<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.

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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.

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Thermo Fisher Scientific

<p><strong>Nitrosamine (genotoxic) impurities have been found in some angiotensin II receptor blocker (ARB) medicines, such as valsartan, and more recently in histamine-2 receptor blocker medicines, such as ranitidine, drawing close scrutiny from FDA, the European Medicines Agency (EMA) and other regulatory bodies leading to product recalls.</strong></p>
<p>Gas chromatography–mass spectrometry (GC-MS) has typically been the detection technique of choice; however, not all nitrosamines can be analyzed this way. As the number of known nitrosamines requiring trace level quantitation increases, the greater the need for robust, sensitive, and high-throughput assays to provide a cost-sensitive approach of a single analysis capable of accurately measuring all compounds. The use of liquid chromatography with high-resolution MS (LC-HRMS) allows low level detection and high confidence of a wider range of nitrosamine impurities.</p>
<h3><strong>Session breakdown:</strong></h3>
<h5>11:00 CEST, 10 minutes + Q &amp; A</h5>
<p><strong>Introduction to impurity analysis challenges and regulatory requirements in Europe</strong></p>
<p><em>Presenter: Jon Bardsley,Pharmaceutical Marketing Manager , Thermo Fisher Scientific</em></p>
<h5>11:20 CEST,  20 minutes + Q &amp; A</h5>
<p><strong>Chromatography and Mass Spectrometry software for GMP impurity testing</strong></p>
<p><em>Presenter: Darren Barrington-Light, Software Product Marketing Manager, Thermo Fisher Scientific</em></p>
<p>This session will give an overview of the current landscape of impurity testing in general and with a focus on nitrosamines and the European regulations.   We will then cover our software, Chromeleon for Mass Spectrometry with an overview and focus on data integrity and compliance. You will have a chance to ask questions to our specialists on these topics.</p>
<h3><strong>Key Learning Objectives:</strong></h3>
<ul>
<li>Why is the analysis of genotoxic impurities important?</li>
<li>Method development considerations for trace level impurities</li>
<li>What are the current regulations in Europe?</li>
<li>The role of compliance in data software with mass spectrometry</li>
</ul>
<blockquote>
<p><strong>Presenter: Darren Barrington-Light (Senior Product Marketing Manager, Enterprise Chromatography Data Systems, Thermo Fisher Scientific)</strong></p>
</blockquote>
<blockquote>
<p>Having worked in Chromatography throughout his careerin the fieldsof analytical chemistry, chromatography hardware and computer software,specifically Chromatography Data Systems,for over25years, Darren has a unique understanding of the requirements of organizations that rely on chromatography data to manage their day to day operations. As capabilities have advanced, Darren has worked with clients across multiple industries to show them how Thermo Scientific Chromeleon CDS software can help them to improve their day to day operations and drive fast, informed decisions.</p>
</blockquote>
<blockquote>
<p><strong>Presenter: Jon Bardsley (Pharma &amp; BioPharma Manager, Thermo Fisher Scientific)</strong></p>
</blockquote>
<blockquote>
<p>Jon Bardsley has over a decade of experience of small-molecule pharmaceutical DMPK and regulated bioanalytical studies within with large Pharmaceutical environments. His passion for development of robust and accurate analytical methods for high-throughput studies has seen him also gain experience in contract research organizations. Jon sits on the ReidBioAnalyticalcommittee of the Chromatography Society and is a subject matter expert in the bioanalysis community. Following a period as Senior Applications Specialist for Chromatography, Jon now holds the position of Vertical Marketing Specialist for Pharma &amp;BioPharmawithin Thermo Fisher Scientific, with a view to bringing relevant technologies together to help solve customer challenges.</p>
</blockquote>


Thermo Fisher Scientific: Virtual seminar session 1: Impurity analysis with a focus on nitrosamines

Virtual seminar session 1: Impurity analysis with a focus on nitrosamines

<p><strong>Proteomics and metabolomics have become widely adopted techniques, often multi-disciplinary, requiring the collaboration of biologists and medical doctors, of protein chemists, mass spectrometrists and bioinformaticians delivering the value of innovative applications and novel workflows as fresh knowledge on health, disease and biology. This field relies on the scientific community pushing the limits of mass spectrometry (MS) technology to gain understanding in various disease areas that can lead to effective diagnostics, treatments and vaccines. Over this day, we will highlight several of these cutting-edge developments and results in single cell analysis, spatial omics and clinical research deploying artificial intelligence for improved data acquisition and interpretation. Our specialists will also share their recommendations for achieving outmost performance with our instruments and software.</strong></p>
<h5><strong>9:00 BST (10:00 CEST - Prague) | Plenary 1 | Your fast-track to confident results in multi-omics: Thermo Scientific Orbitrap Exploris product family expanded</strong></h5>
<ul>
<li><strong>Speaker:</strong> Thomas Moehring, Sr Director Marketing LSMS, Thermo Fisher Scientific</li>
</ul>
<h5><strong>9:30 BST  (10:30 CEST - Prague) | Plenary 2 | Latest developments in native ambient mass spectrometry</strong></h5>
<ul>
<li><strong>Speaker:</strong> Helen Cooper, Professor of Mass Spectrometry, Deputy Head of School, EPSRC Established Career Fellow, Birmingham University</li>
</ul>
<blockquote>
<p><strong>Presenter: Thomas Moehring (Sr Director Marketing LSMS, Thermo Fisher Scientific)</strong></p>
</blockquote>
<blockquote>
<p>Dr. Thomas Moehring studied Chemistry and Environmental Science at the Carl von Ossietzky University Oldenburg, Germany, and completed his Ph.D. project at the Institute of Chemistry and Biology of Marine Environment (ICBM) Oldenburg, Germany.</p>
</blockquote>
<blockquote>
<p>He then became the Team Leader Peptidomics technology at BioVisioN (Hannover, Germany). In 2004 he joined Thermo Fisher Scientific as application/demo chemist, followed by various roles in Product Management.</p>
</blockquote>
<blockquote>
<p>Thomas is currently leading global Product Management efforts for Life Science Mass Spectrometry as Senior Director of Hardware Platform Management.</p>
</blockquote>
<blockquote>
<p><strong>Presenter: Helen Cooper (Professor of Mass Spectrometry, Deputy Head of School, EPSRC Established Career Fellow, Birmingham University)</strong></p>
</blockquote>
<blockquote>
<p>Professor Helen J. Cooper is an expert in the gas-phase ion chemistry of peptides and proteins. She is a world-leader in the field of electron capture dissociation mass spectrometry and is responsible for establishing the University of Birmingham as a centre of excellence in mass spectrometry research. Professor Cooper has published extensively in peer-reviewed journals and serves on a number of national and international committees including the Editorial Board for the Journal of the American Society for Mass Spectrometry and the British Mass Spectrometry Society.</p>
</blockquote>


Thermo Scientific: LC-MS User Meeting 2020 - Omics - Plenary Session

LC-MS User Meeting 2020 - Omics - Plenary Session

<p><strong>Proteomics and metabolomics have become widely adopted techniques, often multi-disciplinary, requiring the collaboration of biologists and medical doctors, of protein chemists, mass spectrometrists and bioinformaticians delivering the value of innovative applications and novel workflows as fresh knowledge on health, disease and biology. This field relies on the scientific community pushing the limits of mass spectrometry (MS) technology to gain understanding in various disease areas that can lead to effective diagnostics, treatments and vaccines. Over this day, we will highlight several of these cutting-edge developments and results in single cell analysis, spatial omics and clinical research deploying artificial intelligence for improved data acquisition and interpretation. Our specialists will also share their recommendations for achieving outmost performance with our instruments and software.</strong></p>
<h5><strong>11:00 BST (12:00 CEST - Prague) | Optimal workflows for spatial proteomics on the Orbitrap Eclipse Tribrid Mass Spectrometer</strong></h5>
<ul>
<li><strong>Speaker:</strong> Prof. Kathryn Lilley, Research Group Head, University of Cambridge, UK</li>
</ul>
<h5><strong>11:30 BST (12:30 CEST - Prague) | Pushing the Limits of Sensitivity: Micropillar Array-Based Chromatography Coupled to a Quadrupole Orbitrap Mass Spectrometer and FAIMS for Low-Input Proteomics</strong></h5>
<ul>
<li><strong>Speaker:</strong> Karl Mechtler, Head of Protein Chemistry Facility bei Research Institute of Molecular Pathology (IMP), Vienna Biocore Facilities, Austria</li>
</ul>
<h5><strong>12:00 BST (13:00 CEST - Prague) | Mass spectrometry-based draft of the Arabidopsis proteome (Mergner et al Nature 2020)</strong></h5>
<ul>
<li><strong>Speaker:</strong> Dr. Julia Mergner, Head of Proteomics, TU - Munich, Germany</li>
</ul>
<h5><strong>12:30 BST (13:30 CEST - Prague) | MS Based Approach for Low Amount Tissue Proteome Profile</strong></h5>
<ul>
<li><strong>Speaker:</strong> Alessandro Cuomo, Coordinator Mass Spectrometry Unit, IEO Research - Milano, Italy</li>
</ul>
<blockquote>
<p><strong>Presenter: Prof. Kathryn Lilley (Research Group Head, University of Cambridge, UK)</strong></p>
</blockquote>
<blockquote>
<p>Kathryn Lilley is a Professor in the Department of Biochemistry and a member of the Milner Therapeutics Institute.She is also Director of theCambridge Centre for Proteomics, and a Director of Studies at Jesus College.</p>
</blockquote>
<blockquote>
<p>Kathryn&#39;s research specialisesin the development of cutting edge proteomics technologies. Her research group is exploring waysto:</p>
</blockquote>
<ul>
<li>Defineresidents of organelles and protein complexes within cells</li>
<li>Usea combination of high throughput mass spectrometry and pattern recognition methods to define genuine residents of complexes and organelles</li>
<li>Monitor concerted changes in location upon cellular perturbation such as drug treatment, mutation etc.</li>
</ul>
<blockquote>
<p>These methods are being used to locate proteins involved in stem cell pluripotency maintenance both in terms of sub cellular location and involvement in multi protein complexes.</p>
</blockquote>
<blockquote>
<p>She is also interested in what controls the location of proteins in cells and is developing methods to determine the spatial location of translation (where proteins are synthesised).</p>
</blockquote>
<blockquote>
<p><strong>Presenter: Karl Mechtler (Head of Protein Chemistry Facility bei Research Institute of Molecular Pathology (IMP), Vienna Biocore Facilities, Austria)</strong></p>
</blockquote>
<blockquote>
<p>Main Research Areas</p>
</blockquote>
<ul>
<li>Major topics: Proteomics, Mass Spectrometry, Bioinformatics</li>
<li>Specialized in: Analysis of post-translational modifications, cross-linking mass spectrometry, single cell proteomics</li>
<li>Development of new mass spectrometry methods to increase sensitivity, accuracy and precision of protein identification and quantification.</li>
<li>Development of novel algorithms to increase the number of identified peptides, determine the localization of post-translational modifications and for label-free quantification.</li>
</ul>
<blockquote>
<p>Main Research Achievements</p>
</blockquote>
<ul>
<li>Establishment of the first Proteomics Core Facility in Austria in 2000, which is embedded in the Campus Vienna Biocenter and available to scientists from the Research Institute of Molecular Pathology (IMP), the Institute of Molecular Biotechnology (IMBA) and the Gregor Mendel Institute (GMI) today.</li>
<li>Development of methods for the analysis of post-translational modifications (phosphorylated arginine, glycoproteomics)</li>
<li>Development of different algorithms for qualitative and quantitative MS data analysis (available at http://ms.imp.ac.at), that are increasingly used by proteomics labs world-wide</li>
<li>(Co-)Author of more than 180 publications including contributions in Nature, Cell and Science.</li>
</ul>
<blockquote>
<p><strong>Presenter: Dr. Julia Mergner (Head of Proteomics, TU - Munich, Germany)</strong></p>
</blockquote>
<blockquote>
<p>I am a molecular biologist running a newly established proteomic competence center at the hospital campus of the TU Munich. I am applying label-free, tandem-mass-tag and targeted proteomic techniques to study global proteome expression, protein complex compositions and PTM site localizations. The aim of my research is to advance technologies for the detection and quantification of proteins and post-translational modifications using liquid-chromatography-based tandem mass spectrometry.</p>
</blockquote>
<blockquote>
<p>Career</p>
</blockquote>
<blockquote>
<p>Professional experience</p>
</blockquote>
<ul>
<li>2020 – present Head of Proteomics at the Bavarian Center for Biomolecular Mass Spectrometry at Klinikum rechts der Isar (BayBioMS@MRI), TU Munich, Germany</li>
<li>2015 - 2020 Post-Doc at the Chair of Proteomics and Bioanalytics, TU Munich, Germany</li>
<li>Research project “The Arabidopsis proteome”, Proteomic Z-project coordinator for SFB924 “Molecular mechanisms regulating yield and yield stability in plants”</li>
</ul>
<blockquote>
<p>Education</p>
</blockquote>
<ul>
<li>2010 - 2015 PhD in Molecular Biology at the Chair of Plant Systems Biology, TU Munich, Germany</li>
<li>Project “Characterization of DENEDDYLASE1 function in Arabidopsis”</li>
<li>2004 - 2010 Biology training at the Albert-Ludwigs-University Freiburg i. Breisgau, Germany</li>
<li>Diploma thesis “Ontogenetic changes in biomechanics and functional morphology of weeping plants”</li>
</ul>
<blockquote>
<p><strong>Presenter: Alessandro Cuomo (Coordinator Mass Spectrometry Unit, IEO Research - Milano, Italy)</strong></p>
</blockquote>
<blockquote>
<p>Alessandro is the Head of <a href="https://www.research.ieo.it/research-and-technology/technological-units/proteomics-unit/">Mass Spectrometry Unit (MSU) at European Institute of Oncology (IEO), Department of Experimental Oncology (DEO).</a></p>
</blockquote>
<blockquote>
<p>Education and Training</p>
</blockquote>
<ul>
<li>January 2015: Staff Scientist at European Institute of Oncology (IEO)</li>
<li>April-October 2012: Visiting Scientist:Max Plank Institute (MPI)-</li>
</ul>
<blockquote>
<p>M. Mann Lab</p>
</blockquote>
<ul>
<li>October 2008: Post-Doc position: European Institute of Oncology (IEO).</li>
<li>October 2008: Doctor of Philosophy (PhD) in Molecular Medicine (SEMM program- http://www.semm.it).</li>
<li>April 2007- Sept. 2008: Visiting Scientist:Utrecht University (The Netherlands) - A. J. Heck Lab</li>
<li>January 2004-Dec. 2004: Temporary staff: CEINGE Biotechnology Institute, School of medicine Naples.</li>
<li>Oct. 2002-Dec. 2003: Temporary staff: DSTB School of medicine of Udine.</li>
<li>June 2002: B. Sc. (Laurea) Chemistry, University of Naples “Federico II”.</li>
</ul>


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