<h5><strong>Why compromise between performance and price when you can have both?</strong></h5><p><strong>With Thermo Scientific factory-certified, pre-owned </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=5&amp;manufacturerItems=3"><strong>mass spectrometers</strong></a><strong>, you can access legendary LC-MS technology—trusted around the world—at a fraction of the cost of buying new. Our refurb program delivers the quality, precision, and reliability you expect from Thermo Fisher Scientific, while helping you stay within budget and on top of your analytical goals.</strong></p><h3><strong>Factory-Certified for confidence</strong></h3><p>Every certified pre-owned system goes through a <strong>rigorous factory reconditioning process</strong>. From updated hardware and software to comprehensive performance testing, each instrument is restored to meet the same high standards as our new products.</p><h4><strong>What’s included?</strong></h4><p>When you choose a certified LC-MS system, you get more than just an instrument—you get the <strong>complete Thermo Scientific experience</strong>:</p><ul><li><strong>Full 1-year factory warranty</strong> for peace of mind</li><li><strong>29-point inspection checklist</strong>, re-certification, and final quality testing</li><li><strong>Software and hardware updates</strong> to current revisions</li><li>Re-certification using <strong>only genuine Thermo Scientific factory parts</strong></li><li><strong>Professional installation</strong> by Unity Lab Services field engineers</li><li><strong>Optional training and application support</strong> to get you up and running fast</li></ul><h4><strong>What gets replaced?</strong></h4><p>Our reconditioning process is comprehensive. 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Personalized equipment </strong><a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/products-and-services/services/financial-leasing-services.html"><strong>financing &amp; leasing options</strong></a></h4><p>If upfront capital is limited, our tailored financing and leasing plans offer flexibility that aligns with your lab’s budget and growth plans.</p><h5><strong>Ready to get started?</strong></h5><ul><li><a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/industrial/mass-spectrometry/mass-spectrometer-price-affordability-programs.html"><strong>Explore our certified systems, trade-in opportunities, and financing solutions.</strong></a></li></ul><p><strong>Visit us on&nbsp;</strong><a target="_blank" rel="noopener noreferrer" href="https://www.linkedin.com/showcase/72003132/admin/dashboard/"><strong><u>LinkedIn:</u></strong></a><strong>&nbsp;</strong>#affordabiliy #LCMS #sustainability #productivity</p><blockquote><h5><strong>Ema Ruzic</strong></h5><p>Vertical Marketing Manager, Chromatography and Mass Spectrometry Division (CMD)</p></blockquote>

Unlock High-Performance LC-MS with Factory-Certified Systems from Thermo Fisher Scientific

<p><strong>Metalloproteins play essential roles in marine phytoplankton, yet their metalloproteomes remain poorly characterized. This study combines protein modeling, quantitative proteomics, and ICP-MS measurements to assess metal requirements across several phytoplankton species, including chlorophytes, a haptophyte, and a cyanobacterium.</strong></p><p>Results show strong agreement between proteome-inferred metal demands and measured cellular metal quotas, while providing deeper insight into biological functions. Mg-containing proteins were most abundant overall, with Zn, Fe, and Mn as dominant trace cofactors. Distinct differences between prokaryotic and eukaryotic phytoplankton were observed, and strain-level analysis demonstrated how metalloproteomes reflect environmental adaptation and metal limitation strategies.</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.est.5c11233"><strong>Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes</strong></a></h4><p>Qiong Zhang*, Jiayou Ge, Fengjie Liu, Shabaz Mohammed, Kedong Yin, and Rosalind E. M. Rickaby</p><p>Environ. Sci. Technol. 2025, 59, 50, 27367–27377</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.est.5c11233">https://doi.org/10.1021/acs.est.5c11233</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><p>Many important biological processes of phytoplankton, including photosynthesis, carbon fixation, and nitrogen reduction, rely on enzymes that have metals as cofactors. <a href="javascript:void(0);">(1)</a> It has been estimated that half of all enzymes must be associated with a particular metal to function. <a href="javascript:void(0);">(2)</a> The availability of metals in the environment has changed over geological time and, given imperfections in the selectivity of metal transport systems, proteins have evolved to make the best use of metals that are more available. <a href="javascript:void(0);">(3−5)</a> Depending on their evolutionary histories, different groups of marine phytoplankton may have differences in their metalloprotein compositions and metal transport strategies. The evolving trace metal availability in the environment, thus, may provide a selective pressure to promote the proliferation of different phytoplankton groups in the oceanic environment, affecting the phytoplankton community structure with knock-on effects on the marine food web and carbon sequestration. <a href="javascript:void(0);">(5)</a> It is crucial to understand the utilization of trace metals by different groups of marine phytoplankton that inhabit contrasting niches in the modern ocean, not only by assessing the accumulation of trace metals in cells but also examining the functions of trace metals in different biological pathways.</p><p>In previous studies, the utilization or requirements of trace metals by marine phytoplankton were mostly determined by measuring the elemental stoichiometry in cells (metallome or quota of trace metals). <a href="javascript:void(0);">(6−8)</a> In the field, attempts have also been made to investigate the elements in phytoplankton <a href="javascript:void(0);">(9,10)</a> which have then been compared with profiles in the abiotic environment to understand their relationships. <a href="javascript:void(0);">(11)</a> The discovery of various metal storage proteins and the plasticity in elemental quotas under different environmental conditions raise the question of whether intracellular trace metal quotas reflect true differences in trace metal usage by phytoplankton. <a href="javascript:void(0);">(12,13)</a> In the past few decades, more and more studies have focused on metal–protein partnerships, using approaches such as genome-wide analysis to identify homologues of known metalloproteins and other deduced metal-binding motifs encoded within sequenced genomes. <a href="javascript:void(0);">(5,14)</a> However, this approach has limitations in estimating metal abundance in cells because not all genes predicted in the genome would be translated and expressed as proteins under all environments, and a single gene for a metalloprotein could be highly expressed, such that a translation from genetic presence to a required concentration is not linear and could be environment-dependent. To obtain <i>in situ</i> metal abundance in metalloproteins in cells, native separation of proteins by HPLC or PAGE followed by the detection of metals using ICP-MS <a href="javascript:void(0);">(15,16)</a> has been used. This approach also has limitations in that, without bioinformatics, it cannot identify the function of proteins within which the metals are found, and it may also depend on the composition of the media to which the organism has been exposed and in which it has been growing. An ideal way to solve the problem would be to separate and purify each of the proteins and then identify both the associated metal (<i>e.g.,</i> by ICP-MS) and the protein sequence (<i>e.g.,</i> by mass spectrometry). However, this approach is constrained by the resolution of chromatographic or electrophoretic techniques, making it challenging to establish the metal–protein associations unambiguously; many proteins often co-occur in metal-containing fractions. Additionally, this method requires huge volumes of biomass and is both time-consuming and complex, complicating the reconstruction of the expressed metalloproteome in cells. The techniques and challenges for metalloproteomics have been discussed in detail in previously published review articles (and the references therein). <a href="javascript:void(0);">(17)</a></p><p>In this study, we determined the trace metal utilization (the metallome) of different phytoplankton from their expressed proteome via a protein modeling and homologue identification approach, and then compared the resulting metallome with the metal quota data measured by the traditional inductively coupled plasma mass spectrometry (ICP-MS). This approach allows the building of a link between the truly used trace elements and their biological functions in phytoplankton. We aim to fill the gap between an estimation of metals encoded in the genome and metal analysis by ICP-MS in phytoplankton, which may be more broadly applicable to infer cellular metallomes.</p><h3><strong>Materials and Methods</strong></h3><h4><strong>ICP-MS Analysis</strong></h4><p>All preparation of samples for ICP-MS measurement was undertaken using trace metal clean methods. All plasticware used in this study, including culture flasks, pipette tips, and centrifuge tubes, was precleaned in 10% quartz-distilled HCl and thoroughly rinsed with 18 MΩ cm water in a clean laboratory. Trace elements in the filtered lysates of <i>G. huxleyi</i> (OA1, OA4, OA8, OA15, OA16, OA23, and RCC 1242) and <i>Synechocystis</i> (FACHB898) strains were measured using an ICP-MS. The detailed ICP-MS method and instrumental settings are described in Zhang et al. (2018). <a href="javascript:void(0);">(31)</a></p><h4><strong>Protein Mass Spectrometry</strong></h4><p>The peptides were resuspended in 5% formic acid and 5% DMSO prior to mass spectrometry. They were separated on an <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=3&amp;search=Ultimate+3000+UHPLC"><strong>Ultimate 3000 UHPLC </strong></a>system (Thermo Fisher Scientific) and electrosprayed directly into a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559"><strong>Q-Exactive Mass Spectrometer</strong></a> (Thermo Fisher Scientific) through an EASY-Spray nanoelectrospray ion source (Thermo Fisher Scientific). The peptides were trapped on a C18 PepMap100 precolumn (300 μm i.d. × 5 mm, 100 Å, Thermo Fisher Scientific) using solvent A (0.1% formic acid in water) at a pressure of 500 bar. The peptides were separated on an in-house packed analytical column (75 μm i.d. × 50 cm packed with ReproSil-Pur 120 C18-AQ, 1.9 μm, 120 Å, Dr. Maisch GmbH) using a linear gradient (length: 65 min, 15% to 35% solvent B [0.1% formic acid in acetonitrile], flow rate: 200 nL/min). The raw data were acquired on the mass spectrometer in a data-dependent mode (DDA). Full scan MS spectra were acquired in the Orbitrap (scan range 350–1500 <i>m</i>/<i>z</i>, resolution 70000, AGC target 3e6, maximum injection time 50 ms). After the MS scans, the 10 most intense peaks were selected for HCD fragmentation at 30% of normalized collision energy. HCD spectra were also acquired in the Orbitrap (resolution 17500, AGC target 5e4, maximum injection time 120 ms, isolation window 1.5 <i>m</i>/<i>z</i>) with the first fixed mass at 180 <i>m</i>/<i>z</i>. Charge exclusion was selected for unassigned and 1+ ions. The dynamic exclusion was set to 20 s.</p><h3><strong>Results and Discussion</strong></h3><h4><strong>Trace Elements Determined from the Expressed Proteomes of Different Phytoplankton</strong></h4><p>Based on the expressed proteome sequences, we predicted metal-binding proteins and compared their distribution among various phytoplankton species (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig2">Figure 2</a>). The inference revealed 28 different metals in <i>G. huxleyi</i>, 31 different metals in <i>C. reinhardtii</i>, and 30 different metals in <i>Synechocystis</i>. Although only 6 different metals were identified in <i>O. tauri</i> proteins, it has to be noted that the analysis for <i>O. tauri</i> was only based on the 40 most abundant proteins reported in this organism <a href="javascript:void(0);">(21)</a> and, hence, the listed elements, including Mg, Fe, Mn, Ca, Zn, and Cu, may represent the most essential metals for the species.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Environ_Sci_Technol_2025_59_50_27367_27377_Figure_2_The_number_of_metal_binding_proteins_identified_in_the_expressed_proteome_of_the_haptophyte_G_9b8ac0f004.jpeg" alt="Environ. Sci. Technol. 2025, 59, 50, 27367–27377: Figure 2. The number of metal-binding proteins identified in the expressed proteome of the haptophyte G. huxleyi (a), the chlorophyte C. reinhardtii (b) and O. tauri(c), and the cyanobacteria Synechocystis (d). Pie charts show the percentages of metalloproteins containing specific metals. Original proteome data for G. huxleyi are from Mckew et al. (2013) (24) for C. reinhardtii are from Hsieh et al. (2013) (77) for O.tauriare from Martin et al. (2012) (21) for Synechocystisare from Chen et al. (2018). (22) *Noted that for O. tauri, only the 40 most abundant proteins were included in this analysis. ND: no metal binding was found in the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Environ_Sci_Technol_2025_59_50_27367_27377_Figure_2_The_number_of_metal_binding_proteins_identified_in_the_expressed_proteome_of_the_haptophyte_G_9b8ac0f004.jpeg 123w," sizes="100vw" width="934" height="1181"></p><p>The number of proteins that bind with different metals varies dramatically in phytoplankton. For metalloproteins, there are variations in the binding affinities of different metals to organic molecules. For example, the affinities of divalent metals to proteins have a tendency to follow a universal order of preference, namely the Irving-Williams series (Mg<sup>2+</sup> and Ca<sup>2+</sup> [weakest binding] &lt; Mn<sup>2+</sup> &lt; Fe<sup>2+</sup> &lt; Co<sup>2+</sup> &lt; Ni<sup>2+</sup> &lt; Cu<sup>2+</sup> &gt; Zn<sup>2+</sup>). <a href="javascript:void(0);">(43)</a> Cells can simultaneously contain proteins having high-affinity-binding metals, such as Cu and Zn, and others that require uncompetitive metals, such as Mg and Ca. One of the least competitive metals for binding with biological chelators, Mg, is even found to be the most widely distributed metal in the metalloproteomes of various phytoplankton species in this study, supporting the observations of high concentrations in the protein fraction of cells (at millimolar concentrations <a href="javascript:void(0);">(31)</a>).</p><p>In all phytoplankton species in our analysis, the Mg-containing proteins are found to have the highest proportion in all metalloproteins identified. About 30% of the metalloproteins in different strains of phytoplankton are found to contain Mg or depend on it for function (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig2">Figure 2</a>), suggesting the important role of Mg in phytoplankton cells. It is generally coordinated in protein complexes by ATP or ADP and has also been found to be largely distributed in the chloroplasts or thylakoids in <i>G. huxleyi</i> and <i>Synechocystis</i>. <a href="javascript:void(0);">(22,24)</a> The essential roles of Mg in plants have been reported in various studies. Mg<sup>2+</sup> is known to be the central atom of the chlorophyll molecule, and its levels in the chloroplast regulate the activity of key photosynthetic enzymes. <a href="javascript:void(0);">(44)</a> It was reported that approximately 15–35% of total Mg is in the chloroplasts of a plant, <a href="javascript:void(0);">(45)</a> and it also serves as an osmotically active ion in the regulation of cells <a href="javascript:void(0);">(46)</a></p><h4><strong>Comparison Between Metallome Measured Directly and Reconstructed from Proteins</strong></h4><p>A large proportion of metals, such as Fe, Mn, and Cu, are found in membrane proteins,and may contribute significantly to total cellular quotas. <a href="javascript:void(0);">(54,55)</a> However, for method development purpose, we endeavored to remove the cell membranes from our samples to focus mostly on the analysis of intracellular metal quotas and metalloproteins in the cytosol fraction in this study. We note that our analysis includes some membrane-bound proteins likely derived from organelles or surface membranes disrupted during sonication.</p><p>The derivation of cellular metal composition, as determined by two different methods, is compared in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>. The abundance of metal in the proteins is determined as the relative abundance of the protein multiplied by the number of metal ions needed for the specific protein. The abundance of the proteins was normalized to ensure that the total intensities from each replicate measurement for the same species were similar. Since the proteomic data used here were generated from different studies using different instruments, we cannot quantify or compare the absolute biomass of proteins used for each species. Therefore, we cannot compare the absolute trace metal abundance between species solely from metal inferences of expressed proteomes. Nevertheless, we can estimate the relative abundance of different metals in the same species. For the elements that are both measured by the ICP-MS and identified in the proteome, there are generally good correlations (<i>r</i><sup>2</sup> = 0.81 in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>a and <i>r</i><sup>2</sup> = 0.74 in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>b) between the two approaches. This indicates that the metal compositions determined from the protein modeling may be reliable and, therefore, can reflect the metal usage in different phytoplankton. This would provide a level of assurance to further investigate the metal binding associated with various proteins, thereby deepening our understanding of the roles that different metals play in phytoplankton.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Environ_Sci_Technol_2025_59_50_27367_27377_Figure_3_Relationship_between_the_abundance_of_metals_determined_by_ICP_MS_analysis_e7b259e376.jpeg" alt="Environ. Sci. Technol. 2025, 59, 50, 27367–27377: Figure 3. Relationship between the abundance of metals determined by ICP-MS analysis (normalized to C, mmol/mol C) and metal abundance determined from the metalloproteome analysis (the unit is arbitrary). To account for strain variations, the ICP-MS data for the cellular metal content of G. huxleyi are average values from 7 G. huxleyi strains isolated from different areas of the ocean, and the proteome-derived metal composition data are average values calculated from 2 of those G. huxleyi strains (OA1 and OA16) isolated previously, and data from Mckew et al., 2013. (24) The ICP-MS data for Synechocystis are from Synechocystis sp. FACHB898 measured in this study, and the proteome data are calculated from Chen et al., 2018. (22) Noted that the abundance of metals from each proteome was calculated by using the metal stoichiometry multiplied by the relative abundance of proteins, which provides only a relative relationship of different trace metals, not absolute abundance. The symbols represent the mean values, and the error bars indicate standard deviations." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Environ_Sci_Technol_2025_59_50_27367_27377_Figure_3_Relationship_between_the_abundance_of_metals_determined_by_ICP_MS_analysis_e7b259e376.jpeg 245w," sizes="100vw" width="1384" height="641"></p><p>Compared to the other metals investigated in this study, Ca and Mg appear to have a much higher relative abundance in the ICP-MS analysis than in the proteomic analysis of <i>G. huxleyi</i> and <i>Synechocystis</i> (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>). These two elements are essential macronutrients for phytoplankton and plants. Ca is the most prominent secondary messenger that plays a crucial role in response to extracellular stimuli in all eukaryotes. Ca<sup>2+</sup> fluxes are transported via Ca channels and transporters, such as Ca-ATPase, regulating a series of important biological functions, including mineral uptake and utilization, K<sup>+</sup> homeostasis adjustment, and regulatory network activity in response to P or N deficiency. <a href="javascript:void(0);">(56)</a> Ca is not always incorporated into protein structures. The Ca abundance determined from the proteins in this study, therefore, is much lower than the actual Ca needed intracellularly. Similarly, the intracellular Mg<sup>2+</sup> and K<sup>+</sup> abundances should also be higher than those determined from the protein structures. Free Mg<sup>2+</sup> and K<sup>+</sup> are known to regulate cation–anion balance and serve as osmotically active ions in the regulation of cells <a href="javascript:void(0);">(46)</a> but free metal ion concentrations cannot be determined through the approach used in this study. Thus, it is not surprising to see much higher relative abundances of Ca and Mg in ICP-MS analysis than in proteomic analysis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>).</p>

Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes

<h3><a target="_blank" rel="noopener noreferrer" href="https://www.isc2026.org/"><strong>ISC 2026</strong></a></h3><p><strong>The </strong><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/companies/314"><strong>International Symposium on Chromatography (ISC)</strong></a><strong> represents the oldest conference series on separation science. ISC symposia have been organised since 1956 in each even year. ISC is one of the premier meetings series for discussion of all modes of chromatography and separation science with a broad coverage of techniques and applications.</strong></p><p>The major focus of the symposium will be on the impact of chromatography and separation science to meet the needs of the pharmaceutical, environmental, food and health industry, as well as science and medicine. The symposium programme will reflect these themes and highlight new challenges and emerging opportunities for the science and marketing of separation and detection systems and methods.</p><p>As an integral part of the scientific programme of lectures and poster sessions, an international exhibition and vendor seminars on instrumentation and services for chromatography, separation science and mass spectrometry will be organised. ISC 2026 will provide the perfect forum for attendees from academia, industry and government research institutions for scientific exchange and networking.</p><h3><strong>ISC 2026 SYMPOSIUM KEY DATES</strong></h3><h4><strong>6-10 SEPTEMBER 2026</strong></h4><ul><li><strong>15 January 2026:</strong> Opening of Early-bird Registration &amp; Abstract submission</li><li><strong>11 March 2026: </strong>Deadline for abstract submission (orals)</li><li><strong>21 April 2026: </strong>Sending acceptance letters (orals)</li><li><strong>15 May 2026: </strong>Deadline of early-bird registration and payment &amp; Author registration deadline (orals)</li><li><strong>1 June 2026: </strong>Preliminary detailed program on web</li><li><strong>1 June 2026: </strong>Deadline for abstract submission (posters)</li><li><strong>16 June 2026: </strong>Sending acceptance letters (posters)<ul><li>Authors who submit their abstracts with a poster preference by 5 May 2026 will be notified of the outcome by 12 May 2026 and will have the opportunity to register at the early-bird rate until 15 May 2026.</li></ul></li><li><strong>30 June 2026:</strong> Author registration deadline (posters)</li><li><strong>30 July 2026:</strong> Deadline for abstract submission (late-breaking posters)<ul><li>without the possibility of competing for the Best Poster Award</li></ul></li><li><strong>11 August 2026: </strong>Sending acceptance letters (late-breaking posters)</li><li><strong>18 August 2026:</strong> Author registration deadline (late-breaking posters)</li><li><strong>25 August 2026: </strong>Deadline for late registration &amp; payment&nbsp;</li><li><strong>6-10 September 2026: </strong>Symposium</li></ul><h3><strong>REGISTRATION</strong></h3><blockquote><p class="cke-user_style-important"><strong>👉</strong><a target="_blank" rel="noopener noreferrer" href="https://www.czech-in.org/cmPortalV15/Account/Login?ReturnUrl=%2FcmPortalV15%2FPortal%2FISC26%2Fnormal"><strong>Register HERE for the ISC 2026</strong></a></p></blockquote><h3><strong>ABSTRACT SUBMISSION</strong></h3><blockquote><p class="cke-user_style-important"><strong>👉</strong><a target="_blank" rel="noopener noreferrer" href="https://www.czech-in.org/cmPortalV15/Account/Login?ReturnUrl=%2FcmPortalV15%2FPortal%2FISC26%2Fnormal"><strong>Submit your Abstract HERE</strong></a></p></blockquote><h3><strong>SCIENTIFIC PROGRAM</strong></h3><h4><strong>SHORT COURSES</strong></h4><h5><strong>SC 4 Hydrophilic Interaction Liquid Chromatography</strong></h5><p><strong>🗓️ SUNDAY, 6 SEPTEMBER 2026</strong></p><p><strong>🕗 8:30 – 11:45</strong></p><p>Hydrophilic Interaction Chromatography (HILIC) has become an essential separation mode for the analysis of polar compounds that are poorly retained in reversed-phase LC. This chromatographic mode is more and more widely used in pharmaceutical analysis, biopharmaceutical characterization, and, above all, metabolomics, where enhanced retention, improved MS sensitivity, and complementary selectivity are indispensable. Despite its power, HILIC remains perceived as complex due to its mixed retention mechanisms, sensitivity to experimental conditions, and limited repeatability. A dedicated short course is therefore required to help users understand this technique in a robust and efficient way.</p><p>This course will provide an in-depth and practical overview of HILIC fundamentals, starting with a discussion of the relatively complex retention mechanism. Particular emphasis will be placed on critical operational parameters such as sample diluent effects, which can drastically impact peak shape and retention, and on achieving good repeatability in gradient mode.</p><p>Participants will also learn how coupling HILIC with MS can maximize sensitivity, and how to select both mobile phase components and stationary phases to obtain reliable and reproducible separations. Numerous applications will be covered, including typical small-molecule analyses, comprehensive metabolomic workflows, and the characterization of large biopolymers such as oligonucleotides, peptides, and proteins.</p><p>In the end, this short course will help participants to confidently implement and troubleshoot HILIC in modern analytical laboratories.</p><h4><strong>Lecturers</strong></h4><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/articles?search=Davy+Guillarme"><strong>Davy Guillarme</strong></a></h5><ul><li>Davy Guillarme currently serves as an associate professor at the University of Geneva in Switzerland. With over 350 published journal his expertise spans various techniques, including UHPLC, HILIC, LC−MS, SFC, SFC-MS, multidimensional LC, and application to the characterization of biopharmaceuticals.</li><li>He is an editor of the Journal of Chromatography A and serves on the editorial advisory board of various other journals.</li><li>Davy Guillarme has been honored with the LC-GC Emerging Leader Award in Chromatography (2013), the Jubilee Medal from the Chromatographic Society (2018), the International Award of the Belgian Society of Pharmaceutical Sciences (2022) and the Csaba Horvath memorial award (2025).</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_2026_Davy_Guillarme_c54bb7dd40.jpg" alt="ISC 2026: Davy Guillarme" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_2026_Davy_Guillarme_c54bb7dd40.jpg 156w," sizes="100vw" width="500" height="500"></p>

ISC 2026 Short Course 4 - Hydrophilic Interaction Liquid Chromatography

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The International Symposium on Chromatography (ISC) represents the oldest conference series focussing on separation science. ISC symposia have been organised since 1956 in each even year. ISC is internationally recognised as one of the premier meeting series for discussion of all modes of chromatography and separation science with a broad coverage of techniques and applications.

International Symposium on Chromatography - (ISC)

Phenomenex Axia Preparative LC Columns

Available in over 40 unique achiral and chiral selectivities, Axia advanced preparative column packings and column hardware designs offer several advantages.

<p class="cke-user_style-important"><strong>Guaranteed, Longest Lasting Preparative HPLC and SFC Column</strong></p><p>Available in over 40 unique achiral and chiral selectivities, Axia advanced preparative column packings and column hardware designs offer several advantages. Unlike traditional preparative HPLC column packing methods, the Axia packing method offers increased sorbent bed density for increased performance and eliminates media bed collapse as a source of premature column failure in preparative HPLC/SFC columns.</p><h3><strong>Axia Packed Preparative HPLC Columns</strong></h3><h4><strong>Axia Single Axial Compression Step</strong></h4><p>Axia packed preparative columns involve a single axial compression step, unlike conventional packed preparative columns. The ideal prep HPLC column bed density is custom calculated and automated for each specific media and column size. Computer control of the entire process ensures both proper bed density and column uniformity every time.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Axia_Packing_Technology_1785ff0442.jpg" alt="Phenomenex: Axia Packing Technology" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Axia_Packing_Technology_1785ff0442.jpg 245w," sizes="100vw" width="917" height="560"></p><h4><strong>Unmatched Column Reproducibility</strong></h4><p>The <strong>automated</strong> <strong>Axia™ packing system</strong> provides <strong>feedback control</strong> and <strong>infinite tuning</strong> of packing density for specific media characteristics such as mechanical strength and porosity. An optimum higher bed density can be consistently reproduced column-to-column. This directly translates into consistent efficiency and peak asymmetry measurements and decreases the column variability seen in traditionally packed preparative columns.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Unmatched_Column_Reproducibility_a752be8dd5.jpg" alt="Phenomenex: Unmatched Column Reproducibility" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Unmatched_Column_Reproducibility_a752be8dd5.jpg 245w," sizes="100vw" width="995" height="534"></p><h3><strong>Seamless Scalability to Increase Sample Load</strong></h3><h4><strong>Increase Column Length</strong></h4><p>Increase sample load without increasing your flow rate by using a longer column. With Axia technology, each preparative column is optimized for:</p><ul><li>Analytical-like efficiency</li><li>Long column lifetime</li><li>High sample load with high surface area media such as Kinetex, Aeris, Gemini, Luna, Luna Omega, or Synergi</li></ul><h4><strong>Increase Column ID</strong></h4><p>For maximizing load without increasing the run time, consider scaling up to a larger column ID. Axia packed columns provide the three important benefits you need.</p><ul><li>Reproducible performance across all column diameters</li><li>Increased throughput without sacrificing purity</li><li>High efficiency from analytical to preparative</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Increase_Column_ID_a45d7f8aa3.jpg" alt="Phenomenex: Increase Column ID" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Increase_Column_ID_a45d7f8aa3.jpg 156w," sizes="100vw" width="908" height="910"></p><h3><strong>Axia Technology Outperforms Traditional Packing Processes!</strong></h3><p>Because of the constant pressure placed on the integrated packing piston, Axia packed columns possess the dynamic capability of maintaining a consistent, homogeneous media bed. This results in superior column performance no matter which media selectivity you choose.</p><h3><strong>How to choose the right column</strong></h3><h5><strong>Acidic Compounds</strong></h5><ul><li>Kinetex XB-C18</li><li>Gemini C18</li></ul><h5><strong>Aromatic</strong></h5><ul><li>Luna Phenyl-Hexyl</li><li>Kinetex Biphenyl</li></ul><h5><strong>Closely Related Compounds</strong></h5><ul><li>Kinetex F5</li><li>Luna PFP(2)</li></ul><h5><strong>Extremely Hydrophobic</strong></h5><ul><li>Kinetex C8</li><li>Luna C8(2)</li></ul><h5><strong>Extremely Polar</strong></h5><ul><li>Luna HILIC(2)</li><li>Kinetex HILIC</li></ul><h5><strong>Hydrophobic Compounds</strong></h5><ul><li>Luna C18(2)</li><li>Kinetex C18</li></ul><h5><strong>Polar Acids</strong></h5><ul><li>Luna Omega Polar C18</li><li>Kinetex Polar C18</li></ul><h5><strong>Polar Bases</strong></h5><ul><li>Luna Omega PS C18</li><li>Kinetex PS C18</li></ul><h5><strong>Sugars</strong></h5><ul><li>Luna NH(2)</li></ul><h5><strong>Chiral</strong></h5><ul><li>Lux i-Amylose-3</li><li>Lux Cellulose-1</li></ul>

Phenomenex Prodigy Phenyl-Ethyl Column

Phenomenex's ethyl-phenyl polar column is a highly reproducible reversed-phase column for the analysis of basic, acidic and amphoteric compounds.

<p>Highly reproducible reveresed phase columns for the analysis of basic, acidic and amphoteric compounds.</p><ul><li><strong>PH-3</strong>: phenyl column with excellent aromatic and polar compound selectivity</li><li><strong>3 μm ODS-3:</strong> high efficiency alternative to the 5 μm ODS-3 columns</li><li>Columns stable from <strong>pH 2 to 9</strong></li></ul><h5><strong>Other Packing material:</strong></h5><ul><li>Prodigy ODS (2)</li><li>Prodigy C8</li><li>Prodigy ODS (3)</li></ul>

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