<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

Separation Science

Agilent Technologies

GERSTEL

SelectScience

C&EN

Shimadzu Corporation

Evosep Biosystems

Waters Corporation

<p><strong>Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.</strong></p>
<p>The PreOmics team will introduce the PreOmics easy-to-use iST technology. This fast 3-step workflow is designed to be a great support for both those new to proteomics and experts alike. The all-in-one iST kits are compatible with a variety of starting materials, including mammalian and plant samples, different types of tissue and cells, as well as various biological fluids in label-free and chemical labelling applications.The protocols promise an incredibly fast processing time (&lt;2.5 hours) and are easily applicable without compromising sample quality or proteomic depth. Furthermore, iST can be fully automated to further increase standardization, reproducibility, and throughput.</p>
<p>The speakers will also introduce PreON, a fully automated sample preparation platform, as well as different levels of automation for established liquid handling platforms. The varying applications for the iST technology ranging from global proteomics to pre-clinical studies will also be discussed.</p>
<h5>Key learning objectives</h5>
<ul>
<li><strong>Discover best practices for proteomics sample preparation with solutions for new users and proteomics experts alike</strong></li>
<li><strong>Learn more about fast, easy, and reliable sample preparation protocols for LC-MS-based proteomics</strong></li>
<li><strong>Explore automation, standardization, and upscaling of proteomics sample preparation</strong></li>
<li><strong>Learn more about the applications of iST sample preparation kits and solutions in global proteomics as well as pre-clinical research</strong></li>
</ul>
<h5>Who should attend?</h5>
<ul>
<li>Users working with proteomics sample preparation for LC-MS:</li>
<li>Researchers, scientists, principal investigators, group leaders and department heads, lab assistants from biotech/pharma industry, CROs, university hospitals as well as academia</li>
<li>Biomedical and clinical scientists in translational and pre-clinical research</li>
<li>Application scientists and technical support</li>
<li>Distributors of sample preparation systems for LC-MS</li>
<li>Scientists looking for a straightforward approach to start with proteomics</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Dr. Ingrid Albrecht-Walz (PreOmics GmbH)</p>
</blockquote>
<blockquote>
<p>Dr. Ingrid Albrecht-Walz joined PreOmics in 2022 as Product Manager for Kits &amp; Reagents. She received her Ph.D. in Biology from the University of Munich, Germany, working on the interaction of different viruses. For the past 10 years, Dr. Albrecht-Walz has worked in the field of in vitro diagnostics of infectious diseases. Since proteomics is a highly promising tool for preclinical and diagnostic applications, Dr. Albrecht-Walz decided in 2022 to follow this opportunity at PreOmics.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Vincenzo Romaniello (PreOmics GmbH)</p>
</blockquote>
<blockquote>
<p>Dr. Vincenzo Romaniello joined PreOmics in 2021 as Product Manager for Automation Systems. He received his Ph.D. in molecular physiology from the University of Göttingen, Germany. During the past 5 years, Dr. Romaniello has worked in both technical and application support roles for automated sample preparation workflows with major biotech and human diagnostics scientific suppliers. As a result, he has experience in PreOmics automation solutions, and Tecan and Eppendorf systems.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Dr. Zuzana Demianova (PreOmics GmbH)</p>
</blockquote>
<blockquote>
<p>Dr. Demianova joined PreOmics in 2021 as a Market Development Manager BioPharma and scientific advisor. Assessing proceedings and challenges in the pharma and biopharma field Dr. Demianova introduces PreOmics’ solutions in customer workflows to enable scientific discovery. She thereby partakes also in the development and market introduction of new products as well as optimization and application of established solutions. Prior to PreOmics, Dr. Demianova was application support specialist at Sciex, concentrating on customer support and training. Later on, she was promoted to a global leader in proteomics, which finally led up to her new role as a biopharma application scientist with a focus on “-omics” and biopharma applications using CE and LC-MS technologies.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Blake Forman (SelectScience)</p>
</blockquote>
<blockquote>
<p>Blake studied chemistry at the University of Surrey, UK, and further went on to study a master’s in chemistry at the University of Southampton, UK. Blake has previously worked in the Medicines and Healthcare Products Regulatory Agency (MHRA) lab at LGC and as a technical sales specialist for Waters. As a member of the Editorial team, he now plays an integral role in shaping the content on SelectScience.</p>
</blockquote>


SelectScience: Next generation solutions for proteomics sample preparation

Next generation solutions for proteomics sample preparation

Join this webinar to learn how to simplify, speed-up, and standardize your proteomics sample preparation for LC-MS.

<p><strong>The webinar will highlight benefits of automation for laboratories with high throughput of samples and laborious manual methods, as well as challenges faced during analysis, including LOQs and matrix factors.</strong></p>
<p>Also discussed will be the method development of a large panel of drugs of abuse, focusing on steps taken to improve recoveries, signal, and RSDs.</p>
<p>The presentation is aimed at laboratories with manual methods looking to improve sample turnaround and reproducibility, and free up time for analysts to perform other important tasks. Laboratories aiming to reach the requested LOQs from the Society of Hair Testing (SOHT) through improvements in sample cleanup will find this presentation of value.</p>
<h5>By attending this presentation you will learn about:</h5>
<ul>
<li><strong>a streamlined and automated method for the extraction of drugs of abuse in hair</strong></li>
<li><strong>the benefits of automation and using the Biotage workflow</strong></li>
<li><strong>a method capable of reaching the required LOQs for hair analysis</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Thomas Smith (Applications Laboratory Team Leader, Biotage)</p>
</blockquote>
<blockquote>
<p>Thomas began his career at Biotage in July 2022 as Applications Laboratory Team Leader. Prior to this, he worked in a UKAS accredited hair analysis laboratory, beginning as a laboratory analyst and working up to R&amp;D team leader. Thomas&#39;s main task was to develop a streamlined and automated method for extracting a large panel of drugs of abuse from hair to help laboratory process with a growing number of samples.</p>
</blockquote>


LabRulez: Selected Applications for Drugs of Abuse Analysis in Hair

Selected Applications for Drugs of Abuse Analysis in Hair

Automation for laboratories with high throughput of samples and laborious manual methods and challenges including LOQs and matrix factors.

<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>The Automated Liquid Sampler (ALS) you have in your LCMS stack can simplify menial tasks. The parameters available in the ALS setup tab and the Sample Pretreatment tab allow the ALS to perform many labor saving functions related to sample prep for LCMS. Examples of functions like internal standard addition or pre-column derivatization to options to simplify Flow Injection Analysis processing will be discussed.</strong></p>
<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: Need help with Sample Prep for LCMS in the Lab? Making use of the Automated Liquid Sampler you already have on your LCMS

Need help with Sample Prep for LCMS in the Lab? Making use of the Automated Liquid Sampler you already have on your LCMS

The Automated Liquid Sampler (ALS) you have in your LCMS stack can simplify menial tasks.

Automated Liquid Sampler for Sample Prep for LCMS in the Lab

<p>Targeted workflows are particularly interesting for identifying established biomarkers in various applications. The focus on these workflows, coupled with technological advancements, is continually expanding the boundaries of high-throughput targeted analysis.</p>
<h3><strong>Next Generation of absolute protein Quantitation in Biological Matrixes; higher multiplexicity while faster, robust and sensitive</strong></h3>
<ul>
<li><strong>Presenter:</strong> Dr. Christoph Borchers (Mcgill university)</li>
</ul>
<p>The accurate and rapid determination of protein concentrations using multiplexed multiple reaction monitoring (MRM) with isotope-labeled internal standards has the potential to revolutionize biochemistry and medical sciences. The combination of an Evosep One LC with an Agilent QQQ6495C allows a several-fold reduction of analysis time while maintaining high multiplexicity. As an example, we show the use of a multi-protein method for the absolute quantitation of 270 proteins, combined with metabolomics and Artificial Intelligence (AI), to analyze the plasma of a COVID cohort for prediction of survival. Moreover, optimization of the Evosep/6495C combination allowed adaptation of the 270-protein MRM method to a 24-minute gradient, thus doubling the throughput compared to before.</p>
<h3><strong>Development of a LC-MS/MS Method for Measurement of Fusion Sarcoma Proteins in Plasma</strong></h3>
<ul>
<li><strong>Presenter:</strong> Phd. AnThony Maus (Clinical Mass Spec. Development Laboratory, Mayo Clinic)</li>
</ul>
<p>Sarcoma is general term for a group of over 70 cancers that are classified using genomic techniques to identify characteristic gene fusions in tumor tissues. However, this technique requires relatively invasive biopsies and is not conducive to monitoring disease progression or response to treatment. Measurements of fusion protein biomarkers in plasma would overcome these limitations. We sought to develop an LC-MS/MS method capable of performing these measurements by conducting discovery experiments on cell lines with an EvoSep coupled to an Exploris 480 mass spectrometer. Using these data, we developed a targeted method and performed measurements in plasma samples.</p>


Targeted Workflows

Targeted workflows are particularly interesting for identifying established biomarkers in various applications.

Targeted LC/MS Workflows

<p><strong>Learn how to automate your SPE procedures with the LCTech FREESTYLE™ system for various sample types.</strong></p>
<p><strong>Presenter:</strong> Fred Foster (Applications Scientist)</p>


GERSTEL: Automation of Solid Phase Extraction Procedures using a Novel Robotic Automation Platform

Automation of Solid Phase Extraction Procedures using a Novel Robotic Automation Platform

Learn how to automate your SPE procedures with the LCTech FREESTYLE™ system for various sample types.

Automation of Solid Phase Extraction - Automation Platform

<p><strong>Solid phase extraction (SPE) is an effective technique for cleaning up and concentrating samples prior to high performance liquid chromatography (HPLC) or gas chromatography (GC) analysis. The technique offers targeted selectivity for analytes of interest. SPE is versatile for a wide range of sample volumes, can be easily automated for high-throughput, and is performed by following quick and simple methods (condition, equilibrate, load, wash, and elute). In this webinar, learn more about an effective sample cleanup method for steroid analysis that targets 19 analytes utilizing a Polymeric Reversed Phase Strata™-X 96-well plate.</strong></p>
<p>Mackenzie Freige, a Clinical Application Scientist at Phenomenex, will explain the foundation of SPE and offer method development insight to a frequently tested clinical application.</p>
<h5><strong>Key learning objectives</strong></h5>
<ul>
<li>Understand the fundamentals of solid phase extraction (SPE)</li>
<li>Discover the common difficulties of steroid analysis</li>
<li>Learn tips for approaching SPE method development</li>
<li>Explore a review of SPE data</li>
</ul>
<h5><strong>Who should attend?</strong></h5>
<ul>
<li>Scientists working in the field of clinical, forensics and/or toxicology.</li>
<li>Scientists looking to improve their sample preparation techniques.</li>
<li>Scientists who want to learn more about steroids.</li>
</ul>
<h5><strong>Certificate of attendance</strong></h5>
<p>All webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes.</p>
<blockquote>
<p><strong>Presenter:</strong> Mackenzie Freige (Phenomenex)</p>
</blockquote>
<blockquote>
<p>Mackenzie Freige received a Bachelor of Science degree in Life Sciences from Kansas State University and a Bachelor of Arts degree in Chemistry from Wichita State University, USA. She has six years’ experience in LC-MS/MS, GC-MS, and sample preparation. She has previously worked in toxicology, environmental chemistry, food science industries, and the pharmaceutical industry.</p>
</blockquote>
<blockquote>
<p>She joined Phenomenex in 2021 as an Application Scientist, specializing in developing applications for clinical research. She has experience in method development and instrumentation, which she uses to help customers solve problems regarding sample preparation, HPLC, and MS methods.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Jemima Arnold (Editorial Team, SelectScience)</p>
</blockquote>
<blockquote>
<p>Jemima studied Cellular and Molecular Medicine at the University of Bristol, UK, and as a member of the Editorial team, she now plays an integral role in shaping the content on SelectScience.</p>
</blockquote>


SelectScience: Method development for solid phase extraction with steroid analytes

Method development for solid phase extraction with steroid analytes

We will explain the foundation of SPE and offer method development insight to a frequently tested clinical application.

Method development solid phase extraction steroid analytes

<p>This webinar will present data and discuss EPA Draft Method 1633 compliant options  to simplify sample clean up and increase sample throughput for PFAS analysis.</p>
<p>Key Learning Points:</p>
<ul>
<li>Learn options for SPE phases for PFAS extraction from water and soil samples.</li>
<li>Utilize acceptable options for EPA 1633 as a guidance method.</li>
<li>Understand how to optimize time and cost for sample preparation.</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Philip Bassignani (Director of Technical Operations with Alpha Analytical)</p>
</blockquote>
<blockquote>
<p>He has over 25 years of environmental analytical and method development experience, working on a wide range of projects. Philip serves as the laboratory’s emerging contaminants and HRMS technical specialist, with a strong emphasis on PFAS extraction and analytical method development.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Richard Jack (Global Market Development Manager, Food and Environmental, Phenomenex)</p>
</blockquote>


Phenomenex: Optimizing PFAS Analysis for Draft Method 1633 Using a Stacked SPE Format

Optimizing PFAS Analysis for Draft Method 1633 Using a Stacked SPE Format

We will present data and discuss EPA Draft Method 1633 compliant options  to simplify sample clean up and increase sample throughput for PFAS analysis.

PFAS Analysis for Draft Method 1633 Using a Stacked SPE

<p><strong>Welcome to the &quot;Ultra-Fast Bites&quot; series - where you can get ultra-fast insights about the latest trends and hottest topics in bite-sized content to stay at the forefront of science.</strong></p>
<p>In our previous For the Love of Food! series, we have previously discussed the use of LC-GC-FID, which is the industry standard for monitoring mineral oil pollutants in edible oils and food contact materials.</p>
<p>These pollutants are frequently encountered as saturated (MOSH) and aromatic hydrocarbons (MOAH), making it essential to analyze for food safety. However, with the analytical challenges, additional sample clean-up procedures (AlOx and Epox) must be used to improve the method&#39;s robustness and sensitivity.</p>
<p>In this presentation, join us as Dr. Andreas, Managing Director of Axel Semrau GmbH &amp; Co KG, introduces a fast and efficient analysis of MOSH/MOAH using a new automated saponification workflow that can save your time and effort while maximizing the results.</p>
<p>For the love of food!</p>
<p>Learning Objectives:</p>
<ul>
<li><strong>Learn more about LC-GC-FID, which is the standard instrumentation to monitor the levels of MOSH/MOAH</strong></li>
<li><strong>Understand automated clean-up techniques for the analysis of MOSH/MOAH samples</strong></li>
<li><strong>Discover how the new automated saponification workflow can help save your time and effort in analysis</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Dr Andreas Bruchmann (Managing Director, Axel Semrau GmbH &amp; Co KG)</p>
</blockquote>
<blockquote>
<p>After studying Analytical Chemistry at the University of Bochum, Andreas Bruchmann joined Axel Semrau in 1992. He worked in different departments before becoming Managing Director in 2010. Now he is responsible for the Chromatography business unit, which supplies automated application solutions for the food and pharmaceutical industry worldwide. He was also involved in the development of the CHRONECT MOSH/MOAH Workstation from the beginning in 2010.</p>
</blockquote>


Shimadzu Corporation: Ultra-Fast Bites - For the Love of Food! Latest Update on the Analysis of MOSH/MOAH Contamination

Latest Update on the Analysis of MOSH/MOAH Contamination

A fast and efficient analysis of MOSH/MOAH using a new automated saponification workflow that can save your time and effort while maximizing the results.

<p><strong>Traditional laboratory analysis of the immunosuppressant drugs cyclosporine, everolimus, sirolimus and tacrolimus is well-established in clinical research. However there remains a need for individuals to undergo an invasive, time-consuming and disruptive process under the supervision of trained staff in order to collect a sufficient volume of whole blood for laboratory analysis.</strong></p>
<p>A reliable, remote sampling method may find utility in a clinical research setting. Here we describe the use of Capitainer® B Devices to obtain analytically sensitive, precise and accurate data for cyclosporine, everolimus, sirolimus and tacrolimus analysis using small sample volumes.</p>
<p>Using Capitainer® B devices and very sample small volumes (30 µL of whole blood resulting in a 10 µL dried blood spot), an in-house laboratory method was used on a LC-MS/MS system to meet validation goals for analytical sensitivity, linearity, precision and accuracy for cyclosporine, everolimus, sirolimus and tacrolimus. Furthermore, the advantages conferred by microsampling, notably removing the requirement for travel and a venous blood draw and facilitating home sampling, render this technique applicable to clinical research. </p>
<p>For Research Use Only. Not for Use in Diagnostic Procedures.</p>
<p>Learning objectives: </p>
<ul>
<li><strong>Discover how the Xevo TQ Absolute can be used to achieve sufficient analytical sensitivity for a microsampling application</strong></li>
<li><strong>Learn how to achieve fast sample throughput (~2 minute injection-to-injection), minimising time to first result</strong></li>
<li><strong>Explore how MassTrak Immunosuppressant Calibrator and QC Sets can be included in the workflow</strong></li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Stephen Balloch (Senior Scientist, Clinical Scientific Operations, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Stephen Balloch graduated from the University of York (UK) with a Masters degree in Chemistry which included a strong focus on analytical chemistry and a year in industry, in which he gained experience in a range of analytical techniques.</p>
</blockquote>
<blockquote>
<p>His first permanent post was at Charles River Laboratories, a GLP compliant contract research laboratory in Edinburgh, in which he progressed to the role of Study Director and gained further exposure to LC-MS and LC-MS/MS instrumentation, including Waters instruments.</p>
</blockquote>
<blockquote>
<p>Since 2010, he has been part of the clinical team in the Scientific Operations group in Waters (Wilmslow, UK). His principal focus has been on the development and validation of bioanalytical methods according to CLSI guidelines, with a focus on therapeutic drug monitoring. Additionally, he has supported newborn screening, steroid and vitamin analysis.</p>
</blockquote>


Waters Corporation: Remote Sampling Analysis of Immunosuppressant Drugs with LC-MS/MS

Remote Sampling Analysis of Immunosuppressant Drugs with LC-MS/MS

We will describe the use of Capitainer® B Devices Discover and Xevo TQ Absolute to achieve sufficient analytical sensitivity for a microsampling application.

Remote Sampling of Immunosuppressant Drugs with LC-MS/MS

<p><strong>The solubility of orally administered drugs is highly influenced by the composition of the intestinal fluids, the presence of fatty acids and cholesterol, and the pH. All these factors can be affected by the individual’s diet (food effect). Typical biorelevant studies, however, fail to capture food effects as the experiments are commonly performed on fixed simulated intestinal fluid (SIF) compositions. Consequently, accurate prediction of the food effect observed in clinical studies is hindered due to lack of reliable data for the model.</strong></p><p>Here, we propose a high-throughput automated workflow for the study of API solubility in complex, ad hoc biorelevant media, and the implementation of the data obtained in vitro into a Physiologically Based Biopharmaceutic Model (PBBM) used to predict the food effect on a BCS IV zwitterionic drug. The automated workflow led to considerable time and material savings, while the model accurately predicted the results of the food effect.</p><p><strong>Key Learning Objectives:</strong></p><ul><li>Determination of food effect, through use of complex biorelevant media, to describe and predict clinical data</li><li>Automated preparation of ad hoc complex biorelevant media</li><li>Automated in vitro biorelevant solubility screen of an API</li><li>Integration of in vitro solubility and permeability into a Physiologically</li><li>Based Biopharmaceutic Model (PBBM)</li></ul><p><strong>Who Should Attend:</strong></p><ul><li>Scientist, Sr. Scientist, Development Chemist, Formulation Chemist, Process Chemist, (Directors of preceding), Research Fellow, Professor</li><li>Product Development Scientists, Biochemist</li></ul><blockquote><p><strong>Presenter:&nbsp;</strong>Paola Ferrini (Investigator, High-Throughput Automation Team, GSK)</p><p><strong>Presenter: </strong>Konstantinos Stamatopoulos (Biopharmaceutics Investigator, GSK)</p><p><strong>Presenter: </strong>Catherine Dold (Health &amp; Environment Writer, C&amp;EN Media Group)</p></blockquote>

C&EN: Automated In Vitro Sample Preparation for PBBM to Predict Food Effect on Oral Drugs

Automated In Vitro Sample Preparation for PBBM to Predict Food Effect on Oral Drugs

We propose a high-throughput automated workflow for the study of API solubility in complex, ad hoc biorelevant media.

LCMS webinars focusing on Sample prep - page 27