<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

Article

Product

Application

Academy

Poster

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

LabRulez

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

Phenomenex

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

KNAUER

New Food magazine

Agilent Technologies

Bruker

SCIEX

<p><strong>Have you ever wondered if you have unlocked every feature of you LC/MS system and software? Ever thought about what extra resources Agilent has to offer?</strong></p>
<p>Tips and tricks will be shared for both triple quad and Q-TOF users, alike. All experience levels will learn something new in this review that will include live demonstrations of some of our software features in Mass Hunter Acquisition, Qual, and Quant. Don’t miss this opportunity to gain new information that could have big impact on your projects! </p>
<blockquote>
<p><strong>Presenter: Karen Yannell (LC/MS Application Engineer, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Karen E. Yannell is a LC/MS Application Engineer at Agilent Technologies. She is an expert in small molecule high throughput analysis by triple quadrupole (TQ) and quadrupole time-of-flight (QTOF) mass spectrometry for applied markets. Her recent work has focused on developing routine Q-TOF workflows for both expert and non-expert users alike. Previously, Karen worked on forensic, metabolomics, and biomarker discovery applications with ambient ionization sources. She received her PhD in Analytical Chemistry from Purdue University where studied under the advisement of Prof. R. Graham Cooks. Outside of the laboratory, she enjoys cooking unique dishes and hiking along the beach with her dog.</p>
</blockquote>


Agilent Technologies: Agilent's Hidden Gems

Agilent's Hidden Gems

<p><strong>As food and environmental safety is larger driven by regulations, identification and quantification of contaminants is vital to meet those requirements and to ensure the safety of consumers.</strong></p>
<p>Food businesses are responsible for complying with maximum residue levels (MRLs) for the food they produce and import, meaning stringent quality and food safety standards should be set and met by all.</p>
<p>In this webinar, the capabilities of the SCIEX 7600 system are demonstrated when conducting a highly multiplexes analysis of 271 pesticide analytes in an olive oil matrix. With new developments in technology aiding accuracy and confidence in food and environmental sample analysis, discover how this workflow could be the solution to the challenges your lab may face.</p>
<h3><strong>Key learning objectives:</strong></h3>
<ul>
<li>Learn about recent advances in food testing, with particular focus on pesticide in an olive oil matrix</li>
<li>Discover how you can improve targeted analysis workflows with increased sensitivity</li>
<li>Find out the benefits of our technology, which performs in linearity, reproducibility, mass accuracy, library spectra and ion ratio</li>
<li>Uncover the wonders of SCIEX OS for data processing techniques for targeted analysis</li>
</ul>
<blockquote>
<p><strong>Presenter: Daniel McMillan (Senior Market Development Manager, food and environmental, SCIEX)</strong></p>
</blockquote>
<blockquote>
<p>Daniel McMillian has been working in the mass spectrometry (MS) industry for more than 20 years as an instrument and applications specialist. He is now responsible for developing the food, environmental and cannabis markets throughout the EMEAI region at Sciex. </p>
</blockquote>
<blockquote>
<p>Daniel has worked with major research and regulatory organisations to develop new applications in line with legislation, traditionally in the area of contaminant analysis.</p>
</blockquote>
<blockquote>
<p>In his current role, he focuses on the development of relevant solutions for the industry’s biggest challenges.</p>
</blockquote>


Pixabay/Erich Westendarp: Pesticide residues – we’re on to you!

Pesticide residues – we’re on to you!

<p>Our events will take place starting on Sunday, October 31st at 8:30 am with our <strong>Virtual eXceed Symposia</strong> then Monday through Thursday starting at 7:00 am with our <strong>Virtual Breakfast Workshops</strong> focusing on Proteomics, Pharma/BioPharma, Imaging/SpatialOMx® and Metabolomics. All sessions include live Q&amp;A.</p>
<p>Be sure to also stop by and visit our <strong>booth #719</strong> if you are attending ASMS in person, where we will feature our new timsTOF SCP, or request a private demo of our newest software.</p>
<p>We are doing everything we can to ensure that everyone has access to the information we are providing either in person or virtually.</p>
<h5><strong>13:00 - 13:05 (CEST - Prague) PaSER in Proteomics on the timsTOF Pro</strong></h5>
<ul>
<li>Chris Adams, Ph.D. (Business Development Director, Global Bioinformatics, Life Science Mass Spectrometry, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>
<h5><strong>13:05 - 13:20 (CEST - Prague) Proteomic Analysis of SARS-CoV-2 Infection of Airway Epithelial Cells</strong></h5>
<ul>
<li>Prof. Peter Jackson, Ph.D. (Baxter Laboratory for Stem Cell Biology, Department of Microbiology &amp; Immunology, Stanford University School of Medicine, CA, USA - Bio)</li>
</ul>
<h5><strong>13:20 - 13:30 (CEST - Prague) Engineered multi-nanoparticle panel enabling unmatched depth and sensitivity in plasma proteomics in combination with the timsTOF SCP</strong></h5>
<ul>
<li>Shadi Ferdosi, Ph.D. (Scientist, Seer, USA - Bio)</li>
</ul>
<h5><strong>13:30 - 13:40 (CEST - Prague) Transformers: Rise of the Attention-based Network</strong></h5>
<ul>
<li>Patrick Garret (Graduate student, Dr. John Yates Lab, The Scripps Research Institute, La Jolla, CA, USA - Bio)</li>
</ul>
<h5><strong>13:40 - 13:50 (CEST - Prague) Cross-platform evaluation of accuracy and precision for DIA methods on the timsTOF SCP and timsTOF Pro</strong></h5>
<ul>
<li>Sebastian Vaca, Ph.D. (Research Scientist, Proteomics Platform, Broad Institute of MIT and Harvard, Cambridge, MA, USA - Abstract)</li>
</ul>
<h5><strong>13:50 - 14:05 (CEST - Prague) Evaluation of the timsTOF SCP for immunopeptidome applications</strong></h5>
<ul>
<li>Susan Klaeger, Ph.D. (Research Scientist, Proteomics Platform, Broad Institute of MIT and Harvard, Cambridge, MA, USA - Abstract)</li>
</ul>
<h5><strong>14:05 - 14:10 (CEST - Prague) Live Q &amp; A</strong></h5>
<ul>
<li>Chris Adams, Ph.D. (Business Development Director, Global Bioinformatics, Life Science Mass Spectrometry, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>


Bruker: Bruker's Virtual Breakfast Workshop - Proteomics

ASMS 2021 -Bruker's Virtual Breakfast Workshop - Proteomics

ASMS 2021 -Bruker's Proteomics

<p>Our events will take place starting on Sunday, October 31st at 8:30 am with our <strong>Virtual eXceed Symposia</strong> then Monday through Thursday starting at 7:00 am with our <strong>Virtual Breakfast Workshops</strong> focusing on Proteomics, Pharma/BioPharma, Imaging/SpatialOMx® and Metabolomics. All sessions include live Q&amp;A.</p>
<p>Be sure to also stop by and visit our <strong>booth #719</strong> if you are attending ASMS in person, where we will feature our new timsTOF SCP, or request a private demo of our newest software.</p>
<p>We are doing everything we can to ensure that everyone has access to the information we are providing either in person or virtually.</p>
<h5><strong>13:00 - 13:05 (CEST - Prague) Introduction</strong></h5>
<ul>
<li>Michael Greig, Ph.D. (Director, Pharma/BioPharma Americas, Bruker Daltonics, Billerica, MA, USA )</li>
</ul>
<h5><strong>13:05 - 13:30 (CEST - Prague) A Multiomics Method Enabled by Sequential Metabolomics and Proteomics for Human Pluripotent Stem Cell-Derived Cardiomyocytes</strong></h5>
<ul>
<li>Elizabeth Bayne (Ph.D. Candidate,  Ying Ge Lab, Department of Chemistry, University of Wisconsin, Madison, WI, USA - Abstract and Bio)</li>
</ul>
<h5><strong>13:30 - 13:40 (CEST - Prague) A Gateway to Mass Spectrometry – The SampleStream Platform for Biomolecular Purification</strong></h5>
<ul>
<li>Philip D. Compton, Ph.D. (CEO, Integrated Protein Technologies, Inc., Evanston, IL, USA, Instrumentation Director, Northwestern Proteomics, Research Associate Professor, Chemistry, Northwestern University, Evanston, IL, USA - Bio)</li>
</ul>
<h5><strong>13:40 - 13:48 (CEST - Prague) A New Microflow LC-MS Platform for Native Mass Spectrometry</strong></h5>
<ul>
<li>Daojing Wang, Ph.D. (Founder &amp; CEO, Newomics, Inc., Berkeley, CA, USA - Bio)</li>
</ul>
<h5><strong>13:48 - 13:53 (CEST - Prague) Accelerating Biologics Development with Ultra High-Resolution LC/MS</strong></h5>
<ul>
<li>Na Pi Parra, Ph.D. (Co-Founder &amp; Executive Vice President of Marketing at LiVeritas Biosciences, Daly City, CA, USA - Bio)</li>
</ul>
<h5><strong>13:53 - 14:01 (CEST - Prague) Bead Assisted Mass Spectrometry ( BAMS™ ) for Targeted Proteomics: Single Bead Multiplexed Immunoassay Platform with MALDI MS Detection</strong></h5>
<ul>
<li>Jeff Silva, Ph.D. (Director of Product Development, Adeptrix Corporation, Product Development, Beverly, MA, USA)</li>
</ul>
<h5><strong>14:01 - 14:09 (CEST - Prague) Meeting challenges of analytical testing for pharmaceutical industry with speed, selectivity, and versatility, from small molecules to biologics to cell-gene therapy, with ZipChip/timsTOF</strong></h5>
<ul>
<li>Kate Yu, Ph.D. (Director of Applications, 908 Devices, Boston, MA, USA - Bio)</li>
</ul>
<h5><strong>14:09 - 14:20 (CEST - Prague) Live Q&amp;A</strong></h5>
<ul>
<li>Michael Greig, Ph.D. (Director, Pharma/BioPharma Americas, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>


Bruker: ASMS 2021 - Bruker's Virtual Breakfast Workshop – Pharma/BioPharma

ASMS 2021 - Bruker's Virtual Breakfast Workshop – Pharma/BioPharma

ASMS 2021 - Bruker's Pharma/BioPharma

<p>Our events will take place starting on Sunday, October 31st at 8:30 am with our <strong>Virtual eXceed Symposia</strong> then Monday through Thursday starting at 7:00 am with our <strong>Virtual Breakfast Workshops</strong> focusing on Proteomics, Pharma/BioPharma, Imaging/SpatialOMx® and Metabolomics. All sessions include live Q&amp;A.</p>
<p>Be sure to also stop by and visit our <strong>booth #719</strong> if you are attending ASMS in person, where we will feature our new timsTOF SCP, or request a private demo of our newest software.</p>
<p>We are doing everything we can to ensure that everyone has access to the information we are providing either in person or virtually.</p>
<h5><strong>13:00 - 13:05 (CEST - Prague) Introduction</strong></h5>
<ul>
<li>Michael Easterling, Ph.D. (Business Unit Manager, Imaging/MRMS, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>
<h5><strong>13:05 - 13:20 (CEST - Prague) Agents of change: Tracking tumor progression with glycan imaging mass spectrometry</strong></h5>
<ul>
<li>Prof. Rick Drake, Ph.D. (Professor, Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, USA)</li>
</ul>
<h5><strong>13:20 - 13:35 (CEST - Prague) What does a renal pathologist do with MALDI (imaging)</strong></h5>
<ul>
<li>Prof. Jan Braesen, Dr. Med. (Nephropathology Unit, Institute of Pathology, Hannover Medical School, Hannover, Germany - Abstract)</li>
</ul>
<h5><strong>13:35 - 13:50 (CEST - Prague) Clinical applications of glycan mass spectrometry imaging</strong></h5>
<ul>
<li>Joseph Ippolito, M.D. Ph.D. (Assistant Professor of Radiology, Medical Director, Center for Clinical Imaging Research, Co-Director, Diagnostic Radiology Residency Research Track, Washington University School of Medicine, St. Louis, MO, USA - Bio)</li>
</ul>
<h5><strong>13:50 - 14:05 (CEST - Prague) Relating single cell function to tissue structure in human tumors using MIBI-TOF</strong></h5>
<ul>
<li>Michael Angelo, M.D. Ph.D. (Assistant Professor, Department of Pathology, Stanford University - Abstract)</li>
</ul>
<h5><strong>14:05 - 14:10 (CEST - Prague) Live Q &amp; A</strong></h5>
<ul>
<li>Michael Easterling, Ph.D. (Business Unit Manager, Imaging/MRMS, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>


Bruker: ASMS 2021 - Bruker's Virtual Breakfast Workshop– Imaging/SpatialOMx

ASMS 2021 - Bruker's Virtual Breakfast Workshop– Imaging/SpatialOMx

ASMS 2021 - Bruker's Imaging/SpatialOMx

<p>Our events will take place starting on Sunday, October 31st at 8:30 am with our <strong>Virtual eXceed Symposia</strong> then Monday through Thursday starting at 7:00 am with our <strong>Virtual Breakfast Workshops</strong> focusing on Proteomics, Pharma/BioPharma, Imaging/SpatialOMx® and Metabolomics. All sessions include live Q&amp;A.</p>
<p>Be sure to also stop by and visit our <strong>booth #719</strong> if you are attending ASMS in person, where we will feature our new timsTOF SCP, or request a private demo of our newest software.</p>
<p>We are doing everything we can to ensure that everyone has access to the information we are providing either in person or virtually.</p>
<h5><strong>13:00 - 13:05 (CEST - Prague) Introduction</strong></h5>
<ul>
<li>Lucy Woods, Ph.D. (Business Unit Manager Phenomics and Metabolomics, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>
<h5><strong>13:05 - 13:25 (CEST - Prague) Mass Spectrometry-Based Imaging to Study Metabolic Crosstalk in Cancer</strong></h5>
<ul>
<li>Prof. Gary Patti, Ph.D. )Professor of Chemistry and of Genetics and Medicine, Michael and Tana Powell Professor of Chemistry, Washington University School of Medicine, St. Louis, MO, USA)</li>
</ul>
<h5><strong>13:25 - 13:45 (CEST - Prague) Applying trapped ion mobility to improve separation of lipids in a pre-cancer cohort</strong></h5>
<ul>
<li>Hannes Röst, Ph.D. (Assistant Professor, Canada Research Chair in Mass Spectrometry-based Personalized Medicine, University of Toronto, Canada)</li>
</ul>
<h5><strong>13:45 - 14:05 (CEST - Prague) Machine Learning-enabled Clinical Metabolomics with Complementary FT-MS Platforms</strong></h5>
<ul>
<li>Prof. Facundo Fernandez, Ph.D. (Vasser Woolley Foundation Chair in Bioanalytical Chemistry, Georgia Institute of Technology, Atlanta, GA, USA)</li>
</ul>
<h5><strong>14:05 - 14:15 (CEST - Prague) Live Q &amp; A</strong></h5>
<ul>
<li>Lucy Woods, Ph.D. (Business Unit Manager Phenomics and Metabolomics, Bruker Daltonics, Billerica, MA, USA)</li>
</ul>


Bruker: ASMS 2021 -Bruker's Virtual Breakfast Workshop – Metabolomics

ASMS 2021 -Bruker's Virtual Breakfast Workshop – Metabolomics

ASMS 2021 -Bruker's Metabolomics

<p><strong>The ever-growing global demand for food supply has led farmers and producers to focus on optimizing yields, frequently using pesticides and other synthetic chemicals, which will unavoidably end up in the food chain. In order to ensure consumer safety and food integrity, testing for adherence to regional and international requirements is necessary to monitor for chemical residues, including pesticides in addition to natural fungal toxins and microbiological hazards.</strong></p>
<p>Traditionally, residue analysis has been performed by triple quadrupole mass spectrometry, due to its sensitivity and quantitative power, and most food laboratories are accustomed to the ease of use and high performance of such instruments. Accurate mass instruments can offer additional levels of confirmation; however, they have traditionally suffered from a lack of sensitivity and precision, especially when performing MS/MS experiments to meet the testing requirements for the regulatory guidelines. The new ZenoTOF 7600 system is set to remove these limitations and open up the technique to labs wishing to increase coverage and confidence in food testing.</p>
<h3><strong>This webinar will cover:</strong></h3>
<ul>
<li>Novel MS technologies to elevate accurate mass sensitivity for MS/MS</li>
<li>The potential of a new fragmentation option for confirmation and identification</li>
<li>Examples of the application to pesticide residue screening and confirmation</li>
</ul>
<blockquote>
<p><strong>Presenter: Daniel McMillan (Snr. Market Development Manager, Food and Environmental, SCIEX)</strong></p>
</blockquote>
<blockquote>
<p>Dan has been working in the MS industry for over 20 years as an instrument and applications specialist and is now responsible for developing the food, environmental and cannabis markets throughout the EMEAI region. He has worked with major research and regulatory organisations to develop new applications in line with legislation, traditionally in the area of contaminant analysis. Dan’s role is now primarily to ensure SCIEX produce relevant solutions and to promote them in industry.</p>
</blockquote>


RAFA 2021: Advancements for food and environmental testing with the ZenoTOF 7600 system

<h4><strong>Using VIP-HESI and Trapped Ion Mobility Spectrometry to improve confidence in identification</strong></h4>
<p>In  the  past  years,  ion  mobility  has  matured  into  an  extremely  valuable  addition  to  high-resolution mass  spectrometry.  Trapped  Ion  Mobility  (TIMS)  technology  ensures  high  resolution  and  highly  accurate  collisional  cross  section  (CCS)  values.  Thus,  this  4th  dimension  is  able  to  filter  out  the  chemical background and separate isobaric co-eluting compounds. The associated CCS values for all detected compounds can be used as an additional criteria for the identification of both knowns and unknowns. As ion mobility becomes more and  more common, the number of CCS references values  in  libraries  and  databases  is  growing  rapidly.  When  used  in  a  targeted  approach,  as  an  additional criteria, CCS values help to increase the reliability of identification and reduce the number of  false  positives,  especially  speeding  up  the  review  of  large  sample  sets.  If  TIMS  is  used  in  combination with the increased sensitivity obtained from a VIP-HESI source then positive identifications is possible at very low level concentrations.  With a duty cycle of 100%, no changes to chromatographic  gradients  are  required  allowing  this  unique  combination  to  provide  analytical  reporting with greater confidence.</p>
<p><strong>Presenter: Dr. Carsten Baessmann (Bruker Daltonics GmbH &amp; Co. KG, Bremen, Germany)</strong></p>
<h4><strong>Workflow for setting up and controlling food authenticity analysis</strong></h4>
<p>Food adulteration and authenticity has a greater interest with the public in general and developments in hardware provides better sensitivity, and more accuracy, in elucidating these topics. Historically, the complexity of the workflow made these analyses a task for specialists. However, due to developments in software workflows, ‘ready-to-go’ solutions have been developed to determine authenticity markers and subsequently use them in a routine process. By having additional separation power  provided  by  Trapped  Ion  Mobility  Spectrometry  (TIMS)  and  better  calculation  algorithms,  minor differences in the food ‘fingerprint’ between different regions of authenticity, or lower levels of adulteration become easier to rapidly discern allowing large numbers of samples to be screened.  Positioning  of  high  through  put  MALDI  and  high  separation  HRMS  will  be  explained  within  this  presentation.</p>
<p><strong>Presenter: Noud van der Borg, Bruker Nederland BV, Leiderdorp, Netherlands)</strong></p>


Bruker/RAFA 2021: Use timsTOF Ion Mobility technology to improve results in Food analysis

RAFA 2021: Use timsTOF Ion Mobility technology to improve results in Food analysis

<p><strong>The authenticity and safety of food are major aspects to ensure consumer trust in food products. Globalized food production and novel foods are constantly challenging the integrity of food.</strong></p>
<p>In this webinar, we provide an introduction to food proteomics as a novel tool in food authenticity and food allergy testing.</p>
<blockquote>
<p><strong>Presenter: Prof. Dr. Jens Brockmeyer (Analytical Food Chemistry, Department of Food Chemistry, University of Stuttgart, Germany)</strong></p>
</blockquote>


Pixabay/Engin Akyurt: Keeping food authentic and safe with protein mass spectrometry

Keeping food authentic and safe with protein mass spectrometry

<h4><strong>Analytical Methods and Control Strategies for Oligonucleotide Therapeutics</strong></h4>
<p>Analytical characterization of biomolecules can be challenging because impurities from the synthesis, expression and degradation of the intended product make the samples complex.  This presentation will provide a broad overview of analytical methods needed to support Critical Quality Attributes (CQA) characterization for oligonucleotide therapeutics. Utilizing the comprehensive set of Agilent analytical products and workflows, biopharmaceutical researchers can efficiently employ Quality by Design (QbD) approaches for their drug development.</p>
<blockquote>
<p><strong>Presenter: Chris Colangelo (Biopharma Business Development Leader, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Christopher Colangelo, PhD, MBA is the Agilent Biopharma Business Development Leader for the Americas. Prior to joining Agilent, he was the 5th employee and co-inventor of the 454-sequencing platform. In 2003, Chris joined Yale University as a Research Faculty in where he mentored and supervised a research group producing 60+ peer-reviewed publications and directed core research laboratories for four NIH P30 grants, totaling over $21 million worth of research funds.</p>
</blockquote>
<h4><strong>Column Considerations for LC-UV Analysis of Oligonucleotides</strong></h4>
<p>To ensure maximum resolution in the analysis of oligonucleotides it is important to balance the impact of the stationary phase with the ability to refine the method parameters.  In this short presentation we will focus on LC-UV approaches for ion-pair reversed-phase separations to improve your analyses.</p>
<blockquote>
<p><strong>Presenter: Andy Coffey, PhD (Senior Applications Scientist, Agilent Technologies)</strong></p>
</blockquote>
<blockquote>
<p>Following his PhD in peptide synthesis, Andrew began his career at Agilent Technologies’ Church Stretton, UK facility over thirty years ago. In August 2011, he became the Senior Applications Chemist for biomolecule chromatography and since then has authored numerous application notes and delivered many seminars and training presentations. His goal is to help customers get the most from Agilent&#39;s Biocolumns portfolio.</p>
</blockquote>
<h4><strong>Analysis of Oligonucleotides Using the Agilent LC-MSD Single Quad Mass Spectrometer</strong></h4>
<p>For the analysis of complex biological molecules like oligos many people assume high-resolution MS is required. There is no doubt the TOF/QTOF will generate higher quality of data and offer many performance advantages, but for many users and applications the LC-MSD can generate fit-for-purpose results at lower footprint and cost. Here we will look at real examples using the LC-MSD as a tool for MW confirmation and purity assessment whether running 1 to 100s of oligo samples per day. Finally, we will stack up the pros and cons of the LC-MSD platform compared to the TOF to help you decide which might be the best fit for your needs.</p>
<blockquote>
<p><strong>Presenter: Richard Blankley Ph.D, Biopharma Application Specialist – Northern Europe, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>As a Biopharma Application Specialist, I spend a lot of time each month helping to develop better workflows for oligo purification and analysis, then get the chance to help support these workflows in customer and collaborator labs. I have been lucky enough to spend nine years here at Agilent.</p>
</blockquote>


LCMS webinars focusing on LC/TOF - page 40