<div><p><strong>Purifying the target protein is crucial for investigating its specific properties and interactions with biomolecules like DNA, RNA, and other proteins. A range of purification strategies is available, and the optimal approach depends on factors such as the required scale, throughput, and downstream application. In many cases, the process must be fine-tuned through empirical optimization to achieve the desired purity and yield.</strong></p></div><div><div><div><div><h3><strong>What is Protein Purification?</strong></h3><p>Protein purification is a critical process in biotechnology and life sciences, aimed at isolating a specific protein from complex biological mixtures such as cell lysates or tissue extracts. The goal is to obtain a highly purified protein sample, free from contaminants like other proteins, nucleic acids, and lipids, to enable accurate analysis of its structure, function, and interactions.</p><p>This process is especially vital in biotechnological areas inside immunology and microbiology. In <strong>immunology</strong>, it underpins the production of vaccines, therapeutic antibodies, and diagnostic assays by enabling the isolation of key immune proteins and antibodies. It also supports the investigation of cell signaling and immune response mechanisms. In <strong>microbiology</strong>, purified proteins are essential for studying pathogens, identifying disease-related antigens, and driving drug discovery efforts. Ultimately, protein purification is fundamental to the development of targeted vaccines, innovative diagnostics, and effective therapeutic strategies.</p></div></div></div></div><div><div><div><div><h3><strong>Types of Protein Purification Methods</strong></h3></div></div></div></div><div><p>There are several types of protein purification methods, each chosen based on the protein’s characteristics such as size, charge, solubility, and binding affinity. Below are some commonly used methods:</p></div><div><div><div><div><h4><strong>Non-Chromatographic Approaches</strong></h4></div></div><div><p>Non-chromatographic approaches use simpler physicochemical principles—such as solubility, molecular size, or diffusional properties—to separate and purify proteins. These techniques are often employed as initial purification or concentration steps before further refinement.</p><h5><strong>Precipitation Techniques</strong></h5><p>Protein precipitation is a widely used approach in purification workflows, typically relying on one of three main methods:</p><ul><li><strong>Organic solvent precipitation</strong> involves adding solvents like ethanol or acetone to lower the solution's dielectric constant. This promotes protein–protein interactions, reducing solubility and leading to aggregation and precipitation.</li><li><strong>Isoelectric point precipitation </strong>exploits the pH at which a protein carries no net charge. At this point, solubility is minimized, causing the protein to precipitate from solution.</li><li><strong>Nonionic polymer precipitation</strong> uses polymers such as dextran, polyethylene glycol (PEG), or NPEP to alter the solution’s physical properties. These agents create crowding effects that promote protein aggregation without directly binding to the proteins.</li></ul><h5><strong>Dialysis</strong></h5><p>Dialysis involves placing a protein solution inside a semi-permeable membrane that allows water and ions to pass while the protein remains inside, facilitating buffer exchange.This method is commonly used during protein expression and purification workflows for buffer exchange, desalting, and removal of unwanted small molecules such as imidazole, urea, or ammonium sulfate. The process helps maintain protein stability and activity by gradually equilibrating the sample with the desired buffer conditions.</p><h5><strong>Immunocapture (Magnetic Bead-Based Purification</strong></h5><p>Immunocapture uses antibodies immobilized on solid supports like magnetic beads to selectively bind and isolate a target protein. This method is highly specific and particularly useful for low-abundance targets or small-scale prep, such as:</p><ul><li>Pulling down proteins from complex mixtures</li><li>Capturing tagged recombinant proteins (e.g., FLAG, HA, or His tags)</li><li>Enrichment before western blotting, MS, or ELISA</li></ul><p>Magnetic beads offer speed, ease of use, and minimal sample loss, making them ideal for lab-scale workflows.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/products/biozenspe-sample-preparation-products/biozen-magbeads">Biozen MagBeads</a> provide a fast and efficient method for purifying, isolating, and cleaning up monoclonal antibodies (mAbs), proteins, and peptides. These paramagnetic beads feature a streptavidin-coated surface, enabling high-affinity binding in immuno-based workflows. Compared to traditional sample preparation techniques, magnetic bead-based immunocapture offers greater speed and consistency by delivering high binding capacity with uniform particle size, ensuring accurate and reproducible results in significantly less time.</p><h5><strong>Centrifugation</strong></h5><p>Centrifugation of crude protein mixtures is an essential step in the investigation of protein purification and aggregation. Outlined below are the various types of centrifugations employed in protein purification.</p><p><strong>Preparative Ultracentrifugation</strong><br>Ultracentrifugation is an effective method of purifying proteins from aggregates based on their size, shape and density. Centrifugation, widely recognized as a robust and versatile method, is commonly used to separate complex mixtures of cellular components. Ultracentrifuges separate small particles by spinning at high speeds, utilizing centrifugal force based on size and density.</p><p><strong>Differential Centrifugation</strong><br>Differential centrifugation operates by separating components based on differences in size and density, using varying speeds of centrifugation to achieve this. Its resolving power ranges from low to medium. A key advantage of this technique is its convenience for processing multiple samples simultaneously, making it effective for purifying crude samples. Additionally, it preserves cell viability and maintains the natural distribution of hematopoietic cell populations.</p><p><strong>Rate-zonal Gradient Centrifugation</strong><br>This technique separates components based on their sedimentation rate within a medium that contains a density gradient. It offers medium resolving power and is particularly effective for separating multiple components in complex mixtures with high precision. It is also considered a cost-effective and widely used technique in molecular biology and biochemistry.</p><p><strong>Isopycnic Centrifugation (Equilibrium Centrifugation)</strong><br>Isopycnic centrifugation is an advanced protein purification method that relies on the principle of separating particles according to their intrinsic buoyant density, irrespective of their size or morphology. During the process, proteins migrate through a density gradient until they equilibrate at a position where their density matches that of the surrounding medium, resulting in precise separation without further sedimentation.</p></div></div></div><div><div><div><div><h4><strong>Chromatographic Approaches</strong></h4><p>Chromatography is a common method of protein purification and is based on the separation of molecules in a mixture as they move through a stationary phase and a mobile phase. Outlined below are the various types of chromatography employed in protein purification.</p><h5><strong>Ion Exchange Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-ion-exchange">Ion exchange chromatography</a> relies on the interaction between a charged stationary phase and oppositely charged analytes, with cation exchange chromatography attracting positively charged molecules to a negatively charged stationary phase. Successful application of this technique requires careful selection of the appropriate ion exchange column, buffer pH, and salt concentration. This approach is often used in the biopharmaceutical industries as mAb polishing steps, viral clearance and charge variant analyses as part of the product quality control.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/">Phenomenex</a> offers a range of protein purification columns. Their ion exchange chromatography solutions include:&nbsp;</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1526"><strong>Luna SCX </strong></a>for strong selectivity of positively charged compounds, such as peptides</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1540"><strong>Biozen WCX</strong></a> for efficient separation of proteins such as monoclonal antibodies charged variants</li><li><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/part/00g-3151-e0">PhenoSphere SAX</a>, a strong anion-exchanger with fully porous 80Å particles, particularly useful for small molecules such as nucleotides</li></ul><h5><strong>Size Exclusion Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-sec">Size exclusion chromatography (SEC)</a> separates molecules based on their size, with larger analytes eluting first due to their exclusion from the pores in the column packing material, while smaller molecules are able to enter the pores, facing a longer travelling path, and hence, eluting later. This method can be categorized into aqueous SEC (gel filtration chromatography, GFC) for analyzing biomolecules such as proteins and antibodies. This type of chromatography is widely used as an analytical tool for quality control in the biopharmaceutical industry and can also be an approach of choice for polishing steps.</p><p>Phenomenex offers a range of <strong>Biozen columns for SEC</strong> separations. In the case of mAbs, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1534"><strong>Biozen dSEC-2</strong></a> and<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1537"><strong> Biozen dSEC-7 </strong></a>columns are the top choices for monoclonal antibody (mAb) analysis, delivering high-resolution separation of monomers, aggregates, and fragments formed during mAb manufacturing, processing, or storage. The dSEC-7 column, featuring a larger pore size and optimized particle design, extends the dynamic range to accommodate larger biomolecules and complex biotherapeutics.</p><p>For more general applications, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1533"><strong>Biozen SEC-2</strong></a><strong> </strong>and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1532"><strong>Biozen SEC-3</strong></a> phases cover different MW ranges for high-efficiency separation of biomolecules (e.g., proteins and antibodies). Additionally, the BioSep and Yarra lines become top choices when looking for preparative scale columns.</p><h5><strong>Reversed-Phase Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-reversed-phase">Reversed-phase chromatography</a>, the most common mode in high-performance liquid chromatography/ ultra-high-performance liquid chromatography (HPLC/UHPLC), separates compounds based on hydrophobic and van der Waals interactions using alkyl (C18, C8, C4) stationary phases or other hydrophobic polymers. For large biomolecules such as proteins and peptides, <a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/resources/blog/wider-pore-biozen-column">wide-pore</a> (typically 300 Å) C4, C8 and C18 columns are ideal, as the larger pore size allows better accessibility of the protein molecules to the stationary phase surface, improving mass transfer and peak shape during separation.</p><p>The Biozen line from Phenomenex offers a wide range of HPLC/UHPLC columns for the analysis of biomolecules.These include phases optimized for high-resolution analysis of intact proteins (Native-RP, Widepore C4, Intact XB-C8) and peptides (Peptide PS-C18, Peptide XB-C18 and Peptide Polar-C18). Kinetex could also be an option when looking for more selectivities for the analysis of peptides and small proteins. Additionally, when aiming to preparative scale processes, several of these media are also available in Phenomenex Axia formats to easily up-scale your separations.</p><h5><strong>Hydroxyapatite Chromatography</strong></h5><p>Hydroxyapatite chromatography (HAC) is a sophisticated mixed-mode chromatographic technique that exploits the unique properties of hydroxyapatite (Ca10(PO4)6(OH)2), utilizing both cation-exchange interactions via its phosphate groups and metal affinity through its calcium sites to achieve highly selective protein separations.</p><p>Renowned for its efficacy in resolving complex biomolecular separations, HAC excels in tasks like aggregate removal from monoclonal antibodies, surpassing the capabilities of traditional single-mode chromatographic methods such as ion-exchange or hydrophobic interaction chromatography.</p><h5><strong>Hydrophobic Interaction Chromatography</strong></h5><p>Hydrophobic interaction chromatography (HIC) is a method of protein purification that separates molecules based on their hydrophobicity, using high-salt buffers to promote protein-ligand interactions while maintaining the protein's biological activity. The process involves gradually reducing the salt concentration to elute proteins in order to increase hydrophobicity, making it effective for purifying target molecules and removing impurities or aggregates, making it a valuable approach for intermediate and polishing steps during purification processes.</p><h5><strong>Affinity Chromatography</strong></h5><p>Affinity chromatography is a powerful and highly selective technique used to purify biomolecules based on specific, reversible interactions between a target molecule and an immobilized ligand. In many cases, recombinant proteins are engineered with affinity tags—such as His-tags or GST-tags—that facilitate binding to complementary ligands on the chromatography matrix.</p><p>This method offers the advantage of achieving several thousand-fold purifications in a single step while preserving the biological activity of the protein. It is widely employed for purifying enzymes, antibodies, and antigens, using a variety of ligands including specific antibodies, enzymes, and multifunctional compounds like concanavalin A and triazine dyes.</p></div></div></div></div>

Exploring Protein Purification Methods: Essential Techniques for Accurate Results

<h3><span><strong>A Practical Guide to Getting the Most from Syringe Filters: Tips, Tricks, and Common Pitfalls</strong></span></h3><p><span><strong>Syringe filters play a crucial role in chromatography and many other laboratory applications by removing particulate matter before analysis. Proper sample filtration helps protect analytical instruments, extends column lifetime, and improves data quality. However, selecting an unsuitable filter—or using one incorrectly—can introduce contamination, reduce filtration efficiency, or even compromise analytical results. The following recommendations will help you avoid common mistakes and ensure reliable filtration every time.</strong></span></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_3_150e8c1c2b.webp" alt="KNAUER: Avoiding Common Syringe Filter Mistakes" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_3_150e8c1c2b.webp 133w," sizes="100vw" width="1276" height="1496"></p><h4><span><strong>1. Improper Filter Handling</strong></span></h4><p><span>Using excessive force during filtration or attempting to reuse disposable syringe filters can damage the membrane and increase the risk of sample contamination.</span></p><ul><li><span><strong>Solution:</strong> Apply slow, even pressure throughout the filtration process and always dispose of single-use filters after one use. If the flow rate decreases noticeably, replace the filter instead of applying additional force.</span></li></ul><h4><span><strong>2. Selecting an Inappropriate Pore Size</strong></span></h4><p><span>Using the wrong pore size may either fail to remove unwanted particles or cause the membrane to clog prematurely, reducing filtration efficiency.</span></p><ul><li><span><strong>Solution:</strong> A 0.45 µm membrane is generally suitable for routine particulate removal, while a 0.22 µm membrane is recommended for finer filtration and bacterial removal. Samples with higher viscosity may require a pre-filter to prevent rapid clogging. It is also important to consider the intended analytical technique. For example, 0.22 µm filters are typically preferred for UHPLC and LC-MS applications, whereas 0.45 µm filters are often sufficient for conventional HPLC analyses.</span></li></ul><h4><span><strong>3. Choosing the Wrong Membrane Material</strong></span></h4><p><span>Different membrane materials exhibit different chemical resistance. Using an incompatible membrane may lead to degradation of the filter, sample contamination, or complete filtration failure.</span></p><ul><li><span><strong>Solution:</strong> Always verify solvent compatibility before filtration. PTFE membranes are an excellent choice for organic solvents, while PES and nylon membranes are better suited to aqueous samples. If compatibility is uncertain, perform a small-scale trial before filtering valuable samples.</span></li><li><span><strong>Pro Tip:</strong> For additional guidance, see our blog article <strong>"How to Choose the Right Membrane for your Syringe Filter"</strong>, which provides a detailed comparison of membrane materials and their recommended applications.</span></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_2_e47021fb11.jpg" alt="KNAUER Sepapure® Syringe Filters are available with multiple membrane materials, each identified by a dedicated color code for quick and reliable selection." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_2_e47021fb11.jpg 245w," sizes="100vw" width="1580" height="902"></p><h4><span><strong>4. Ignoring Filter Capacity</strong></span></h4><p><span>Using a filter with insufficient capacity can result in rapid membrane blockage, increasing filtration time and reducing laboratory productivity.</span></p><ul><li><span><strong>Solution:</strong> When filtering larger sample volumes, choose high-capacity syringe filters or introduce a pre-filtration step. Never force liquid through a clogged membrane, as doing so may damage the filter and negatively affect sample quality.</span></li></ul><h4><span><strong>5. Overlooking Sample Adsorption</strong></span></h4><p><span>Certain membrane materials may adsorb analytes of interest, leading to lower recoveries and potentially affecting quantitative results.</span></p><ul><li><span><strong>Solution:</strong> For protein samples or other adsorption-sensitive analytes, select membranes with low binding characteristics, such as nylon or glass fiber, whenever appropriate. Performing a small recovery test before routine analysis can help identify potential analyte losses.</span></li></ul><h4><span><strong>6. Failing to Optimize Filtration Performance</strong></span></h4><p><span>Slow filtration is more than just an inconvenience—it often indicates that the filtration conditions are not optimal.</span></p><ul><li><span><strong>Solution:</strong> If filtration becomes unusually slow, investigate possible causes such as membrane clogging, excessive sample viscosity, or an unnecessarily small pore size. Depending on the sample, dilution or sequential filtration using progressively finer filters may significantly improve performance.</span></li></ul><h4><span><strong>Final Thoughts</strong></span></h4><p><span>Selecting the appropriate syringe filter is a straightforward process, but overlooking small details can have a significant impact on analytical performance. Choosing the correct membrane material, pore size, and filtration strategy helps improve laboratory efficiency, protects chromatography systems and columns, and contributes to accurate, reproducible analytical results.</span></p><p><span>With the right syringe filter and proper filtration technique, you can minimize sample preparation problems and maximize confidence in every analysis.</span></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_4_983a15e289.jpg" alt="KNAUER: Sepapure® Syringe Filter Selection" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_4_983a15e289.jpg 245w," sizes="100vw" width="1160" height="627"></p><p><span><strong>Happy filtering!</strong></span></p>

Avoiding Common Syringe Filter Mistakes

News from LabRulezLCMS Library - Week 27, 2026

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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

Phenomenex is a global technology leader committed to developing novel analytical chemistry solutions that solve the separation and purification challenges of researchers in industrial, government and academic laboratories.

Phenomenex

Based in Berlin, KNAUER is a medium-sized, owner-managed company that has been serving the sciences since 1962. We develop and manufacture scientific instruments of superior quality for liquid chromatography, including: Analytical HPLC/UHPLC, Preparative HPLC, Fast protein liquid chromatography (FPLC), Multi-column chromatography/Simulated moving bed (SMB) chromatography. High pressure dosing, in-line detection systems, and osmometry are additional business areas.

KNAUER

Agilent Technologies

Technology Networks

Thermo Fisher Scientific

Wiley

Evosep Biosystems

Waters Corporation

<p><strong>Accessed via mobile, tablet or PC, this free to attend online symposium will highlight the latest advances in proteomics and metabolomics research and their applications in modern medicine.</strong></p>
<p>The insights offered by proteomic and metabolomic approaches are helping to shape our understanding of diseases, accelerate the development of novel clinical biomarkers and facilitate drug discovery. </p>
<p>If you want to learn how proteomics and metabolomics insights are fundamental in our pursuit towards personalized medicine, you don&#39;t want to miss this symposium.</p>
<h3><strong>Attend this online symposium to:</strong></h3>
<ul>
<li>Learn how proteomics and metabolomics are shaping the landscape of modern medicine</li>
<li>Explore some of the challenges that scientists face in this exciting yet complex research space</li>
<li>Discuss proteomics and metabolomics with research leaders and peers</li>
</ul>
<blockquote>
<p><strong>Keynote Presenter: Prof. Stephen Pennington, PhD (Professor of Proteomics, University College Dublin)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Prof. Matthias Mann, PhD (Director Dept. Proteomics and Signal Transduction, Max Planck Institute of Biochemistry)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Prof. Paola Picotti, PhD (Professor and Deputy Head of the institute for Molecular Systems Biology, ETZ Zürich)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Genevieve Van De Bittner, PhD (R&amp;D Researcher, Agilent Research Laboratories, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Gary H. Kruppa, PhD (Vice President, Proteomics, Bruker Daltonics, Billerica, MA)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Gerard Hopfgartner (Life Sciences Mass Spectrometry, Department of Inorganic and Analytical Chemistry, University of Geneva)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Prof. Helen Cooper, PhD (Professor of Mass Spectrometry, University of Birmingham)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Christopher Wiley, PhD (Scientist II, Jean Mayer USDA Human Nutrition Research Center on Aging)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Jeffrey Spraggins, PhD (Research Assistant Professor, Department of Biochemistry, Vanderbilt)</strong></p>
</blockquote>
<blockquote>
<p><strong>Presenter: Prof. Birgit Schilling, PhD (Associate Professor, Director of the Mass Spectrometry Technology Center, Buck Institute)</strong></p>
</blockquote>


Technology Networks: Advances in Proteomics & Metabolomics 2021

Advances in Proteomics & Metabolomics 2021

<p><strong>Proteomics analysis of human blood offers an attractive and challenging pipeline for discovery of biomarkers. Over the last few years the need for, large cohort, plasma analysis using proteomic techniques has become more and more prevalent for both discovery and targeted workflows.</strong></p>
<p><strong>High throughput MS-based proteomics is being coupled with Machine learning, in order to identify significant biomarkers. Targeted workflows are then used to detect and quantify previously identified biomarkers.</strong></p>
<h5><strong>Balancing depth, throughput and pragmatism in plasma proteomics</strong></h5>
<p>Recent advances in robustness and throughput of LC-MS/MS platforms allow unprecedented coverage of clinical cohorts for biomarker discovery in acute disease and epidemiology. However, high analysis costs have to be met with pragmatism and what is archivable in a clinical environment, also with view on global emergencies such as the COVID pandemic.</p>
<blockquote>
<p><strong>Presenter: Roman Fischer (ASSOCIATE PROFESSOR AND HEAD OF DISCOVERY PROTEOMICS FACILITY at University of Oxford)</strong></p>
</blockquote>
<h5><strong>High-throughput plasma proteomics enables robust biomarker discovery for liver disease</strong></h5>
<p>Mass spectrometry (MS)-based clinical proteomics has a great potential to revolutionize disease detection. Previously we have identified novel proteins associated with liver disease using plasma proteomics leveraged by the BoxCar acquisition method. In this presentation, we show that BoxCar/DIA on an Evosep One coupled to quadrupole-Orbitrap mass spectrometers enables the robust identification of circulating biomarker panels for liver disease, surpassing existing clinical tests in terms of both diagnostic and prognostic power. The biomarker panels are further validated in an independent cohort. These results lay the foundation for developing a generic MS-based blood test for liver disease.</p>
<blockquote>
<p><strong>Presenter: Lili Niu (Postdoc at University of Copenhagen, Novo Nordisk Foundation Center for Protein Research,Groups of Human Proteome Variation and Clinical Proteomics)</strong></p>
</blockquote>


EVOSEP: Plasma Proteomics with the Evosep One

Plasma Proteomics with the Evosep One

<p><strong>Lipidomics can be a challenging analytical pursuit. The rewards are obvious with lipids playing major roles in biological processes associated with disease, but by the very nature of their chemistry, they can pose major challenges in both chromatography, identification and quantification. In this webinar series we will discuss some of the latest analytical approaches which have been developed to address these hurdles.</strong></p>
<p>We will hear from researchers in lipidomics using mass spectrometry to quantify lipid expression and determine the spatial localization of lipids in tissue samples. We will introduce the concepts of cloud computing tools to help review quality control in large lipidomics studies and the use of DESI imaging for the study of liver disease.</p>
<h3><strong>Agenda</strong></h3>
<h4><strong>The Combined Use of C18 and HILIC Separations for Discovery Lipidomics</strong></h4>
<blockquote>
<p><strong>Presenter: Jace W. Jones, Ph.D. (Assistant Professor and Associate Director of the Mass Spectrometry Center, University of Maryland)</strong></p>
</blockquote>
<blockquote>
<p>Dr. Jones received his B.S. degree from Whitworth University. He obtained his Ph.D. from the Department of Chemistry at the University of Washington under the mentorship of Dr. František Tureček. Following his PhD, he held a post-doc position in the laboratory of Dr. David R. Goodlett (University of Washington). He then spent several years in industry investigating the role of environmental contaminants on land resources and human health. Following his transition back to academics, he progressed from research scientist to research faculty under the mentorship of Dr. Maureen A. Kane (University of Maryland). His research program seeks to understand the synergistic relationship between chemistry and biology, and how this profound interaction influences human health. Specifically, his lab is focused on developing mass spectrometry-based analytical platforms to probe the structure/function dynamics of lipids. The knowledge gained by comprehensively characterizing lipid structure and anchoring structure to quantitative abundance provides a unique opportunity to investigate how disruption in lipid metabolism impacts human health. He has been awarded the ASMS Research Award (2020) and the New Investigator Award (2020) from the American Association of Colleges of Pharmacy (AACP).</p>
</blockquote>
<h4><strong>Spatial metabolic imaging of non-alcoholic fatty liver disease using desorption electrospray ionization mass spectrometry</strong></h4>
<blockquote>
<p><strong>Presenter: Patcharamon Seubnooch (PhD student, Department for BioMedical Research, Hepatology, University of Bern)</strong></p>
</blockquote>
<blockquote>
<p>Patcharamon is a a PhD student from Hepatology, Department for BioMedical Research, University of Bern, Switzerland. Her research interests are in the field of spatial metabolomics and lipidomics analysis. Currently, her PhD project is focusing on spatial metabolic imaging of non-alcoholic fatty liver disease using Desorption electrospray ionization mass spectrometry (DESI-MS).She has optimized the spatial lipidomics for biological samples in pre-clinical and clinical sample.</p>
</blockquote>
<h4><strong>Redefining clarity in mass spectrometry imaging with the SELECT SERIES MRT</strong></h4>
<blockquote>
<p><strong>Presenter: Emmanuelle Claude (Consulting Scientist, Waters Corporation)</strong></p>
</blockquote>
<blockquote>
<p>Miss Emmanuelle Claude (Master in Fine Chemistry and Business and M.Phil in spectroscopy analysis in organic chemistry and biology) has started at Waters Corporation in October 2000 as an Application Chemist in the Proteomics and Genomics Marketing group, developing automated Peptide Mass Fingerprint (PMF) MS methods using a MALDI-TOF mass spectrometer.</p>
</blockquote>
<blockquote>
<p>Over the years she developed a number of methods in the proteomics analytical space using MALDI TOF and naturally moved in starting the development of Mass Spectrometry Imaging (MSI) at Waters corporation over 12 years ago.</p>
</blockquote>
<blockquote>
<p>She has been involved with hardware and software R&amp;D to ensure that the solutions are fit-for-purpose for the MSI community and beyond. She has worked extensively with the main MSI leaders in Europe and the US such as Prof Heeren in the Netherlands, Prof Clench, Prof Takats and Bunch in the UK and Prof Caprioli in the US. She has been a Principal Scientist since 2014 and became a Consulting scientist in 2021. She is managing the MS imaging application team at Waters where data are generated for collaborations and marketing activities (i.e. application literature, customer presentation, papers, posters...), hardware and software requirements are defined for the R&amp;D teams. The team evaluates and develops new applications &amp; methods for imaging by both MALDI and DESI mass spectrometry, support sales staff with customers visit and demonstration laboratory.</p>
</blockquote>
<h3><strong>Key Learning Objectives</strong></h3>
<ul>
<li>How the application of technology and informatics are used to overcome the challenges in lipidomics</li>
<li>The importance of quality control and standardization in lipidomics research</li>
<li>How desorption electrospray ionisation (DESI) can be used to map the spatial distribution of lipids in tissue samples</li>
<li>The roll of high-resolution mass spectrometry in tissue imaging</li>
</ul>
<h3><strong>Who should attend</strong></h3>
<ul>
<li>Researchers studying lipids in biomedical research applications</li>
<li>Those interested in maximizing liquid chromatography methods for lipidomics</li>
<li>Anyone interested in learning about state-of-the-art imaging techniques using mass spectrometry</li>
<li>Researchers looking to start lipidomics efforts for the first time, moving from other discovery omics areas or just wanting to expand their lipidomics research</li>
</ul>
<p>This is part 2 of our Get Prepared for Lipidomics webinar series. To access part 1, please <a href="https://lcms.cz/webinar/996"><strong>click this link</strong></a>. </p>
<blockquote>
<p><strong>Presenter: David Heywood (Senior Manager Biomedical Research Marketing, Waters Corporation)</strong></p>
</blockquote>
<blockquote>
<p>David has 28years of experience in the mass spectrometry business andhasperformed many rolesboth in the UK and the Americas,including technicalhardware and software support, sales,marketingandbusiness development.Now based at Waters’ Mass Spectrometry Head Quarters in Wilmslow UK,Davidhas helped commercializemany of Waters successful high-resolution mass spectrometrybasedsolutions for discovery omicsandis now responsible for global marketing strategies of these platforms.</p>
</blockquote>


Waters Corporation: Get Prepared for Lipidomics 2.0 with Waters 2nd Edition

Get Prepared for Lipidomics 2.0 with Waters 2nd Edition

<p><strong>The ultimate goal of targeted metabolomics and lipidomics is to report absolute metabolite and lipid concentrations. The Agilent Metabolomics dMRM Database and Method is a supported solution for 219 central carbon metabolites in negative ion mode.  It is a fully tested rugged method that provides incredibly stable retention times across large numbers of samples with excellent inter-day and extended (over 4000 biological samples) retention-time reproducibility.</strong></p>
<p>IDMS gets rid of Ionization suppression effects as well as any bias from sample preparation and instrument conditions. The only downside is the cost and availability of isotopically labeled internal standards, especially in an assay with 219 metabolites. We have circumvented the cost of purchasing individual internal standards by using 13C incorporated yeast from Cambridge Isotope Labs.  These cells are grown in 13C enriched media and the resulting metabolites in the extract have &gt;99% isotopic enrichment.  Using this technique, we show linearity for fragile metabolites over six orders of magnitude ranging in most cases from attomole to nanomoles concentrations on column.</p>
<p>We will also present the method and results for targeted lipidomics with the use of deuterated internal standards that covers a wide range of lipid classes.</p>
<p><em>For Research Use Only. Not for use in diagnostic procedures.</em></p>
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<p><strong>Presenter: Sheher Banu Mohsin, PhD (Senior Applications Scientist, Agilent Technologies, Inc.)</strong></p>
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<p>Sheher Mohsin is a senior applications scientist at Agilent Technologies. She received her Ph. D in physical chemistry from the University of Illinois and an MBA from Rockhurst University. She started her career at the US Environmental Protection Agency working on dioxin analysis with high resolution mass spectrometers. She later joined Bayer and worked in the special analysis lab using mass spectrometry to solve problems in synthesis, impurity determination and submission of final product impurity profile to regulatory agencies. Sheher’s current focus is on lipidomics using GC, LC and SFC separations and mass spectrometry. Sheher collaborates with academic and government researchers working on complex problems to come up with innovative, simplified workflows using the latest tools in separation and mass spectrometry.</p>
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Agilent Technologies: Absolute and Relative Quantitation for Targeted Metabolomics and Lipidomics

Absolute and Relative Quantitation for Targeted Metabolomics and Lipidomics

<p><strong>Metabolomic studies cover a broad variety of analyte chemistries and require various analysis needs to tease out the impactful information.</strong></p>
<p>This talk will focus on the latest tools for a metabolomics lab to answer your research questions with ease. These include sample preparation methods and automation, LC/MS approaches, targeted and untargeted data analysis techniques, and chemometrics. Emphasis will be given to hardware workflow solutions that can easily be transferred to a new lab and that utilize intuitive software tools.</p>
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<p><strong>Presenter: Karen Yannell (LC/MS Application Engineer, Agilent Technologies, Inc.)</strong></p>
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<p>Karen E. Yannell is a LC/MS Application Engineer at Agilent Technologies. She is an expert in small molecule high throughput analysis by triple quadrupole (TQ) and quadrupole time-of-flight (QTOF) mass spectrometry for applied markets. Her recent work has focused on developing routine Q-TOF workflows for both expert and non-expert users alike. Previously, Karen worked on forensic, metabolomics, and biomarker discovery applications with ambient ionization sources. She received her PhD in Analytical Chemistry from Purdue University where studied under the advisement of Prof. R. Graham Cooks. Outside of the laboratory, she enjoys cooking unique dishes and hiking along the beach with her dog.</p>
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Agilent Technologies: LC/MS and Software Solutions for Your Metabolomic Studies

LC/MS and Software Solutions for Your Metabolomic Studies

<p><strong>Even with a lipid content of over 10% in the human body, lipids were not in the central scientific focus during the last decade. However, more and more evidence is provided that non-genetically determined biomolecules such as metabolites and lipids are the key to biomolecular regulation.</strong></p>
<p>Today it is obvious that lipids are not only important for energy homeostasis and as an environmental-cellular barrier, but also represent a central part of our signal transduction machinery. Disruptions of the sensitive lipid metabolism are highly correlated with different types of diseases including thrombocytopenia, metabolic syndrome, diabetes, obesity and hyperlipidemia. This is especially true for the latter ones, which are also reaching pandemic levels, causing a larger annual health burden than infectious diseases.</p>
<p>Therefore, lipid metabolism is again becoming an emerging scientific field and is a central part of pharmacological research today (statins, cyclooxygenase inhibitors). Therefore, the mission of the Lipidomics group in Vienna is to understand lipids in context with their proteins (enzymes) and building blocks (metabolites) in a true systems biology way.</p>
<h5><strong>Who should attend:</strong></h5>
<p>Anybody with a basic analytical knowledge.</p>
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<p><strong>Presenter: Prof. Dr. rer. nat. Robert Ahrends (Department of Analytical Chemistry, University of Vienna (Austria))</strong></p>
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<p>Robert Ahrends is Professor of Analytical Chemistry at the University of Vienna (Austria), Robert founding member of the International Lipidomics Society and Member of the Lipid Standard Initiative. He obtained his Dr. rer. nat. at the Humboldt University zu Berlin and spend his postdoctoral time at Stanford Medical School in the Department of Chemical&amp; Systems Biology. His lab’s research focus on lipid research by developing omics tools to analyze lipids and their metabolizing enzymes in a cardiovascular context.</p>
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Wiley Analytical Science: Lipidomics from Structure to Function

Lipidomics from Structure to Function

<p><strong>Quantitative bottom-up shotgun lipidomics of molecular lipid species is based on the direct infusion of lipid extracts with standards into a high-resolution Orbitrap tandem mass spectrometer. A single shotgun analysis generates hundreds of spectra, each comprising thousands of peaks, but only a small percentage of these are attributable to lipids. Noise reduction is therefore required for an appropriate data processing.</strong></p>
<p>Furthermore, is it necessary for the quantification of the molecular species to account for structure-dependent fragmentation differences. To address both items, the group at Shevchenko Lab / MPI-CBG Dresden developed two software applications: PeakStrainer for peak intensity-independent noise filtering of spectra and LipidXte for accurate quantification of molecular lipid species using a fragment intensity model.</p>
<h5><strong>Who should attend:</strong></h5>
<p>High resolution Orbitrap FTMS, bottom-up lipidomics, molecular lipid species quantification.</p>
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<p><strong>Presenter: Dr. Kai Schuhmann (Postdoctoral Researcher, Shevchenko laboratory at MPI-CBG Dresden)</strong></p>
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<p>In the past 12 years of PhD and PostDoc research, Kai Schuhmann built up a strong lipidomics expertise in the group of Andrej Shevchenko at the MPI-CBG. His achievements include several method developments from high-throughput clinical lipidomics, over ultra-high resolution Orbitrap-FTMS with &gt;1M resolution for lipid flux analysis and a fragment intensity model for compensating analyte-specific differences and the accurate quantification of molecular lipid species from MSMS.</p>
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Wiley Analytical Science: Quantitative Bottom-Up Shotgun Lipidomics Using High-Resolution Orbitrap FTMS

Quantitative Bottom-Up Shotgun Lipidomics Using High-Resolution Orbitrap FTMS

<p><strong>Proteins exist in many similar but unique molecular entities known as proteoforms. In practice, important protein targets are often not amongst the most abundant proteoform. Traditional digest based analyses further complicate this problem because peptide level evidence is incomplete, resulting in inferred protein group identities. What can we do when peptides do not answer our question?</strong></p>
<p>There will be a special focus on analyzing top-down proteomics data with Thermo Scientific ProSightPD 4.0 software in Proteome Discoverer software.</p>
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<p><strong>Presenter: Mick Greer, PhD (Software Product Manager, Chromatography and Mass Spectrometry, Thermo Fisher Scientific)</strong></p>
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<p>Dr. Mick Greer earned his BS in Chemistry Drexel University ’12 and his PhD in Analytical Chemistry UT Austin ’18. Mick’s PhD project involved developing proteomics methods utilizing a novel photo-dissociation method (UVPD). The last three years of my PhD I spent working on Top-Down method development using UVPD and other activation methods. In his current role Mick is the product manager for Thermo Scientific Top Down proteomics ProSight PD software.</p>
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<p><strong>Presenter: Rosa Viner, PhD (Sr. Manager, Proteomics Vertical Marketing, Chromatography and Mass Spectrometry, Thermo Fisher Scientific)</strong></p>
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<p>Dr. Rosa Viner is currently the Senior Manager, Vertical Marketing Omics responsible for structural proteomics at Thermo Fisher Scientific. She joined Thermo Fisher Scientific in 2004. She is involved in all areas of proteomics research with specific focus on relative quantification, PTM characterization and integrated structural biology workflows.</p>
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<p><strong>Presenter: Mike Baynham, PhD (Sr. Product Manager, Chromatography and Mass Spectrometry, Thermo Fisher Scientific)</strong></p>
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<p>Dr. Mike Baynham is a Senior Product Manager and the Manager of the Product Management Team responsible for the Thermo Scientific LC column portfolio. Mike has worked for Thermo Fisher Scientific in Runcorn, UK since 2015. Mike has a doctorate in capillary separation techniques coupled to mass spectrometry from the University of Nottingham and has more than 25 years’ experience of working with liquid chromatography.</p>
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Thermo Scientific: Virtual Software Workshops

Increasing proteoform level insight with quantitative Top-Down proteomics using Proteome Discoverer 2.5 software

<p><strong>The new tims-TOF pro-mass spectrometer offers improved capabilities for the targeted acquisition. The prm-PASEF method uses the multiplexing capability provided by the trapped ion mobility separation, allowing more than 200 peptides to be monitored over a 30 min liquid chromatography separation. Compared to conventional parallel reaction monitoring (PRM), precursor ions are accumulated in the TIMS cells and separated according to their shape and charge before eluting into the Q-TOF part of the mass spectrometer.</strong></p>
<p>Using these improved mass spectrometric capabilities, we detected and quantified 216 isotope-labeled synthetic peptides (AQUA peptides) spiked in HeLa human cell extract with limits of quantification of 17.2 amol for some peptides. </p>
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<p><strong>Presenter: Prof. Dr. Gunnar Dittmar (Group leader proteomics of cellular signalling, Luxembourg Institute of Health, Department of Infection and Immunity)</strong></p>
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<p>Prof Dr Gunnar Dittmar is the Head of proteomics of cellular signalling group at the LIH’s Quantitative Biology Unit. He has a strong background in proteomics, bioinformatics, chemistry and biochemistry. He completed a PhD in cell biology at the DKFZ (German Cancer Research Centre), in Heidelberg in 1997, followed by six years at the Harvard Medical School in Boston (USA), first as a postdoctoral fellow and later as an instructor of Cell Biology.Back to Germany, he was recruited as a group leader at the Max Delbru¨ck Center for Molecular Medicine (MDC), in Berlin in 2003. In 2007, he established the Mass Spectrometry Core Unit at MDC, and in 2014 he additionally built up the Proteomics Unit of the Berlin Institute of Health (BIH), a translational research centre resulting from the joint forces of MDC and the Charite´ – medical school of the Freie and Humboldt University, Berlin. During these years, he further intensified his knowledge in proteomics and mass spectrometry techniques, oriented towards a clinical perspective. Since 2011 he is a visiting professor at the Technion University in Haifa, Israel.In 2016 he was recruited to the Luxembourg institute of health (LIH) where he created the new proteomics research group, a bioinformatics group and built the new multi-centre LuxGen NGS sequencing platform (a joined effort of the LIH and LNS – Laboratoire National de Sante´). Starting in 2018 he worked on setting up the new quantitative biology unit, which was officially inaugurated in 2019. The unit consists of ten different technology-oriented groups and platforms, spanning from bioinformatics to in vivo imaging. Since 2019 he has been appointed as an affiliated professor for proteomics at the University of Luxembourg.</p>
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<p><strong>Moderator: Dr. Martin Graf-Utzmann (Wiley Analytical Science, Lab Automation &amp; Equipment)</strong></p>
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<p>Dr. MartinGraf-Utzmann studied Chemistry at the FAU Erlangen-Nuremberg, worked on his PhD. Thesis at the Max-Planck-Institute for Coal Research in Mülheim an der Ruhr. Since 2008 he works for Wiley, starting in the books editorial team and since2013 in the B2B group.</p>
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Wiley Analytical Science: Highly Multiplexed Targeted Proteomics Acquisition on a TIMS-QTOF

Highly Multiplexed Targeted Proteomics Acquisition on a TIMS-QTOF

<p><strong>Lipidomics can be a challenging analytical pursuit. The rewards are obvious with lipids playing major roles in biological processes associated with disease, but by the very nature of their chemistry, they can pose major challenges in both chromatography, identification and quantification.</strong></p>
<p>We will introduce a new class of UPLC designed to minimize losses and improve detection of important lipid species; the latest scalable ion mobility high-resolution mass spectrometer capable of teasing out differences in isomeric lipid structure combined with a comprehensive discovery lipidomics method ready for LC-IMS-MS and finally the latest developments in mass spectrometry imaging of lipids using desorption electrospray ionisation.  </p>
<h3><strong>Key Learning Objectives</strong></h3>
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<li><p>How to overcome the challenges of using liquid chromatography for the separation of lipids </p>
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<li><p>How ion mobility can benefit complex lipid sample analysis </p>
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<li><p>The benefits of combing liquid chromatography and ion mobility into one cohesive analytical lipidomics method  </p>
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<li><p>How desorption electrospray ionisation (DESI) can be used to map the spatial distribution of lipids in tissue samples</p>
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<h3><strong>Who should attend</strong></h3>
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<li><p>Researchers studying lipids in biomedical research applications </p>
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<li><p>Those interested in maximizing liquid chromatography methods for lipidomics </p>
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<li><p>Anyone interested in learning about state-of-the-art ion mobility mass spectrometry and its application to discovery metabolomics and lipidomics </p>
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<li><p>Researchers looking to start lipidomics efforts for the first time, moving from other discovery omics areas or just wanting to expand their lipidomics research </p>
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<li><p>Anyone interested in the latest developments in imaging mass spectrometry with DESI techniques</p>
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<p><strong>Presenter: David Heywood (Senior Manager Omics Business Development, Waters Corporation)</strong></p>
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<p>David has28years of experience in the mass spectrometry business andhasperformed many rolesboth in the UK and the Americas,including technicalhardware and software support, sales,marketingandbusiness development.Now based at Waters’ Mass Spectrometry Head Quarters in Wilmslow UK,Davidhas helped commercializemany of Waters successful high-resolution mass spectrometrybasedsolutions for discovery omicsandis now responsible for global marketing strategies of these platforms.</p>
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<p><strong>Presenter: Dr. Robert Plumb (Director Metabolic Phenotyping, Health Sciences, Waters Corporation)</strong></p>
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<p>Dr Robert Plumb is the Director of Omics and Small Molecule Pharma in the Waters Scientific Operations Division, based in Milford, Massachusetts. Dr Plumb has published over 100 paperson the subject of HPLC/MSand NMR for bioanalysis, metabolomics and metabolite identification. He is a recognized expert in the use of liquid chromatography with mass spectrometry, capillary scale LC, purifications scale LC andmetabonomics, giving many invited papers at international meetings around the world. After obtaining anhonorsdegree in Chemistry from the University of Hertfordshire in 1992, he started work in at Glaxo Research and Development Drug Metabolism Department. During his time at Glaxo and laterGlaxoWellcomehe continued his research in liquid chromatography combined with NMR and mass spectrometry for metabolite identification and bioanalysis obtaining his PhD in 1999. Dr Plumb continued his work forGlaxoWellcomewith the responsibility of metabolite identification using HPLC/MS/NMR and new analytical technology development. In 2001 he moved to Waters Corporation in Milford, MA, USA where he was responsible for the Life Science Chromatography group and latterly LC/MS applications in the Pharmaceutical Market Development Group before becoming the Director of Metabolic Phenotyping in 2013 and the Director of Omics and Small molecule Pharma in the Scientific Operations Division in 2017. He has been awarded several visiting Professorships including visiting Professor in at Kings College London, visiting Professor at Imperial College in the Dept Surgery and Cancer, Visit Professor at MurdochUniversityand a Fellow of the Royal Society of Chemistry. In 2014 he was awarded Highly Cited Researcher by Thompson Reuters.</p>
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<p><strong>Presenter: Dr. Nyasha Munjoma (Senior Scientist, Waters Corporation)</strong></p>
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<p>Dr Nyasha Clarence Munjoma is a Senior Scientist in the Biomedical and OMICS research group at Waters Corporation, Wilmslow UK. He has worked in Systems Biology for over 10 years with an emphasis on Lipidomics. After completing his PhD in Systems Biology (University of Cambridge) he joined Waters helping to run and provide training to medics and students in Metabolomics at the Imperial College International Phenome Training Centre in London (2016). He has since moved to Wilmslow where he has been involved in the development of various Lipidomic platforms and applications both for targeted and untargeted analysis.</p>
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<p>Before working for Waters and moving into the field of Systems Biology, he worked in the pharmaceutical industry for Pfizer (Sandwich, UK) and the Medical and Healthcare Regulatory Agency (MHRA) (Teddington, UK) as an analytical chemist. He graduated from Birkbeck College (University of London) in 2004 with an MSc in Analytical Chemistry and holds a BSc in Chemistry and Geology from Rhodes University in South Africa.</p>
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<p><strong>Presenter: Dr. Giorgis Isaac (Principal Scientist, Waters Corporation)</strong></p>
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<p>Dr. Giorgis Isaac is a Consulting Principal Scientist in the Biomedical and OMICS research group at Waters Corporation, Milford, MA, USA. He has over 10 years of experience in metabolomics and lipidomics LC-MS method development and various data handling informatics tools. He graduated from Asmara University, Eritrea with a B.Sc. in Chemistry (1997) and Ph.D. in Analytical Chemistry at Uppsala University, Sweden (2005). He conducted postdoctoral research in biological mass spectrometry at Kansas Lipidomics Research Centre, Kansas, USA. Prior to joining Waters Corporations in 2010 he was a senior postdoctoral research scientist at the Pacific Northwest National Laboratory (PNNL) Richland, WA, USA. He has authored over 42 publications (PubMed Publication Link), three book chapters and holds 6 patents. Dr. Isaac current research is focusing on novel analytical and informatics method developments to solve biological challenges.</p>
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<p><strong>Presenter: Emmanuelle Claude (Principal Scientist, Waters Corporation)</strong></p>
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<p>Miss Emmanuelle Claude (Master in Fine Chemistry and Business and M.Phil in spectroscopy analysis in organic chemistry and biology) has started at Waters Corporation in October 2000 as an Application Chemist in the Proteomics and Genomics Marketing group, developing automated Peptide Mass Fingerprint (PMF) MS methods using a MALDI-TOF mass spectrometer.</p>
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<p>Over the years she developed a number of methods in the proteomics analytical space using MALDI TOF and naturally moved in starting the development of Mass Spectrometry Imaging (MSI) at Waters corporation over 12 years ago.</p>
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<p>She has been involved with hardware and software R&amp;D to ensure that the solutions are fit-for-purpose for the MSI community and beyond. She has worked extensively with the main MSI leaders in Europe and the US such as Prof Heeren in the Netherlands, Prof Clench, Prof Takats and Bunch in the UK and Prof Caprioli in the US. She has been a Principal Scientist since 2014 and became a Consulting scientist in 2021. She is managing the MS imaging application team at Waters where data are generated for collaborations and marketing activities (i.e. application literature, customer presentation, papers, posters...), hardware and software requirements are defined for the R&amp;D teams. The team evaluates and develops new applications &amp; methods for imaging by both MALDI and DESI mass spectrometry, support sales staff with customers visit and demonstration laboratory.</p>
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LCMS webinars focusing on OMICS - page 27