantly—apply repeatedly. Learn from rejections and overcome possible frustration from failures. Read blogs and books by successful people, where you will find not only the glorious results of their work, but also the hardships they faced over their entire journeys. Of course, building your team and laboratory is impossible without finances. I&nbsp;myself still hope that I&nbsp;will be able to receive even bigger grants in the future.</p><h5><strong>How has your international experience influenced your scientific approach?</strong></h5><p>A&nbsp;lot and on several levels. Different laboratories teach you how to do&nbsp;things differently. You gain varied experience about how different institutions function. You see other people’s&nbsp;positive motivations, their ability to be ambitious without negativity, their involvement in institutional matters, their openness to cooperation with companies (e.g., tech transfers, spin-offs). The most important thing is to broaden your horizons. I&nbsp;see going abroad as a&nbsp;necessity. What I&nbsp;have taken away the most is drive, great support, and the idea that scientific output is not just about metrics, but also about dedication to one’s&nbsp;topic.</p><h5><strong>What is your </strong><i><strong>Illuminating Flow: Transport Phenomena in Photocatalysis</strong></i><strong> about, in layperson’s&nbsp;terms, and how is it unique?</strong></h5><p>Most of today’s&nbsp;chemical industry is still based on thermal processes and fossil fuels. Photochemistry enables electrification, where the energy source is photons delivered by LEDs, which can generate electricity from renewable sources. Current research focuses mainly on chemical reactions and their mechanisms, but as a&nbsp;chemical engineer, I&nbsp;focus on designing processes and reactors suitable for industrial use. In batch reactors, light fades rapidly with distance from a&nbsp;source, so much of a&nbsp;reaction mixture is not illuminated. Flow reactors solve this problem, but they bring new challenges such as working with solid catalysts and subsequently scaling up production and achieving higher production rates of the desired chemicals at a&nbsp;given scale.</p><p>One can imagine a&nbsp;transparent tube with a&nbsp;catalyst on the walls, upon which light shines and through which reactants flow. This project has a&nbsp;unique emphasis on engineering solutions and overall process efficiency.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_3_b978abf25c.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_3_b978abf25c.jpg 241w," sizes="100vw" width="1228" height="799"></p><h5><strong>So, were you inspired by a&nbsp;gap in the market to connect photocatalysis with transport phenomena?</strong></h5><p>Exactly. I&nbsp;combine my areas of expertise: microfluidics, photocatalytic degradation of organic substances (CAS), and synthesis (MSCA Postdoctoral Fellowship). The idea itself is not new, and pharmaceutical companies are very interested in “greener” photochemistry, but in practice, there is often a&nbsp;lack of appropriate engineering solutions and apparatus for industrial use.</p><h5><strong>What are the practical applications of your work and what substances are you focusing on?</strong></h5><p>Mainly on pharmaceuticals and on the synthesis of so-called fine chemicals, which are often the building blocks for the production of pharmaceuticals. There is also a&nbsp;geopolitical dimension to this, i.e. less dependence on imports from China and sustainable synthesis in Europe where it makes economic sense.</p><h5><strong>And what chemicals are you specifically talking about?</strong></h5><p>For example, building blocks for advanced synthesis, compounds prepared by trifluoromethylation reactions, or products of oxidation reactions with singlet oxygen. At the same time, we focus on reactions that are, in the classical design process, less safe or technologically demanding, where new approaches, such as photochemistry in flow reactors, could be safer and have better process control. Of course, this is not a&nbsp;universal solution for all types of reactions.</p><h5><strong>The goal of this project?</strong></h5><p>I&nbsp;plan to start a&nbsp;fully functional laboratory and research team, create high-quality experimental data on selected molecules and based on them, try to build cooperation with industrial partners. Without data, it is impossible to come to companies with just an idea. Within three years, I&nbsp;would like to have results that can be realistically presented and further developed.</p><h5><strong>What are the main challenges in transport phenomena during photocatalysis?</strong></h5><p>The methodology for repeatability of experiments in photochemistry is relatively demanding and there are unforeseen obstacles in building apparatus. Also, the scale-up from microliters to a&nbsp;larger scale.</p><h5><strong>What methodology will you use, and how big are the microreactors and their flow rates?</strong></h5><p>I&nbsp;have two different directions in methodological design. The first direction involves microreactors the size of a&nbsp;laboratory slide. You make a&nbsp;structure using a&nbsp;laser, and then you have to cast it and make a&nbsp;microreactor. This allows you to quickly adjust the geometry of the reactor. This method is, of course, not applicable in the commercial setting, but it is ideal for studying transport phenomena and precise measurements.</p><p>The second direction involves reactors that are flow cells. These are already larger, approximately 15 x 15 centimetres, and their flow rates are in the order of millilitres per hour. This is the initial scale that we will further increase during the project.</p><h5><strong>There is a&nbsp;big difference between a&nbsp;flow rate of microlitres per hour and industrial needs. Will it not work differently in reality?</strong></h5><p>Our research will focus on studying the phenomena themselves for now, and scaling will be addressed later. In addition, we will combine the experimental data obtained with computer simulations that will help design suitable conditions for a&nbsp;larger scale. For some high-value fine chemicals, these scales, combined with continuous operation or parallelization of reactors, may already be practically usable.</p><h5><strong>What catalysts will you use and how will you attach them to the reactor walls?</strong></h5><p>I&nbsp;am focusing on heterogeneous photocatalysis, and we will mainly use graphitic carbon nitride and its more advanced modifications. These are semiconductor materials that can be synthesized relatively easily and are suitable for immobilization on glass reactor walls. A&nbsp;key part of this project is the creation of a&nbsp;stable catalytic layer for long-term flow-through operations. To increase the contact of reactants with the catalyst, we will also consider multiphase modes, for example, gas bubbling, in order to disrupt the otherwise laminar flow.</p><h5><strong>Why did you choose this field and the Department of Chemical Engineering?</strong></h5><p>During my postdoc in Belgium, the department had an opening for an Assistant Professor position that caught my attention and I&nbsp;applied for it. I&nbsp;did my undergraduate, graduate, and initial doctoral studies here, and I&nbsp;love the department. I&nbsp;have a&nbsp;Bachelor’s&nbsp;degree in Chemistry.</p><h5><strong>Are you collaborating with anyone?</strong></h5><p>We collaborate with BUT Brno focusing on creating layers and immobilizing catalysts on glass, as well as with the Institute of Chemical Process Fundamentals of the Academy of Sciences of the Czech Republic. And as for organic synthesis, we are connected with Ghent University via postdoc internships. At the same time, my colleague Viola Tokárová and I&nbsp;received a&nbsp;Czech Science Foundation grant in cooperation with BUT Brno and Masaryk University, with our part of the project focusing on the use of flow reactors for photochemical reactions and testing the antibacterial properties of photocatalytic materials. And I&nbsp;am writing other grant proposals in which I&nbsp;am trying to build new collaborations.</p><h5><strong>What does the creation of an independent research group at UCT Prague look like?</strong></h5><p>I&nbsp;started by renovating the premises that were assigned to me and gradually building my team. It is important for research work to have Ph.D. students; I&nbsp;have already hired one and we will recruit more. In addition to building the group, I&nbsp;will engage in securing further funding for the group, so I&nbsp;will be writing more grant proposals. It is important to think far enough in advance when it comes to prospective funding for a&nbsp;research group.</p><h5><strong>What type of students are you looking for?</strong></h5><p>The laboratory and team I&nbsp;are building will be very multidisciplinary, just like the area I&nbsp;am working on. That is why I&nbsp;am looking for students who are attracted to true multidisciplinary research, those who, for example, have knowledge of engineering, but who don’t&nbsp;mind a&nbsp;little bit of pure chemistry. One student in their own right does not have to (and cannot) know every subject, so I&nbsp;will ideally have a&nbsp;team consisting of different people with different research backgrounds. Motivated, DIY-type students who would rather enthusiastically build or invent something themselves than conduct repetitive measurements. Organic or analytical chemists will also find their place here. If this topic is interesting to students in any way, they can definitely contact me. I&nbsp;am also open to interdepartmental cooperation with other UCT Prague Faculties.</p><h5><strong>How would you describe your path to photocatalysis/chemical engineering?</strong></h5><p>Studying Chemistry as an undergrad gave me a&nbsp;broad perspective, but I&nbsp;was gradually narrowing my focus and eventually chose engineering. Chemical engineering intrigued me with its logic and was the easiest for me to grasp at the time. But I&nbsp;have always enjoyed working on projects more than the studies themselves. Even during my Bachelor studies, I&nbsp;really enjoyed and was interested in the Professor Štěpánek Group’s&nbsp;projects, where I&nbsp;was doing something completely different than I&nbsp;do&nbsp;now. I&nbsp;only got into photochemistry during my time at CAS and then, during my postdoctoral fellowship, I&nbsp;devoted myself to electrochemistry. My current focus is, thus, a&nbsp;natural interlinking of all these areas. Consequentially, I&nbsp;developed an awareness of the necessity to become independent and return to the department with my own, different research agenda, which, in my opinion, is an important and correct basis for establishing my own research group.</p><h5><strong>What is the biggest challenge of this project for you?</strong></h5><p>The transition from being a&nbsp;postdoc to a&nbsp;leadership position is a&nbsp;big change for me and I&nbsp;think it is not talked about enough. It means a&nbsp;shift from my own experimental work to leading a&nbsp;team, planning and delegating tasks, and motivating students. From a&nbsp;practical point of view, one of the main challenges is the transfer of reactions from the microscale to functional systems, the construction of reactors, the immobilization of catalysts, and generally confirming that this direction makes sense in the long term and that it has future potential.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_1_66ac267e06.jpg" alt="VŠCHT Prague/Tomáš Balický: I waited two years for a start-up grant and wrote ten versions of my project idea" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_VSCHT_Praha_Na_startovaci_grant_jsem_cekala_dva_roky_a_napsala_deset_verzi_projektu_1_66ac267e06.jpg 155w," sizes="100vw" width="830" height="839"></p>

I waited two years for a start-up grant and wrote ten versions of my project idea

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Bioanalytic Quantitative LC-MS/MS analysis training

The goal of the training is to introduce users to the procedures and capabilities of the LC-MS/MS system and software to achieve sensitivity, selectivity, precision and reproducibility in quantitative analysis.

<h4><strong>BASIC INFORMATION</strong></h4><ul><li>TITLE: <strong>Quantitative LC-MS/MS analysis training</strong></li><li>CATEGORY: <strong>LC-MS/MS training</strong></li><li>LOCATION: <strong>Lodz, PL</strong></li><li>TRAINING TIME: <strong>3 days</strong></li><li>NUMBER OF PARTICIPANTS: <strong>up to 5 people</strong></li><li>EQUIPMENT:<strong> SCIEX QTRAP LC-MS/MS</strong></li></ul><figure class="image"><img style="aspect-ratio:1200/675;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Quantitative_LC_MS_MS_analysis_training_d13b5d8127.jpg" alt="Bioanalytic: Bioanalytic Quantitative LC-MS-MS analysis training." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Quantitative_LC_MS_MS_analysis_training_d13b5d8127.jpg 245w," sizes="100vw" width="1200" height="675"></figure><h4><strong>TRAINING DESCRIPTION</strong></h4><p>Quantitative LC-MS/MS analysis - the training is designed for laboratory personnel using LC-MS/MS systems for quantitative analysis. The following topics are covered during the training:</p><ul><li>Triple quadrupole spectrometer calibration</li><li>MRM pair formation and optimization</li><li>Optimization of ion source parameters</li><li>Optimization of chromatographic parameters</li><li>Sample preparation using the example of blood drawn on <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1283"><strong>Mitra®</strong></a> samplers (VAMS)</li><li>Matrix effect, internal standards (ISTD), matrix curves</li><li>Validation of the quantitative method</li><li>Reporting of results</li></ul><p>The goal of the training is to introduce users to the procedures and capabilities of the LC-MS/MS system and software to achieve sensitivity, selectivity, precision and reproducibility in quantitative analysis while covering the widest possible linear range of concentrations.</p><h3><strong>Training program</strong></h3><h4><span style="font-size:20px;"><strong>Day I</strong></span></h4><h5><strong>Theoretical part:</strong></h5><p>Triple quadrupole structure, ionization, MRM and sMRM scanning, chromatography, multimethods</p><h5><strong>Practical part:</strong></h5><ul><li>Q1/Q3 calibration (10 Da/s), MS/MS - resolution, m/z, intensity.</li><li>MRM pair formation and optimization (manual, semi-automatic, automatic).</li><li>Ion source optimization - T-concector and FIA</li><li>Gradient vs isocrat, dosing, column selection, temperature selection, other important parameters</li><li>Establishment and optimization of LC-MS/MS method.</li><li>How to take care of MS cleanliness - ionization time programming, multi-way valve, cleaning of ion source and instrument front end</li></ul><p>Sample preparation in pure solvent (standard curve, QC, solvent, solvent+ISTD, test samples), overnight analysis sequence.</p><h4><span style="font-size:20px;"><strong>Day II</strong></span></h4><h5><strong>Practical part - preparation of whole blood samples (Mitra®):</strong></h5><ul><li>Preparation of matrix standard curves</li><li>Preparation of quality control (QC) samples in three concentrations</li><li>Preparation of blank samples (without ISTD and with ISTD).</li><li>Preparation of samples for recovery determination (“pre-spiked” and “post-spiked”)</li><li>Preparation of test samples</li></ul><h5><strong>Theoretical part:</strong></h5><ul><li>Samples in the matrix - discussion of the matrix effect and ways to level it.</li><li>Optimization of sample preparation method and LC-MS/MS method</li></ul><h5><strong>Practical part:</strong></h5><ul><li>Sample extraction from Mitra® samplers for LC-MS/MS analysis.</li><li>Sequence of analysis of prepared samples overnight</li></ul><h4><span style="font-size:20px;"><strong>Day III</strong></span></h4><h5><strong>Theoretical part:</strong></h5><ul><li>Validation of the quantitative LC-MS/MS method</li></ul><h5><strong>Practical part:</strong></h5><ul><li>Software - data integration algorithms, signal smoothing, weighing.</li><li>Matrix curves vs curves in solvent, influence of ISTD (Sciex OS).</li><li>Method validation - validation criteria, determination of LOD, LLOQ, ULOQ, linearity, working range of the method, repeatability, recovery.</li><li>Preparation of summary validation reports</li><li>Reporting of results from test samples - report vs export of data to Excel.</li><li>Summary and discussion.</li></ul>

Bioanalytic QTRAP vs QTOF Quality analysis training

The training includes a presentation of the basic differences in application and a comparison of the capabilities of QTRAP and QTOF instruments in qualitative analysis.

<h4><strong>BASIC INFORMATION</strong></h4><ul><li>TITLE: <strong>QTRAP vs QTOF Quality analysis training</strong></li><li>CATEGORY: <strong>LC-MS/MS training</strong></li><li>LOCATION: <strong>Lodz, PL</strong></li><li>TRAINING TIME: <strong>3 days</strong></li><li>NUMBER OF PARTICIPANTS: <strong>up to 5 people</strong></li><li>EQUIPMENT:<strong> SCIEX QTRAP </strong><span class="ts-pf-details-content"><strong>&amp; </strong></span><strong>QTOF LC-MS/MS</strong></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_QTRAP_vs_QTOF_Quality_analysis_training_18ca66163f.jpg" alt="Bioanalytic: Bioanalytic QTRAP vs QTOF Quality analysis training." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_QTRAP_vs_QTOF_Quality_analysis_training_18ca66163f.jpg 221w," sizes="100vw" width="1000" height="707"></p><h4><strong>TRAINING COURSE DESCRIPTION</strong></h4><p><strong>QTRAP vs QTOF qualitative analysis</strong> - the training is aimed at people who perform analyses related to substance identification or metabolite search in their research work. The training includes a presentation of the basic differences in application and a comparison of the capabilities of QTRAP and QTOF instruments in qualitative analysis. In addition to the theoretical session, participants will undergo a course in the development and optimization of <strong>DDA (IDA)</strong> (QTRAP &amp; QTOF) and <strong>DIA (SWATH) </strong>(QTOF) methods. Analysis and comparison of results will be conducted using <a target="_blank" rel="noopener noreferrer" href="https://sciex.com/products/software/sciex-os-software">SciexOS</a>, <a target="_blank" rel="noopener noreferrer" href="https://sciex.com/products/software/markerview-software">MarkerView</a>, <a target="_blank" rel="noopener noreferrer" href="https://sciex.com/products/software/lightsight-software">LightSight</a> and <a target="_blank" rel="noopener noreferrer" href="https://sciex.com/products/software/molecule-profiler-software">MoleculeProfiler</a> software.</p><h5><strong>Training program</strong></h5><h4><span style="font-size:20px;"><strong>Day I</strong></span></h4><h5><strong>Theoretical part</strong></h5><ul><li>Principle of operation of MS/MS systems</li><li>Differences and capabilities of QTRAP and QTOF</li><li>Comparison of typical analytical procedures and their application</li><li>DDA (IDA) vs DIA (SWATH) methodology.</li><li>Supporting software - LightSight, Molecule Profiler, ACD Labs, MarkerView</li><li>General principles of compound fragmentation</li></ul><h4><span style="font-size:20px;"><strong>Day II</strong></span></h4><p><strong>Objective - to develop methods to search for metabolites of a known substance.</strong></p><h5><strong>QTRAP</strong></h5><ul><li>Development of IDA screening methods (pMRM, Prec/NL, EMS)</li><li>Optimization of LC-MS/MS IDA method</li><li>Data acquisition</li></ul><h5><strong>QTOF</strong></h5><ul><li>Development and optimization of LC-MS/MS IDA and SWATH methods</li><li>Data acquisition</li></ul><h4><span style="font-size:20px;"><strong>Day III</strong></span></h4><p><strong>Objective - identification and profiling of metabolites of a known substance</strong></p><h5><strong>QTRAP data analysis</strong></h5><ul><li>Manual search and identification</li><li>LightSight, MarkerView</li></ul><h5><strong>QTOF data analysis</strong></h5><ul><li>Search and data analysis methods</li><li>Manual search and identification</li><li>IDA vs SWATH</li><li>Automated search and identification - SciexOS, databases</li><li>Molecule Profiler, MarkerView</li></ul><p>Summary and discussion<br>&nbsp;</p>

Bioanalytic QTOF quantitative and qualitative analysis training

The purpose of the training is to introduce users to the capabilities of the LC-HR-MS/MS (QTOF) system in quantitative and qualitative analysis.

<h4><strong>BASIC INFORMATION</strong></h4><ul><li>TITLE:&nbsp;<strong> QTOF quantitative and qualitative analysis training</strong></li><li>CATEGORY: <strong>LC-MS/MS training</strong></li><li>LOCATION: <strong>Lodz, PL</strong></li><li>TRAINING TIME: <strong>3 days</strong></li><li>NUMBER OF PARTICIPANTS: <strong>up to 5 people</strong></li><li>EQUIPMENT:<strong> SCIEX</strong><span class="ts-pf-details-content"><strong> </strong></span><strong>QTOF LC-MS/MS</strong></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_QTOF_quantitative_and_qualitative_analysis_training_af1620ae8c.jpg" alt="Bioanalytic: Bioanalytic QTOF quantitative and qualitative analysis training." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_QTOF_quantitative_and_qualitative_analysis_training_af1620ae8c.jpg 221w," sizes="100vw" width="1000" height="707"></p><h4><strong>TRAINING COURSE DESCRIPTION</strong></h4><p><strong>Qualitative and quantitative analysis of QTOF</strong> - the training is designed for laboratory personnel using <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?instrumentationItems=30&amp;mainauthorItems=55"><strong>high-resolution (HR) LC-MS/MS</strong></a> systems for qualitative and quantitative analysis. The following topics are covered during the training:</p><ul><li><strong>QTOF spectrometer calibration</strong></li><li><strong>Targeted and untargeted methods</strong></li><li><strong>Quantitative analysis (TOF MS, MRMhr)</strong></li><li><strong>Qualitative and quantitative analysis - DDA (IDA) vs DIA (SWATH) methodology</strong></li><li><strong>Software and its use in high-resolution data analysis</strong></li><li><strong>Reporting of results</strong></li></ul><p>The purpose of the training is to introduce users to the capabilities of the LC-HR-MS/MS (QTOF) system in quantitative and qualitative analysis. To point out the advantages of high resolution in identifying or confirming the presence of substances in a sample and also the strengths of modern QTOF systems in parallel quantitative analysis.</p><h3><strong>Training program</strong></h3><h4><span style="font-size:20px;"><strong>Day I</strong></span></h4><h5><strong>Theoretical part</strong></h5><ul><li>The principle of operation and capabilities of the QTOF system</li><li>Comparison of typical analytical procedures and their application</li><li>Targeted and quantitative analysis (TOF MS vs MRMhr)</li><li>DDA (IDA) vs DIA (SWATH) methodology.</li><li>Supporting software - Molecule Profiler, ACD Labs, MarkerView</li><li>General principles of compound fragmentation</li></ul><h4><span style="font-size:20px;"><strong>Day II</strong></span></h4><p><strong>Objective</strong> - to develop methods for quantitative analysis, confirmation or search for metabolites of a known substance, general characterization of the sample.</p><h5><strong>Practical part:</strong></h5><ul><li>Creation and optimization of the MRMhr targeted method</li><li>Creation and optimization of a non-targeted method IDA</li><li>Creation and optimization of the non-targeted method SWATH</li><li>Data acquisition (overnight)</li></ul><h4><span style="font-size:20px;"><strong>Day III</strong></span></h4><p><strong>Objective</strong> - quantitative analysis, confirmation of the presence or identification of metabolites of a known substance, general characterization of the sample (identification of compounds present in the sample), profiling.</p><h5><strong>Practical part:</strong></h5><ul><li>Quantitative analysis - TOF MS vs MRMhr</li><li>Methods for searching and analyzing data</li><li>IDA vs SWATH data</li><li>Manual search and identification</li><li>Automated search and identification - SciexOS, databases</li><li>Molecule Profiler, MarkerView</li><li>Summary and discussion</li></ul>

Watrex SYRINGE FILTERS

Syringe filters (filters for syringes) are a universal tool that ensures sample purity and prevents contamination of analytical instruments.

<p><strong>Syringe filters (filters for syringes) are a universal tool that ensures sample purity and prevents contamination of analytical instruments. They are single-use filters used for precise filtration of liquids before their application or analysis.</strong></p><p><strong>Pore Size: </strong>Filters come in various pore sizes, ranging from 0.2 μm to 5 μm, depending on the required level of filtration. Smaller pores (e.g., 0.22 μm) are often used for sterilizing solutions, as they capture bacteria and other microorganisms.</p><p>We offer syringe filters in the following sizes: <strong>4 mm, 13 mm, 25 mm, and 30 mm</strong>, all available with pore sizes of <strong>0.22 μm and 0.45 μm</strong>.</p><p><strong>Filter Material:</strong> Syringe filters are made from different materials that are compatible with various sample types. It is important to select the correct filter material based on the chemical composition of the sample. We offer syringe filters made from the following materials:</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_SYRINGE_FILTRY_b6ffda00e2.jpg" alt="Watrex: Watrex SYRINGE FILTERS" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Watrex_Watrex_SYRINGE_FILTRY_b6ffda00e2.jpg 245w," sizes="100vw" width="1808" height="1017"></p><h4><strong>Nylon</strong></h4><ul><li>Suitable for <strong>aqueous solutions</strong> and most <strong>organic solvents</strong>.</li><li>It has strong <strong>mechanical stability</strong> and excellent chemical compatibility with <strong>esters, bases, phenols, and alcohols.</strong></li></ul><h4><strong>PTFE (Polytetrafluoroethylene)</strong></h4><ul><li>Chemically resistant to most <strong>organic solvents</strong>.</li><li>It has very broad chemical and thermal compatibility.</li><li>PTFE filters are recommended for <strong>strong acids and bases</strong> and are excellent for filtration and degassing chromatography.</li></ul><h4><strong>PVDF (Polyvinylidene fluoride)</strong></h4><ul><li>Suitable for <strong>biological samples</strong>.</li><li>It has good <strong>chemical resistance</strong> and low UV absorption.</li><li>Commonly used for filtering all water-based samples and most solvents.</li></ul><h4><strong>PES (Polyester)</strong></h4><ul><li>Ideal for <strong>water-based samples</strong>, especially <strong>biological ones</strong>, with a fast and high flow rate.</li></ul><h4><strong>MCE (Mixed Cellulose Esters)</strong></h4><ul><li>Ideal for <strong>aqueous samples</strong>, <strong>tissue cultures</strong>, and <strong>sensitive biological samples</strong>.</li><li>It has lower chemical resistance, excellent water flow, and a better cutoff effect.</li></ul><h4><strong>PP (Polypropylene)</strong></h4><ul><li>Ideal for filtering all water-based samples and most solvents.</li><li>Used for general <strong>filtration of biological samples</strong>, <strong>solvents</strong>, <strong>deionized water</strong>, and reducing biological load.</li><li>It has good thermal compatibility.</li></ul><h5><strong>Examples of Use:</strong></h5><ol><li><strong>Sterilization of solutions: </strong>Filtration can remove bacteria and other microorganisms from solutions.</li><li><strong>Sample purification: </strong>Samples are filtered before analysis to remove solid particles that could contaminate analytical instruments or affect analysis results.</li><li><strong>Preparation for chromatography:</strong> Filtration before entering devices like HPLC (High-Performance Liquid Chromatography) to ensure sample purity.</li></ol><p><strong>You can also visit the full range of syringe filters on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=syringe+filters&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>Watrex website</strong></a><strong>.</strong></p>

Watrex application and R&D laboratory

Watrex application and R&D laboratory is providing a range of analyses.

<p><strong>Watrex application and R&amp;D laboratory is providing a range of analyses with special focus in the following fields:</strong></p><ul><li>Chemical analysis for construction industry</li><li>Environmental analysis</li><li>Sample preparation including online solid-phase extraction protocols</li><li>Development of methods for pharmaceutical analysis</li><li>Characterization of synthetic polymers by GPC</li><li>Column technology and methods for chiral separation</li><li>Parameters evaluation and testing in ion chromatography applications</li></ul><h5><strong>Our ready-to-go tests include:</strong></h5><ul><li>Analysis of carbohydrates</li><li>Characterization of polymers</li><li>Analysis of organic acids</li><li>Construction analysis</li><li>Analysis of ions, pH and water hardness</li></ul>

ECOM ECP201L Preparative HPLC Pump

Preparative HPLC pump with a flow rate range of up to 1000 ml/min.

<div style="display:block;" aria-labelledby="tab_item-0"><p>The <strong>ECP201L Preparative Pump</strong> is an innovative, powerful, and cost-effective unit for preparative liquid chromatography where high pressure is needed.&nbsp;The pump with 4 low-pressure valves delivers a flow rate of up to <strong>1000 ml/min</strong> at a very&nbsp;high output pressure of up to <strong>15 MPa (2176 psi).</strong></p><h3><strong>Main features and benefits</strong></h3><ul><li><strong>Durability&nbsp;</strong>– The pump is constructed for high pressure and flow rates. This makes it suitable for day-to-day long-term use in production</li><li><strong>Wide application possibilities</strong> – The unit is used for pharmaceutical separations and plant extract purification, such as cannabinoids, peptides, and oligonucleotides. Also, it has much wider use in other chemical production, such as dosing into chemical reactors, and in various laboratory uses. Another advantage is the usability of the same device for separation method development.</li><li><strong>Smart controls and diagnostics</strong>&nbsp;– It is easy to operate, especially with ECOMAC and Clarity software. This makes unit management powerful and convenient. The <strong>basic version</strong> of the <strong>ECOMAC software</strong> is available <strong>free of charge</strong>. It is also used f<strong>or service and diagnostics</strong>.</li><li><strong>Other useful features</strong><ul style="list-style-type:circle;"><li>A new learning algorithm for <strong>pulsation suppression</strong></li><li>A <strong>leakage sensor</strong></li><li>A <strong>seal wash kit for longer piston seal life</strong></li><li>Also available in configurations made of&nbsp;<strong>certified bio-inert materials</strong></li></ul></li></ul><h4><strong>Parameters</strong></h4><ul><li><strong>Flow rate: </strong>1– 1000 ml/min</li><li><strong>Maximum operating pressure: </strong>15 MPa up to 1000 ml/min</li><li><strong>Flow rate setting: </strong>1 ml/min steps</li><li><strong>Repeatability of flow rate adjusting:&nbsp;</strong>± 1 %</li><li><strong>Accuracy of flow rate setting:&nbsp;</strong>± 2 %</li><li><strong>Wetted materials:&nbsp;</strong>stainless steel, PEEK, TefzelTM, PE, ceramic, seals</li><li><strong>Communication:&nbsp;</strong>RS232,Ethernet (LAN),USB,Remote digital I/O</li><li><strong>Power supply:&nbsp;</strong>100-240V VAC</li><li><strong>Power input: </strong>500 VA</li><li><strong>Dimensions W x H x D:&nbsp;</strong>276 x 153 x 620 mm (10.87 x 6.14 x 24.40 in)</li><li><strong>Weight:&nbsp;</strong>26 kg (57.32 lb)</li><li><strong>Pressure Compensation Learning:&nbsp;</strong>yes&nbsp;</li></ul></div>

ECOM PREPBOX A3L8E Chromatography Separation System

PREPBOX is a compact alternative to modular preparative systems. It is assembled according to the customer's wishes.

<div style="display:block;" aria-labelledby="tab_item-0"><p><strong>Complete preparative modular system</strong> with one basic gradient pump and optionally secondary pump for repetitive sampling or with injection valve. Also switching valve for&nbsp;<abbr title="Countercurrent Chromatography"><strong>CCC</strong></abbr><strong> applications</strong>. PDA four channel detector up to 800&nbsp;nm.&nbsp;It is assembled according to the customer's wishes. It is used for high-capacity systems or with centrifugal chromatography systems like in pharmaceutical purification of <strong style="caret-color:auto;">cannabis extracts</strong><span style="caret-color:auto;"> (</span><abbr title="Cannabidiol"><span style="caret-color:auto;"><strong>CBD</strong></span></abbr><span style="caret-color:auto;">, </span><abbr title="Cannabinol"><span style="caret-color:auto;"><strong>CBN</strong></span></abbr><span style="caret-color:auto;">, </span><abbr title="Cannabigerol"><span style="caret-color:auto;"><strong>CBG</strong></span></abbr><span style="caret-color:auto;">, </span><abbr title="Cannabichromene"><span style="caret-color:auto;"><strong>CBC</strong></span></abbr><span style="caret-color:auto;">, </span><abbr title="Tetrahydrocannabinol"><span style="caret-color:auto;"><strong>THC</strong></span></abbr><span style="caret-color:auto;">...).</span></p><p><strong>ECOMAC SW</strong> installed at internal PC controls the system. Fractions are collected by means of&nbsp;<strong>10 position valve</strong>&nbsp;<br><br><strong>It is necessary to purchase an operating system for the PREPBOX</strong>&nbsp;- in most cases we recommend <strong>Windows OS</strong>&nbsp;(P/N:&nbsp;ABB90000) or <strong>Linux</strong>&nbsp;(on request).<br>The system also supports the Clarity software. It is also possible to purchase a wireless mouse and keyboard set&nbsp;(P/N:&nbsp;EPC-0028) and a computer monitor&nbsp;(P/N:&nbsp;EPC-0027).</p><h5><strong>TOY18DAD 800L Detector</strong></h5><p>It is UV-VIS diode array detector, which allow measuring absorbance of four wavelengths in range of 200-800&nbsp;nm simultaneously in one cell just as scanning of whole spectra.</p><h5><strong>ECP201L Preparative HPLC Pump</strong></h5><p>Preparative pump suited for preparative liquid chromatography with very high pressure <strong>up to 15&nbsp;MPa</strong>&nbsp;at flow rate of <strong>1000&nbsp;ml/min</strong>. Advantage of this pump is a very stable run even at low flow rates.</p><h5><strong>ECP2300 Preparative Gradient Pump</strong></h5><p><strong>Preparative HPLC pump</strong> suited for&nbsp;<strong>preparative</strong>&nbsp;applications in liquid chromatography with a pressure <strong>up to 15 MPa</strong> at flow rate of <strong>300&nbsp;ml/min</strong>.&nbsp;New sophisticated unit allows achieving a precise&nbsp;<strong>low-pressure gradient</strong>, i.e. gradual changes of solvent composition by mixing&nbsp;<strong>up to four liquids</strong>&nbsp;at the pump entry.</p><h3><strong>Parameters</strong></h3><ul><li><strong>Interface: </strong>5x USB, HDMI, 2X RS232, LAN, VGA</li><li><strong>Power supply: </strong>100 - 240 V AC</li><li><strong>Power input: </strong>490 W</li><li><strong>Dimensions W x H x D: </strong>405x490x525 mm (15.94x19.29x20.67 in)</li><li><strong>Weight: </strong>55 kg</li></ul></div>

ECOM COMPACT SEMI-PREPARATIVE SYSTEM (10 ml/min, ECS08)

A highly effective Compact semi-preparative system containing UV-VIS DAD detector, analytical gradient pump with degasser, automatic inject valve and fraction collector.

<p>A highly effective Compact semi-preparative system containing&nbsp;<strong>UV-VIS DAD detector, analytical gradient pump with degasser, automatic inject valve and fraction collector</strong>. The detector allows absorbance measuring at four wavelengths at the same time or scanning through entire spectrum.</p><p>The system is <strong>controlled by a built-in PC and touchscreen</strong>.</p><p>A modular solution <strong>allows configuring the unit according to customer needs</strong>. This system contains a detector with a wavelength range of 200 –&nbsp; 800 nm, a pump with a flow rate up to 10 ml/min and a fraction collector.</p><h3><strong>Main parts</strong></h3><h5><strong>TOY18DAD800L DETECTOR</strong></h5><p>It is a UV-VIS diode array detector, which allows measuring the absorbance of&nbsp;<strong>four wavelengths in a range of 200–800 nm simultaneously in one cell&nbsp;just as scanning of whole spectra. Standardly is assembled with preparative cell PLCC07L, but other cells are available</strong>.</p><h5><strong>ECF2096 FRACTION COLLECTOR</strong></h5><p>Fractions are collected according to chosen method, which is simply created using a touch screen. Racks for 8, 21,40 ml tubes, 60 ml vials or 12 funnels, 30 mm.</p><h5><strong>AUTOMATIC INJECT VALVE</strong></h5><p>The valve is driven by a step motor and it is automatically switched by software. The system also allows manual sample injection by opening the column.</p><h5><strong>SYSTEM PC INFO</strong></h5><p>Installed industrial PC with Intel Atom 4 core processor. OS Linux, Touch screen 12,1“ 1024 x 786, SW QUEEN controls: gradient, flow rate, wavelengths, fractions collection etc. Remote administration is available. Possibility of measuring at four wavelengths at the same time or scanning through entire spectra. Furthermore, the possibility of <strong>displaying 3D data</strong>.&nbsp;</p><h5><strong>ECP2010 ANALYTICAL GRADIENT PUMP</strong></h5><p>Modified for the compact system,&nbsp;<strong>analytical gradient pump with degasser</strong>&nbsp;and with flow rate up to 1<strong>0 ml/min</strong>&nbsp;(40 MPa, 5082 PSI).&nbsp;Unit software includes a new learning algorithm for pulsation suppression and many testing and diagnostic functions. Four gradient valves allow changing mobile phases without bottles alternation.&nbsp;</p><h3><strong>COMPACT PREPARATIVE SYSTEM &nbsp;&nbsp;</strong>&nbsp;&nbsp;&nbsp;</h3><ul><li><strong>Interface:</strong> 3xUSB, 2xLAN, RS232</li><li><strong>Power supply:</strong> 100 - 240 V AC</li><li><strong>Power input: </strong>400 W</li><li><strong>Dimensions (W x H x D):</strong> 500 x 678 x 482 mm (19.69 x 26.69 x 18.98")</li><li><strong>Weight:</strong> 55 kg (121.30 lb)</li></ul><h5><strong>Detector</strong></h5><ul><li><strong>Wavelength range: </strong>200 - 800 nm &nbsp; (256 elements on CCD)</li><li><strong>Number of channels (Signals):</strong> 4</li><li><strong>Scan: </strong>200 - 800 nm,up to &nbsp;20 Hz, step 1 nm</li><li><strong>Typical spectral half-width:</strong> 10 mn</li><li><strong>Accuracy of adjustment / Reproducibility:</strong> ± 1 nm / ±0.5 nm</li><li><strong>Noise level at test cell (254 nm, TC 0.75s): </strong>± 5 x 10<sup>-5</sup> AU</li><li><strong>Drift at test cell (254 nm after 1 h):</strong> 1 x 10<sup>-3</sup> AU/hr</li><li><strong>Materials in contact with mobile phase: </strong>FEP; fused silica, stainless steel, PEEK</li><li><strong>Time constant (T63):</strong> 0.5 s, 0.75 s, 1.0 s, 2.0 s, 4.0 s, 8.0 s, 16.0 s, 0.2 s, 0.1 s</li></ul><h5><strong>Fraction collector</strong></h5><ul><li><strong>Available racks (two racks per unit)</strong><ul><li>EC08 48 tubes of 8 ml</li><li>EC21 36 tubes of 21 ml</li><li>EC40 24 tubes of 40 ml</li><li>EC60 20 vials of 60 ml</li><li>F12A 12 funnels, 30 mm</li></ul></li><li><strong>Maximum flow rate for tubes 8 ml: </strong>max. 50 ml/min</li><li><strong>Maximum flow rate for tubes 21, 40 ml:</strong> max. 300 ml/min</li><li><strong>Maximum flow rate for vials 60 ml: </strong>max. 300 ml/min</li><li><strong>Maximum flow rate for funnels: </strong>max. 500 ml/min</li><li><strong>Wetted materials: </strong>FEP, Tefzel®, PPS, KEL-F, PTFE, PEEK, SS 316, SIMAX glass</li><li><strong>Input tubing:</strong> OD 1/8“ x ID 1/16“ FEP</li></ul><h5><strong>Pump</strong></h5><ul><li><strong>Flow rate: </strong>0.02 - 10.00 ml/min</li><li><strong>Maximum operating pressure:</strong> 40 MPa (5082 PSI)</li><li><strong>Repeatability of flow rate adjusting:</strong> ± 0.5 %</li><li><strong>Accuracy of flow rate setting: </strong>± 2 %</li><li><strong>Wetted materials: </strong>stainless steel, sapphire, KEL-F, seals*</li><li><strong>Output capillary outer diameter: </strong>1/16”</li><li><strong>Input tubing outer diameter: </strong>1/8”</li><li><strong>Gradient valves control module - OPTIONALLY:</strong> Up to four valves</li></ul>

ECOM COMPACT PREPARATIVE SYSTEM (50 ml/min, ECS58)

A highly effective Compact preparative system containing UV-VIS DAD detector, analytical gradient pump with degasser, automatic inject valve and fraction collector.

<p>A highly effective Compact preparative system containing&nbsp;<strong>UV-VIS DAD detector, analytical gradient pump with degasser, automatic inject valve and fraction collector</strong>. The detector allows absorbance measuring at four wavelengths at the same time or scanning through entire spectrum.</p><p>The system is <strong>controlled by a built-in PC and touchscreen</strong>.</p><p>A modular solution <strong>allows configuring the unit according to customer needs</strong>. This system contains a detector with a wavelength range of 200 –&nbsp; 800 nm, a pump with a flow rate up to 10 ml/min and a fraction collector.</p><h3><strong>Main parts</strong></h3><h5><strong>TOY18DAD800L DETECTOR</strong></h5><p>It is a UV-VIS diode array detector, which allows measuring the absorbance of&nbsp;<strong>four wavelengths in a range of 200–800 nm simultaneously in one cell&nbsp;just as scanning of whole spectra. Standardly is assembled with preparative cell PLCC07L, but other cells are available</strong>.</p><h5><strong>ECF2096 FRACTION COLLECTOR</strong></h5><p>Fractions are collected according to chosen method, which is simply created using a touch screen. Racks for 8, 21,40 ml tubes, 60 ml vials or 12 funnels, 30 mm.</p><h5><strong>AUTOMATIC INJECT VALVE</strong></h5><p>The valve is driven by a step motor and it is automatically switched by software. The system also allows manual sample injection by opening the column.</p><h5><strong>SYSTEM PC INFO</strong></h5><p>Installed industrial PC with Intel Atom 4 core processor. OS Linux, Touch screen 12,1“ 1024 x 786, SW QUEEN controls: gradient, flow rate, wavelengths, fractions collection etc. Remote administration is available. Possibility of measuring at four wavelengths at the same time or scanning through entire spectra. Furthermore, the possibility of <strong>displaying 3D data</strong>.&nbsp;</p><h5><strong>ECP2050 PREPARATIVE GRADIENT PUMP</strong></h5><p>Modified for the compact system,&nbsp;<strong>quaternary gradient pumps</strong>&nbsp;with flow rate up to&nbsp;<strong>50 ml/min</strong>&nbsp;(30 MPa, 4351 PSI).&nbsp;Unit software includes a new learning algorithm for pulsation suppression and many testing and diagnostic functions.</p><h3><strong>COMPACT PREPARATIVE SYSTEM &nbsp;&nbsp;</strong>&nbsp;&nbsp;&nbsp;</h3><ul><li><strong>Interface:</strong> 3xUSB, 2xLAN, RS232</li><li><strong>Power supply:</strong> 100 - 240 V AC</li><li><strong>Power input: </strong>400 W</li><li><strong>Dimensions (W x H x D):</strong> 500 x 678 x 482 mm (19.69 x 26.69 x 18.98")</li><li><strong>Weight:</strong> 55 kg (121.30 lb)</li></ul><h5><strong>Detector</strong></h5><ul><li><strong>Wavelength range: </strong>200 - 800 nm &nbsp; (256 elements on CCD)</li><li><strong>Number of channels (Signals):</strong> 4</li><li><strong>Scan: </strong>200 - 800 nm,up to &nbsp;20 Hz, step 1 nm</li><li><strong>Typical spectral half-width:</strong> 10 mn</li><li><strong>Accuracy of adjustment / Reproducibility:</strong> ± 1 nm / ±0.5 nm</li><li><strong>Noise level at test cell (254 nm, TC 0.75s): </strong>± 5 x 10<sup>-5</sup> AU</li><li><strong>Drift at test cell (254 nm after 1 h):</strong> 1 x 10<sup>-3</sup> AU/hr</li><li><strong>Materials in contact with mobile phase: </strong>FEP; fused silica, stainless steel, PEEK</li><li><strong>Time constant (T63):</strong> 0.5 s, 0.75 s, 1.0 s, 2.0 s, 4.0 s, 8.0 s, 16.0 s, 0.2 s, 0.1 s</li></ul><h5><strong>Fraction collector</strong></h5><ul><li><strong>Available racks (two racks per unit)</strong><ul><li>EC08 48 tubes of 8 ml</li><li>EC21 36 tubes of 21 ml</li><li>EC40 24 tubes of 40 ml</li><li>EC60 20 vials of 60 ml</li><li>F12A 12 funnels, 30 mm</li></ul></li><li><strong>Maximum flow rate for tubes 8 ml: </strong>max. 50 ml/min</li><li><strong>Maximum flow rate for tubes 21, 40 ml:</strong> max. 300 ml/min</li><li><strong>Maximum flow rate for vials 60 ml: </strong>max. 300 ml/min</li><li><strong>Maximum flow rate for funnels: </strong>max. 500 ml/min</li><li><strong>Wetted materials: </strong>FEP, Tefzel®, PPS, KEL-F, PTFE, PEEK, SS 316, SIMAX glass</li><li><strong>Input tubing:</strong> OD 1/8“ x ID 1/16“ FEP</li></ul><h5><strong>Pump</strong></h5><ul><li><strong>Flow rate:</strong> 0.1 – 50 ml/min</li><li><strong>Maximum operating pressure:</strong> 30 MPa (4351 PSI)</li><li><strong>Flow rate setting: </strong>0.1 ml/min steps</li><li><strong>Repeatability of flow rate adjusting:</strong> ± 0.5 %</li><li><strong>Accuracy of flow rate setting: </strong>± 2 %</li><li><strong>Wetted materials: stainless steel, PEEK, TefzelTM, PE, ceramic, seals *</strong></li><li><strong>Output capillary outer diameter: 1/8”</strong></li><li><strong>Input tubing outer diameter: </strong>1/8”</li><li><strong>Gradient valves control module - OPTIONALLY:</strong> Up to six valves</li></ul>

ECOM COMPACT PREPARATIVE SYSTEM (250 ml/min, ECS28)

A highly effective Compact preparative system containing UV-VIS DAD detector, preparative gradient pump, an automatic inject valve, and a fraction collector. 

<p>A highly effective Compact semi-preparative system containing&nbsp;<strong>UV-VIS DAD detector, preparative gradient pump, an automatic inject valve, and a fraction collector</strong>. The detector allows absorbance measuring at four wavelengths at the same time or scanning through entire spectrum.</p><p>The system is <strong>controlled by a built-in PC and touchscreen</strong>.</p><p>A modular solution <strong>allows configuring the unit according to customer needs</strong>. This system contains a detector with a wavelength range of 200 –&nbsp; 800 nm, a pump with a flow rate up to 10 ml/min and a fraction collector.</p><h3><strong>Main parts</strong></h3><h5><strong>TOY18DAD800L DETECTOR</strong></h5><p>It is a UV-VIS diode array detector, which allows measuring the absorbance of&nbsp;<strong>four wavelengths in a range of 200–800 nm simultaneously in one cell&nbsp;just as scanning of whole spectra. Standardly is assembled with preparative cell PLCC07L, but other cells are available</strong>.</p><h5><strong>ECF2096 FRACTION COLLECTOR</strong></h5><p>Fractions are collected according to chosen method, which is simply created using a touch screen. Racks for 8, 21,40 ml tubes, 60 ml vials or 12 funnels, 30 mm.</p><h5><strong>AUTOMATIC INJECT VALVE</strong></h5><p>The valve is driven by a step motor and it is automatically switched by software. The system also allows manual sample injection by opening the column.</p><h5><strong>SYSTEM PC INFO</strong></h5><p>Installed industrial PC with Intel Atom 4 core processor. OS Linux, Touch screen 12,1“ 1024 x 786, SW QUEEN controls: gradient, flow rate, wavelengths, fractions collection etc. Remote administration is available. Possibility of measuring at four wavelengths at the same time or scanning through entire spectra. Furthermore, the possibility of <strong>displaying 3D data</strong>.&nbsp;</p><h5><strong>ECP2200 PREPARATIVE GRADIENT PUMP</strong></h5><p>Modified for the compact system,&nbsp;<strong>quaternary gradient pumps</strong>&nbsp;with flow rate up to&nbsp;<strong>250 ml/min</strong>&nbsp;(30 MPa at 100 ml/min and then linearly down up to 15 MPa at 250 ml/min).&nbsp;Unit software includes a new learning algorithm for pulsation suppression and many testing and diagnostic functions.</p><h3><strong>COMPACT PREPARATIVE SYSTEM &nbsp;&nbsp;</strong>&nbsp;&nbsp;&nbsp;</h3><ul><li><strong>Interface:</strong> 3xUSB, 2xLAN, RS232</li><li><strong>Power supply:</strong> 100 - 240 V AC</li><li><strong>Power input: </strong>400 W</li><li><strong>Dimensions (W x H x D):</strong> 500 x 678 x 482 mm (19.69 x 26.69 x 18.98")</li><li><strong>Weight:</strong> 55 kg (121.30 lb)</li></ul><h5><strong>Detector</strong></h5><ul><li><strong>Wavelength range: </strong>200 - 800 nm (256 elements on CCD)</li><li><strong>Number of channels (Signals):</strong> 4</li><li><strong>Scan: </strong>200 - 800 nm,up to &nbsp;20 Hz, step 1 nm</li><li><strong>Typical spectral half-width:</strong> 10 mn</li><li><strong>Accuracy of adjustment / Reproducibility:</strong> ± 1 nm / ±0.5 nm</li><li><strong>Noise level at test cell (254 nm, TC 0.75s): </strong>± 5 x 10<sup>-5</sup> AU</li><li><strong>Drift at test cell (254 nm after 1 h):</strong> 1 x 10<sup>-3</sup> AU/hr</li><li><strong>Materials in contact with mobile phase: </strong>FEP; fused silica, stainless steel, PEEK</li><li><strong>Time constant (T63):</strong> 0.5 s, 0.75 s, 1.0 s, 2.0 s, 4.0 s, 8.0 s, 16.0 s, 0.2 s, 0.1 s</li></ul><h5><strong>Fraction collector</strong></h5><ul><li><strong>Available racks (two racks per unit)</strong><ul><li>EC08 48 tubes of 8 ml</li><li>EC21 36 tubes of 21 ml</li><li>EC40 24 tubes of 40 ml</li><li>EC60 20 vials of 60 ml</li><li>F12A 12 funnels, 30 mm</li></ul></li><li><strong>Maximum flow rate for tubes 8 ml: </strong>max. 50 ml/min</li><li><strong>Maximum flow rate for tubes 21, 40 ml:</strong> max. 300 ml/min</li><li><strong>Maximum flow rate for vials 60 ml: </strong>max. 300 ml/min</li><li><strong>Maximum flow rate for funnels: </strong>max. 500 ml/min</li><li><strong>Wetted materials: </strong>FEP, Tefzel®, PPS, KEL-F, PTFE, PEEK, SS 316, SIMAX glass</li><li><strong>Input tubing:</strong> OD 1/8“ x ID 1/16“ FEP</li></ul><h5><strong>Pump</strong></h5><ul><li><strong>Flow rate:</strong> 0.5 – 250 ml/min</li><li><strong>Maximum operating pressure:</strong> 30 MPa (4351 PSI) up to 100 ml/min then &nbsp;linearly down up to</li><li><strong>Flow rate setting: </strong>0.1 ml/min steps</li><li><strong>Repeatability of flow rate adjusting:</strong> ± 1 %</li><li><strong>Accuracy of flow rate setting: </strong>± 2 %</li><li><strong>Wetted materials: stainless steel, PEEK, TefzelTM, PE, ceramic, seals *</strong></li><li><strong>Output capillary outer diameter: 1/8”</strong></li><li><strong>Input tubing outer diameter: </strong>1/8”</li><li><strong>Gradient valves control module - OPTIONALLY:</strong> Up to six valves</li></ul>

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