<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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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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<h4><strong>European Free Educational Webinar Series</strong></h4>
<p><strong>Let&#39;s go back to the basics of Chromatography, Mass Spectrometry, Data Analysis and Trouble-shooting: understanding the importance of the basics will enable you to be more effective in your daily laboratory life.</strong></p>
<h4><strong>EPISODE 7</strong></h4>
<p><strong>Introduction to Mass Spectrometry</strong></p>
<p><strong>What will you learn?</strong></p>
<ul>
<li>Fundamentals of MS: LC/MS, LC/MS/MS &amp; TOF Systems</li>
<li>How to modify your LC Method when adding MS Detection</li>
</ul>
<blockquote>
<p><strong>Prezenter:</strong>  Antonia Wierzbicki (Principal MS Market Dev Manager, EMEA, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Antonia Wierzbicki is a MS market development manager at Waters working in EMEA. Antonia has BSc in Pharmaceutical Science and a MSc in Cancer Pharmacology.</p>
</blockquote>
<blockquote>
<p>Following several years working as an analytical chemist in drug development roles within both academic labs and contract research organizations, Antonia has more recently spent time working with analytical chemists to provide solutions using cutting edge technologies to meet their needs and requirements, with a specific interest in ultra-sensitive quantitation of small molecules.</p>
</blockquote>
<blockquote>
<p>Antonia is based in Cambridge UK and keen to connectwith like-minded scientists in the field.</p>
</blockquote>
<h4><strong>What&#39;s next?</strong></h4>
<p>Full Webinar Series Episodes List is available <a href="https://event.on24.com/wcc/r/4551012/F69479929A905500D8B21508527807E5/5385652"><strong>here</strong></a></p>
<p>Back to Basics - Sample Preparation: Theory and Overview</p>
<ul>
<li>Tuesday, May 07, 2024, 11:00 AM CEST</li>
</ul>
<p>Back to Basics - Sample Preparation: Tips &amp; Tricks to make it simple</p>
<ul>
<li>Wednesday, June 05, 2024, 11:00 AM CEST</li>
</ul>
<p>Back to Basics - Theory of Liquid Chromatography</p>
<ul>
<li>Wednesday, July 03, 2024, 11:00 AM CEST</li>
</ul>
<p>Back to Basics - Basics of Liquid Chromatography</p>
<ul>
<li>Tuesday, September 10, 2024, 11:00 AM CEST</li>
</ul>
<p>Back to Basics - Analytical Method Development</p>
<ul>
<li>Wednesday, October 02, 2024, 11:00 AM CEST</li>
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<p>Back to Basics - The importance of Compliance</p>
<ul>
<li>Tuesday, October 22, 2024, 11:00 AM CEST</li>
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<p>Back to Basics - Introduction to Mass Spectrometry</p>
<ul>
<li>Wednesday, November 13, 2024, 11:00 AM CET</li>
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<p>Back to Basics - Troubleshooting your LC and MS Systems</p>
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<li>Tuesday, December 10, 2024, 11:00 AM CET</li>
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<p>Register today and watch the webinars on-demand</p>


Waters Corporation: Back to Bacisc Free Educational Webinar Serries

Introduction to Mass Spectrometry

Fundamentals of MS in LC/MS, LC/MS/MS & TOF Systems.

<p><strong>Join us for an insightful webinar where we will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results. From screening to quantification, discover the value of targeted data analysis workflows using non-targeted data with our innovative software and hardware.</strong></p><p>Find by Formula algorithm. Learn to identify the most suitable MS/MS approach for your experiments, initiate quantitation for your compounds of interest, and incorporate retention times (RTs) and MS/MS spectra into a custom database and library.</p><p>This session is designed to enhance your understanding and application of Q-TOF data analysis, ensuring robust and reliable outcomes.</p><blockquote><p><strong>Presenter:</strong> Hannah Florance (Agilent Technologies)</p><p>Hannah has had multiple roles in the life sciences, starting as a protein chemist, before moving into proteomics and then metabolomics. A major part of her time working in academia involved running LC and GCMS core facilities supporting projects ranging from synthetic biology to cancer research. She is currently an LCMS applications specialist for Agilent.<br><br><strong>Presenter:</strong> Stefan Schaebler (Application Specialist LC/MS, Agilent Technologies)</p><p>Stefan completed his PhD in Biology, specializing in LC-MS-based lipidomics and metabolomics. Following his doctoral studies, he joined Agilent Technologies as an LC/MS Application Specialist. In this role, Stefan focuses on small molecule applications using LC-QTOF, with a strong emphasis on software tools and data interpretation.</p></blockquote>

Agilent Technologies: MassHunter Masterclass Months

MassHunter Qual – The Solid Pillar in Q-TOF Data Analysis

We will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results.

<p><strong>Join our upcoming webinar on the MassHunter Quant Screener Tool to discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds.</strong></p><p>This session will provide in-depth guidance on creating methods from PCDL databases, evaluating result parameters, and generating straightforward summary reports. Additionally, learn how retention time (RT) prediction can enhance your screening process by significantly accelerating and simplifying large database searches.</p><p>Don’t miss this opportunity to elevate your analytical capabilities!</p><blockquote><p><strong>Presenter:</strong> &nbsp;Jonathan Spencer (Application Specialist, Agilent Technologies)</p><p>Jonathan studied BSc Natural Sciences at the University of Nottingham and later went on to Sheffield Hallam University to study a MSc in Forensic Science.</p><p>Following graduation, he spent 2 years as a Confirmatory Analyst in an anti-doping and forensic toxicology lab, before joining Agilent as an LC/MS Applications Scientist. At Agilent, he focuses on small molecule applications using LC/TQ and LC/Q-TOF in fields of like food, forensic and environmental analysis.</p></blockquote>

MassHunter Quant Screener Tool

Discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds. 

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 1 – October 30</strong></h4><h5><strong>15:00 – 15:50 GMT: The Human Protein Atlas – Creating a Pan-Disease Resource Based on Next Generation Blood Profiling</strong></h5><ul><li>Mathias Uhlén, PhD (KTH Royal Institute of Technology)</li></ul><h5><strong>15:50 – 15:55 GMT:</strong> Networking Break</h5><h5><strong>15:55 – 16:15GMT: Mitigating Sorter-Induced Cellular Stress with Cartridge, Microfuildics-Based Sorting</strong></h5><ul><li>Crystal Montoya (Miltenyi Biotec)</li></ul><h5><strong>16:15 – 16:20 GMT:</strong> Networking Break</h5><h5><strong>16:20 – 16:40 GMT: Speaker to be announced</strong></h5><h5><strong>16:40 – 16:45 GMT</strong>: Networking Break</h5><h5><strong>16:45 – 17:35 GMT: Spatial Tissue Proteomics to Assess Health and Disease</strong></h5><ul><li>Fabian Coscia, PhD (Max Delbrück Center)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:00 GMT: The Sulpho-Phospho-Vanillin Assay: Accurate Lipid Normalization in Quantitative Lipidomics</strong></h5><ul><li>Karri Basso, PhD (University of Florida)</li></ul><h5><strong>18:00 – 18:05 GMT:</strong> Networking Break</h5><h5><strong>18:05 – 18:55 GMT: Proteomics for Cancer Precision Medicine</strong></h5><ul><li>Janne Lehtiö, PhD (Karolinska Instutet)</li></ul><h5><strong>18:55 – 19:00 GMT: </strong>Networking Break</h5><h5><strong>19:00 – 19:20 GMT: How Breakthroughs in Depth, Scale and Speed are Unlocking New Proteomic Discovery</strong></h5><ul><li>Aaron Gajadhar, PhD (Seer Bio)</li></ul><h5><strong>19:20 – 19:25 GMT: </strong>Networking Break</h5><h5><strong>19:25 – 19:55 GMT:</strong> Phantom Metabolites: Unraveling Metabolic Shadows</h5><ul><li>Gary Siuzdak, PhD (Scripps Research Institute)</li></ul><h5><strong>19:55 GMT:</strong> End of Day 1</h5><div><div><div><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote></div></div></div>

Technology Networks: Advances in Proteomics & Metabolomics 2024

Advances in Proteomics & Metabolomics 2024 (Day 1)

Hear about the latest advancements in translational proteomics and metabolomics. 

Advances in Proteomics & Metabolomics 2024  (Day 1)

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 2 – October 31</strong></h4><h5><strong>15:00 – 15:50 GMT: A Novel Strategy for the Absolute Quantification of Human Proteins</strong></h5><ul><li>Christoph Borchers, PhD (McGill University)</li></ul><h5><strong>15:50 – 15:55 GMT: </strong>Networking Break</h5><h5><strong>15:55 – 16:15 GMT: From Single Cells to the Metaproteome: Latest Developments in timsTOF Technology for Proteomics</strong></h5><ul><li>Matt Willetts, PhD (Bruker)</li></ul><h5><strong>16:15 – 16:20 GMT: </strong>Networking Break</h5><h5><strong>16:20 – 17:10 GMT: Single-Cell Chromatin Proteomics to Investigate the Biology of Exceptional Longevity</strong></h5><ul><li>Simone Sidoli, PhD (Albert Einstein College of Medicine)</li></ul><h5><strong>17:10 – 17:15 GMT: </strong>Networking Break</h5><h5><strong>17:15 – 17:35 GMT: Optimizing Metabolomics Workflows: From Sample Preparation to Multi-omics Integration</strong></h5><ul><li>Hagen Magnus Gegner, PhD (CTC Analytics)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:10 GMT: Analyzing Metabolic Responses to a Standardized Meal Challenge Using Exhaled Breath</strong></h5><ul><li>Matteo Tardelli, PhD (Owlstone Medical)</li></ul><h5><strong>18:10 GMT: </strong>Event Close</h5><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote>

Advances in Proteomics & Metabolomics 2024 (Day 2)

<div><div><div><p><strong>Targeted protein degradation (TPD) is a powerful therapeutic modality to eliminate disease-causing proteins that are resistant to conventional drugs. In this webinar, we present a high-throughput scalable proteomics approach that utilizes label-free, single-shot dia-PASEF<sup>®</sup> mass spectrometry to identify novel degrader targets on a large scale with unmatched coverage, accuracy, and speed. A combination of DIA-NN software and advanced statistical tools guarantees rapid, automated analysis of large proteomics datasets with highest precision of quantification, data completeness and sensitivity. A slice-PASEF-based global ubiquitinomics approach will be presented that verifies degrader-induced modifications with an unprecedented depth of 50,000 ubiquitination sites. In addition, a data analysis suite designed for user-friendly evaluation and in-depth meta-analysis will be shown, making proteomics data easily accessible for target identification, SAR optimization, library expansion and strategic drug discovery decisions.</strong></p></div></div></div><div><div><div><p><strong>About NEOsphere Biotechnologies:</strong></p><p>NEOsphere Biotechnologies is a leading partner in TPD (Targeted Protein Degradation) proteomics, collaborating with pharmaceutical and biotechnology companies to advance drug discovery and develop innovative degrader pipelines. The platform combines cutting-edge mass spectrometry technologies with advanced biostatistical data analysis, enabling high-throughput proteomic screening of entire degrader libraries and mechanistic target validation, including global ubiquitinomics. NEOsphere Biotechnologies offers unmatched sensitivity, precision, and turnaround times, facilitating the large-scale identification of novel degrader targets and the systematic exploration of previously undruggable therapeutic targets.<br><br><strong>You will learn about:&nbsp;</strong></p><ul><li>A high-throughput proteomics approach that utilizes label-free, single-shot dia-PASEF to identify novel degrader targets on a large scale with unmatched coverage, accuracy, and speed</li><li>The verification of degrader-induced modifications using an optimized acquisition strategy based on slice-PASEF-based global ubiquitinomics</li><li>The benefit of combining the capabilities of a timsTOF HT and a timsTOF Ultra 2</li></ul><blockquote><p><strong>Presenter: </strong>Uli Ohmayer, Ph.D. (Head of Mass Spectrometry and Founder, NEOsphere Biotechnologies GmbH, Munich, Germany)</p></blockquote></div></div></div>

Bruker: Unlock the therapeutic potential of targeted protein degradation with deep proteomic screening

Unlock the therapeutic potential of targeted protein degradation with deep proteomic screening

High-throughput scalable proteomics approach that utilizes label-free, single-shot dia-PASEF® mass spectrometry

Targeted protein degradation with deep proteomic screening

<p><strong>The complexity of biological systems and diseases, such as Alzheimer’s disease, necessitates spatial multiomics techniques to gain a holistic understanding of cell-cell interactions and communication. A singular approach to spatial multiomics is possible with MALDI Imaging, including label-free imaging of small molecules, lipids, drugs, and glycans. Additionally, with technology developed by AmberGen, Inc., photocleavable mass-tag (PCMT) conjugated affinity probes are available for antibodies, oligos, and lectins.</strong></p><p><strong>Key Learning Objectives:</strong></p><ul><li>Learn the spatial biology utility of MALDI Imaging</li><li>Understand multiomics workflows and the applications to disease-based research</li></ul><p><strong>Who Should Attend:</strong></p><ul><li>Researchers interested in multiomics brain analysis</li><li>Investigators researching Alzheimer’s disease</li></ul><blockquote><p><strong>Presenter: </strong>Mark Lim, Ph.D. (Chief Scientific Officer and Executive VP, AmberGen Inc., Billerica, MA, USA)</p><p>Mark Lim Ph.D. is the Chief Scientific Officer and Executive VP at AmberGen Inc. He has over 23 years’ experience in the biotechnology industry and has been awarded over 20 patents which underlie key technologies in the biotechnology industry, including in the fields of proteomics, genomics/transcriptomics, and diagnostics. His early work at AmberGen on photocleavable linkers and protein engineering contributed to the commercialization of a variety of novel reagents including PC-Biotin, PC-Phosphoramidites and fluorescent suppressor tRNAs. Dr. Lim now leads the application of these core AmberGen technologies to multiomic biomarker discovery and biomarker-driven diagnostics.</p><p><strong>Presenter:</strong> Kate Stumpo, Ph.D. (Senior Market Manager, Bruker Scientific, Billerica, MA, USA)</p><p>Dr. Kate Stumpo is a Market Manager which entails messaging and marketing for MALDI Imaging. Dr. Stumpo completed her Ph.D. at Texas A&amp;M University, and is an expert in MALDI applications, including MALDI Imaging.</p></blockquote>

Bruker: Advancing understanding of Alzheimer’s disease using multiomics spatial biology

Advancing understanding of Alzheimer’s disease using multiomics spatial biology

Learn the spatial biology utility of MALDI Imaging. Understand multiomics workflows and the applications to disease-based research.

Understanding of Alzheimer’s with multiomics spatial biology

<div><div><div><p><strong>Pure MHC, a pioneer in immunopeptidomics, has partnered with Bruker, a leader in state-of-the-art mass spectrometry, to demonstrate one of Pure MHC’s immunopeptidomics workflows. In this Live from the Lab webinar, tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis will be reviewed as tools for the development and validation of HLA peptide targets for immunopeptidomic development.</strong></p><p><strong>Key Learning Objectives:</strong></p><ul><li>Get insights into Pure MHC's sample preparation strategies to maximize the yield of immunopeptides from tissue samples</li><li>Discover how the unparalleled sensitivity and robustness of the Bruker timsTOF Ultra empowers users to maximize the potential of their immunopeptide samples</li><li>Understand data processing workflows for both DDA and DIA data processing</li></ul><blockquote><p><strong>Presenter:</strong> Curtis McMurtrey, Ph.D. (Director of Immunoproteomics, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. McMurtrey earned his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2010. He currently serves as the Director of Immuno-Proteomics at Pure MHC, LLC.</p><p>Dr. McMurtrey has studied HLA and its role in immunity since 2005. He is a member of American Society for Histocompatibility and Immunogenetics (ASHI) and holds the distinction of having won four ASHI Top Scholar Awards, more than any other scientist in the history of ASHI. Dr. McMurtrey is most notable for his work on West Nile virus epitope discovery and validation with HLA-A*02:01 and B*07:02; epitopes he discovered have been successfully tested in a WNV vaccine (collaboration with Drs. Hansen and Diamond at Washington University). His most recent accolades come from discovery of MR1 ligands from Mycobacterium tuberculosis (Mtb) as well as over 200 novel ligands from Toxoplasma gondii utilizing Deep Ligand Sequencing (DLS).</p><p>Dr. McMurtrey has expertise in BSL-3 containment techniques, protein purification, HLA ligand isolation, HPLC separation, mass spectrometric analysis, ELISPOT, and multicolor flow cytometry as well as provides bioinformatics expertise. To date, he has directed mass spectrometry (both IDA and SWATH) acquisition as well as comparative analysis and interpretation for a wide variety of MHC ligands including those from tuberculosis, toxoplasmosis, influenza, WNV, HIV and multiple cancers. Dr. Curtis McMurtrey oversees DLS acquisition and analyses and also manages database library collection.</p><p><strong>Presenter: </strong>Jason R. Krawic, Ph.D. (Business Development Manager, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. Krawic earned his Master’s degree in Biomolecular Sciences from Central Connecticut State University in 2012 before returning to academia and earning his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2024. He currently serves as the Director of Business Development at Pure MHC, LLC.</p><p>Dr. Krawic began his scientific career teaching Microbiology, Biology, and Chemistry to community college students in Connecticut and Oklahoma. He has studied HLA and non-classical MHC molecules since 2018. He is most recognized for discovering multiple isomeric conformations of MR1 ligands, as well as his work in MHC Class I and Class II ligands and cancer immunotherapies.</p><p>Dr. Krawic’s expertise ranges from classical microbiology and bacteriology to HPLC separation, protein purification, negative ion mode small molecule mass spectrometry, DDA, DIA and MRM acquisition and a variety of bioinformatics tools. In addition to his scientific career, Dr. Krawic has more than a decade of experience in sales and retail management. With this skill set he combines his science and sales backgrounds to serve Pure MHC’s customer base.</p><p><strong>Presenter: </strong>Kris Looney, MBA (President, Pure MHC, LLC, Austin, TX, USA)</p><p>As President of Emergent Technologies, the manager of Pure MHC, Kris Looney is responsible for conceiving and executing key business initiatives, developing strategic plans, and managing business processes including accounting, marketing, intellectual property, and business development. Kris has more than two decades of experience as a business generalist with a background in start-ups, management, accounting, marketing, negotiation, and sales.</p><p>Before joining Emergent, Kris served as the COO and Interim CEO of the American Red Cross of Central Texas, where he balanced multiple stakeholder needs with service responsibilities in a competitive philanthropic environment. Prior to that, he was the CFO of Transformation Enzyme Corporation, where his financial management and business development helped a bootstrapped entrepreneurial start-up become a leader in the nutritional supplement market. Kris has a B.A. in marketing and an M.B.A. from the University of Texas at Austin.</p><p><strong>Presenter: </strong>Matt Willetts, Ph.D. (Proteomics Applications Manager, Bruker Scientific LLC, Billerica, MA, USA)</p><p>Matt received his Ph.D. in mass spectrometry with Prof. Malcolm Clench at Sheffield Hallam University in the UK. He then joined Waters as the Technical Marketing Specialist for LCMS and MALDI products, focusing on application development for proteomics-based workflows. Matt joined Bruker in 2010 and is responsible for proteomics applications and support in North America.</p></blockquote><p>&nbsp;</p></div></div></div>

Bruker: Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis for immunopeptidomic development.

<p><strong>This presentation outlines a study on small cells using a 750 milliseconds injection time via the reticle method, allowing detailed analysis of cell states and functional protein covariates. Labels were transferred between modalities, enabling comparisons without requiring a Pet set of data.</strong></p><p>Differences in processes were identified, providing insights into important proteins not suggested by mRNA levels. A multi-omics analysis, combining transcriptomics and proteomics, was conducted using a self-created single cell transcriptomics dataset annotated with Asimov's reference mapping approach.</p><p>This allowed the identification of differentiation trajectories and heterogeneity within cell populations. However, transcriptomics alone was insufficient, as mRNA may not effectively represent protein levels. Therefore, a single cell proteomics dataset of the HSC compartment was measured from human bone marrow using mass spectrometry-based methods. TMT Pro with 14 single cells and a carrier channel was employed to enhance protein identification rates. The study identified proteins crucial for HSC maintenance, revealing insights not apparent from mRNA data, thus advancing understanding of cell state biology.&nbsp;</p><p>Learning points:</p><ul><li><strong>Integration of Multi-Omics Data &nbsp;</strong></li><li><strong>Advanced Analytical Techniques&nbsp;</strong></li><li><strong>Functional Insights into Stem Cells&nbsp;</strong></li></ul><p>Who should attend:</p><ul><li>Researchers involved in multi-omics studies, particularly those combining transcriptomics and proteomics&nbsp;</li><li>Specialists in mass spectrometry and proteomics can gain knowledge on the latest techniques and methodologies</li><li>Scientists studying hematopoietic stem cells (HSCs) and their differentiation processes</li></ul><div><div dir=""><div><blockquote><div><strong>Presenter:</strong> Benjamin Furtwängler (PhD Student, DTU, Copenhagen)</div></blockquote><blockquote><div>Benjamin Furtwängler is a PhD student in the Porse Group at the Copenhagen University. The group is part of the Finsen Laboratory, a department for basic cancer research, and is interested in understanding stem cells and their differentiation in hematopoiesis and leukemia.</div><p>Benjamin is also supervised by Erwin Schoof, Associate Professor at the Technical University of Denmark. Erwin’s group is developing mass spectrometry-based single-cell proteomics methods and together with the Porse group, aims to apply these methods to further the understanding of stems cells in healthy and malignant hematopoiesis.</p><p>He earned his bachelor's and master's degree from the Technical University Berlin, during which time he conducted research utilizing mass spectrometry-based proteomics methods in both the Rappsilber Laboratory and the Selbach Laboratory.</p></blockquote></div></div></div>

Thermo Fisher Scientific: Single-cell proteomics and transcriptomics of human hematopoiesis reveals proteome specific features

Single-cell proteomics and transcriptomics of human hematopoiesis reveals proteome specific features

A study on small cells using a 750 milliseconds injection time via the reticle method, allowing detailed analysis of cell states...

Single-cell proteomics and transcriptomics

<p><strong>This presentation discusses the work being done to understand how drugs work and how they can be repurposed for new indications. Prof. Küster’s lab uses various technologies and methods, such as sample preparation, mass spectrometry, and informatics, to study the proteome and fosso-proteome of cancer patients.</strong></p><p>The goal is to find the right drug for the right person by understanding what is going wrong in the patient and what the drugs can do. By studying drug-protein interactions and pathway engagement in a dose-dependent fashion, this research aims to make better treatment recommendations. The lab has developed a technology platform that allows for the systematic profiling of kinase inhibitors and the measurement of proteome expression changes in response to drugs.</p><p>This information can help prioritize biological effects and facilitate drug repurposing. This presentation highlights the importance of studying proteins in understanding drug mechanisms of action and identifying potential targets for cancer treatment.</p><p><strong>Learning points:</strong></p><ul><li>Importance of Repurposing Drugs &nbsp;</li><li>Role of Proteomics in Precision Oncology &nbsp;</li><li>Dose-Dependent Analysis &nbsp;</li></ul><blockquote><p><strong>Presenter: </strong>Prof. Bernhard Küster (Technical University Munich)</p><p>Bernhard Küster holds a chemistry degree from Cologne, a PhD in Biochemistry from Oxford and did a PostDoc at the EMBL in Heidelberg and the University of Southern Denmark. After seven years as Vice President Analytical Sciences and Informatics at Cellzome (now GSK), he became.​</p><p>Full Professor of Proteomics at the TU Munich in 2007. He also directs the Bavarian Biomolecular Mass Spec-trometry Center and the Clinical Mass Spectrometry Center Munich.​</p><p>Bernhard’s research focuses on proteomics and its application to chemical and cancer biology. He is interested in understanding how cancer drugs actually work and has received an ERC Advanced Grant in 2019 aiming to integrate proteomics into precision medicine. Bernhard has received several awards, including from HUPO for a draft human proteome and his contri-butions to chemical proteomics. Bernhard is a member of the German National Academy of Science, Leopoldina and has co-founded two start-up companies that operate in the area of proteomics and artificial intelligence.</p></blockquote>

Thermo Fisher Scientific: Understanding drugs using proteomics

Understanding drugs using proteomics

This presentation highlights the importance of studying proteins to understand drug mechanisms and identify potential targets for cancer treatment

LCMS webinars focusing on LC/HRMS - page 23