<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

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Watrex Streamline VD1 Viscosimetric HPLC detector

 Watrex Streamline™ VD1 viscosimetric detector is designed for detailed characterization of polymer compounds in both aqueous and organic solvents.

<p><strong>Streamline™ VD1 viscosimetric detector measures absolute intrinsic viscosity and is ideal as a detector for online monitoring in any GPC system. VD1 enables measurement of absolute molecular size using Wheatstone bridge operating principle.</strong></p><h3><strong>FEATURES</strong></h3><ul><li>High sensitivity and stability</li><li>Low-noise</li><li>Open protocol digital data format</li><li>Direct dual analog output</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_Streamline_VD_1_Viscosimetric_detector_Universal_calibration_from_VD_1_data_1_149c741933.jpg" alt="Watrex: Watrex Streamline VD1 Viscosimetric detector - Universal calibration from VD1 data 1"></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_Streamline_VD_1_Viscosimetric_detector_Universal_calibration_from_VD_1_data_2_a616c498e8.jpg" alt="Watrex: Watrex Streamline VD1 Viscosimetric detector - Universal calibration from VD1 data 2"></p><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><strong>Wavelength Range:</strong> 190 – 720 nm</li><li><strong>Baseline Noise:</strong> ± 1 x 10-5 AU (@240 nm, 2 sec. risetime)</li><li><strong>Baseline Drift:</strong> &lt; 3 x 10-4 AU/h</li><li><strong>Wavelength Accuracy:</strong> ± 0.5 nm</li><li><strong>Wavelenghth Reproducibility:</strong> ± 0.1 nm</li><li><strong>Mean Pixel Pitch:</strong> 2.2 nm</li><li><strong>Resolution (λ FWHM):</strong> 7 nm</li><li><strong>Linearity:</strong> &gt; 2.5 AU</li><li><strong>Wavelength Program:</strong> Programmable, 10 steps</li><li><strong>Analog Output (optional):</strong> 1x 1 V</li><li><strong>Options:</strong> Dual channel configuration, thermostated flow cell</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_Streamline_VD_1_Viscosimetric_detector_Technical_specification_76756715f6.jpg" alt="Watrex: Watrex Streamline VD1 Viscosimetric detector - Technical specification"></p><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>SVD101-001</strong> Watrex Streamline™ VD1 viscosimetric detector (<strong>Price 19 741 € ex VAT</strong>)</li></ul><p><strong>You can also visit this product on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/detectors/other-hplc-detectors/streamline-vd1-detector/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>Watrex website</strong></a><strong>.</strong></p>

Watrex Streamline CT1/CT1i HPLC Column thermostat

Watrex Streamline™ CT1i column thermostat is an ideal tool for maintaining stable separation temperatures.

<p>Watrex Streamline CT1/CT1i column thermostat is an ideal tool to grant <strong>stable separation temperature</strong> even if laboratory temperature fluctuates during the day. It is also essential instrument in sugar analysis and/or many applications requiring higher column temperature. An optional built-in <strong>manual syringe</strong> front loaded sample injector increases usage comfort.</p><h3><strong>FEATURES</strong></h3><ul><li>Excellent temperature stability</li><li>Heating up to 100°C</li><li>Thermal fuse against overheating</li><li>Up to 3 columns with length of 250 mm can be placed in the thermostat</li><li>Color touch panel control</li><li>Possibility of installing manual injection valve</li></ul><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><strong>Temperature range:</strong> 10 °C above ambient temperature to 100 °C</li><li><strong>Temperature accuracy:</strong> max. 0,5 % of actual temperature</li><li><strong>Temperature stability:</strong> RSD &lt; 0,4 %</li><li><strong>Settability:</strong> 0,1 °C</li><li><strong>Internal dimensions:</strong> 320 x 50 x 30 mm (L x W x H)</li><li><strong>Compartment material:</strong> PTFE coated metal</li><li><strong>Compartment connection:</strong> USB</li><li><strong>Control:</strong> build-in color touch panel, datasystem</li></ul><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>ST101-001</strong> Streamline CT1 Columm Thermostat (<strong>Price 1 720 € ex VAT</strong>)</li><li><strong>ST101-002</strong> Streamline CT1i Columm Thermostat with manual injector</li></ul><p><strong>You can also visit this product on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/column-thermostats/streamline-ct1-columm-thermostat/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>Watrex website</strong></a><strong>.</strong></p>

Watrex Streamline GPC system

GPC system is an isocratic HPLC system consisting of one P1 pump, CT1i column thermostat with manual injector and RI1 refractive index detector.

<p><strong>GPC system is an isocratic HPLC system consisting of one P1 pump, CT1i column thermostat with manual injector and RI1 refractive index detector.</strong></p><h3><strong>FEATURES</strong></h3><ul><li>Optimized pump mechanics of P1 pump with parallel piston design offers excellent flow rate accuracy and low RI signal pulsation.</li><li>The thermal isolated optic with a counter-current heat exchanger and programmable temperature control, results in an extremly stable baseline and an optimal Signal/Noise ratio od RI1.</li><li>The system can be upgraded with autosampler and fraction collector, or VD 400 Viscometer Detector.</li><li>Data acquisition, processing and instrument control is done by Clarity Chromatography Station with GPC option or Agilent TriSEC software.</li></ul><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=streamline+p1+pump&amp;post_type=product&amp;dgwt_wcas=1?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>P1 HPLC pump: Flow Rates</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/detectors/other-hplc-detectors/streamline-ri1-detector/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>RI1 refractive index detector</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/column-thermostats/streamline-ct1-columm-thermostat/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>CT1 Column thermostat</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/999"><strong>Clarity™ Chromatography Station</strong></a></li></ul><h5><strong>COMPONENT SPECIFICATION - P1 HPLC pump: Flow Rates</strong></h5><ul><li><strong>Flow Rates:</strong> 0.001 to 10.000 mL/min</li><li><strong>Pressure:</strong> 0 to 6,000 psi (42 MPa)</li><li><strong>Flow precision:</strong> &gt; 0.2% RSD</li><li><strong>Flow accuracy:</strong> ± 1 % @ 1mL/min and 7 MPa,</li><li><strong>Pressure accuracy:</strong> ± 2% of full-scale, with 80:20 H2O/IPA @ 7 MPa</li><li><strong>Pulsation:</strong> ± 0.5 % @ 1mL/min and 7 MPa</li><li><strong>Remote inputs:</strong> USB</li></ul><h5><strong>COMPONENT SPECIFICATION - RI1 refractive index detector</strong></h5><ul><li><strong>Light Source:</strong> Long-life LED</li><li><strong>Refractive index Range:</strong> 1.00 - 1.75 RIU</li><li><strong>Baseline Noise:</strong> ± 2.5 nRIU</li><li><strong>Baseline Drift:</strong> 200 nRIU/h</li><li><strong>Linearity:</strong> &gt; 1000 μRIU</li><li><strong>Flow cell pressure resistance:</strong> 5 bar</li><li><strong>Flow cell volume:</strong> 15 μl</li><li><strong>Time constant:</strong> 0.00/0.01/0.02/0.05/0.1/0.2/0.5/1.0/2.0/5.0/10.0 s</li><li><strong>Analog Output:</strong> 1x 0-2.5V</li><li><strong>Outputs:</strong> Event 1, Start (OUT), Error (OUT), + 5 V, 24 V Valve</li></ul><h5><strong>COMPONENT SPECIFICATIONS - CT1 Column thermostat</strong></h5><ul><li><strong>Temperature range:</strong> 10 °C above ambient temperature to 100 °C</li><li><strong>Temperature accuracy:</strong> max. 0,5 % of actual temperature</li><li><strong>Temperature stability:</strong> RSD &lt; 0,4 %</li><li><strong>Settability:</strong> 0,1 °C</li><li><strong>Internal dimensions:</strong> 320 x 50 x 30 mm (L x W x H)</li><li><strong>Compartment material:</strong> PTFE coated metal</li><li><strong>Compartment connection:</strong> USB</li><li><strong>Control:</strong> build-in color touch panel, datasystem</li></ul><h5><strong>COMPONENT SPECIFICATIONS - </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/999"><strong>Clarity™ Chromatography Station:</strong></a></h5><p>Advanced chromatographic datastation for data acquisition and evaluation supported with <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1004"><strong>GPC module for MWD, Mw, Mn, Mz calculation</strong></a>. Enables rutine separations with pre-set methods, containing all experimental and conditions and data evaluation settings. PC Win 10 Professional with LCD monitor included.</p><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>SGPC01-001</strong> Streamline™ manual GPC system with Refractive index detector (Includes P1 pump, RI1 detector, CT1i column thermostat with manual injector, solvent rack, Clarity PC station)</li></ul><p><strong>Optional configurations:</strong></p><ul><li><strong>ST99-002</strong> Remove CT1i column thermostat with manual injector from system</li><li><strong>SAS90-001</strong> Add AS1 Autosampler to system</li><li><strong>SFC90-001</strong> Add FC1 Fraction collector to system</li></ul>

Watrex SCS 205 GPC Sample cleanup system

The Watrex Streamline SCS 205 Sample Clean-up System is designed for GPC sample pretreatment.

<p>Sample clean-up is an <strong>essential method</strong> for many routine chromatography applications. One of the most common cases is analysis of <strong>polyaromatic hydrocarbons</strong> (PAHs), <strong>polychlorinated biphenyls</strong> (PCBs) and <strong>pesticides</strong> in complex mixtures.</p><p>The initial step is an isolation of hydrophobic (lipophilic) components from the rest of the sample mixture by <strong>gel-permeation</strong><br><strong>chromatography</strong> (GPC).</p><p>In such configuration, triglycerides (700-900Da) can be isolated from low molecular (200-300Da) PAHs, PCBs or pesticides using<br>GPC steric exclusion. SCS 205 is a dedicated system for GPC sample pretreatment. SCS 205 includes an isocratic pump double piston pump, manual injector with preparative sample loop, PAH/PCB preparative column (200mg sample loading capacity), fraction collector and start-up kit. .The entire system is controlled from a TFT touch display through intuitive screens.</p><p>After injection and GPC separation, the purified sample (PAHs, PCBs etc.) is captured by an automated fraction collection usinga3-way motorized switching valve. The timing of the collection is predetermined from the elution profile of the pollutants.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_SCS_205_Sample_cleanup_system_column_7dce4f25e0.jpg" alt="Watrex: Watrex SCS 205 Sample cleanup system - column"></p><h3><strong>FEATURES</strong></h3><ul><li>High performance pollutant izolation from complex matrices</li><li>Eluent flexibility</li><li>Easy programmable</li><li>Easy installation &amp; Simple operation</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_SCS_205_Sample_cleanup_system_schema_ad45276ad0.jpg" alt="Watrex: Watrex SCS 205 Sample cleanup system - schema"></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_SCS_205_Sample_cleanup_system_graph_10ce455cc3.jpg" alt="Watrex: Watrex SCS 205 Sample cleanup system - graph"></p><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><strong>Sampling System:</strong> manual valve</li><li><strong>Sample volume:</strong> 2 mL loop</li><li><strong>Fraction collection:</strong> 50mL flask</li><li><strong>Collection time programming:</strong> alternating valve switching to waste/collect/waste</li><li><strong>Display:</strong> 4-character</li></ul><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>SCS205-001</strong> SCS 205 Sample Clean-up System (<strong>Price 8 627 € ex VAT</strong>)</li><li><strong>WI02077</strong> WATREX 250x16 mm PAH Prep column, 10 um</li><li><strong>DGD.3008</strong> WATREX 300x8 mm DeltaGel Mixed-D column, 5 um</li><li><strong>DGB.25020</strong> WATREX 250x20 mm DeltaGel Mixed-B column, 5 um</li></ul><p><strong>You can also visit this product on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/chromatography/dedicated-instruments/scs-205-sample-clean-up-system/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>Watrex website</strong></a><strong>.</strong></p>

Watrex xTrovert XT Automatic DNA/RNA extractor

Watrex xTrovert XT is an automatic DNA/RNA extractor. It streamlines the extraction process, making it more efficient and reproducible.

<p><strong>Automatic extractor utilises a simple principle of two pipetting heads serving a 96-well plate.</strong></p><p>Thanks to easy replacement head options of pipetting with <strong>300 μl tips</strong> or <strong>1000 μl</strong> tips are available. <strong>Automatic optical sensor calibration</strong> enables the use of pipetting tips and <strong>96-well plates</strong> from virtually any supplier. The device is equipped with two magnetic arms for protocols including paramagnetic SPR beads. It also allows for thermal incubation in the range of <strong>25 to 85 °C</strong>. In addition to internal <strong>LED lighting</strong>, the station is equipped with an integrated <strong>UV-C sterilisation unit</strong>. Intuitive control from <strong>TFT touch panel</strong> user interface facilitates easy set-up. xTrovert™ XT is a <strong>fully programmable open system</strong> where user can create their own workflow scripts downloadable as text files from USB flas disk.</p><h3><strong>APPLICATIONS</strong></h3><ul><li><strong>Sample prep for PCR testing</strong></li><li><strong>NGS library prep</strong></li><li><strong>Sanger DNA sequencing</strong></li></ul><h3><strong>CURRENT PROTOCOLS</strong></h3><ul><li><strong>DNA/RNA extraction</strong></li><li><strong>DNA purification</strong></li><li><strong>PCR clean-up/desalting</strong></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_x_Trovert_XT_Automatic_DNA_RNA_extractor_Compatible_with_any_magnetic_bead_based_kit_23886eea52.jpg" alt="Watrex: Watrex xTrovert XT Automatic DNA/RNA extractor - Compatible with any magnetic bead based kit"></p><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><strong>Capacity:</strong> 16 or 32 samples/run</li><li><strong>Volume range:</strong> 10 – 600 μl</li><li><strong>Temperature:</strong> 25 – 85 °C</li><li><strong>Sterilization:</strong> UV-C</li><li><strong>Display:</strong> 3,5“ TFT touch display</li><li><strong>Connectivity:</strong> USB 1.0/2.0</li><li><strong>Power source:</strong> 24 V adaptor</li><li><strong>Dimensions in cm:</strong> 65(w) x 65(h) x 34(d)</li><li><strong>Weight:</strong> 25 kg</li></ul><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>XTR000-001</strong> xTrovert™ XT Universal robotic pipettor for DNA/RNA extraction &amp; handling</li><li><strong>XTR000-003</strong> Replaceable 8-channel 1000uL pipetting head for xTrovert™ XT</li><li><strong>XTR000-004</strong> Replaceable 8-channel 300uL pipetting head for xTrovert™ XT</li><li><strong>XTR000-100</strong> Deepwell plates (empty) for xTrovert™ XT</li><li><strong>XTR000-220</strong> DNA/RNA extraction kit, mgn. beads, 16-rxns per plate</li></ul><p>The entire system was designed and developed by Watrex Praha and is <strong>manufactured in the Czech Republic</strong> and promises a shift in the performance and efficiency of laboratory processes worldwide!</p><p><strong>You can also visit this product on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/laboratory-automation/xtrovert-xt/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty"><strong>Watrex website</strong></a><strong>.</strong></p>

Watrex SPR-200 Solvent saver

Watrex SPR-200 Solvent Recycler is designed to save up to 90% of mobile phase during isocratic HPLC.

<p>This Solvent Recycler <strong>saves up to 90% of mobile phase</strong> by redirection of the pure solvent to the solvent reservoir during the isocratic HPLC. The stand alone device is powered by 5 V DC from <strong>power adapte</strong>r or from computer <strong>USB port</strong>. Working parameters (<strong>Threshold and Delay</strong>) are easily set on the display using a membrane keyboard.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_SPR_200_Solvent_saver_I_Nputs_694d991f2c.jpg" alt="Watrex: Watrex SPR-200 Solvent saver - INputs"></p><p>The SPR-220™ Solvent Recycler <strong>continuously monitors the output signal</strong> of the chromatography detector and displays its current value on the built-in display. A <strong>highresolution analog-to-digital converter</strong> provides data for further evaluation in the built-in processor. If the input signal level exceeds a preset value (Threshold), the SPR-200 will redirect the flow to the waste.</p><p>When the signal drops, the solvent recycler waits for the transport delay and then switches the mobile phase <strong>back to the reservoir</strong>. An autosampler injection marker connected to the SPR-200 ZERO input can be used to zero the input signal at the time of injection.</p><h3><strong>FEATURES</strong></h3><ul><li>Stand alone operation</li><li>Detachable valve</li><li>Possibility of manual Waste/Recycle switching</li></ul><h3><strong>TECHNICAL SPECIFICATION</strong></h3><ul><li><strong>Detector compatibility:</strong> compatible with any HPLC detector</li><li><strong>Connection:</strong> 1/16″ O.D. tubing, 1/4″-28 flat bottom fittings</li><li><strong>Maximum pressure:</strong> 30 p.s.i./0,2 MPa</li><li><strong>Wetted material:</strong> PEEK, PTFE</li><li><strong>Input range:</strong> +/- 1 V or +/- 100 mV, user selectable</li><li><strong>Computer connection:</strong> μUSB</li><li><strong>TTL/contact closure input:</strong> configurable (ZERO, start, valve position)</li><li><strong>Power:</strong> 5V DC/&lt;100 mA (power supply or computer USB port)</li><li><strong>User interface:</strong> large character LCD alphanumeric display + membrane keypad</li></ul><h3><strong>Ordering information:</strong></h3><h5><strong>PN/Component:</strong></h5><ul><li><strong>SPR200-001</strong> SPR-200 Solvent Recycler, PEEK version (<strong>Price 1 250 € ex VAT</strong>)</li><li><strong>SPR200-002</strong> SPR-200 Solvent Recycler, PTFE version (<strong>Price 1 250 € ex VAT</strong>)</li></ul><p><strong>You can also visit this product on the </strong><a target="_blank" rel="noopener noreferrer" href="https://watrex.com/?s=SPR-200+Solvent&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>

Waters Xevo MRT QTof Mass Spectrometer

Achieve exceptional science with the Xevo™ MRT Mass Spectrometer—100K resolution at 100 Hz, sub-ppm accuracy, and confident identification for greater lab productivity.

<h3><strong>Delivering Performance and SPEED</strong></h3><ul><li><strong>Resolution AND Speed Without Compromise</strong></li></ul><p><strong>Whether you’re in academia or industry achieve exceptional science - 100% of the time with the Xevo™ MRT Mass Spectrometer. This state-of-the art QTof delivers 100K resolution at 100 Hz with sub ppm mass accuracy for confident identification and greater productivity in your lab.</strong></p><h4><strong>Delivering performance at speed</strong></h4><p>The high resolution and mass accuracy of the Xevo MRT Mass Spectrometer are independent of acquisition rate. Working at maximum resolution ensures you can resolve analytes in complex matrices, providing comprehensive, high accurate mass data for scientific interpretation.</p><h4><strong>Increase compound identification confidence</strong></h4><p>Probe deeper at biologically relevant concentrations with high levels of mass accuracy. Search tolerances can be minimized resulting in efficient data review, improving turnaround times for increased lab productivity.</p><h4><strong>Connected solutions</strong></h4><p>A complete workflow for metabolomics, lipidomics, and metabolite identification through market leading chemistry and cutting-edge, informatics ensures your lab is operating with maximum efficiency – reducing the time to result.</p><h4><strong>Exceptional science - every day</strong></h4><p>System performance is critical. From instrument stability and robustness for extended studies to precision measurements in every injection, innovative multi reflecting time-of-flight technology delivers high quality experimental outcomes for every lab, every day.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_1_63e746d310.jpg" alt="Waters Xevo MRT Mass Spectrometer" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_1_63e746d310.jpg 244w," sizes="100vw" width="1119" height="715"></p><h3><strong>Extraordinary Performance</strong></h3><h4><strong>Without compromises</strong></h4><h5><strong>Exceptional science for every lab, scientist, problem, question, and sample… Solved</strong></h5><p>The exceptional combination of high mass resolving power of 100,000 FWHM and mass accuracy of &lt;500 part per billion (ppb) of the Xevo MRT Mass Spectrometer are achieved independent of acquisition rates, up to 100Hz. Maximum performance, matched to throughput levels that matter for complex and challenging analyses, increases statistical power and confidence in results.</p><h5><strong>Feeling trapped?</strong></h5><p>Unlike other high-resolution MS technologies, multi-reflecting time-of-flight delivers mass resolution consistent over a broad m/z range independent of scan speed, even at the fastest acquisition rates for MS and MS/MS data, ensuring confident identification of analytes across a range of samples and matrices – an ideal solution for metabolite profiling and discovery.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Mass_Spectrometer_Extraordinary_Performance_d8879eda23.jpg" alt="Waters Xevo MRT Mass Spectrometer: Extraordinary Performance." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Mass_Spectrometer_Extraordinary_Performance_d8879eda23.jpg 245w," sizes="100vw" width="1309" height="774"></p><h3><strong>Connected Solutions</strong></h3><h4><strong>From advanced chemistry to flexible informatics</strong></h4><p>Make meaningful scientific discoveries more efficient with dedicated workflows combining column chemistries, separations, and informatics with the exceptional data quality of the Xevo MRT Mass Spectrometer. The waters_connect™ platform allows you to process and report your data in the way that you want. Whether using a Waters supported solution or exporting data via mzML to custom scripted workflows, we have you covered.</p><h4><strong>The Xevo MRT mass spectrometer readily integrates with your existing pipeline and workflow strategy</strong></h4><p>Waters has partnered with Mass Analytica™ (mass-analytica.com) and their market leading metabolomic, lipidomic, and metabolite identification software packages, MARS, Lipostar2, and MassMetaSite, respectively. Through either the waters_connect Application Programming Interface (API) or via mzML*, there is the option for you to transfer your data into the relevant software package for statistical interpretation and identification of analytes.</p><p>The DATA Convert Application within the waters_connect Platform enables you to convert to and export mzML file formats, ensuring a seamless integration of technology and informatics for every lab.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_6_d0fc257136.jpg" alt="Waters Xevo MRT Mass Spectrometer: Connected Solutions." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_6_d0fc257136.jpg 236w," sizes="100vw" width="1212" height="802"></p><p>The waters_connect platform provides flexible data processing options, either using third-party applications via the waters_connect API or conversion of data sets to mzML file format via DATA Convert.&nbsp;</p><h3><strong>Unlocking a New Level of Confidence&nbsp;</strong></h3><h4><strong>By bringing an analytical powerhouse to every lab</strong>&nbsp;</h4><p>To meet the most challenging analytical problems that you experience head on, Waters has taken cutting edge technology that was pioneered in the SELECT SERIES™ MRT, scaling the raw power and resolution at speed into a compact flexible, benchtop platform.</p><h4><strong>The MRT Xevolution</strong></h4><p>The Xevo MRT Mass Spectrometer has been engineered to deliver high-end technology into a benchtop platform to solve your most challenging problems. The novel acquisition system, with dual gain analogue-to-digital converter, delivers long term system stability over a high dynamic range, ensuring exceptional quality data with consistent robustness and reproducibility.</p><p>The 4 m flight path with a total of 8 reflections within the MRT mass analyzer, achieves 100,000 FWHM resolution at scan rates of up to 100 Hz - for ultimate MS/MS performance.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Xevo_MRT_Hmotnostni_spektrometr_Schema_2448b0bc8d.jpg" alt="Waters Xevo MRT Mass Spectrometer: The Xevo MRT Mass Spectrometer schematic. ​" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Xevo_MRT_Hmotnostni_spektrometr_Schema_2448b0bc8d.jpg 236w," sizes="100vw" width="1199" height="794"></p>

Thermo Scientific Stellar Mass Spectrometer

Move biomarker candidates from discovery to validation more efficiently, confidently, and at lower cost with breakthroughs in extended scale, massive throughput, higher sensitivity, greater specificity, and unrivaled productivity.

<div><div id="container-a1c36dfacf"><div><div><div id="text-913638046"><p><strong>A new paradigm for targeted quantitation.&nbsp;Move biomarker candidates from discovery to validation more efficiently, confidently, and at lower cost with breakthroughs in extended scale, massive throughput, higher sensitivity, greater specificity, and unrivaled productivity.</strong></p><p>The Thermo Scientific Stellar Mass Spectrometer introduces revolutionary technology combining robust quantitation with the specificity of rapid full scan MS<sup>n</sup>&nbsp;acquisition creating unrivaled improvements in laboratory productivity.</p><div><div id="text-801893275"><h3><strong>Expanded experimental capabilities to meet the most challenging biomarker verification</strong></h3></div></div><div><div id="container-1e8e478f3a"><div><div><div id="text-1204752335"><p>The Thermo Scientific Stellar Mass Spectrometer offers an array of data acquisition capabilities to deliver robust and reproducible quantitation for a wide range of analytes across an extended dynamic range.</p></div></div></div></div></div><h4><strong>System highlights</strong></h4><div><div id="container-a89a56f063"><div><div><div id="text-451891225"><h5><strong>Improve ionization efficiency for more compounds at higher LC flow rates&nbsp;</strong></h5></div></div><div><div id="text-1671602085"><p>For a wider range of compounds separated using liquid chromatography operated at analytical flow rates, the Stellar Mass Spectrometer comes equipped with the Thermo Scientific OptaMax Plus Ion Source, which can deliver higher vaporizer temperatures to improve desolvation and ionization potentials.</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/725;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_Opta_Max_c303cf500a.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys OptaMax" width="1290" height="725"></figure><div><div id="container-d79c3b2946"><div><div><div id="text-251514658"><h5><strong>Spend less time on instrument set-up and focus on the science</strong></h5></div></div><div><div id="text-989104128"><p>Trigger on-demand or scheduled system calibrations remotely and without disruption to your LC-MS system with the integrated Auto-Ready ion source.</p></div></div></div></div></div><div><div id="container-81dd07c9bb"><div><div><div id="text-1289282711"><h5><strong>Improve ion utilization by extending the capabilities of the new collision cell</strong></h5></div></div><div><div id="text-1641484825"><p>The ion concentrating routing multipole (ICRM) is a curved collision cell performing both beam-type fragmentation (HCD) and precursor/product ion accumulation capabilities as controlled by dynamic automatic gain control (AGC) with synchronized ion packet release to the high-pressure linear ion trap for downstream manipulation or detection.</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/725;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_ICRM_3b2326f3af.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys ICRM" width="1290" height="725"></figure><div><div id="container-dbf5a6cdd9"><div><div><div id="text-813962034"><h5><strong>Efficiently manage ion populations for fast and sensitive analysis</strong></h5></div></div><div><div id="text-2033771024"><p>The&nbsp;hyper-fast dual-pressure linear ion trap mass analyzer expands analytical capabilities while maximizing fast, high-quality data acquisition.</p><p>The differential neutral pressures maintained in the high- and low-pressure linear ion traps prepares ions for higher-order manipulation or fast and sensitive ion ejection at scan rates up to 220 kDa/S, but typically operates at 125 kDa/S for robust data acquisition.</p></div></div></div></div></div><div><div id="container-9a523f34e0"><div><div><div id="text-1491120095"><h5><strong>Extended analytical capabilities to increase laboratory productivity</strong></h5></div></div><div><div id="text-328051555"><p>The high-pressure linear ion trap maximizes ion packet manipulation enabling multi-notch RF excitation for dissociation or ejection for SIM, higher order MS<sup>n</sup>, SPS MS<sup>3</sup>, or data-independent acquisition (DIA) to address the most challenging quantitative experiments.&nbsp;</p><div><div id="container-82e5907416"><div><div><div id="text-693866740"><h5><strong>Leverage single ion detection sensitivity to address the most challenging quantitation demands</strong></h5></div></div><div><div id="text-737565098"><p>Efficient and sensitive ion detection drives improved quantitative performance at scale. The dual conversion dynode configuration coupled to the photomultiplier tube detects ca. 84% of trapped ions for single ion sensitivity.</p></div></div></div></div></div></div></div></div></div></div><figure class="image"><img style="aspect-ratio:2048/1152;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_hmotnostni_spektrometr_SF_Sys_Extended_Scale_750dc20128.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys Extended Scale" width="2048" height="1152"></figure><div><div id="text-1993749933"><h5><strong>Automated intelligence manages tMSn acquisition</strong></h5></div></div><div><div id="text-1206797739"><p>Streamline tMSn method creation and data acquisition management. PRM Conductor software effectively and efficiently creates robust targeted quantitative methods and manages reproducible data acquisition and processing.</p></div></div><div><div id="container-b03b606507"><div><div><div id="text-2005266584"><h5><strong>Maximize data completeness with the Adaptive RT routine</strong></h5></div></div><div><div id="text-671832198"><p>Eliminate the cost and time of optimizing RT kits to the study samples to boost timed/scheduled data acquisition performance using the Adaptive RT routine.</p><p>The method leverages a novel real-time mapping routine to dynamically adjust timed/scheduled data acquisition windows at narrower time intervals to eliminate missing values that compromise data quality.&nbsp;</p></div></div></div></div></div><figure class="image"><img style="aspect-ratio:1290/654;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Pragolab_Thermo_Scientific_Stellar_revolucni_hmotnostni_spektrometr_SF_Sys_PRM_Conductor_5b596e7e4c.jpg" alt="Thermo Fisher Scientific: Thermo Scientific Stellar Mass Spectrometer - SF Sys PRM Conductor" width="1290" height="654"></figure><div><div id="container-a192ba4b83"><div><div><div id="container-38d4c699d2"><div><div><div id="text-1578189934"><h5><strong>Industry-leading polarity switching speeds increase laboratory productivity</strong></h5></div></div><div><div id="text-1173595596"><p>Reduce the time, cost, and challenges associated with creating and implementing highly multiplexed quantitative metabolite analysis. Fast polarity switching speeds enable comprehensive compound interrogation in +ESI and -ESI at all MS<sup>n</sup> levels on an LC timescale.</p><div><div id="container-b5fb525888"><div><div><div id="text-18006314"><h5><strong>Environmentally friendly dry pumps decrease energy usage and maintenance</strong></h5></div></div><div><div id="text-1704557304"><p>Changing from two oil-based fore pumps to a single dry pump reduces heat output by 22% and decreases maintenance.</p><p>The use of a single dry pump also eliminates oil vapors and the need for oil checks and changes.</p><h3><strong>Solutions for additional research support</strong></h3><div><h4><strong>Translational proteomics</strong></h4><p>The Stellar Mass Spectrometer offers new possibilities for translational proteomics with improved specificity for greater quantitative performance at scale.</p><h4><strong>Quantitative proteomics</strong></h4><p>Accurate and precise quantitation for label-free and TMT multiplexing sample analysis strategies with the Stellar Mass Spectrometer.</p><div><h4><strong>Metabolomics and Lipidomics</strong></h4><p>Extended analytical capabilities quantify more metabolites and lipids with greater specificity using faster liquid chromatography gradients to increase laboratory productivity.</p></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div></div>

Modern HPLC separations in theory and practice

This book is a unique combination of theory and practice, but also overviews of stationary phases, sample prep materials, and vendor’s brief presentations.

Galochrom Chiral ION-QD HPLC columns

These HPLC columns are based on high-quality spherical silica from the world's leading silica manufacturer from Japan.

<p><strong>Chiral ion exchanger GEN-QD is highly efficient in the enantiomer resolution of acidic compounds.</strong></p><p>This product is now available in high quality and at a reasonable price at our company!</p><p>To create our <strong>chiral sorbent</strong>, we use <strong>3µm fully porous spherical silica particles</strong>, which provide greater efficiency than the original product.</p><p>Additionally, our <strong>Galo-ION-QD-200</strong> is recommended for <strong>biological applications</strong> due to its larger pore size, which improves the separation efficiency for large molecules.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Galochrom_Galochrom_Chiral_ION_QD_HPLC_kolony_ION_QD_selector_10dd9c7ee5.jpg" alt="Galochrom: Galochrom Chiral ION-QD selector."></p><h5><strong>Premium Quality</strong></h5><p>In every manufactured product, we guarantee the highest standards of quality.</p><h5><strong>Cost-effective</strong></h5><p>Our unique products optimize your budget &amp; enhance efficiency in your laboratory operations.</p><h5><strong>High-performance</strong></h5><p>Besides their outstanding performance, our HPLC columns also expand your separation possibilities.</p><h3><strong>Ordering information</strong></h3><blockquote><p><strong>Stationary phase Chiral ION-QD is provided in these column types: analytical and preparative</strong></p></blockquote><h4><strong>Analytical Columns</strong></h4><ul><li><strong>Dimensions [mm]: 150 x 3</strong></li><li>Porosity: [Å] 200</li><li>Cat. No.: ION02-A150</li><li><strong>Price [€]: 1 300</strong></li></ul><blockquote><h4><strong>Get up to a 20% discount on your first purchase with us.</strong></h4></blockquote><h3><strong>Reach new heights</strong></h3><p>Spend more time on testing and less time on troubleshooting</p><blockquote><h4><strong>How can our unique columns help you succeed?</strong></h4><p>Chiral ION-QN and Chiral ION-QD empower researchers with their daily tasks, such as:</p><ul><li>Seamless method development</li><li>Enantioseparation</li><li>Quality control</li><li>Monitoring of asymmetric reactions</li><li>Intermolecular interaction studies</li><li>Pharmacokinetic studies</li><li>Preparative separation</li><li>Production scale-up</li><li>Efficient purification</li></ul></blockquote><h4><strong>What makes Chiral </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1241"><strong>ION-QN</strong></a><strong> and ION-QD unique?</strong></h4><p><span style="font-size:20px;"><strong>Designed for stability</strong></span></p><p>The manufacturing of Chiral ION-QN and Chiral ION-QD was designed to produce highly reproducible and reliable HPLC columns. Our high standards in synthesis of organic selectors and robust packing technology ensures that each customer receives identical high-performance product.</p><p><strong>The chromatographic results are reproducible from run-to-run, column-to-column and batch-to-batch.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Designed_for_stability_1_9dea7516f4.jpg" alt="Galochrom: Chiral ION-QN &amp; Chiral ION-QD HPLC columns - Designed for stability." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Designed_for_stability_1_9dea7516f4.jpg 245w," sizes="100vw" width="655" height="376"></p><p>During our manufacturing, we implement strict quality control measures over all aspects from silica chemistry up to column packing. As a result, almost no variation is observed among manufactured batches of chiral stationary phases.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Designed_for_stability_2_50c42d67e6.jpg" alt="Galochrom: Chiral ION-QN &amp; Chiral ION-QD HPLC columns - Designed for stability." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Designed_for_stability_2_50c42d67e6.jpg 245w," sizes="100vw" width="1176" height="442"></p><h3><strong>Achieve your results</strong></h3><p>Increase your productivity with uniform, stable, and reproducible results</p><h4><strong>High-Quality Silica</strong></h4><p>Our columns contain fully-porous spherical particles from world’s leading manufacturer based in Japan. These ultra-pure silica particles have narrow size distribution to ensure reproducible, robust and reliable results.</p><p>In comparison to other manufacturers, Galochrom’s custom packing technology produces very stable and uniform bed with intact silica particles. As a<br>result, our columns:</p><ul><li>Enhance productivity and resolution</li><li>Provide accurate and consistent performance</li><li>Generate significantly higher plate counts</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_High_Quality_Silica_522d14ecf7.jpg" alt="Galochrom: Chiral ION-QN &amp; Chiral ION-QD HPLC columns - High-Quality Silica." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_High_Quality_Silica_522d14ecf7.jpg 245w," sizes="100vw" width="617" height="386"></p><h4><strong>Elution Order</strong></h4><p>Chiral ION-QN and Chiral ION-QD represent a pair of columns that enable the reversal of elution order of enantiomers.<strong> Now you can position your desired enantiomer first and easily achieve 100% purity at higher pace.</strong></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Elution_Order_85c5b02411.jpg" alt="Galochrom: Chiral ION-QN &amp; Chiral ION-QD HPLC columns - Elution Order." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Galochrom_Chiral_ION_QN_and_Chiral_ION_QD_HPLC_columns_Elution_Order_85c5b02411.jpg 245w," sizes="100vw" width="953" height="545"></p><p>The elution order was investigated with other QN/QD derivatives using enantiomeric pairs of Leucine derivatives. The conclusions for the first eluent are following:</p><ul><li>Chiral ION-QN ⇒ L-Enantiomer</li><li>Chiral ION-QD ⇒ D-Enantiomer</li></ul>

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