<div>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.</div><div><div><div><div><h3>What is Protein Purification?</h3>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.This process is especially vital in biotechnological areas inside immunology and microbiology. In immunology, 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 microbiology, 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.</div></div></div></div><div><div><div><div><h3>Types of Protein Purification Methods</h3></div></div></div></div><div>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:</div><div><div><div><div><h4>Non-Chromatographic Approaches</h4></div></div><div>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.<h5>Precipitation Techniques</h5>Protein precipitation is a widely used approach in purification workflows, typically relying on one of three main methods:<ul><li>Organic solvent precipitation 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>Isoelectric point precipitation 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>Nonionic polymer precipitation 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>Dialysis</h5>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.<h5>Immunocapture (Magnetic Bead-Based Purification</h5>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:<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>Magnetic beads offer speed, ease of use, and minimal sample loss, making them ideal for lab-scale workflows.<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.<h5>Centrifugation</h5>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.Preparative Ultracentrifugation 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.Differential Centrifugation 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.Rate-zonal Gradient Centrifugation 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.Isopycnic Centrifugation (Equilibrium Centrifugation) 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.</div></div></div><div><div><div><div><h4>Chromatographic Approaches</h4>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.<h5>Ion Exchange Chromatography</h5><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.<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;<ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1526">Luna SCX </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">Biozen WCX</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>Size Exclusion Chromatography</h5><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.Phenomenex offers a range of Biozen columns for SEC separations. In the case of mAbs, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1534">Biozen dSEC-2</a> and<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1537"> Biozen dSEC-7 </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.For more general applications, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1533">Biozen SEC-2</a> and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1532">Biozen SEC-3</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.<h5>Reversed-Phase Chromatography</h5><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.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.<h5>Hydroxyapatite Chromatography</h5>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.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.<h5>Hydrophobic Interaction Chromatography</h5>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.<h5>Affinity Chromatography</h5>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.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.</div></div></div></div>

Exploring Protein Purification Methods: Essential Techniques for Accurate Results

<h3>A Practical Guide to Getting the Most from Syringe Filters: Tips, Tricks, and Common Pitfalls</h3>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.<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"><h4>1. Improper Filter Handling</h4>Using excessive force during filtration or attempting to reuse disposable syringe filters can damage the membrane and increase the risk of sample contamination.<ul><li>Solution: 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.</li></ul><h4>2. Selecting an Inappropriate Pore Size</h4>Using the wrong pore size may either fail to remove unwanted particles or cause the membrane to clog prematurely, reducing filtration efficiency.<ul><li>Solution: 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.</li></ul><h4>3. Choosing the Wrong Membrane Material</h4>Different membrane materials exhibit different chemical resistance. Using an incompatible membrane may lead to degradation of the filter, sample contamination, or complete filtration failure.<ul><li>Solution: 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.</li><li>Pro Tip: For additional guidance, see our blog article "How to Choose the Right Membrane for your Syringe Filter", which provides a detailed comparison of membrane materials and their recommended applications.</li></ul><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"><h4>4. Ignoring Filter Capacity</h4>Using a filter with insufficient capacity can result in rapid membrane blockage, increasing filtration time and reducing laboratory productivity.<ul><li>Solution: 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.</li></ul><h4>5. Overlooking Sample Adsorption</h4>Certain membrane materials may adsorb analytes of interest, leading to lower recoveries and potentially affecting quantitative results.<ul><li>Solution: 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.</li></ul><h4>6. Failing to Optimize Filtration Performance</h4>Slow filtration is more than just an inconvenience—it often indicates that the filtration conditions are not optimal.<ul><li>Solution: 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.</li></ul><h4>Final Thoughts</h4>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.With the right syringe filter and proper filtration technique, you can minimize sample preparation problems and maximize confidence in every analysis.<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">Happy filtering!

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

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Waters Corporation

<h4>Virtual event: Pharma conclave series 2024</h4>
SCIEX offers the platform for the experts to take the stage and drive technological progress
Welcome to Pharma conclave series 2024 – where our customers’ expertise meets innovation, transforming your knowledge and empowering you to revolutionize your work processes. Join us in discovering techniques that will enhance your skills to accelerate your daily operations in the development of new drugs.
From the research of new markers to the drug development moving into non and GLP bioanalysis. Confidently plan your next lab expansion with the knowledge gained from industry leaders and pioneers.
<ul>
<li>May 16 Event 1: Pharma omics</li>
<li>September 17 Event 2: Impurities</li>
<li>October 23-24 Event 3: Pharma</li>
</ul>
10:00 a.m.–12:00 p.m. CET
<h3>Event 2: Impurities</h3>
Impurities in the pharmaceutical industry. What&#39;s next?
While the regulatory landscape is changing faster than ever, having the right information on impurities available to you at every stage of the drug development is vital to bring safe and effective therapies to the market. Whether you want to optimize your lab’s current capabilities or scale up to meet your future demands, this event creates a platform to share the customer’s expertise.
<blockquote>
Presenter: Bruno Manadas, PhD
</blockquote>
<blockquote>
Dr Manadas is a prominent Cell Biology researcher at CNC-UC since 2017. With expertise in biochemistry, psychology, and biotechnology, he&#39;s authored 130+ publications and led multiple projects. As head of CNC&#39;s Mass Spectrometry node and Associate Editor for Frontiers, he&#39;s contributed significantly to neuroscience and psychiatry. Bruno&#39;s research focuses on cell biology mechanisms, translational biomarker research, and MS-based approaches for studying protein oxidation. He played a pivotal role in establishing the hospital biobank and teaches at the Portuguese Catholic University.
</blockquote>
<blockquote>
Presenter: Dorte Bekker-Jensen
</blockquote>
<blockquote>
Dorte is heading the Applications Development team in Proteomics Research at Evosep. She has long-term experience within proteomics and has focused on technology development by developing simple and automated workflows for high-throughput applications.
</blockquote>
<blockquote>
Presenter: Stefan Ledinger
</blockquote>
<blockquote>
Stefan has 20 years of experience in the life sciences and diagnostic industries. For the last dozen years, he has been serving various functions within biocrates life sciences ag. Most recently, he has been responsible for the market development for metabolomics solutions in the pharmaceutical and biotech industries. He currently serves as Global Head of Sales. Stefan holds degrees in business administration and bioengineering, combining commercial know-how with a passion for science.
</blockquote>
<blockquote>
Presenter: Markus Langsdorf
</blockquote>
<blockquote>
Markus has 14 years of experience in life sciences industries. As he joined biocrates in 2010, he worked for 11 years as application support specialist for biocrates’ metabolomics profiling solutions. 3 years ago he changed his position withing the company to his new function as product manager. Markus studied chemistry and graduated with a PhD in Analytical Chemistry.
</blockquote>

Pharma conclave series 2024: Impurities

Mass spectrometry (MS)-based omics technologies have revolutionized our understanding of molecular changes in organisms and are crucial for studying metabolism and related diseases through lipidomics and metabolomics.
Despite significant advances, there is still a need for robust analytical methodologies in data acquisition, data processing and annotation.
This webinar will demonstrate how LC-Zeno SWATH DIA outperforms conventional DDA in annotating metabolites and lipids in the model organism Gammarus fossarum. Additionally, the presentation will showcase the effectiveness of electron activated dissociation (EAD) in characterizing lipid species and elucidating metabolite isomers. Finally, the webinar will illustrate how EAD and high-resolution targeted approaches improve structural elucidation and molecular network construction.
Attend this webinar to:
<ul>
<li>Learn about the benefits of LC-Zeno SWATH DIA over conventional DDA methods for metabolite and lipid annotation
</li>
<li>Explore the implementation of EAD for enhanced lipid species characterization and metabolite isomer elucidation
</li>
<li>Understand how EAD improves structural elucidation and molecular network construction
</li>
</ul>
<blockquote>
Presenter: Dr. Valentina Calabrese (Postdoctoral Researcher at Institute of Analytical Sciences)
</blockquote>
<blockquote>
Valentina Calabrese received her Ph.D. in Analytical and Bioanalytical Sciences at University of Palermo, Italy and is currently a postdoctoral researcher at the Institute of Analytical Sciences in Lyon, France. During her career, she specialized in high resolution, ultra-high resolution, and ion mobility mass spectrometry for application on fundamental topics and -omics research, such as metabolomics and lipidomics. Her research activity focuses on new method development and unknown compound annotation through high-resolution mass spectrometry and molecular networking in biological complex samples. She is currently involved in the study of sentinel freshwater organisms, as Gammarus fossarum and works on DDA and SWATH DIA methods with CID or EAD fragmentation strategies along with molecular networking construction for improving structural characterization of small molecules.
</blockquote>

Technology Networks: Enhancing MS-Based Omics Analysis in a Model Organism

Enhancing MS-Based Omics Analysis in a Model Organism

How LC-Zeno SWATH DIA outperforms conventional DDA in annotating metabolites and lipids in the model organism Gammarus fossarum.

<h4>Live from the Lab hosted by NIBRT: Solutions for biotherapeutic analysis</h4>
By your side to accelerate your biopharmaceutical development journey
Join us for the second Live from the Lab of 2024, taking place on September 17th, an exciting biopharma hybrid event featuring the latest advancements in separation technology and mass spectrometry. Focusing on all stages of biotherapeutics development, from discovery and research, all the way to routine and QC analysis, this event will give you valuable insights to accelerate your biopharmaceutical development journey.
The following speakers will talk at this event at the NIBRT research facility which will be streamed live all over Europe:
<ul>
<li>Dr. Jonathan Bones, NIBRT</li>
<li>Prof. Mark Dickman, University of Sheffield</li>
<li>Dr. Dan Bach Kristensen, Symphogen</li>
<li>Dr. Mark Hilliard, Pfizer</li>
<li>Dr. Ken Cook, Thermo Fisher Scientific</li>
<li>Jon Bardsley, Thermo Fisher Scientific</li>
</ul>
Whether you are a researcher, scientist, or industry professional in our region, this biopharma event is not to be missed. Expand your knowledge, network with experts, and discover how the Thermo Scientific solutions will stand by your side to accelerate your biopharmaceutical development journey.
Mark your calendars for September 17th and join us for this impactful hybrid event foster collaboration within the scientific community.
Participation is free of charge, registration is required.
For any questions about this event or regarding your registration, please email CMDEvents@thermofisher.com.
<h4>How to attend?</h4>
3 ways of attending:
<h5>Online attendees (remote):</h5>
Unable to travel to a satellite? Not a problem! You can register to attend conveniently online from your desk or anywhere else through the live stream from NIBRT.
<ul>
<li><a href="https://assets.thermofisher.com/TFS-Assets/CMD/Flyers/fl-003119-pb-live-from-the-lab-ms-biotherapeutics-agenda-online-fl003119-em-en.pdf">Agenda</a></li>
</ul>
<h5>NIBRT Research Facility (in-person event):</h5>
Join the heart of the event where the main agenda will be hosted and live streamed across our region to our satellite events and our online audience. Attendance through VIP invitation only!
<h5>Join a ‘Satellite’ location (in-person event):</h5>
Across Europe, our in-person satellite events will be broadcasting the main agenda live streamed from NIBRT, Dublin and supplement the day with local speakers/lab tours pending on the satellite. Take this opportunity to network with fellow scientists and meet your Thermo Fisher representatives from technical, commercial, and service functions. Check out the closest location to you and their individual agenda!
<ul>
<li>Søborg, Denmark (AGC Biologics)</li>
<li>Dreieich, Germany (Thermo Fisher Scientific)</li>
<li>Segrate, Italy (MI) (Thermo Fisher Scientific S.P.A.)</li>
<li>Leiden, Netherlands (Janssen Biologics BV)</li>
<li>Ljubljana, Slovenia (Four Points by Sheraton Ljubljana Mons)</li>
<li>Reinach, Switzerland (Thermo Fisher Scientific)</li>
<li>Hemel Hempstead, UK (Thermo Fisher Scientific)</li>
</ul>

Thermo Fisher Scientific: Live from the Lab: Solutions for biotherapeutics

Live from the Lab: Solutions for biotherapeutics

An exciting biopharma hybrid event featuring the latest advancements in separation technology and mass spectrometry.

<h4>Rebroadcast of the Live from the Lab: Solutions for Multi-Omics Research from June 13, 2024</h4>
Native nano-DESI mass spectrometry imaging of proteins up to 230 kDa: Advances in proteoform discovery and identification
In this presentation, Prof. Cooper discusses her recent work in developing native ambient mass spectrometry (NAMs) for structural analysis and spatial analysis of proteins.
In this session, you will hear how to
<ul>
<li>identify intact protein assemblies and protein-ligand complexes directly from tissue sections using Native ambient mass spectrometry (NAMs) </li>
<li>understand the structure and function of proteins and their role in complex biological systems </li>
<li>overcome challenges in NAM, including complex mass spectra and low abundance signals Can&#39;t attend the webinar broadcast? No problem! Register anyway and you will automatically receive the link to the recording.</li>
</ul>
<blockquote>
Presenter: Prof. Helen Cooper (University of Birmingham)
</blockquote>

ThermoFisher Scientific: Advances in proteoform discovery and identification

Advances in proteoform discovery and identification

Native nano-DESI mass spectrometry imaging of proteins up to 230 kDa

The sample throughput of high-sensitivity liquid chromatography-mass spectrometry (LC-MS) based proteomics analysis is restricted by the pressure limitations of LC and column hardware, with some methods wasting as much as 50% of the method cycle time outside of MS acquisition.
Traditional routes for boosting throughput include shorter columns and gradients, higher flow rates, and using trap-and-elute workflows – all of which introduce trade-offs in sensitivity and proteome depth.
The Thermo Scientific™ Vanquish™ Neo tandem direct injection workflow leverages hardware innovations and software intelligence to eliminate method overhead while maintaining data quality across nano, capillary, and micro-flow LC-MS.
In this webinar experts from Evotec and Bayer will showcase how they implemented the tandem direct injection workflow for their proteomics work. Dr. Nagarjuna Nagaraj will present on how Evotec is using tandem direct injection with nano-LC columns packed in-house to boost sample throughput of their chemoproteomics screening pipeline, while Dr. Alexander Boychenko from Bayer will discuss how his lab is using a micro-flow tandem direct injection approach to analyze plasma samples for translational proteomics.
Learning Objectives
<ul>
<li>See how minimizing LC-MS method overhead can accelerate sample throughput while maintaining proteome depth
</li>
<li>Discover how labs are using tandem direct injection for chemoproteomics and translational proteomics applications
</li>
<li>Learn how to implement tandem direct injection in your proteomics workflow
</li>
</ul>
<blockquote>
Presenter: Dr. Nagarjuna Nagaraj (Group Leader High Sensitivity Proteomics, Evotec)
</blockquote>
<blockquote>
Dr. Nagarjuna Nagaraj is a proteomics group leader at Evotec focusing on high sensitivity and high throughput proteomics applications with more than 18 years of experience in proteomics and mass spectrometry. Nagarjuna obtained his PhD from the Matthias Mann lab focusing on sample preparation and MS data acquisition strategies for clinical applications. After a postdoc he directed the mass spectrometry core facility at the Max-Planck-Institute of Biochemistry working on a wide range of protein and peptide mass spectrometry projects such as bottom-up proteomics, structural mass spectrometry including HDX, native and crosslinking MS, intact protein and small molecule analysis.
</blockquote>
<blockquote>
Presenter: Dr. Alexander Boychenko (Head of R&amp;D Laboratory Precision Medicine Markers, Bayer)
</blockquote>
<blockquote>
Alexander Boychenko is leading Omics Research within the Translational Sciences team of the Pharmaceuticals division at Bayer Group. He is focused on implementing innovative analytical technologies and developing novel methodologies for proteomics, metabolomics, and ligand-binding assays (LBA) to comprehensively characterize human and animal model phenotypes, enabling disease understanding and novel biomarker discovery. He holds a Ph.D. in Analytical Chemistry from Kharkiv National University, Ukraine. During his post-doctoral work at the University of Groningen, The Netherlands, he combined LC-MS and immunoassays to discover and validate protein biomarkers in biofluids for cancer screening. Before joining Research and Early Development at Bayer AG, he developed and introduced new liquid chromatography-mass spectrometry products at Thermo Fisher Scientific. Alexander is a subject matter expert in LC-MS, biological data interpretation, and precision medicine. He utilizes his passion for applying technical expertise to develop new medicines.
</blockquote>
<blockquote>
Presenter: Dr. Alec Valenta (Product Marketing Manager, Thermo Fisher Scientific)
</blockquote>
<blockquote>
Alec is the product marketing manager for the Vanquish Neo UHPLC system and low-flow LC columns. Prior to joining Thermo Fisher Scientific he earned his PhD in analytical chemistry from the University of Michigan where he helped advance microdialysis sampling of neurochemicals and developed LC-MS methods to quantify small molecule neurotransmitters, neuropeptides, and metabolites in a variety of complex biological samples.
</blockquote>

Thermo Scientific: A Tandem LC Workflow for Maximizing Mass Spectrometer Utilization in Proteomics

A Tandem LC Workflow for Maximizing Mass Spectrometer Utilization in Proteomics

How experts from Evotec and Bayer implemented the tandem direct injection workflow for their proteomics work.

A Tandem LC Workflow for Maximizing Mass Spectrometer

With the timsTOF Pro, powered by the PASEF® acquisition modes, Bruker has largely contributed to take proteomics analysis to a new dimension, by removing the need to compromise speed for sensitivity or selectivity, while reaching unprecedented levels of robustness.
Introduced @ ASMS 2024, the timsTOF Ultra 2 is the pinnacle of timsTOF evolution, combining ultimate sensitivity, speed, selectivity and dynamic range with the field-proven legendary timsTOF robustness. During this live from the lab, you will witness through real-life examples how sensitive and versatile the timsTOF Ultra 2 can be.

Bruker: Taking 4D-Proteomics™ to the routinely exceptional with the timsTOF Ultra 2j

Taking 4D-Proteomics™ to the routinely exceptional with the timsTOF Ultra 2

Through real-life examples how sensitive and versatile the timsTOF Ultra 2 can be.

Taking 4D-Proteomics™ to the routinely exceptional

Fragmentation-based molecular annotations are the gold standard in high-confidence biomarker identification using mass spectrometry.
The new iprm-PASEF workflow integrates CCS-enabled MALDI Imaging of lipids with a targeted MS/MS imaging approach that allows spatial fragmentation and analysis of multiple targets in a single acquisition. The workflow includes a fully integrated pipeline within our software ecosystem to generate accurate identifications with spatial fidelity.
Key Learning Objectives:
<ul>
<li>Fragmentation based MALDI Imaging capabilities
</li>
<li>iprm-PASEF workflow for the timsTOF fleX
</li>
<li>Fragmentation based annotation pipeline using SCiLS™ Lab
</li>
</ul>
Who should attend:
<ul>
<li>Researchers interested in expanding their spatial biology toolkit
</li>
<li>Researchers focused on maximizing confidence of molecular annotations for MALDI Imaging
</li>
<li>Anyone who wants to expand their MALDI Imaging workflows
</li>
</ul>
<blockquote>
Presenter: Michael Becker, Ph.D. (Principal Scientist DMPK, Boehringer Ingelheim Pharma GmbH &amp; Co KG, Mainz, Germany)
</blockquote>
<blockquote>
Dr. Michael Becker is the head of the Mass Spectrometry Imaging lab at Boehringer Ingelheim. He received his Ph.D. in Neurobiology, and transitioned into the imaging field more than 15 years ago. He uses MSI to study drugs and drug-induced changes in tissue. To do so, he tries to push the sensitivity, reproducibility and specificity of the method.
</blockquote>
<blockquote>
Presenter: Arne Behrens, Ph.D. (Application Specialist in MALDI Imaging, Bruker Daltonics GmbH &amp; Co. KG, Bremen, Germany)
</blockquote>
<blockquote>
Dr. Arne Behrens is an Imaging Applications Scientist  at Bruker in Bremen with more than 6 years of experience on the timsTOF fleX platform. He received his Ph.D. in Analytical Chemistry and is an expert for CCS-enabled MALDI Imaging applications.
</blockquote>
<blockquote>
Presenter: Björn Wendik, Ph.D. (Business Development Manager, Bruker Daltonics GmbH &amp; Co. KG, Bremen, Germany)
</blockquote>
<blockquote>
Björn studied biology at the University of Würzburg and University of Freiburg with focus on developmental biology. In Freiburg he did his Ph.D. working on motoneuron development and pancreas formation. He became an expert on life cell imaging, timelapse studies and 3d-image software analyses. He continued his work as lecturer at the University of Freiburg where he also took care of parts of the Imaging core facility. When stepping into industry, he worked as a specialist for confocal microscopy and from there moved on into multispectral imaging, antibody based multi- and hiplexing and tissue analysis platforms. With this expertise, Björn started as a Business Development Manager for the MALDI Imaging at Bruker in July 2023.
</blockquote>

Bruker: Confidence in spatial identifications using iprm-PASEF on the timsTOF fleX

Confidence in spatial identifications using iprm-PASEF on the timsTOF fleX

The new iprm-PASEF workflow integrates CCS-enabled MALDI Imaging of lipids with a targeted MS/MS imaging approach.

Confidence in spatial identifications using iprm-PASEF

<h3>Session #1 - Advancements in Targeted Quantitation of PFAS</h3>We are thrilled to invite you to our upcoming webinar focused on enhancing laboratory efficiency and accuracy in PFAS analysis. Join us to explore innovative solutions that streamline processes and improve detection capabilities.1. Harnessing the Power of Mass Spectrometry and Automation to Reduce Sample Size, Sample Preparation Time and Increase Laboratory Efficiency of PFAS Analysis for EPA 1633<ul><li>Presented by Kari Organtini</li></ul>EPA Method 1633 is widely used for analyzing PFAS in non-potable water, soils, biosolids, and tissues. This presentation will show how advanced mass spectrometry and automation can significantly reduce sample size, cut down preparation time, and boost overall laboratory efficiency.2. Identification of short chain per and polyfluorinated alkyl substances (PFAS) using ion ratios with low mass product ions<ul><li>Presented by Stuart Adams</li></ul>As long-chain PFAS are replaced by short and ultrashort-chain alternatives, their detection becomes more challenging. This talk will cover how modified tandem quadrupole mass spectrometry enhances sensitivity, enabling the identification of these difficult-to-detect PFAS compounds using low-mass product ions.3. Evaluation of DESI mounted on Q-TOF and TQ mass spectrometers to image PFAS compounds in different matrices<ul><li>Presented by Emmanuelle Claude</li></ul>Direct analysis with minimum sample preparation as well spatial dimension of PFAS in samples can add simplicity and localization information, to complement state of the art detection and quantification by UHPLC-MRM analysis. Results are presented to evaluate the level of detection of few tens of PFAS compounds that were spotted on porcine liver tissue section, after updating the DESI imaging workflow to minimize external contamination. Several mass spectrometers such as discovery workflow in full scan TOF mode on the MRT and Cyclic mass spectrometers as well as targeted workflow using MRM acquisition mode on the DESI XS Xevo TQ Absolute MS were compared. Finally the benefit of ion mobility separation for the MSI analysis of PFAS is described. 61% and 55% of the PFAS compounds were detected as low as 10 ng/mL spotted on tissue when analyzed by negative mode DESI in discovery full scan MS acquisition mode. The targeted MRM workflow is the most sensitive system with 77% of the PFAS compounds detected as low as 10 ng/mL spotted on tissue.Join us to learn how these technologies are transforming PFAS analysis, helping laboratories meet the growing demand for more efficient and accurate testing.<blockquote>Presenter: Dr. Stuart Adams (Principal Scientist, Market Development, Food and Environmental Applications, Europe, Waters Corporation)Stuart has been developing methods for the determination of contaminants in food and the environment for over 17 years and has been with Waters Corporation since 2018. Stuart's previous role was as a senior analytical chemist at Fera (the UK’s National Reference Laboratory) and moved to Waters to focus on application development in the European region. He now serves as the attached scientist to the European Market Development team responsible for the food and environmental application areas. In his role, he works with customers to understand their analytical challenges and helps address them with Waters technologies.Presenter: Kari Organtini, Ph.D. (Principal Scientist, Food &amp; Environmental, Waters Corporation)Kari Organtini is a senior scientist at WatersCorporation and has been with the company for five years. She received her PhD from Penn State University in 2015 studying the occurrence of dioxins and furans in fire debris and their implications to first responder health. At Waters, Kari is part of the food and environmental applications team. Kari has developed applications using both LC and GC techniques for a variety of applications ranging from pesticides to persistent organic pollutants during her career. She is currently the scientific lead for developing PFAS applications at Waters.Presenter: Emanuelle Claude (Consulting Scientist D&amp;C Imaging, Waters Corporation)Miss Emmanuelle Claude (Master in Fine Chemistry and Business and M.Phil in spectroscopy analysis in organic chemistry and biology) is currently a Consulting scientist in the Scientific Operations Department, Wilmslow, UK.She 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.Over the years she developed several 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 15 years ago.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 and is part of 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 with customers visit and demonstration laboratory worldwide.Presenter: Ken Rosnack (Principal Market Development Manager, Waters Corporation)Ken Rosnack is a Principal Market Development Manager in the Testing &amp; Lab Services Group for Waters Corporation. His primary focus is within regulated and routine LC-MS/MS environmental market where he is responsible for world-wide strategy implementation and performance. He maintains collaborations within regulatory agencies as well as with global industrial partners. Over his career, Ken has been primary author on numerous publications, been an invited speaker multi-nationally, and has presented at many conferences. He has been involved with MS for the past 40 years.</blockquote>

Waters Corporation: Advancements in Targeted Quantitation of PFAS

Advancements in Targeted Quantitation of PFAS

Learn how technologies are transforming PFAS analysis, helping laboratories meet the growing demand for more efficient and accurate testing.

<h3>Session #2 - Innovative Approaches in HRMS and Software for PFAS Analysis</h3>We are excited to invite you to our upcoming webinar, where we will explore the latest advancements in PFAS analysis through innovative screening methods and technologies. Our expert speakers will cover various approaches to enhance the detection and identification of per- and polyfluoroalkyl substances (PFAS).<h4>1. Nontarget Screening workflow (NTS) for the Analysis of Per and Polyfluoroalkyl Substances (PFAS) using High resolution mass spectrometry (HRMS)</h4><ul><li>Presented by Hania Khoury-Hollins</li></ul>This session will focus on using HRMS as an effective tool to detect both regulated and non-regulated PFAS. We’ll explore the UNIFI™ screening workflow and discuss the use of comprehensive PFAS libraries to improve detection capabilities.<h4>2. Untargeted Screening for PFAS Chemicals Using Comprehensive Feature Detection</h4><ul><li>Presented by Jeff Goshawk</li></ul>Discover how advanced feature detection methods can identify a wide range of PFAS chemicals, including those not covered by traditional reference standards. This talk will highlight techniques to detect novel PFAS-like chemicals, providing a broader understanding of total organic fluorine content in samples.<h4>3. Elevating Specificity and Identification Confidence for PFAS Liquid Chromatography and Cyclic Ion Mobility Mass Spectrometry</h4><ul><li>Presented by Michael McCullagh</li></ul>Learn how cyclic ion mobility (cIM) enhances the separation and identification of PFAS isomers. By using this method, we can achieve greater specificity and reduce analysis time, providing insights into PFAS exposure and its potential health impacts.Join us to learn how these cutting-edge approaches are revolutionizing PFAS detection and analysis, offering more accurate and efficient solutions for environmental monitoring and public health protection.<blockquote>Presenter: Hania Khoury-Hollins (Principal Scientist, Waters Corporation)Hania Khoury-Hollins is a scientist and researcher at Waters Corporation. She holds a bachelor’s degree in science, which laid the foundation for her scientific pursuits. In 2001, Hania earned her master’s degree in Toxicology, deepening her understanding of the impact of chemicals on living organisms. In 2005 she successfully defended her Ph.D. in physical chemistry from University René Descartes - Paris V (France). After undertaking several different projects in academia Hania spent some time working at Agilent before joining Waters.At Waters, her work revolves around developing cutting-edge analytical techniques and their applications with a focus on Liquid Chromatography coupled with High-Resolution Mass Spectrometry (LC-HRMS). Her expertise encompasses a diverse range of applications, including drug development, proteomics, metabolomics, and lipidomics. More recently, Hania has been developing applications strategies for per- and polyfluoroalkyl substances (PFAS).Presenter:&nbsp;Mike McCullagh (Consulting Scientist, Waters Corporation)Michael has worked at Waters Corporation for over 23 years. His main focus has been non-targeted analysis using time of flight mass spectrometry and ion mobility mass spectrometry. Michael has made contributions to various teams, including Food and Environmental, MS Evaluation, Life Science, Scientific Operations, the Advanced Mass Spectrometry Team and currently in Research, Development and Advanced Testing. Research has been performed across multiple application areas including, impurity profiling, pesticide screening, natural products, food analysis, metabolite identification and more recently non-targeted PFAS analysis. Having worn a number of different “hats”, the common thread has been the privileged opportunity to work with new technologies, new informatics solutions and to collaborate with industry and global collaborative partners, to forge a path to new discoveries and contribute to solutions to analytical challenges across multiple disciplines.Presenter:&nbsp;Jeff Goshawk (Consulting Scientist, Waters Corporation)Jeff is a Consulting Scientist at Waters Corporation and has been with the company for twenty-four years. Jeff started his career at Waters as a software developer working on MassLynx and its associated application managers. Jeff subsequently transitioned into the applications development group where he joined the toxicology team as a Principal Scientist. Jeff is now back in the software development world at Waters, and is currently working on the Pattern Analysis Application.Presenter:&nbsp;Frank L. Dorman, PhD, FRSC (Principal Environmental Market Manager, Waters Corporation)Frank Dorman is currently Senior Business Development Manager for Waters focusing on their global environmental business and, concurrently, Associate Professor (adjunct) in the Department of Biochemistry and Molecular Biology (BMB) at Penn State University in University Park, PA. In his role at Waters, Frank manages the research-focused environmental market, external collaborations and also interfaces with R&amp;D for new product development. Prior to Waters, Frank was employed full-time as a tenure-line Faculty member of Penn State and served as a member of the Graduate Faculty in: Biochemistry, Microbiology and Molecular Biology (BMMB), Chemistry (CHEM) and the Programs in Forensics Science (FRNSC), and Biogeochemistry (BGC). Frank is also a member of the Center for Molecular Toxicology and Carcinogenesis at Penn State. Frank’s scientific interests are in gas and liquid chromatography fundamental characterization, instrumentation and column development, as well and mass spectrometry and atomic spectroscopy as applied to trace analysis in complex sample matrices. This work is directed towards environmental forensics, traditional forensic chemistry and where environmental exposure events may contribute to human disease; an area sometimes referred to as “exposomics”.Prior to joining the faculty at PSU, Frank was at Restek Corporation for 14 years as the Director of Technical Development, and R&amp;D Senior Chemist. During most of this same time, Frank was also an Adjunct Research Professor at Juniata College where he maintained an active undergraduate research program. Prior to that he was at Inchcape Testing Services for 5 years as a Senior Chemist, Organics Section Manager for Sample Preparation and Corporate Methods Development Chemist. As such, Frank has extensive experience in both the Industrial and Academic sectors giving him a relatively rare combination of skills and experience.</blockquote>

Waters Corporation: Innovative Approaches in HRMS and Software for PFAS Analysis

Innovative Approaches in HRMS and Software for PFAS Analysis

Learn how these cutting-edge approaches are revolutionizing PFAS detection and analysis, offering more accurate and efficient solutions.

<div class="summary-section section" style="-webkit-text-stroke-width:0px;background-color:rgb(255, 255, 255);box-sizing:border-box;color:rgb(51, 51, 51);font-family:&quot;Segoe UI&quot;, Frutiger, &quot;Frutiger Linotype&quot;, &quot;Dejavu Sans&quot;, &quot;Helvetica Neue&quot;, Arial, sans-serif;font-size:14px;font-style:normal;font-variant-caps:normal;font-variant-ligatures:normal;font-weight:400;letter-spacing:normal;margin-bottom:34px;orphans:2;text-align:start;text-decoration-color:initial;text-decoration-style:initial;text-decoration-thickness:initial;text-indent:0px;text-transform:none;white-space:normal;widows:2;word-spacing:0px;">This interactive session will bring together the MS community to discuss some of the most popular and exciting peer-reviewed publications in a friendly and open forum. Ahead of each meeting, we will send out a link to the discussion article, then during the session an expert will summarise the main findings and answer your questions.<h5 style="margin-left:0px;">Be prepared make sure you read&nbsp;<a style="box-sizing:border-box;color:rgb(66, 139, 202);text-decoration:none;user-select:auto;" target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acscentsci.0c00049" fr-original-style="">Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy</a></h5>We're going to be joined by Dr Rebecca Beveridge from the University of Strathclyde, a senior lecturer with a host of experience with development of native ion mobility mass spectrometry methods to study proteins and protein complexes&nbsp;This paper describes how Waters' SYNAPT MS can be utilized&nbsp;demonstrate the strength of native mass spectrometry to delineate the complex binding mechanisms of protein degraders, involving the formation of three-component protein−ligand complexes.<h5 style="margin-left:0px;">Reasons to Attend:</h5><ul style="box-sizing:border-box;margin-bottom:10px;margin-top:0px;"><li style="box-sizing:border-box;">Debate some of the most topical papers from all-time favourites to some of the latest releases &nbsp;</li><li style="box-sizing:border-box;">Focus on understanding the benefit of SYNAPT MS and how to get the most out of the system for native mass spectrometry and biomolecule analysis &nbsp;</li><li style="box-sizing:border-box;">Gain a greater understanding of applications and technologies by asking questions of the authors and/or expert panel &nbsp;</li><li style="box-sizing:border-box;">No pre-recorded content, authors will be LIVE and on camera to answer questions</li></ul>Abstract&nbsp;Protein degraders, also known as proteolysis targeting chimeras (PROTACs), are bifunctional small molecules that promote cellular degradation of a protein of interest (POI). PROTACs act as molecular mediators, bringing an E3 ligase and a POI into proximity, thus promoting ubiquitination and degradation of the targeted POI. Despite their great promise as next-generation pharmaceutical drugs, the development of new PROTACs is challenged by the complexity of the system, which involves binary and ternary interactions between components. Here, we demonstrate the strength of native mass spectrometry (nMS), a label-free technique, to provide novel insight into PROTAC-mediated protein interactions. We show that nMS can monitor the formation of ternary E3-PROTAC-POI complexes and detect various intermediate species in a single experiment. A unique benefit of the method is its ability to reveal preferentially formed E3-PROTAC-POI combinations in competition experiments with multiple substrate proteins, thereby positioning it as an ideal high-throughput screening strategy during the development of new PROTACs<div style="box-sizing:border-box;clear:both;">&nbsp;</div><div class="speaker-fields-container" style="box-sizing:border-box;padding-top:5px;"><div class="section" style="box-sizing:border-box;margin-bottom:34px;"><div class="sp-begin" style="box-sizing:border-box;clear:both;color:rgb(0, 0, 0);font-size:14px;"><blockquote><div style="box-sizing:border-box;">Presenter: Dr Rebecca Beveridge (Senior Lecturer, University of Strathclyde)</div><div style="box-sizing:border-box;">&nbsp;</div><div style="box-sizing:border-box;">Rebecca is a Senior Lecturer and UKRI Future Leaders Fellow who joined the University of Strathclyde in June 2020 as a Chancellor's Fellow. She obtained a BSc in biochemistry and chemistry from the University of Leeds in 2011 and completed her PhD at the University of Manchester in 2015. Rebecca spent 4 years at the Institute for Molecular Pathology in Vienna, Austria as a postdoctoral researcher/ Lise Meitner Postdoctoral Fellow. Throughout her career, she has collected experience in a plethora of mass spectrometry methods to study protein structure such as native mass spectrometry, ion mobility, hydrogen-deuterium exchange, and crosslinking.</div>Rebecca’s current research is centered around the development of native ion mobility mass spectrometry methods to study proteins and protein complexes, particularly those that are challenging to study with conventional biochemistry methods.Such systems include intrinsically disordered proteins that exist in a wide range of different shapes, and protein complexes formed by protein-degrading molecules such as PROTACs, the complex binding modes of which are challenging to delineate.</blockquote></div></div></div></div>

Waters Corporation: Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy

Native Mass Spectrometry Can Effectively Predict PROTAC Efficacy

Discuss some of the most popular and exciting peer-reviewed publications in a friendly and open forum.

LCMS webinars focusing on LC/HRMS - page 26