<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

Agilent Technologies

Bruker

Wiley

Shimadzu Corporation

SCIEX

Evosep Biosystems

Waters Corporation

<p><strong>ADCs represent complex biologics combing a targeting antibody molecule with a cytotoxic warhead via a linker system. The design of the linker systems is crucial to ensure the warhead is only released at the target site, whilst enabling conjugation to an active site on the protein.</strong></p>
<p>Mass spectrometry can be utilized in various modalities to monitor loss of payloads when incubated in plasma providing a rapid measurement of relative stability.</p>
<p>This webinar will detail how mass spectrometry is used in ADC development and how the X500B QTOF system represents a versatile platform for measurement of intact, reduced, and digested proteins.</p>
<p>Attend this webinar to:</p>
<ul>
<li><strong>Understand how LC-MS can be used to study the stability of an ADC in plasma</strong></li>
<li><strong>Find out how LC-MS can be used to calculate the antibody drug ratio of an intact ADC</strong></li>
<li><strong>Discover how LC-MS has been used to study the payload release of an ADC</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Chris Nortcliffe (Mass Spectrometry Manager | Sterling Pharma Solutions | UK)</p>
</blockquote>
<blockquote>
<p>Dr Christopher Nortcliffe is the mass spectrometry manager in the UK at Sterling Pharma Solutions, a CDMO pharmaceutical partner company. He has a background in protein and DNA analysis, obtaining his PhD from the University of Manchester on studying noncovalent interactions by mass spectrometry in 2016. After Manchester, Christopher worked for SCIEX as a specialist in LC-MS analysis of biologics before moving to Sterling Pharma Solutions, where he manages the LC-MS service and is an expert in the LC-MS analysis of biotherapeutics and ADCs.</p>
</blockquote>


SCIEX: Use of mass spectrometry to assess plasma stability of Antibody Drug Conjugates

Use of mass spectrometry to assess plasma stability of Antibody Drug Conjugates

How mass spectrometry is used in ADC development and how the X500B QTOF system represents a versatile platform.

Use of mass spectrometry to assess plasma stability of ADCs

<p><strong>Unlock new perspectives with our accurate mass 101 webinar series.</strong></p>
<p>Accelerate your workflows and expand your knowledge around accurate mass with these informative webinars.</p>
<p>In this webinar series, SCIEX applications scientists will explain the benefits of using accurate mass, sample analysis, instrument operation and data processing in real-time.</p>
<p>Get the inside scoop and register today!</p>
<h3><strong>Accurate mass 101: non-targeted analysis</strong></h3>
<p>Join us for this webinar to see how to discover the unknown using non-targeted analysis. We will showcase workflows and strategies to drive success with suspect screening and non-target identification. Discover the ability to identify peaks of interest and confidently identify unknown compounds.</p>


SCIEX: Accurate mass 101: non-targeted analysis

Accurate mass 101: non-targeted analysis

SCIEX applications scientists will explain the benefits of using accurate mass, sample analysis, instrument operation and data processing in real-time.

<p><strong>Unleash the power of DIA and enable the exploration of complex biological systems with unprecedented depth and precision for large-scale quantitative protein analysis combined with short methods on the Evosep One.</strong></p>
<h3><strong>Global proteomics with Evosep and DIA-PASEF</strong></h3>
<p>Recent progress in liquid chromatography and mass spectrometry, as well as sample preparation and search algorithms for spectra deconvolution and identification, plays an important role in bringing proteomics to the forefront of drug discovery and development. Nanoflow liquid chromatography coupled to tandem mass spectrometry is one of the most essential elements in a proteomics workflow. The four dimensional ion detection achieved with the latest generation of Bruker’s trapped ion mobility spectrometers led to superior speed and sensitivity. Evosep One liquid chromatography platform offers speed and robustness while maintaining, even exceeding previously achieved performance level with high-performing nano LC systems. We share here some results only possible with this combination of LC-MS and dia-PASEF.</p>
<blockquote>
<p><strong>Presenter:</strong> Anh Reynolds (Scientist, Bristol Myers Squibb)</p>
</blockquote>
<h3><strong>Extending sensitivity limits with Evosep and Slice-PASEF</strong></h3>
<p>Sensitivity improvements in LC-MS proteomics have recently led to exciting new applications, such as comprehensive proteomic profiling of single cells or 2-dimensional proteomics of tissue slices. In this talk, I will describe Slice-PASEF, a new acquisition technology for timsTOF instruments, which, in combination with the DIA-NN data analysis software, provides a fold-change signal boost. When paired with the Evosep system, Slice-PASEF allows to achieve high sensitivity in robust high-throughput workflows, paving a way for accessible sensitive proteomics on a large scale.</p>
<blockquote>
<p><strong>Presenter:</strong> Vladim Demichev (Group Leader, Quantitative ProteomicS, Charité – Universitätsmedizin Berlin)</p>
</blockquote>


Pixabay/sethink: Revolutionizing proteomics with Evosep-DIA

Revolutionizing proteomics with Evosep-DIA

Global proteomics with Evosep and DIA-PASEF & Extending sensitivity limits with Evosep and Slice-PASEF.

<p><strong>Cell line development scientists and upstream bioprocess engineers aim at optimizing biotherapeutics production processes to maximize drug product quality, yield, and manufacturing efficiency. Currently, information on critical process and product attributes required for informed decision making is often insufficient and not readily available. This has a negative impact on the process robustness, throughput, and outcome.</strong></p>
<p>Direct measurement of cell culture media and product quality attributes (PQAs) has recently been offered thanks to the Waters BioAccord™ LC-MS system with dedicated workflows for process analytics of biopharmaceuticals. The BioAccord™ LC-MS can be directly coupled to multi parallel bioreactor systems, like the Sartorius Ambr® 15 or 250 HT platforms, for accelerated process development. </p>
<p>With this integrated solution, process engineers have direct access to the information they need to be in control: drug substance quality and yield can be maximized, process and product related impurities minimized, and more robust processes can be developed, thereby de-risking batch failure. This ultimately results in accelerated drug product development and manufacturing release from months or weeks to days, saving time and resources but more importantly enable faster delivery of safer treatments to patients.  </p>
<p>Please join us as Magnus Wetterhall will present how Waters BioAccord™ LC-MS system offer enhanced capabilities for direct measurements of critical process and product quality attributes in cell line and process development and thereby enabling you to make more informed decisions with your own high-quality data. </p>
<blockquote>
<p><strong>Presenter:</strong> Magnus Wetterhall, Ph.D. (Global Marketing Manager – Bioprocessing, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Magnus Wetterhall has more than 25 years’ experience in upstream &amp; downstream bioprocessing, advanced mass spectrometry, biomarker discovery, protein characterization, working at start-ups, large biotech companies as well as academics. Magnus earned his M.Sc. and Ph.D. degree in analytical chemistry at Uppsala University, Sweden. He has published over 40 scientific papers and 50 posters in the areas of mass spectrometry, biomolecule characterization and bioseparations, and has been an invited presenter at national and international conferences on these topics. He is currently the Global Marketing Manager at Waters Corporation – Bioprocessing, where he is dedicated to deliver analytical solutions to advance upstream and downstream bioprocess.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Terence Teo (BioPharma/BMR Market Development Manager, APAC, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Terence Teo has more than 15 years of experience in bioprocessing, specializing in downstream processing R&amp;D during the early phase of his career before moving to business development roles in GE Life Sciences (now Cytiva), Pall Biotech and most recently, Waters Corporation. Terence is motivated in supporting regional customers in APAC with technologies enabling continuous bioprocessing. He is currently working actively in Waters to drive the use of LC-MS analytical solutions to support near real-time CQA measurement in bioprocess applications, as well as use of LC-MS in multi-attribute method (MAM) and emerging drug modalities such as mRNA and viral vectors. Terence earned his M.Eng degree in Chemical and Biomolecular Engineering at National University of Singapore (NUS).</p>
</blockquote>


Waters Corporation: Accelerating Upstream Bioprocess Development Through Data Driven Decisions

Accelerating Upstream Bioprocess Development Through Data Driven Decisions

We will present how Waters BioAccord™ LC-MS system offer enhanced capabilities for direct measurements of critical process and product quality attributes.

Accelerating Upstream Bioprocess Development

<p><strong>While the application of Mass Spectrometry (MS) Imaging is rapidly growing, its usage is largely limited to experienced scientists. Shimadzu’s Benchtop MALDI-TOF, however, offers a compact, affordable, and user-friendly option to all. Moreover, when combined with the automated matrix applicator (iMLayer suite), our Benchtop MALDI-TOF provides a game-changing solution suitable to all users regardless of skill level.</strong></p>
<p>In this webinar, we will showcase how our workflow offers simplified sample preparation, a complete imaging solution in a compact footprint, an imaging starter kit customizable based on your needs, and intuitive software for data analysis. This workflow will be suitable in research applications from analysis of small molecules such as lipids to large molecules such as protein, peptides, polymers etc.</p>
<p>Join us to learn how you can become an expert in MS imaging with Shimadzu&#39;s MALDI-TOF today.</p>
<p>Learning Objectives:</p>
<ul>
<li><strong>Learn how Shimadzu offers total solutions for MALDI Imaging</strong></li>
<li><strong>Learn about our patented Two-step Vapour Deposition Method for optimal sample preparation</strong></li>
<li><strong>Learn about our user-friendly interface for easy data analysis of MALDI Images</strong></li>
<li><strong>Applications of Shimadzu&#39;s Benchtop MALDI Imaging suite</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Naatasha Isahak (Product Specialist, Shimadzu (Asia Pacific) Pte Ltd)</p>
</blockquote>
<blockquote>
<p>Naatasha Isahak is a Product Specialist for MALDI and Life Sciences Products from Shimadzu Asia Pacific Pte Ltd. She has received her PhD from the University of Sydney (Chemistry) working on surface initiated polymerisation on silica nanoparticles using RAFT polymerisation and bioorthogonal conjugation of peptides using Native Chemical Ligation. She then spent 5 years working on developing platforms for stem cells and organoids characterization that included working with microfluidic devices and helical polymers. Naatasha joined Shimadzu in 2022 to expand her experiences to MALDI characterization on materials and biological samples.</p>
</blockquote>


Shimadzu: MALDI-Imaging For All: A Researcher’s Guide

MALDI-Imaging For All: A Researcher’s Guide

Join us to learn how you can become an expert in MS imaging with Shimadzu's MALDI-TOF today.

<p>Dear user and other PaSER interested customers,</p>
<p>You are hereby invited to our 2nd Virtual PaSER Workshop. A lot of new possibilities has been introduced since last time – including, but not limited to PaSER Novor for de novo sequencing of dda-PASEF® data on the PaSER Box as well as TIMS DIA-NN 2.0 -which will be demonstrated during this Workshop. Data virtualization has been a requested feature – and this is now possible with Mass Dynamics for PaSER. Not limited to above – stay tuned for even more approaching features, we will discuss as well.</p>
<h3><strong>The tentative agenda looks like this:</strong></h3>
<h5><strong>1:00 – 1:15 pm:  Introduction</strong></h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
<h5><strong>1:15 – 1: 35pm:  New Applications on the timsTOF Platform</strong></h5>
<ul>
<li>Lars Kristensen (Field Application Specialist)</li>
</ul>
<h5><strong>1:35 – 1:55 pm:  PaSER as a bioinformatic platform - what’s new and what’s coming</strong></h5>
<ul>
<li>Jonathan Krieger (Software R&amp;D Department)</li>
</ul>
<h5><strong>5 minute break</strong></h5>
<h5><strong>2:00 – 2:20 pm: Live Demo/workshop of PaSER</strong></h5>
<ul>
<li>Tharan Srikumar (Software R&amp;D Department)</li>
</ul>
<h5><strong>2:20 – 2:50 pm: Mass Dynamics</strong></h5>
<ul>
<li>Mark Condina and Giuseppe Infusini</li>
</ul>
<h5><strong>2:50 – 3:10 pm: Questions and discussions</strong></h5>
<h5><strong>3:10 – 3:15 pm:  Conclusion</strong></h5>
<ul>
<li>Willy Bjørklund</li>
</ul>
<p>We aim for a lively interaction so take the timing as an indication. Please feel free to share with colleagues or others you think could benefit from attending this workshop. Looking forward to “meet”</p>


Bruker Virtual PaSER Workshop

Dear user and other PaSER interested customers, You are hereby invited to our 2nd Virtual PaSER Workshop. 

<p><strong>This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results. An emphasis will be spent on an End-to-End HILIC metabolomics workflow for our LC/Q-TOF platform.</strong></p>
<p>This includes automate sample preparation for cells and plasma, a Bio LC that is fit for purpose for metal sensitive analysis, robust and transferable HILIC chromatography, the 6546 LC/Q-TOF data independent analysis of samples, with an ID workflow that includes a new HILIC PCDL with 500 core metabolism analytes with spectra and retention time annotation.</p>
<p>For unknowns not found in Agilent PCDLs, SIRIUS/CSI:FingerID which uses AI predict structure from spectra and conducts online identification search will be demonstrated. A complementary targeted multi-omics workflow will be briefly mentioned before sharing the new Ion Mobility and ExD technologies for high end LC/MS Omics investigations.</p>
<blockquote>
<p><strong>Presenter:</strong> Karen E. Yannell (Omics Workflow Specialist, Agilent Technologies)</p>
</blockquote>
<blockquote>
<p>Karen E. Yannell is an Omics Workflow Specialist at Agilent Technologies. She is an expert in small molecule high throughput analysis by triple quadrupole (TQ) and quadrupole time-of-flight (Q-TOF) mass spectrometry for applied markets. Her recent work has focused on developing targeted metabolomics methods and 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. </p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Martin Graf-Utzmann (Editor, Wiley Analytical Science, Moderator)</p>
</blockquote>
<blockquote>
<p>Dr. Martin Graf-Utzmann has a Ph.D. in Theoretical Chemistry and is an editor for Wiley Analytical Science. His interests are mainly Laboratory Automation, Digitalization, and Lab Equipment.</p>
</blockquote>


Wiley Analytical Science: Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

Jump Start Your LC/Q-TOF Omics Investigation with Reliable Workflows

This webinar will focus on untargeted LC/MS Omics solutions that will provide the biological insights needed to produce meaningful results.

Your LC/Q-TOF Omics Investigation with Reliable Workflows

<p><strong>Thousands of polymeric compounds and materials have been developed over the years to optimize the properties and performance of products spanning nearly every industry.   There are a few areas where characterizing these products can be important: first is performing a quick polymer identification for recycling purposes; second is quality control to identify product defects or failures; and third is reverse engineering to facilitate product development in a highly competitive marketplace.</strong></p>
<p>Infrared (IR) and Raman spectroscopy are especially useful for the analysis of polymers in an industrial setting because in most cases it does not require sample preparation or expensive consumables. Examples will be presented demonstrating the effectiveness of IR and Raman analysis in each of these categories.</p>
<p>Mass Spectrometry (MS) has become an indispensable tool for polymer analysis and has been widely used to study polymer structure and composition, end groups and additives, molecular weight distribution, and so on. MS analysis is extremely sensitive, allowing the detection and identification of minor polymer components and synthesis by-products, as well as low-level impurities and products of decomposition. Matrix Assisted Laser Desorption Ionization (MALDI) allows performing rapid MS analysis without lengthy pre-separation and with minimal sample preparation. MALDI MS can provide structural and copolymer composition information, as well as be used for imaging of polymer surfaces, characterization of complex polymer mixtures, and many other analytical tasks.</p>
<p>In this webinar, we will discuss several MS analytical techniques and their applications for polymer analysis using real-life examples from the industry and academia.</p>
<blockquote>
<p><strong>Presenter:</strong> Sergey V. Shilov, Ph.D. (R&amp;D Product Manager for North America, Bruker Optics)</p>
</blockquote>
<blockquote>
<p>Dr. Sergey V. Shilov is the R&amp;D Product Manager for North America at Bruker Optics. Sergey joined Bruker in 2001. He is responsible for the support and development of new applications for the Bruker research FTIR systems. He received his Ph.D in 1992 from the Russian Academy of Sciences in Polymer Physics and his M.S. from St. Petersburg State University (Russia) in Physics in 1986. Alexander Von Humboldt foundation (Germany) awarded him research fellowship in 1996. Sergey published 37 papers in peer-reviewed journals. His research interests include time-resolved FTIR spectroscopy, surface science, polymer and life-science applications. </p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Kushal Modi (Business Development Manager, Polymers, and Industrial Chemicals, Bruker Applied Mass Spectrometry)</p>
</blockquote>
<blockquote>
<p>Kushal Modi has been serving the scientific community for over 10 years. He joined Bruker in 2022 under the Applied Mass Spectrometry division after a legacy with Waters Corporation. He is a leading expert as a Business Development Manager and is currently supporting the polymers and industrial chemical markets nationally.  </p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Rebecca Pool (Editor Microscopy and Analysis, Wiley, Moderator)</p>
</blockquote>
<blockquote>
<p>Rebecca is news editor of Microscopy&amp;Analysis and a freelance science journalist with a doctorate in Materials Science. She has published in Wiley Analytical Science, Nature Photonics, SPIE Photonics Focus, Physics World, Sci Fi Generation, Engineering and Technology magazine, WorldSteel and more.</p>
</blockquote>


Wiley Analytical Science: Effective Analysis of Polymers Using IR, Raman Spectroscopy, and MALDI-TOF Mass Spectrometry

Effective Analysis of Polymers Using IR, Raman Spectroscopy, and MALDI-TOF Mass Spectrometry

Examples will be presented demonstrating the effectiveness of IR and Raman analysis and will discuss several MS techniques and apps for polymer analysis.

Polymers Using IR, Raman Spectroscopy, and MALDI-TOF MS

<ul>
<li><p>Wait what?! Who knew!? There are so many things that a mass spec can do.</p>
</li>
<li><p>I&#39;ve used it for years, yes this may be true.</p>
</li>
<li><p>I&#39;ve processed some samples, more than a few.</p>
</li>
<li><p>But between me and you, I had no idea all the things it could do!</p>
</li>
<li><p>From sample prep to separation, you just won&#39;t believe…</p>
</li>
<li><p>All of the tips and tricks we have up our sleeve.</p>
</li>
<li><p>So, take a few minutes, about 15 should do.</p>
</li>
<li><p>And learn all the things your mass spec can do.</p>
</li>
</ul>
<p><strong>An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented.  Scan speeds for reproducible quantitation, chromatographic resolution, retention time definition, proper threshold adjustment for optimum datafile size, and how this can result in faster processing times will all be discussed.</strong></p>
<blockquote>
<p><strong>Presenter:</strong> Rebecca Glaskin, Ph.D. (LC/MS Application Scientist, Agilent Technologies, Inc.)</p>
</blockquote>
<blockquote>
<p>Rebecca Glaskin is an LC/MS Application Scientist at Agilent with a focus on BioPharma applications supporting the LC-Q/TOF and IM-QTOF platforms. Prior to joining Agilent, Rebecca received her Ph.D. in analytical chemistry from Indiana University in the lab of Professor David Clemmer. While there she designed and constructed home-built instruments, pushing the limits of the mobility resolution that can be obtained with a circular drift tube for the separation of biomolecules (peptides, proteins, carbohydrates, and metabolites). While there, she also studied hydrogen/deuterium exchange of proteins in the gas-phase as a function of time and pressure. Rebecca then went to Boston University as a Postdoctoral Associate in the lab of Professor Catherine Costello to develop a database containing collision cross section values for glycans, peptides, and glycopeptides utilizing Agilent Technologies 6560 IM-QTOF. This database can be used to determine how the collision cross section is altered with the addition of individual saccharide units. The trendlines obtained from this database will be used to predict collision cross sections for glycopeptides based on the conformation and structure of the specific glycoform.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Jim Lau, PhD (HRAMS LC/MS Application Engineer, Agilent Technologies, Inc.)</p>
</blockquote>
<blockquote>
<p>Jim Lau received his Ph.D. From the University of Colorado. There he worked in the laboratories of Peter Albersheim and Robert Shapiro. This work involved the structure elucidation of plant natural products and, in particular, elucidating the structures of oligosaccharides derived from plant cell wall polysaccharides. This work was done in the early days of LCMS and made use of DLI-LCMS and (at the time) recently invented Thermospray-LCMS.</p>
</blockquote>
<blockquote>
<p>After the completion of his Ph.D., Jim joined Hewlett-Packard to work on LCMS ionization techniques with Paul Goodley during the early days of Electrospray-LCMS. He then moved to work on field applications and collaborations with Hewlett-Packard’s LCMS customers. More than 30 years later, Jim continues to work with Agilent’s customers in High Resolution Accurate Mass applications of LCMS. While involved in many areas of HRAMS LCMS, his recent work has focused on the area of Screening/Qual&amp;Quant of small molecules and on the high throughput confirmation of oligonucleotide synthesis.</p>
</blockquote>


Agilent Technologies: How to set MS Scan Parameters for your LCMS Experiment

How to set MS Scan Parameters for your LCMS Experiment

An easy to follow guide detailing how to set MS scan parameters for an LCMS experiment will be presented.

<p>Webinar in collaboration with the Polish Society of Metabolomics.</p>
<h3><strong>14:00 - 14:20 Benefits of Trapped Ion Mobility Spectrometry (TIMS) for Metabolomics and Lipidomics</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Stefanie Wernisch ( Business Development Manager Metabolomics/Multiomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>After revolutionizing the area of proteomics, trapped ion mobility spectrometry (TIMS) is now conquering the fields of metabolomics and lipidomics. Bruker&#39;s unique timsTOF technology addresses the complexity of biological samples by adding an orthogonal dimension of separation before mass spectrometric analysis, thus reducing the complexity of MS/MS data and improving annotation confidence for untargeted analysis. The ability to determine Collisional Cross Sections (CCS) can further aid identification and outlier detection in lipidomics studies.</p>
<h3><strong>14:20 - 14:40 SpatialOMx® for in-depth 4D-Lipidomics™</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Janina Oetjen (Application Specialist MALDI Imaging, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>The combined possibilities of ESI and MALDI in one instrument enables powerful SpatialOMx® applications. In short, ion mobility-based annotation can connect confident LC-TIMS-MS/MS identification with meaningful spatial information from MALDI Imaging, specifically in the field of lipidomics. Further, segmentation results based on lipid imaging can define specific regions of interest for subsequent, in-depth analysis. Thus, the information content of MALDI Imaging can be enhanced with SpatialOMx® workflows on the timsTOF fleX platform.</p>
<h3><strong>14:40 - 15:00 Application Round-up: 4D-Metabolomics™ and 4D-Lipidomics™</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Matthias Szesny (Application Scientist Metabolomics, Bruker Daltonics Bremen, Germany)</li>
</ul>
<p>We will highlight the capabilities of the timsTOF platform and introduce new applications, method developments, and software solutions in the field of metabolomics and lipidomics. Those help scientists gain a faster and deeper understanding of diverse research areas such as health and disease as well as agriculture.</p>


Bruker: Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Expanding the Horizons of 4D-Metabolomics and 4D-Lipidomics

Benefits of TIMS for Metabolomics and Lipidomics. SpatialOMx for in-depth 4D-Lipidomics, Application Round-up: 4D-Metabolomics and 4D-Lipidomics.

LCMS webinars focusing on LC/TOF - page 28