<h5>Why compromise between performance and price when you can have both?</h5>With Thermo Scientific factory-certified, pre-owned <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=5&amp;manufacturerItems=3">mass spectrometers</a>, 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.<h3>Factory-Certified for confidence</h3>Every certified pre-owned system goes through a rigorous factory reconditioning process. From updated hardware and software to comprehensive performance testing, each instrument is restored to meet the same high standards as our new products.<h4>What’s included?</h4>When you choose a certified LC-MS system, you get more than just an instrument—you get the complete Thermo Scientific experience:<ul><li>Full 1-year factory warranty for peace of mind</li><li>29-point inspection checklist, re-certification, and final quality testing</li><li>Software and hardware updates to current revisions</li><li>Re-certification using only genuine Thermo Scientific factory parts</li><li>Professional installation by Unity Lab Services field engineers</li><li>Optional training and application support to get you up and running fast</li></ul><h4>What gets replaced?</h4>Our reconditioning process is comprehensive. These critical components are replaced on every system:<ul><li>All hoses</li><li>Probes</li><li>Ion sources</li><li>Ion transfer tube</li><li>Multiplier</li><li>Mechanical pumps</li><li>Acquisition PC and software</li><li>PCBs (when required for revision)</li></ul><h3>Maximize uptime with expert support</h3>Behind every certified system is a global team of Thermo Fisher specialists committed to helping your lab succeed. Support doesn’t stop after installation:<ul><li>Flexible service contract options through Unity Lab Services</li><li>Guaranteed response times for select contracts</li><li>Financing solutions to meet your budget</li><li>System qualifications and validations</li><li>Technology refresh solutions to keep you ahead of the curve</li></ul><h3>A smarter, more sustainable choice</h3>Investing in a factory-certified pre-owned system isn’t just cost-effective—it’s a sustainable solution that extends the life of high-performance equipment and reduces waste. You get the data quality and instrument reliability your work depends on, while making an environmentally conscious choice.<h3>More ways to access Thermo Scientific excellence—affordably</h3>We understand that every lab’s financial situation is different. That’s why Thermo Fisher offers multiple paths to help you acquire the right mass spectrometry solution, when you need it.<h4>1. <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/industrial/mass-spectrometry/mass-spectrometer-price-affordability-programs/factory-certified-refurbished-mass-spectrometers.html">Factory-certified refurbished systems</a></h4>Already covered above, this option gives you fully reconditioned, factory-tested LC-MS instruments at a lower price point—without compromising performance or support.View our brochure for a comprehensive overview.<h4>2. <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/industrial/mass-spectrometry/mass-spectrometer-price-affordability-programs/mass-spectrometer-trade-upgrade.html">Trade-in and trade-up</a>: Turn your old into increased productivity</h4>Already own a system—Thermo Fisher or otherwise? Trade it in and upgrade to a newer model with greater capabilities and sensitivity.How it works:<ul><li>Receive a discount on your next system based on the residual value of your current instrument</li><li>Avoid the hassle of selling or decommissioning your old system</li><li>Transition with minimal downtime and disruption</li></ul>Why labs choose this path:<ul><li>Keeps productivity high while moving to new technology</li><li>Eases the financial burden of upgrading</li><li>Helps labs stay competitive with improved system performance</li></ul><h4>3. Personalized equipment <a target="_blank" rel="noopener noreferrer" href="https://www.thermofisher.com/content/lifetech/global/en/home/products-and-services/services/financial-leasing-services.html">financing &amp; leasing options</a></h4>If upfront capital is limited, our tailored financing and leasing plans offer flexibility that aligns with your lab’s budget and growth plans.<h5>Ready to get started?</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">Explore our certified systems, trade-in opportunities, and financing solutions.</a></li></ul>Visit us on&nbsp;<a target="_blank" rel="noopener noreferrer" href="https://www.linkedin.com/showcase/72003132/admin/dashboard/">LinkedIn:</a>&nbsp;#affordabiliy #LCMS #sustainability #productivity<blockquote><h5>Ema Ruzic</h5>Vertical Marketing Manager, Chromatography and Mass Spectrometry Division (CMD)</blockquote>

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

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.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.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233">Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes</a></h4>Qiong Zhang*, Jiayou Ge, Fengjie Liu, Shabaz Mohammed, Kedong Yin, and Rosalind E. M. RickabyEnviron. Sci. Technol. 2025, 59, 50, 27367–27377<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.est.5c11233">https://doi.org/10.1021/acs.est.5c11233</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.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.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 in situ 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 (e.g., by ICP-MS) and the protein sequence (e.g., 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>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.<h3>Materials and Methods</h3><h4>ICP-MS Analysis</h4>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 G. huxleyi (OA1, OA4, OA8, OA15, OA16, OA23, and RCC 1242) and Synechocystis (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><h4>Protein Mass Spectrometry</h4>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">Ultimate 3000 UHPLC </a>system (Thermo Fisher Scientific) and electrosprayed directly into a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559">Q-Exactive Mass Spectrometer</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 m/z, 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 m/z) with the first fixed mass at 180 m/z. Charge exclusion was selected for unassigned and 1+ ions. The dynamic exclusion was set to 20 s.<h3>Results and Discussion</h3><h4>Trace Elements Determined from the Expressed Proteomes of Different Phytoplankton</h4>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 G. huxleyi, 31 different metals in C. reinhardtii, and 30 different metals in Synechocystis. Although only 6 different metals were identified in O. tauri proteins, it has to be noted that the analysis for O. tauri 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.<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">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 (Mg2+ and Ca2+ [weakest binding] &lt; Mn2+ &lt; Fe2+ &lt; Co2+ &lt; Ni2+ &lt; Cu2+ &gt; Zn2+). <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>).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 G. huxleyi and Synechocystis. <a href="javascript:void(0);">(22,24)</a> The essential roles of Mg in plants have been reported in various studies. Mg2+ 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><h4>Comparison Between Metallome Measured Directly and Reconstructed from Proteins</h4>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.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 (r2 = 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 r2 = 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.<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">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 G. huxleyi and Synechocystis (<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. Ca2+ 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+ 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 Mg2+ and K+ abundances should also be higher than those determined from the protein structures. Free Mg2+ and K+ 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>).

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/">ISC 2026</a></h3>The <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/companies/314">International Symposium on Chromatography (ISC)</a> 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.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.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.<h3>ISC 2026 SYMPOSIUM KEY DATES</h3><h4>6-10 SEPTEMBER 2026</h4><ul><li>15 January 2026: Opening of Early-bird Registration &amp; Abstract submission</li><li>11 March 2026: Deadline for abstract submission (orals)</li><li>21 April 2026: Sending acceptance letters (orals)</li><li>15 May 2026: Deadline of early-bird registration and payment &amp; Author registration deadline (orals)</li><li>1 June 2026: Preliminary detailed program on web</li><li>1 June 2026: Deadline for abstract submission (posters)</li><li>16 June 2026: 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>30 June 2026: Author registration deadline (posters)</li><li>30 July 2026: Deadline for abstract submission (late-breaking posters)<ul><li>without the possibility of competing for the Best Poster Award</li></ul></li><li>11 August 2026: Sending acceptance letters (late-breaking posters)</li><li>18 August 2026: Author registration deadline (late-breaking posters)</li><li>25 August 2026: Deadline for late registration &amp; payment&nbsp;</li><li>6-10 September 2026: Symposium</li></ul><h3>REGISTRATION</h3><blockquote>👉<a target="_blank" rel="noopener noreferrer" href="https://www.czech-in.org/cmPortalV15/Account/Login?ReturnUrl=%2FcmPortalV15%2FPortal%2FISC26%2Fnormal">Register HERE for the ISC 2026</a></blockquote><h3>ABSTRACT SUBMISSION</h3><blockquote>👉<a target="_blank" rel="noopener noreferrer" href="https://www.czech-in.org/cmPortalV15/Account/Login?ReturnUrl=%2FcmPortalV15%2FPortal%2FISC26%2Fnormal">Submit your Abstract HERE</a></blockquote><h3>SCIENTIFIC PROGRAM</h3><h4>SHORT COURSES</h4><h5>SC 4 Hydrophilic Interaction Liquid Chromatography</h5>🗓️ SUNDAY, 6 SEPTEMBER 2026🕗 8:30 – 11:45Hydrophilic 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.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.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.In the end, this short course will help participants to confidently implement and troubleshoot HILIC in modern analytical laboratories.<h4>Lecturers</h4><h5><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/articles?search=Davy+Guillarme">Davy Guillarme</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><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">

ISC 2026 Short Course 4 - Hydrophilic Interaction Liquid Chromatography

Article

Product

Events

Scientific article

Science and research

Video

A unique company dedicated to serving science helping our customers drive productivity and accelerate results. Through our premier brands – Thermo Scientific, Applied Biosystems, Invitrogen, Fisher Scientific and Unity Lab Services.

Thermo Fisher Scientific

Everything from the world of analytical chemistry in one place. We connect people in solving their problems. At Labrulez you will find all the necessary information easily, quickly and clearly. Stop searching and start finding.

LabRulez

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)

KNAUER AppliChrom® ABOA VivoSep SEC Columns

AppliChrom® SEC columns for water soluble (bio)polymers are multi hydrophilic layered SEC media for highest efficiency and low interaction.

AppliChrom® SEC columns for water soluble (bio)polymers<h4>Properties:</h4><ul><li>Multi hydrophilic layered SEC media for highest efficiency and low interaction</li><li>Available seperation ranges: from small molecules up to 5 500 kDa</li><li>Temperature stability: 10-90 °C</li><li>Stable between: pH 2–10</li><li>Pressure stability: up to 200 bar</li><li>Simple adaptation from HPLC to SEC with stainless steel instruments</li><li>Versatile tool for accurate protein molecular weight or size determination</li><li>Low column bleed for low detector noise</li><li>Increased lifetime of SEC columns through combination of proprietary particle and packing technology</li><li>Recommended eluents: H₂O, buffers</li></ul><h4>Applications</h4><ul><li>Water soluble proteins, humic substances</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER AppliChrom® ABOA Cat-Phil SEC Columns

Interaction-free pure GPC & SEC base material with focus on polycationic, polyelectrolytic or funktional amine analytes

AppliChrom® SEC columns for neutral, anionic and additional cationic polymers<h4>Properties:</h4><ul><li>Interaction-free pure GPC &amp; SEC base material with focus on polycationic, polyelectrolytic or funktional amine analytes</li><li>No salt addition is needed to surpress surface adsorption</li><li>No ion exclusion phenomena</li><li>Possible to be used in universal calibration &amp; accurate molecular weight determination even for small polycationic molecules</li><li>Temperature stability between: 10–90 °C</li><li>Stable with: pH 2–10</li><li>Simple, reliable and robust GPC &amp; SEC calibration from dextrans, pullulans et al.</li><li>Low column bleed for low detector gain for improved refractive index, light scattering or viscosity detection</li><li>Large volume and optimized mass transfer for polymers with optimized resolution</li><li>Low cost due to long column lifetime - result of the combination of optimized particle and packing technology</li><li>Recommended eluents: H₂O, buffers</li></ul><h4>Applications</h4>Water soluble analytes like:<ul><li>polycations, polyamines (chitosanes), polyethylenoxides, polysaccharides, polyanions (heparins, pectins), polyethylene oxide (PEO), polyethylene glycol (PEG), Ppolyethyleneimins (PEI), polyvinylimidazole</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER AppliChrom® ABOA StyDiViBe GPC Columns

Organic polystyrene-divinylbenzene copolymer base material with high porosity for high resolution

AppliChrom® GPC columns for GPC analysis of organic molecules with THF, toluene, chloroform<h4>Properties:</h4><ul><li>Organic polystyrene-divinylbenzene copolymer base material with high porosity for high resolution</li><li>High pressure stability: up to 150 bar</li><li>Temperature stable: between 10-145 °C</li><li>GPC range: from 0.1 up to 50 000 kDa</li><li>Low column bleed for low detector noise</li><li>High purity to eliminate adsorptive effects and combine pure GPC with long lifetime</li><li>Large calibration ranges for several decades due to the unique process of BPT technology</li><li>Range of individual porosities that can be used individually or in combination</li><li>Optimized for: 1 ml/min flow rate for 8 mm ID columns</li><li>High level of reproducibility and peak precision due to the advanced packing procedure</li><li>Recommended eluents: THF, Toluene, CHCl₃, dichlorbenzene, hexane/EtOAc (10:90, V:V)</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_Sty_Di_Vi_Be_P_Molecular_sizes_range_ca9a682d2e.jpg" alt="KNAUER: AppliChrom® ABOA StyDiViBe-P - Molecular sizes range" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_Sty_Di_Vi_Be_P_Molecular_sizes_range_ca9a682d2e.jpg 235w," sizes="100vw" width="1072" height="712"><h4>Applications</h4>Hydrophobic oligomers or polymers like:<ul><li>PVC, PMMA, polystyrene, epoxy resins, polyesters, bisphenol A resins</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER AppliChrom® ABOA DMAc-Phil GPC Columns

Organic polymer base material with high porosity for high resolution

AppliChrom® GPC columns for organic GPC analyses in DMAc or DMF<h4>Properties:</h4><ul><li>Organic polymer base material with high porosity for high resolution</li><li>Wide range of porosities and particle sizes</li><li>Pressure stability: up to 150 bar</li><li>Stable between: 35-145 °C</li><li>Excellent reproducibility and resolution due to the advanced packing procedure</li><li>High purity to eliminate adsorptive effects and combine pure GPC with long lifetime</li><li>GPC range from: 100-1 000 000 Da</li><li>Optimal for: 0.5 ml/min flow rates with 8 mm ID colums</li><li>Recommended eluents: DMAc, DMF, NMP, LiBr additive</li></ul><h4>Applications</h4>Slightly polar analytes like:<ul><li>PMMA, polyacryl nitril (PAN), acrylnitrile butadiene styrene (ABS), cellulose, and all DMF and DMAc soluble polymers</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER AppliChrom® ABOA DMSO-Phil GPC Columns

AppliChrom® DMSO-PHIL optimized for DMSO-GPC applications from an interaction-free pure GPC base material

AppliChrom® DMSO-PHIL optimized for DMSO-GPC applications<h4>Properties:</h4><ul><li>Interaction-free pure GPC base material</li><li>Temperature stabel between: 40-90 °C (145 °C) depending on application</li><li>Simple, reliable and robust GPC &amp; SEC calibration from dextrans, pullulans et al.</li><li>Low column bleed for low detector gain for improved refractive index, light scattering or viscosity detection</li><li>12 µm particle technology for low back pressure</li><li>Tolerates traces of water and NaNO₃ additve</li><li>Large volume and optimized mass transfer for polymers with optimized resolution</li><li>Low cost due to long column lifetime - result of the combination of optimized particle and packing technology</li><li>Recommended eluents: DMSO, 0.075 M NaNO₃</li></ul><h4>Applications</h4>Polar, not water soluble oligomers or polymers like:<ul><li>polysaccharides, lignin, amylose, starch, humic acids, polyvenyl pyridin, PNIPA, polyvinyl alcohol (PVA), melamin-urea-formaldehyd resin (MUF) or urea-formaldehyd resin (UF)</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER AppliChrom® ABOA HFIP-Phil GPC Columns

AppliChrom® GPC columns for separations in HFIP with broad pore technology for GPC for analytes with challenging solution behavior

AppliChrom® GPC columns for separations in HFIP<h4>Properties:</h4><ul><li>Broad pore technology for GPC for analytes with challenging solution behavior</li><li>Separation range beween: 0.1–50 000 kDa</li><li>Range of individual porosities that can be used individually or in combination</li><li>Temperature stable between: 35–145 °C</li><li>Long column lifetime - result of the combination of optimized particle and packing technology</li><li>Low column bleed for low detector noise</li><li>Excellent reproducibility and resolution due to the advanced packing procedure</li><li>Calibration standard: PMMA or PEO &nbsp;</li><li>Recommended eluents: Hexafluoroisopropanol (HFIP), 0.1 % KTFa as modifier</li></ul><h4>Applications</h4>Crystalline highperformance polymers like:&nbsp;<ul><li>polyamides (PA), polyethylen terepthalate (PET), polybutylen terepthalate (PBT), polylactic acid (PLA), polyamid 6 (PA6), polycaprolactam, paraformaldehyde, polyoxymethylene (POM), polyacetal, several polyoxazolines</li></ul><h3>GPC &amp; SEC Columns</h3>GPC &amp; SEC systems offer solutions for various applications and laboratoriesGel permeation chromatography (GPC) and size exclusion chromatography (SEC) separate analytes by size using special columns with a porous matrix. The basic separation principle is based on the fact that smaller molecules penetrate these pores more strongly and therefore move more slowly through the matrix than larger molecules. GPC/SEC is often used as gentle and powerful purification technique or for quality control in research and development. Typical target molecules are polymers, dissolved in organic solvents for GPC, and macro biomolecules like proteins, antibodies or polysaccharides, dissolved in aqueous eluents for SEC.Separation is facilitated by selecting optimal particle and pore sizes. Therefore we offer a wide range of pore sizes (35, 100, 150, 250, 350, 500, 1000, 1500, 10E5, 10E6, 10E7 Å) and several particle sizes (5, 7, 10, 12, 20 µm) as a choice to customize for every application task.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_principle_2a432edcc1.webp" alt="KNAUER: Size Exclusion - principle" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_principle_2a432edcc1.webp 228w," sizes="100vw" width="1024" height="700"><h3>KNAUER AppliChrom® ABOA columns for aqueous SEC, organic GPC, and special applications</h3><ul><li>AppliChrom® ABOA StyDiViBe Series GPC-columns for GPC analysis of organic molecules using THF, toluene, chloroform.</li><li>AppliChrom ABOA SuperOH-P Series for aqueous GPC/SEC-analysis of mainly neutral and anionic polymers like heparins, polysaccharides, PEO, PEG,....</li><li>AppliChrom® ABOA DMSO-Phil-P Series for DMSO GPC/SEC analysis (humic substances, UF/MUF-glue, p-NIPA, many polycondensates, protein from pea or leguminosae,...)</li><li>AppliChrom® ABOA DMAc-Phil-P Series for GPC/ SEC analysis in DMAc, DMF, NMP. Good for many medium polar substances, polyoxazolines, lignin,...</li><li>AppliChrom® ABOA Cat-Phil-P Series for aqueous GPC/SEC-analysis of special aminic and polycationic polymers like p-DADMAc, PEI/ polyethylenimin, chitosan, copolymers with polyaminofunctions, but also useful for polyanions or neutral polymers like heparin or PEO/PEG, dextran or pullulan.</li><li>Seperation Ranges: 100–50 000 000 Da</li></ul><h4>You decide between classical GPC/SEC columns with conventional mixed pore technology or AppliChrom® BPT technology:</h4>Separate oligomers and polymers with the new GPC media line from AppliChrom® BPT synthesis technology for large range, high resolution separations with increased accuracy in calibration (patent pending).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg" alt="KNAUER: AppliChrom® ABOA columns." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Appli_Chrom_ABOA_columns_58d5d380f6.jpg 245w," sizes="100vw" width="1379" height="718">

KNAUER Sepapure® FPLC Columns for Antibody Affinity Chromatography

 The FPLC media is functionalized either with Protein A or Protein G ligands for the binding of antibodies or antibody fragments.

FPLC media based on cross-linked agarose beads with a mean diameter of 100 µm. &nbsp;The FPLC media is functionalized either with Protein A or Protein G ligands for the binding of antibodies or antibody fragments.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Antibody_Affinity_Protein_A_and_G_08afa2179e.webp" alt="KNAUER: FPLC Column for Antibody Affinity - Protein A and G" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Antibody_Affinity_Protein_A_and_G_08afa2179e.webp 236w," sizes="100vw" width="690" height="456"><h4>Properties:</h4>Sepapure® Affinity media for antibodies or antibody fragments is designed to be used with most aqueous buffer systems. It is long lasting when correctly handled and are compatible with common CIP strategies. All Sepapure® media is stored in 20 % ethanol upon delivery. Available as prepacked 1 ml or 5 ml cartridge or as bulk material.<h4>Technical data:</h4>Agarose beads with typical loading ranges of 1 - 30 mg/l (Protein A column) or 1 - 15 mg/ml (Protein G column). The maximum operating pressure the Sepapure® columns should be used at is 3 bar, while the recommended flowrate is 1 CV/ml.<h4>Recommended application areas:</h4>Typically used in the first step („capture“) of an FPLC purification procedure.<h3>KNAUER Sepapure®&nbsp;</h3>In protein purification, a combination of different methods is needed for a successful separation. The purity of the wanted biomolecule is increased in three steps: Capture - Intermediate - PolishingIn the “capture step” the crude biomolecule is extracted from major side products. In the “intermediate step” further contaminations are removed, and the highly pure biomolecule is gained in the “polishing step”. For each step a different method and therefore different columns are used.&nbsp;FPLC Sepapure® columns are dedicated for purification of biomolecules. Sepapure® media for affinity chromatography (AC) and Ion-Exchange chromatography (IEX) is based on Agarose and depending on the specific purification mode functionalized with ligands e.g. Protein A, Ni-NTA or quaternary ammonium (Q). These FPLC media are available packed in 1 ml and 5 ml cartridges or as bulk media.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg" alt="KNAUER: FPLC Sepapure® columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg 245w," sizes="100vw" width="1372" height="562"><h5>Physical properties FPLC Sepapure® columns</h5><ul><li>Resin 100 µm Agarose particles with 4 % or 6 % crosslinking</li><li>Flowrate Recommended: 1 CV/ml</li><li>pH Stability 3 – 9 long term</li><li>Max. pressure 3 bar</li></ul>Sepapure® Desalting columns are based on Dextran with an exclusion limit of 5 kDa and available in 1 ml and 5 ml cartridges.&nbsp;<h5>Physical properties Sepapure® Desalting columns</h5><ul><li>Resin 20 – 50 µm Dextran particles</li><li>Flowrate Recommended: 1 CV/ml</li><li>Exclusion limit 5 kDa</li><li>Max. pressure 3 bar</li></ul>

KNAUER Sepapure® FPLC Columns for Tag-Affinity Chromatography

FPLC media based on cross-linked agarose beads with a mean diameter of 100 µm.  The FPLC media is functionalized with NTA ligands for His-Tag.

FPLC media based on cross-linked agarose beads with a mean diameter of 100 µm. &nbsp;The FPLC media is functionalized with NTA ligands for His-Tag.&nbsp;<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Antibody_Affinity_Protein_A_and_G_08afa2179e.webp" alt="KNAUER: FPLC Column for Tag-Affinity Chromatography" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Antibody_Affinity_Protein_A_and_G_08afa2179e.webp 236w," sizes="100vw" width="690" height="456"><h4>Properties:</h4>Sepapure® Affinity media for recombinantly tagged proteins is designed to be used with most aqueous buffer systems. It is long lasting when correctly handled and compatible with common CIP strategies. All Sepapure® media is stored in 20 % ethanol upon delivery. Available as prepacked 1 ml or 5 ml cartridge or as bulk material.<h4>Technical data:</h4>Agarose beads with typical loading ranges of 1–40 mg/l (Ni-NTA). The maximum operating pressure the Sepapure® columns should be used at is 3 bar, while the recommended flowrate is 1 CV/ml. &nbsp;Available as prepacked 1 ml or 5 ml cartridge or as bulk material.<h4>Recommended application areas:</h4>Typically used in the first step („capture“) of an FPLC purification procedure.<h3>KNAUER Sepapure®&nbsp;</h3>In protein purification, a combination of different methods is needed for a successful separation. The purity of the wanted biomolecule is increased in three steps: Capture - Intermediate - PolishingIn the “capture step” the crude biomolecule is extracted from major side products. In the “intermediate step” further contaminations are removed, and the highly pure biomolecule is gained in the “polishing step”. For each step a different method and therefore different columns are used.&nbsp;FPLC Sepapure® columns are dedicated for purification of biomolecules. Sepapure® media for affinity chromatography (AC) and Ion-Exchange chromatography (IEX) is based on Agarose and depending on the specific purification mode functionalized with ligands e.g. Protein A, Ni-NTA or quaternary ammonium (Q). These FPLC media are available packed in 1 ml and 5 ml cartridges or as bulk media.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg" alt="KNAUER: FPLC Sepapure® columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg 245w," sizes="100vw" width="1372" height="562"><h5>Physical properties FPLC Sepapure® columns</h5><ul><li>Resin 100 µm Agarose particles with 4 % or 6 % crosslinking</li><li>Flowrate Recommended: 1 CV/ml</li><li>pH Stability 3 – 9 long term</li><li>Max. pressure 3 bar</li></ul>Sepapure® Desalting columns are based on Dextran with an exclusion limit of 5 kDa and available in 1 ml and 5 ml cartridges.&nbsp;<h5>Physical properties Sepapure® Desalting columns</h5><ul><li>Resin 20 – 50 µm Dextran particles</li><li>Flowrate Recommended: 1 CV/ml</li><li>Exclusion limit 5 kDa</li><li>Max. pressure 3 bar</li></ul>

KNAUER Sepapure® FPLC Columns for Ion-Exchange Chromatography

The FPLC media is functionalized with different linkers ranging from strong anion exchange ligands to weak cation exchange ligands. 

FPLC media based on cross-linked agarose beads with a mean diameter of 100 µm. &nbsp;The FPLC media is functionalized with different linkers ranging from strong anion exchange ligands to weak cation exchange ligands.&nbsp;<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Ion_Exchange_Chromatography_640e6f5ba7.jpg" alt="KNAUER: Sepapure FPLC Columns for Ion Exchange Chromatography" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Ion_Exchange_Chromatography_640e6f5ba7.jpg 236w," sizes="100vw" width="1920" height="1270"><h4>Properties:</h4>Sepapure® Ion-Exchange media is designed to be used with most aqueous buffer systems. It is long lasting when correctly handled and is compatible with common CIP strategies. All Sepapure® media is stored in 20 % ethanol upon delivery. &nbsp;<h4>Technical data:</h4>The agarose beads are functionalized with a quaternary ammonium for the strong anion exchanger (Q) and with diethylaminoethyl for the weak anion exchanger (DEAE). The strong cation exchanger is functionalized with sulphopropyl (SP) and the weak cation exchanger with carboxymethyl (CM).&nbsp;The maximum operating pressure the Sepapure® columns should be used at is 3 bar, while the recommended flowrate is 1 CV/ml.&nbsp;Available as prepacked 1 ml or 5 ml cartridge or as bulk material.&nbsp;<h4>Recommended application areas:</h4>Typically used in the intermediate step of an FPLC purification procedure.<h3>KNAUER Sepapure®&nbsp;</h3>In protein purification, a combination of different methods is needed for a successful separation. The purity of the wanted biomolecule is increased in three steps: Capture - Intermediate - PolishingIn the “capture step” the crude biomolecule is extracted from major side products. In the “intermediate step” further contaminations are removed, and the highly pure biomolecule is gained in the “polishing step”. For each step a different method and therefore different columns are used.&nbsp;FPLC Sepapure® columns are dedicated for purification of biomolecules. Sepapure® media for affinity chromatography (AC) and Ion-Exchange chromatography (IEX) is based on Agarose and depending on the specific purification mode functionalized with ligands e.g. Protein A, Ni-NTA or quaternary ammonium (Q). These FPLC media are available packed in 1 ml and 5 ml cartridges or as bulk media.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg" alt="KNAUER: FPLC Sepapure® columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg 245w," sizes="100vw" width="1372" height="562"><h5>Physical properties FPLC Sepapure® columns</h5><ul><li>Resin 100 µm Agarose particles with 4 % or 6 % crosslinking</li><li>Flowrate Recommended: 1 CV/ml</li><li>pH Stability 3 – 9 long term</li><li>Max. pressure 3 bar</li></ul>Sepapure® Desalting columns are based on Dextran with an exclusion limit of 5 kDa and available in 1 ml and 5 ml cartridges.&nbsp;<h5>Physical properties Sepapure® Desalting columns</h5><ul><li>Resin 20 – 50 µm Dextran particles</li><li>Flowrate Recommended: 1 CV/ml</li><li>Exclusion limit 5 kDa</li><li>Max. pressure 3 bar</li></ul>

KNAUER Sepapure® FPLC Desalting Columns

Desalting columns based on dextran for group separations of large molecular weight biomolecules from small molecular weight compounds and salts.

FPLC media based on dextran beads with a mean diameter of 20–50 µm. Size exclusion chromatography (SEC) separates molecules on the basis of size differences. KNAUER offers desalting columns based on dextran for group separations of large molecular weight biomolecules from small molecular weight compounds and salts.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Size_Exclusion_chromatography_fb9d43e34b.jpg" alt="KNAUER: Sepapure FPLC - Desalting or Buffer Exchange" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Size_Exclusion_chromatography_fb9d43e34b.jpg 156w," sizes="100vw" width="1500" height="1500"><h4>Properties:</h4>Sepapure® Desalting media is designed to be used for removal of small molecules below the exclusion limit and for covenient rebuffering. It is long lasting when correctly handled and compatible with common CIP strategies. All Sepapure® media is stored in 20 % ethanol upon delivery. Available as prepacked 5 ml cartridge or as bulk material.&nbsp;<h4>Technical data:</h4>The Sepapure® dextran beads have an exclusion limit of 5 kDa. The maximum operating pressure of the Sepapure® columns is 3 bar, while the recommended flowrate is 1 CV/ml.<h4>Recommended application areas:</h4>Typically used in the final step of an FPLC purification procedure or inbetween steps for fast buffer exchange.<h3>KNAUER Sepapure®&nbsp;</h3>In protein purification, a combination of different methods is needed for a successful separation. The purity of the wanted biomolecule is increased in three steps: Capture - Intermediate - PolishingIn the “capture step” the crude biomolecule is extracted from major side products. In the “intermediate step” further contaminations are removed, and the highly pure biomolecule is gained in the “polishing step”. For each step a different method and therefore different columns are used.&nbsp;FPLC Sepapure® columns are dedicated for purification of biomolecules. Sepapure® media for affinity chromatography (AC) and Ion-Exchange chromatography (IEX) is based on Agarose and depending on the specific purification mode functionalized with ligands e.g. Protein A, Ni-NTA or quaternary ammonium (Q). These FPLC media are available packed in 1 ml and 5 ml cartridges or as bulk media.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg" alt="KNAUER: FPLC Sepapure® columns" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_FPLC_Sepapure_columns_ad980345f3.jpg 245w," sizes="100vw" width="1372" height="562"><h5>Physical properties FPLC Sepapure® columns</h5><ul><li>Resin 100 µm Agarose particles with 4 % or 6 % crosslinking</li><li>Flowrate Recommended: 1 CV/ml</li><li>pH Stability 3 – 9 long term</li><li>Max. pressure 3 bar</li></ul>Sepapure® Desalting columns are based on Dextran with an exclusion limit of 5 kDa and available in 1 ml and 5 ml cartridges.&nbsp;<h5>Physical properties Sepapure® Desalting columns</h5><ul><li>Resin 20 – 50 µm Dextran particles</li><li>Flowrate Recommended: 1 CV/ml</li><li>Exclusion limit 5 kDa</li><li>Max. pressure 3 bar</li></ul>

Products focused on Consumables - page 22

Related content

ISC 2026 Short Course 4 - Hydrophilic Interaction Liquid Chromatography

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

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