<div><p><strong>Protein purification is a critical step in biopharmaceutical research, proteomics, and industrial biotechnology. It involves isolating a specific protein from complex biological mixtures while preserving its native structure and activity. Traditional methods such as precipitation or dialysis lack the precision required for high-purity protein isolation, especially when dealing with therapeutic targets or complex protein assemblies.</strong></p><p>High-performance liquid chromatography (HPLC) protein purification has transformed this field by providing high resolution, reproducibility, and speed, making it indispensable for both analytical and preparative workflows.</p></div><div><div><div><div><h3><strong>What is HPLC Protein Purification?</strong></h3><p>HPLC purification is based on the principle of selective interactions between proteins and the stationary phase under high-pressure liquid flow. The separation relies on differences in size, charge, hydrophobicity, or affinity of proteins toward the stationary phase material.</p><p>Unlike conventional low-pressure methods such as gel filtration or affinity batch purification, HPLC purification operates under high pressure (up to 6000 psi), enabling faster separation with enhanced resolution and quantitative recovery. It also offers precise control over parameters like gradient composition, pH, and temperature, minimizing variability between runs.</p><p>In contrast to traditional column chromatography, HPLC uses smaller stationary phase particles (3–10 µm), resulting in increased surface area and sharper <a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/resources/knowledge-center/hplc-knowledge-center/how-to-reduce-peak-tailing-in-hplc"><strong>peak shapes</strong></a>, which are vital for protein purity assessment and scale-up purification.</p></div></div></div></div><div><div><div><div><h3><strong>Types of HPLC Used for Protein Purification</strong></h3></div></div></div></div><div><p>Different HPLC modes can be employed depending on the physicochemical properties of the target protein. Each method offers unique advantages in terms of selectivity and recovery.</p><h4><strong>Reversed-Phase HPLC (RP-HPLC)</strong></h4><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-reversed-phase"><strong>Reversed-Phase HPLC</strong></a> separates proteins based on hydrophobic interactions between the analyte and the stationary phase, typically C4, C8, or C18 silica-based columns. Proteins are eluted using gradients of organic solvents (usually acetonitrile or methanol) in the presence of volatile acids like formic or trifluoroacetic acid (TFA).</p><p>This method provides exceptional resolution and is commonly used for protein fragment purification, and analysis of recombinant proteins. For example, reversed-phase HPLC is routinely employed in peptide therapeutic workflows, such as the<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/labrulez-bucket-strapi-h3hsga3/an59280424_w_fc6c3ac6f0.pdf"><strong> Tirzepatide Preparation and Purification </strong></a>process, where purity and recovery are critical to product efficacy. However, due to exposure to organic solvents, RP-HPLC may cause partial denaturation, limiting its use for native proteins.</p><h4><strong>Ion Exchange HPLC (IEX-HPLC)</strong></h4><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-sec"><strong>IEX-HPLC</strong></a> separates proteins based on net surface charge. Cation exchange (with negatively charged stationary phases) binds positively charged proteins, while anion exchange does the reverse.</p><p>By gradually increasing salt concentration or changing the mobile phase pH, proteins are eluted according to their isoelectric points (pI).By gradually increasing salt concentration or changing the mobile phase pH, proteins are eluted according to their isoelectric points (pI).</p><p>This approach is highly suitable for native purification, protein isoform analysis, and charge variant characterization essential steps in therapeutic protein production.</p><h4><strong>Size Exclusion Chromatography (SEC-HPLC)</strong></h4><p>SEC separates molecules based on their hydrodynamic radius. Larger proteins elute first, as they are excluded from the pores of the stationary phase, while smaller molecules penetrate and elute later.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-sec"><strong>SEC-HPLC</strong></a> is non-denaturing and ideal for determining protein molecular weight, oligomeric state, and aggregate content. It is frequently used as a final polishing step following ion exchange or affinity chromatography.</p><h4><strong>Affinity HPLC</strong></h4><p>Affinity-based HPLC leverages specific biological interactions between the target protein and a ligand immobilized on the stationary phase (e.g., antibodies, metal ions, or tags such as His-tag or GST).</p><p>When integrated into an HPLC system, affinity chromatography provides high selectivity and purity (&gt;95%) in a single step, often used in recombinant protein purification and biomarker capture applications.</p></div><div><div><div><div><h3><strong>Benefits of Using HPLC for Protein Purification</strong></h3><p>HPLC-based protein purification combines the analytical precision of chromatography with the preparative capability needed for research and biomanufacturing. The main advantages include:</p><h5><strong>Benefit &nbsp;/ &nbsp;Description</strong></h5><p><strong>High Resolution and Selectivity:</strong></p><ul><li>Smaller stationary phase particles and optimized flow dynamics allow HPLC to resolve proteins differing by minimal physicochemical properties. This precision is vital for distinguishing isoforms, mutants, and post-translationally modified variants.</li></ul><p><strong>Accuracy and Reproducibility</strong></p><ul><li>Automated systems maintain stable flow rates, gradient control, and detection sensitivity, ensuring reproducible results essential for regulated biopharmaceutical workflows.</li></ul><p><strong>Speed and Efficiency</strong></p><ul><li>Modern UHPLC systems equipped with fully porous or core–shell particles achieve faster separations without sacrificing resolution, reducing run times by up to 50% compared to classical methods.</li></ul><p><strong>Compatibility and Scalability</strong></p><ul><li>HPLC systems are highly adaptable, supporting both analytical-scale characterization and preparative-scale purification. Methods developed at microgram scale can be seamlessly transferred to milligram or gram scales used in process development.</li></ul><div><div><div><div><h3><strong>Factors Affecting the Efficacy of Protein Purification by HPLC</strong></h3></div></div></div></div><div><p>Optimizing HPLC for protein purification requires balancing purity, recovery, and throughput. The following parameters significantly influence results:</p><ul><li><strong>Purification goal:</strong> Define whether the priority is yield, purity, or throughput. Analytical separations prioritize resolution, while preparative runs emphasize recovery and process speed.</li><li><strong>Protein solubility and stability:</strong> Unstable or aggregation-prone proteins may require low temperatures or additives (e.g., glycerol, mild detergents).</li><li><strong>Column chemistry and particle size:</strong> Select appropriate stationary phase chemistry (silica, polymeric, or mixed-mode) and particle size to suit molecular weight and hydrophobicity.</li><li><strong>Mobile phase pH and ionic strength:</strong> pH should be optimized near but not at the protein’s pI; salt gradients influence both resolution and elution strength.</li><li><strong>Flow rate and gradient profile:</strong> Steeper gradients shorten run time but may compromise separation quality.</li><li><strong>Purified protein final form:</strong> Consider buffer composition and concentration for storage or downstream assays to maintain bioactivity.</li></ul></div><div><div><div><div><h3><strong>Best Practices for Protein Purification by HPLC</strong></h3></div></div></div></div><div><p>Following good chromatographic practices ensures consistent, high-quality results:</p><ul><li><strong>Column conditioning and storage:</strong> Always equilibrate new <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=48&amp;manufacturerItems=50"><strong>HPLC columns</strong></a> with 10 column volumes of buffer; store in appropriate solvent containing preservatives.</li><li><strong>Avoid protein precipitation:</strong> Maintain appropriate ionic strength and, when native state is desired, avoid exposure to denaturing solvents or high organic content.</li><li><strong>Prevent sample loss:</strong> Use low-protein-binding tubing and vials; minimize dead volume in the system.</li><li><strong>Troubleshooting:</strong><ul><li>Peak fronting - may indicate column overloading.</li><li>Peak broadening – may indicate column channeling.</li><li>Carryover – reduce by extending wash cycles or using stronger regeneration solvents.</li><li>Clogging – prefilter samples (0.22 µm) and periodically flush the system.</li></ul></li></ul></div></div></div></div></div>

Protein Purification by HPLC: Methods, Benefits, and Best Practices

<p><strong>Scientists from CEITEC Brno University of Technology&nbsp;have succeeded in a highly competitive international selection process and secured a prestigious Human Frontier Science Program (HFSP) grant, which supports groundbreaking fundamental research. The Brno-based team led by Eric Daniel Glowacki will contribute a unique technology to an international project that enables precise control of oxygen levels in tissues. Changes in oxygen availability may play a crucial role in determining how cells specialize during early embryonic development.</strong></p><p>The project, entitled “Beyond Theory: Regulation of Mammalian Embryo Patterning by Electrochemical Gradients,” is being carried out by CEITEC BUT in collaboration with biologists from the <strong>Max Planck Institute of Molecular Cell Biology and Genetics</strong> and <strong>Yale University</strong>. The Brno team’s role is central to the project: providing technology that enables the deliberate creation of regions with different oxygen concentrations in tissues and the observation of how cells respond to these changes.</p><p><i>“Our research group specializes in electrochemistry, particularly in studying how electric current affects tissue oxygenation and the resulting chemical changes. To perform certain types of experiments, we developed our own integrated system of needle probes, electrodes, and software, which allows us to influence and control the amount of oxygen present in tissues through which current is passed,” </i>explains team leader <strong>Eric Daniel Glowacki</strong>. Using these tools, researchers can create regions within samples where oxygen is scarce or even completely absent. Changes in oxygen levels are fundamental to biology because they affect cellular metabolism and, consequently, cell behaviour. In some types of research, such precise environmental control is essential.</p><p><i>“Our system is not universal; we tailor it to each application. In the future, however, we aim to expand its variants so that it can be used across the widest possible range of research fields,”</i> adds Eric.</p><p>Scientists at the Max Planck Institute have already used CEITEC’s technology in previous studies of early embryonic development. They investigated how the metabolic activity of stem cells – undifferentiated cells capable of self-renewal and transformation into specialized cells such as muscle, nerve, or blood cells – affects both their own development and that of neighbouring cells.</p><p>The newly funded HFSP project builds on this work. Its goal is to revisit the nearly century-old theory&nbsp;proposed by the American zoologist Charles Manning Child, which explains how stem cells in multicellular organisms gradually develop into mature cells with specific functions and structures. The three-year project, supported by a grant of<strong> CZK 7.5 million </strong>for each partner, will test a new hypothesis in mouse embryos directly in the uterus: that the specific transformation of cells depends not only on oxygen depletion itself but also on the cell’s location within the tissue and the timing of the oxygen decrease.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Technologie_vedcu_z_CEITEC_pomuze_odhalit_jak_kyslik_ridi_vyvoj_embryi_2_1ea86be296.jpeg" alt="CEITEC/ Lukáš Havlák: CEITEC Technology Will Help Reveal How Oxygen Controls Embryo Development: HFSP technological setup at CEITEC BUT." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Technologie_vedcu_z_CEITEC_pomuze_odhalit_jak_kyslik_ridi_vyvoj_embryi_2_1ea86be296.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>A better understanding of the mechanisms that govern early embryonic development could, in the future, contribute to advances in regenerative medicine, research into developmental disorders, and the more effective use of stem cells in biomedicine.</p><p><i>“The success of our project is both a great honour and a significant responsibility. HFSP is a unique programme dedicated to fundamental research, where investigators seek answers to the most basic and still unresolved questions in biology,”</i> says Eric. The programme is extremely competitive, with only two to three percent of the thousands of submitted projects receiving funding. Requirements include international collaboration across continents and a genuinely innovative approach.</p><p><i>“Through this, we have become part of a community of world-class scientists from around the globe. Although the results of this kind of research are not immediately applicable, their long-term benefit to society is immense,” </i>Eric concludes.</p><blockquote><h4><strong>About HFSP</strong></h4><p>The Human Frontier Science Program Organization (HFSPO) was established in France in 1989, although the idea of creating such an international community dedicated to fundamental research originated several years earlier in Japan. The programme funds cutting-edge research in life sciences, particularly in biology, physics, chemistry, mathematics, and computer science, and supports innovative interdisciplinary projects that would otherwise be difficult to finance.</p><p>HFSPO receives funding from governments and institutions, including those of France, Japan, Switzerland, South Korea, the United States, the European Union, Singapore, New Zealand, and the United Kingdom. Since the programme’s launch in 1989, 31 HFSP-supported scientists have gone on to receive Nobel Prizes. The most recent awardees, in 2024, were David Baker, who received the Nobel Prize in Chemistry for computational protein design, and Gary Ruvkun, who received the Nobel Prize in Physiology or Medicine for the discovery of microRNA.</p></blockquote>

CEITEC Technology Will Help Reveal How Oxygen Controls Embryo Development

<p><strong>🎤Rajas Poorna and Charles Anderson</strong></p><h4><strong>What if you could dry biofluid samples in the field—without a vacuum system, freeze dryer, or full lab setup?</strong></h4><p>In this episode of Concentrating on Chromatography, I sit down with Rajas Poorna and Charles Anderson to explore their work on a frugal, field-deployable alternative to traditional lyophilization through the Evapinator project.</p><p>Originally inspired by the principles of frugal science, their approach rethinks how we stabilize and prepare biofluid samples like blood and plasma—especially in environments where traditional lab infrastructure simply isn’t available.</p><h4><strong>What This Episode Covers:</strong></h4><h5><strong>A Frugal Take on Lyophilization</strong></h5><p>Can you replicate the outcome of a lyophilizer without the complexity?<br>Why traditional freeze drying is often too expensive and impractical for field use<br>How simplifying evaporation could unlock entirely new workflows</p><h5><strong>Drying Biofluids in the Field</strong></h5><p>The real-world challenge of handling blood and other biofluids outside the lab<br>Why sample stability during transport is such a critical bottleneck<br>How a portable system could enable on-site sample prep in remote or resource-limited settings</p><h5><strong>Rethinking Evaporation (No Vacuum Required)</strong></h5><p>The core idea behind the Evapinator—and how it challenges conventional assumptions<br>The role of airflow, heat, and design in drying sensitive samples<br>Where this approach fits relative to traditional evaporation and lyophilization techniques</p><h5><strong>Early Results &amp; Practical Insights</strong></h5><p>What’s working so far—and where limitations still exist<br>The types of applications where this approach shows the most promise<br>What still needs to be validated in upcoming peer-reviewed work</p><h4><strong>Why This Matters</strong></h4><p>From clinical research in remote regions to decentralized diagnostics, the ability to dry and preserve biofluid samples in the field could fundamentally change how and where analysis happens.</p><p>This conversation challenges a core assumption in analytical science:</p><p>Do you really need a full lyophilizer—or even a vacuum—to stabilize biofluid samples?</p><h3><strong>Video Transcription</strong></h3><p>The interview opens with a welcome to an episode of <i>Concentrating on Chromatography</i>. The host introduces guests <strong>Rajas Poorna</strong> and <strong>Charles Anderson</strong> and asks about their scientific backgrounds and how they became involved in solving evaporation challenges.</p><h4><strong>Scientific background and project origin</strong></h4><p>Rajas explains that he is trained as a physicist and is now pursuing a PhD in bioengineering. His lab focuses on building low-cost scientific equipment to make science more accessible, especially for schools and low-resource settings. This work is part of a broader “frugal science” approach, where students and researchers develop affordable versions of instruments that are normally expensive.</p><p>The original challenge came from synthetic biology education. High school teams working on synthetic biology projects needed access to equipment such as lyophilizers, but conventional systems can cost tens of thousands of dollars. The team therefore began exploring whether a more affordable lyophilizer-like system could be built for education and field use.</p><p>Charles describes joining the project early in his undergraduate studies. He was drawn to it because it had a clear practical purpose and seemed like something that could become useful outside the laboratory rather than remaining only a research prototype.</p><h4><strong>Why evaporation became the key challenge</strong></h4><p>The discussion turns to the practical limitations of traditional evaporation and drying systems. Rajas explains that during a collaboration in Thailand, researchers working on Raman spectroscopy for tuberculosis diagnostics needed to dry blood-derived samples before transporting them to a central laboratory. They used a centrifugal vacuum evaporator, but the system was slow, expensive, and difficult to service when it broke down.</p><p>This experience led to a central question: could sample drying be achieved without a vacuum? Rajas notes that everyday drying processes, such as drying clothes, do not require vacuum. This insight opened the path toward a simpler, smaller, lower-cost and potentially battery-powered drying system.</p><h4><strong>How Rajas and Charles began collaborating</strong></h4><p>Charles explains that he met the lab’s principal investigator while discussing a different project. He was then invited to work on what would later become the Evaponator. At the beginning, the project was still small and exploratory.</p><p>Rajas adds that Charles joined at a stage when the team was trying to understand the physics and engineering behind vacuum-free drying. Within a few months, they developed a prototype costing under 100 USD that could dry samples much faster than the conventional vacuum evaporator used by collaborators.</p><h4><strong>Main limitations of conventional drying systems</strong></h4><p>The interview identifies several major limitations of existing evaporation technologies:</p><ul><li>High cost</li><li>Limited reliability in remote or low-resource settings</li><li>Long drying times</li><li>Poor field portability</li><li>Challenges with sterility and cross-contamination</li></ul><p>Charles emphasizes that freeze drying can take 12–24 hours, which is impractical for field use. Rajas adds that centrifugal vacuum evaporators are not necessarily sterile and may pose a risk of cross-sample contamination. Together, these challenges shaped the requirements for the Evaponator.</p><h4><strong>What the Evaponator is</strong></h4><p>Charles introduces the Evaponator as a low-cost, portable drying system designed to dry small numbers of samples quickly without a vacuum chamber. The name was inspired by an episode of <i>Phineas and Ferb</i>.</p><p>The system is based on the same principles as drying clothes: low humidity, gentle heating and airflow. Instead of using vacuum, the Evaponator generates dry air, directs it over the sample, removes moisture through a cold trap and repeats the process in a closed or semi-closed loop.</p><p>The current design is aimed at drying approximately four 1 ml samples, which fits the intended use case of field diagnostics or low-throughput sample collection in remote settings.</p><h4><strong>How the system works</strong></h4><p>Rajas explains the operating principle in more detail. Moist air is passed through a cooled metal block using a thermoelectric cooler. As the air cools, moisture condenses inside the cold trap, producing dry air. This dry air is then directed over warmed samples, helping water evaporate while keeping the sample temperature moderate.</p><p>The system can operate in a loop to improve efficiency. HEPA filtration and aerosol filtration help prevent contamination. The team also developed an ozone-based sterilization approach, allowing the device to sterilize itself using ozone generated from air rather than relying on consumables such as ethanol or peroxide.</p><p>To prevent sample-to-sample contamination, the design uses separate airflow paths for individual samples, which merge only later in the system.</p><h4><strong>Design assumptions and engineering constraints</strong></h4><p>A key design assumption is that not every drying process needs sublimation or deep vacuum. For the biofluid applications targeted by the Evaponator, the team works around 40 °C, a temperature chosen because it is close to fever temperature and should be mild enough for many biological samples.</p><p>The engineering constraints included:</p><ul><li>Use of widely available components</li><li>No specialized machining</li><li>Bill of materials under 100 USD</li><li>Low power consumption</li><li>Portability</li><li>Simple assembly</li><li>Robust airflow without splashing or sample loss</li></ul><p>Charles notes that the team intentionally selected accessible parts, including components similar to those used in computer cooling systems, vacuum-cleaner-style HEPA filters and disposable pipette tips for directing airflow.</p><h4><strong>Sample types and solvents</strong></h4><p>The prototype is currently focused mainly on aqueous biological samples. Rajas explains that using organic solvents such as ethanol would introduce ignition risks with the current architecture, so the early work is focused on water-based samples and biofluids.</p><p>Charles adds that the system is intended primarily for blood-derived fluids, urine, saliva and similar samples where the target analytes can remain stable after drying and rehydration.</p><h4><strong>Potential analytical applications</strong></h4><p>The Evaponator is being developed for field sample preparation rather than as a replacement for every laboratory evaporator. The main idea is to dry samples near the point of collection, transport them more easily and then rehydrate them before analysis.</p><p>Potential use cases include:</p><ul><li>Field diagnostics</li><li>Biofluid sample stabilization</li><li>Remote sample collection</li><li>Clinical or public-health testing in low-resource settings</li><li>Applications where dried plasma, serum, urine or saliva can later be analyzed</li><li>Situations where conventional dried blood spot methods lack enough sample volume</li></ul><p>Rajas notes that red blood cells may not be suitable for drying directly because they can rupture, so serum or plasma is expected to be more appropriate. He also points out that oxygen exposure during forced-air drying still needs further testing for oxygen-sensitive analytes.</p><h4><strong>Current development status</strong></h4><p>Charles explains that the project is approaching important validation milestones, especially around batch-to-batch and sample-to-sample sterility. The ozone cleaning system appears promising because it may reduce the need for cleaning consumables, aside from inexpensive items such as pipette tips and occasional filter replacement.</p><p>He also mentions tests with trehalose-based solutions and collaboration with a Georgia Tech startup working on room-temperature-stable mRNA vaccines. In that context, the Evaponator was able to dry samples in about 30 minutes, compared with 12–24 hours using previous drying approaches.</p><h4><strong>Commercialization and future direction</strong></h4><p>Rajas explains that the team is exploring commercialization and has participated in a startup accelerator. They are investigating where the technology could have the strongest product-market fit, with particular interest from cost-sensitive and geographically dispersed healthcare settings, including India.</p><p>The goal is to move beyond a lab prototype toward a manufacturable, user-friendly device with a straightforward interface and reliable sealing, sterilization and operation.</p><h4><strong>Closing remarks</strong></h4><p>The interview concludes with the host thanking Rajas Poorna and Charles Anderson for sharing the technical and practical challenges behind the Evaponator. Both guests emphasize that the conversation was a valuable opportunity to explain the project in depth and reflect on its progress.</p><blockquote><p><strong>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</strong></p></blockquote><blockquote><h4><strong>Concentrating on Chromatography Podcast</strong></h4><p>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!</p><p>You can find <strong>Concentrating on Chromatography Podcast </strong>in podcast apps:</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL"><strong>Spotify</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185"><strong>Apple podcast</strong></a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography"><strong>podscan</strong></a></li></ul><p>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos"><strong>YouTube channel</strong></a></p></blockquote>

Frugal Science Meets Sample Prep: A Field-Ready Lyophilizer for Biofluids

Article

Product

Academy

Video

Scientists

Interview

Science and research

Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

CEITEC

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

Organomation, founded in 1959, designs and manufactures high-quality nitrogen evaporators and extraction systems. Known for innovation and durability, their lab instruments are used globally for efficient sample preparation with strong customer support.

Organomation

Metrohm

Mettler-Toledo

MSACL

Agilent Technologies

Wiley

SCIEX

Waters Corporation

<p><strong>Do you have an older method that is no longer meeting your needs? Are you trying to decide if it’s worth updating it? Or have you already chosen to update but are now asking yourself, “Where do I go from here?”</strong></p>
<p>Modernizing a legacy method can improve accuracy, ruggedness, and sample throughput.</p>
<p>In this webinar, we will look at the decision-making process and steps to make it happen, including:</p>
<ul>
<li><p><strong>Is the goal to reduce analysis time and/or improve resolution?</strong></p>
</li>
<li><p><strong>What HPLC parameters will be key to success?</strong></p>
</li>
<li><p><strong>What are the column options, and will they work with your instrumentation?</strong></p>
</li>
<li><p><strong>How do I navigate the allowable adjustments to USP methods?</strong></p>
</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Mark Powell (Application Engineer, Agilent Technologies, Inc.)</p>
</blockquote>
<blockquote>
<p>Mark Powell is an Applications Engineer located at Agilent’s Little Falls site in Wilmington, DE. Before joining Agilent in 2011, Mark worked in the pharmaceutical industry synthesizing, purifying and analyzing drug candidates. He provides applications assistance and technical support for Agilent’s HPLC columns and consumables.</p>
</blockquote>


Agilent Technologies: Method Makeover: Updating Older HPLC Methods

Method Makeover: Updating Older HPLC Methods

Modernizing a legacy method can improve accuracy, ruggedness, and sample throughput.

<p><strong>Pyrrolizidine alkaloids (PAs) are a class of toxic natural compounds found in various plant species worldwide. Many PAs have been identified as contaminants in tea, dried herbs, and herbal dietary supplements. The presence of PAs in these products is mainly associated with co-harvest of PA-containing weeds. Considering PA are genotoxic carcinogens to humans, maximum levels have been set by the European Commission in Regulation 2020/2040 for a number of commodities. This talk will cover challenges and pitfalls encountered in quantitative LC-MS/MS analysis of PAs. Results generated during optimization experiments and validation of an LC-MS/MS method in a wide range of matrices will be presented.</strong></p>
<p><strong>Key Learning Objectives/What attendees will learn:</strong></p>
<ul>
<li><p>Information on pyrrolizidine alkaloids and contamination of dietary supplements and ingredients including applicable legislation.</p>
</li>
<li><p>Overview of pitfalls and challenges that need to be addressed in quantitative pyrrolizidine alkaloid analysis.</p>
</li>
<li><p>Summary of experiments and results collected during optimization and validation of internal LC-MS/MS method.</p>
</li>
</ul>
<p><strong>Who Should Attend:</strong> food testing lab personnel, researchers and regulators interested in pyrrolizidine alkaloid testing.</p>
<blockquote>
<p><strong>Presenter:</strong> Lukas Vaclavik, PhD (Eurofins Food Chemistry Testing, Madison, WI)</p>
</blockquote>
<blockquote>
<p>Lukas Vaclavik currently works as technical manager at Eurofins Food Chemistry Testing and supports the area of contaminant and residue testing. Prior to joining Eurofins, Lukas worked at the CFSAN of the U.S. FDA. Lukas has authored or co-authored over 40 scientific publications focused on chromatographic and mass spectrometric analysis of chemical residues, contaminants and adulterants. He received his Ph.D. in Food Chemistry and Analysis from the University of Chemistry and Technology, Prague, Czech Republic.</p>
</blockquote>


Agilent: Use of LC-MS/MS Technique for Quantitative Analysis of Pyrrolizidine Alkaloids in Dietary Supplements and Foods

Use of LC-MS/MS Technique for Quantitative Analysis of Pyrrolizidine Alkaloids in Dietary Supplements and Foods

This talk will cover challenges and pitfalls encountered in quantitative LC-MS/MS analysis of Pyrrolizidine alkaloids.

LC-MS/MS for Analysis of Pyrrolizidine Alkaloids

<h4><strong>Live Interactive Web Series</strong></h4>
<p>We’ll work through a topic of the week (roughly 60 minutes) and discuss any questions that come up along the way. During these sessions, we’ll talk about how to care for your SEC-MALS or FFF-MALS system, help you brush up on your ASTRA and DYNAMICS data processing, discuss measuring <em>dn</em>/<em>dc</em> values and why <em>dn</em>/<em>dc</em> is important, and see how stable RI baselines are achievable.</p>
<p>Working with polydisperse samples? We’ll see how to leverage ASTRA’s distribution analysis and results fitting features. Special topics on error analysis, batch MALS work, and more.</p>
<p>The live interactive web series are 100% live sessions, with anonymous Q&amp;A welcome during and after the discussion. Free for all to attend.</p>
<ul>
<li><p>Part 1 of 6: Why we love Multi-Angle Light Scattering! How MALS works and what it measures. Modes of operation and when to use them*</p>
<ul>
<li>MALS theory and operating principles</li>
<li>Batch MALS vs. flow mode MALS: when and why</li>
<li>What MALS can and cannot measure directly</li>
</ul>
</li>
<li><p>Part 2 of 6: Getting to know your MALS hardware, including ‘proper care &amp; feeding’ of the system, practical guides for optimizing data quality, and how to know when your DAWN hardware needs special attention*</p>
<ul>
<li>Understanding the MALS hardware internal and external components</li>
<li>Diagnosing hardware issues</li>
<li>How to help your MALS operate at its best</li>
</ul>
</li>
<li><p>Part 3 of 6: Let it flow - Leveraging MALS with Size Exclusion Chromatography SEC / Gel Permeation Chromatography GPC. Considerations for successful SEC-MALS / GPC-MALS operation. How to process ASTRA data on and after day 1*</p>
<ul>
<li>Practical considerations for MALS in SEC/GPC mode</li>
<li>Understanding system settings &amp; coefficients such as inter-detector band broadening and normalization</li>
<li>Squeezing the most information from your SEC-MALS data</li>
</ul>
</li>
<li><p>Part 4 of 6: Advanced topics in ASTRA data analysis - uncertainty calculations, MW averages, mass recovery, distribution analysis, results fitting, and data exporting*</p>
<ul>
<li>Understanding the ways ASTRA tracks and calculates system errors</li>
<li>Leveraging peak integration to understand what’s in your sample</li>
<li>When and why to use the various MW averages: Mn, Mw, Mz, Mp, Mavg, Mv, etc.</li>
<li>Efficient and easy ways to export exactly the data and results you want, right out of ASTRA</li>
</ul>
</li>
<li><p>Part 5 of 6: All about dn/dc values and concentration detectors (UV and RI) for MALS*</p>
<ul>
<li>Understanding dn/dc, what it is, and how it is used with MALS</li>
<li>Measuring / determining dn/dc for your samples</li>
<li>UV detectors and their role in MALS</li>
<li>Mass recovery in ASTRA</li>
</ul>
</li>
<li><p><strong>Part 6 of 6: MALS flow cell care: diagnosing and cleaning your flow cell</strong>*</p>
<ul>
<li>How to avoid the need to clean your MALS flow cell in the first place</li>
<li>How to diagnose a dirty MALS flow cell</li>
<li>How to take apart and clean your MALS flow cell</li>
</ul>
</li>
</ul>
<p>*It is recommended but not required that you attend all the sessions in this series.</p>
<blockquote>
<p><strong>Presenter:</strong> Dr. Andy Meyer</p>
</blockquote>
<blockquote>
<p>Dr. Andy Meyer joined Wyatt Technology in 2001, serving for several years as an Applications Scientist, then as Dean of Wyatt&#39;s &quot;Light Scattering University&quot; and as Director of Customer Service &amp; Support. After managing multiple regions in North America, Dr. Meyer is now a Senior Application Scientist for Wyatt. As a Wyatt customer, he completed his Ph.D. in Applied Science – Polymer Chemistry from the College of William and Mary in Virginia.</p>
</blockquote>


Waters Corporation: MALS flow cell care: diagnosing and cleaning your flow cell

MALS flow cell care: diagnosing and cleaning your flow cell

MALS flow cell care: diagnosing and cleaning your flow cell.

<h3><strong>LC-MS/MS 201 webinar series</strong></h3>
<p><strong>Advanced techniques for data acquisition and processing</strong></p>
<h4><strong>Elevate your analytical expertise with advanced techniques and workflows</strong></h4>
<p>Sharpen your data acquisition and processing skills with our <strong>LC-MS/MS 201 webinar series</strong>. Based on our LC-MS/MS 101 webinar series, these sessions will go <strong>beyond the fundamentals of LC-MS/MS</strong> and introduce ways to advance your analytical methods and data processing workflows. Every other week, we will explore how to optimize <strong>SCIEX OS software</strong> with short, 30-minute expert-led presentations.</p>
<h3><strong>This webinar:</strong></h3>
<h4><strong>April 18, 2024</strong></h4>
<h5>10:00 a.m. PT/ 1:00 p.m. ET - <strong>Troubleshooting at the source</strong></h5>
<ul>
<li><em>Acquire the knowledge needed to optimize source parameters and identify and resolve ionization-related problems.</em></li>
</ul>
<h3><strong>Other webinars from the series:</strong></h3>
<h4><strong>March 21, 2024</strong></h4>
<h5>10:00 a.m. PT/ 1:00 p.m. ET - <a href="https://lcms.labrulez.com/webinar/3705"><strong>Mastering chromatography</strong></a></h5>
<ul>
<li><em>Discover how to optimize your chromatography for even the most challenging compounds while creating and building LC methods.</em></li>
</ul>
<h4><strong>April 4, 2024</strong></h4>
<h5>10:00 a.m. PT/ 1:00 p.m. ET - <a href="https://lcms.labrulez.com/webinar/3706"><strong>It&#39;s a TRAP! Getting the most out of your QTRAP system</strong></a></h5>
<ul>
<li><em>Learn when to utilize QTRAP functionality to create more selective and sensitive methods.</em></li>
</ul>
<h4><strong>May 2, 2024</strong></h4>
<h5>10:00 a.m. PT/ 1:00 p.m. ET - <a href="https://lcms.labrulez.com/webinar/3708"><strong>Automating data processing</strong></a></h5>
<ul>
<li><em>Learn how to automate your data processing with custom flagging and rules for efficient data review in SCIEX OS software.</em></li>
</ul>
<h4><strong>May 16, 2024</strong></h4>
<h5>10:00 a.m. PT/ 1:00 p.m. ET - <a href="https://lcms.labrulez.com/webinar/3709"><strong>Excel strategies for mass spectrometry data analysis</strong></a></h5>
<ul>
<li><em>Take an in-depth look at when and how to use Excel to increase your productivity.</em></li>
</ul>


Troubleshooting at the source (LC/MS)

Acquire the knowledge needed to optimize source parameters and identify and resolve ionization-related problems.

<p><strong>Liquid handling is one of the most important yet also tedious tasks in the analytical laboratory. Only the correct volume of sample, solvent, reagent, titrant, or auxiliary solution makes sure analytical results are accurate and reproducible.</strong></p>
<p>In this webinar, Jennifer Lüber, Product Specialist Liquid Handling and Lab Robotics at Metrohm International Headquarters, will give you an introduction to the automation of liquid handling. After a brief overview of the capabilities of various dosing systems, Jennifer will demonstrate how the automation of basic liquid handling tasks will help you improve the quality of your analytical results while freeing up valuable time for other tasks. From this, a path forward can emerge to an automation solution that supports your analytical workflow best.</p>
<p>During a Q&amp;A session at the end of her webinar you can ask Jennifer any questions you may have about liquid handling and the solutions from Metrohm. Join us on April 17 and get inspired by what’s possible when it comes to the automation of your liquid handling!</p>
<p><strong>Key learnings of this webinar:</strong></p>
<ul>
<li>Better results, less risk of errors – the benefits of automated liquid handling</li>
<li>When to automate and what: How to find the best automation solution to support your analytical workflow</li>
<li>Tips and tricks how to keep your system at peak performance</li>
</ul>
<p><strong>Who should attend?</strong></p>
<p>Lab technicians, chemists, and everybody else performing liquid handling tasks in the laboratory.</p>
<blockquote>
<p><strong>Presenter:</strong> Jennifer Lüber (Product Specialist for Liquid Handling and Lab Robotics, Metrohm International Headquarters)</p>
</blockquote>
<blockquote>
<p>Jennifer Lüber is currently the Product Specialist for Liquid Handling and Lab Robotics at Metrohm International Headquarters in Switzerland. She finished her apprenticeship as a Lab Technician in 2014 and joined the Competence Center Titration at Metrohm International Headquarters in 2015. In 2020 Jennifer received her bachelor degree in business process management and in 2023, she joined the Competence Center Liquid Handling and Lab Robotics to support the team with her experience.</p>
</blockquote>


Metrohm: Automated liquid handling – the key to accurate and reproducible results

Automated liquid handling – the key to accurate and reproducible results

In this webinar, we will give you an introduction to the automation of liquid handling.

Automated liquid handling

<p><strong>The European Union (EU) has one of the highest levels of food safety standards in the world, largely due to the extensive body of legislation in place, which ensures that food is safe. The rules apply from farm to fork, whether food is produced in the EU or imported from elsewhere in the world.</strong></p>
<p>One key tool used to react rapidly to food and feed safety crises and incidents is the <strong>Rapid Alert System for Food and Feed</strong> (<strong>RASFF</strong>) which enables information to be shared rapidly and efficiently between food control authorities in Member States and the European Commission when a risk to health has been identified. In this way, countries can act rapidly and in a coordinated manner to avert food safety risks before they can harm consumers including the management of costly product recalls.</p>
<h5><strong>What will I learn?</strong></h5>
<p>In this webinar, you will learn about <strong>how RASFF operates as applied to residues and contaminants in food of animal origin</strong>, some historical trends (veterinary drug residues), and emerging threats (PFAS). </p>
<p>We will also delve into the <strong>analytical methods suitable for determination of key chemical hazards</strong>, for checking compliance with EU regulations, which will avoid RASFF notifications, both prior to export but also for official control within the EU (and elsewhere).</p>
<blockquote>
<p><strong>Presenter:</strong> Simon HIRD, Ph.D, MRSC, CChem. (Strategic Analyst, Testing and Laboratory Services, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Simon Hird has worked for Waters since 2014 as a Principal Scientist, in the Food and Environmental Market area and now as a Strategic Analyst in Waters’ new Testing and Laboratory Service business unit. Simon contributes to scientific projects, is involved in the commercialisation of new technologies, and provides advice, training, and context to various parts of the Waters organisation and to customers globally. Simon instructs on internationally recognised training courses, such as SARAF, GFoRSS and for AOAC India section. Simon continues to be invited to present at international conferences and has 24 peer-reviewed publications, including one of the most downloaded Trends in Analytical Chemistry articles, “Liquid chromatography-mass spectrometry for the determination of chemical contaminants in food”. Prior to joining Waters, Simon spent almost 20 years at a government laboratory in the UK (now called Fera Science), where he had various roles associated with residues testing and food authenticity before leading an LC-MS/MS team responsible for determination of residues and contaminants in food and environmental samples.</p>
</blockquote>
<blockquote>
<p><strong>Moderator:</strong> Moderator - Joanne Ho, Ph.D. (Food and Environmental, APAC Market Development Manager, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Joanne Ho is the Food and Environmental Market Development at Waters Corporation. She received her PhD in Chemistry from the University of New South Wales, Australia. During her career, Joanne has developed applications using LC and LC-MS techniques for a variety of applications ranging from active ingredients like organic acids to food contaminant residues like mycotoxins. Joanne is part of the Asia Pacific team and works with customers in the region to understand their analytical challenges and helps address them with Waters solutions.</p>
</blockquote>


Waters Corporation: Historical and Emerging Trends for Residues and Contaminants in Products of Animal Origin

Historical and Emerging Trends for Residues and Contaminants in Products of Animal Origin

Learn how RASFF operates as applied to residues and contaminants in food of animal origin, veterinary drug residues, and PFAS.

Residues and Contaminants in Products of Animal Origin

<p><strong>Event Program</strong></p>
<ul>
<li>Introduction</li>
<li>Temperature effects on sensors</li>
<li>Temperature effects on buffers/solutions</li>
<li>Temperature compensation on the part of the sensor</li>
<li>Temperature compensation on the part of the buffers</li>
<li>Summary</li>
<li>Q&amp;A and feedback</li>
</ul>
<p>The temperature plays a critical role in pH measurements. Achieving accurate pH values is not only about the chemical composition of a solution but also about understanding the impact of temperature fluctuations. Temperature can significantly influence the behavior of pH electrodes and the characteristics of the sample, making it essential to understand its effects on pH measurements. Challenges arise when temperature differentials between the electrode and the sample lead to unstable readings, highlighting the need for a deeper understanding of temperature&#39;s influence on pH.</p>
<p>During our webinar, you will learn about the relationship between temperature and pH. From the temperature dependence of the dissociation constant of water to the impact of temperature on the activity coefficient and acid constants, we will see the complexities of temperature effects on pH measurements. Understanding these nuances can help you enhance the accuracy and reliability of your pH measurements, ensuring precise results across diverse temperature conditions.</p>
<p>Register now for our upcoming webinar to gain valuable insights into the effect of temperature on pH and deepen your understanding of this relationship. Join us and gain the knowledge to optimize your pH measurements and achieve consistent, reliable results.</p>
<h5><strong>How does temperature affect pH measurements?</strong></h5>
<p>Temperature can significantly impact pH measurements by altering the behavior of pH electrodes and the characteristics of the sample. Temperature changes can cause the pH electrode to drift until the temperature of the electrode and the sample become equal, leading to unstable readings. Additionally, the temperature dependence of the dissociation constant of water and the solution&#39;s activity coefficient and acid constants can cause changes in the H+ concentration and real pH value changes.</p>
<h5><strong>How can I compensate for temperature effects on pH measurements?</strong></h5>
<p>Temperature compensation tables have been determined for standard buffer solutions, which can be programmed into pH meters to ensure the correct pH value is used for the buffer at the temperature at which the calibration is performed. However, it is almost impossible to compensate for the temperature coefficient of every sample solution, making it essential to measure samples at the same temperature to make accurate comparisons.</p>
<h5><strong>What are the best practices for handling pH electrodes in temperature-sensitive environments?</strong></h5>
<p>To ensure accurate pH measurements in temperature-sensitive environments, it is crucial to use the correct pH electrode for the specific sample and give the electrode enough time to equilibrate and to maintain the electrode properly.</p>
<p>When measuring in samples that do not consist of easy-to-measure clear, aqueous solutions, problems of electrical or chemical origin can occur, which should be addressed by following the manufacturer&#39;s instructions for electrode handling and maintenance.</p>
<blockquote>
<p><strong>Presenter:</strong> Dr Reena Mascarenhas</p>
</blockquote>
<blockquote>
<p>Reena is an electrochemist, working for METTLER TOLEDO, with over five years of experience in training others in various aspects of the field. Her in-depth understanding, technical expertise, and engaging and informative training style make her a prominent speaker for this webinar.</p>
</blockquote>


Mettler-Toledo: Temperature Effects on pH Measurement

Temperature Effects on pH Measurement

A Live Webinar to Understand the Relation between Varying Temperature and pH.

<p><strong>The scientific community aims to enhance transparency and reliability in published research, with a specific focus on the quality of biological reagents, notably recombinant proteins. Concerns have been raised regarding irreproducible results, prompting discussions on common quality issues associated with recombinant proteins and their impact on downstream applications. In response, professionals in protein purification and characterization have collaboratively developed guidelines for improved quality control.</strong></p>
<p>These guidelines include minimal information requirements for protein identity, production parameters, and long-term stability, as well as a minimal set of quality tests for purity, homogeneity, and identity. Additional recommendations cover DNA contamination, “spectral and thermal denaturation signatures”, homogeneity, “competent fraction”, storage conditions, batch-to-batch reproducibility, and other factors based on intended applications. Evaluation of these guidelines over a one-year period suggests that their implementation can enhance experimental reliability and optimize protein quality. Investing in protein QC benefits all stakeholders in life sciences, including researchers, editors, and funding agencies, by improving data veracity and minimizing resource wastage.</p>
<blockquote>
<p><strong>Presenter:</strong> Dr. André Matagne (Full Professor at the University of Liège, Belgium)</p>
</blockquote>


Waters: Quality control of purified proteins to improve research data reproducibility: improving the time-efficiency and quality of your results

Quality control of purified proteins to improve research data reproducibility: improving the time-efficiency and quality of your results.

Quality control of purified proteins

<p><strong>The recent pandemic has forced the field of medicine to witness groundbreaking advancements with the development and widespread adoption of novel therapeutic modalities, particularly concerning nucleic acid-based medicines. Among these, messenger RNA (mRNA), lipid nanoparticle (LNP) delivery systems, and viral vector-based medicines have emerged as transformative technologies, unlocking new possibilities for treating a myriad of genetic diseases and cancers. As such, ensuring the quality and integrity of these therapeutics becomes paramount.</strong></p>
<p>Impurities and structural integrity issues can impact the safety and efficacy of these medicines. Herein lies the emerging significance of size exclusion chromatography (SEC) combined with MALS for impurity and integrity analysis. In this webinar, we will highlight the critical quality attributes using new 1000 Å ultrawide pore columns with MALS detection to resolve and analyze long-chain nucleic acids (RNA/DNA), lipid nanoparticles (LNPs) and viral vector formulations.</p>
<ul>
<li>Development of high-resolution and robust multiattribute methods for mRNA integrity and aggregate analysis</li>
<li>Method conditions for Intact Lipid Nanoparticle (LNP) heterogeneity analysis</li>
<li>Aggregate analysis and elucidating degradation pathways with high efficiency and low adsorption hardware using the new 1000 Å ultrawide pore columns</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Dr. Adam Crowe (Sr. Manager Analytical Development, Precision NanoSystems ULC - part of Cytiva)</p>
</blockquote>
<blockquote>
<p>Adam Crowe manages a mult-discipline team at Precision NanoSystems ULC (part of Cytiva) tasked with developing novel analytical assays related to lipid nanoparticles (LNP) and nanomaterials for drug delivery. Notably, Adam and his team have increasingly leveraged cutting-edge technologies, such as LC-MS approaches, to tackle complexities of LNP characterization. Latest studies were focused on the detail characterization of impurities found in ionizable liquids.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Lavelay Kizekai (Principal Scientist, Waters Corporation, Milford, Massachusetts)</p>
</blockquote>
<blockquote>
<p>Lavelay Kizekai is a Principal Scientist at Waters Corporation. He joined Waters in 2009 and has since applied himself to developing new LC methods, leading column technology product development work, and establishing insight-based QC procedures for Waters products. His primary area of focus is biomolecule separations using Size-Exclusion Chromatography (SEC). He was a core member of the team that recently bought to market a column suited to platform methods for monoclonal antibodies and antibody drug conjugates. He is currently leveraging these SEC technologies and even newer breakthroughs for the characterization of gene-based therapeutics by multi-angle light scattering (SEC-MALS).</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Mandana Fasth (Principal Product Manager, Waters Corporation)</p>
</blockquote>
<blockquote>
<p>Mandana Fasth is the Global Principal Product Manager at Waters Corporation. She received her Master degree in Biochemistry from Uppsala university in Sweden. With more than 20 years&#39; experience working with biologics workflows such as Sized-Exclusion Chromatography and column development projects, she is a well versed at training and supporting scientists with method development for characterization and purification of biologics.</p>
</blockquote>


Waters Corporation: Unveiling CQA Insights for mRNA, LNPs and Viral Vectors by SEC and MALS with Novel 1000 Å Ultrawide Pore Particle Columns

Unveiling CQA Insights for mRNA, LNPs and Viral Vectors by SEC and MALS with Novel 1000 Å Ultrawide Pore Particle Columns

This webinar will highlight the critical quality attributes using new 1000 Å ultrawide pore columns with MALS detection.

CQA Insights for mRNA, LNPs and Viral Vectors by SEC/MALS

<p><strong>In Vitro Diagnostic Regulation (IVDR) is the European Union’s new set of rules aimed at improving the quality, safety and reliability of IVDs. The new regulation is impacting the in vitro diagnostic landscape, affecting laboratories using their own “Laboratory Developed Tests” (LDTs) and those compliant with certain accreditation e.g. standard EN ISO 15189.</strong></p>
<p><strong>In this webinar you will learn:</strong></p>
<ul>
<li>What is IVDR and what are the timelines</li>
<li>What are the requirements for in-house tests (LDTs)</li>
<li>What are the next steps for your lab</li>
</ul>
<blockquote>
<p><strong>Presenter:</strong> Fabian Reijn (Diagnotix)</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Magali Wolff (Tecan)</p>
</blockquote>


Making sense of IVDR for LC-MS

In this webinar you will learn what is IVDR and what are the timelines, what are the requirements for in-house tests, and what are the next steps for your lab.