<p><strong>Scientists from CEITEC Masaryk University, together with colleagues from the United States, have discovered a critical vulnerability in bacteria: without the protein RimM, they recover only very slowly under nutrient limitation or after stress. The proper assembly of ribosomes – the cell’s protein factories – plays a key role in their ability to resume multiplication. These findings open up a new way to disrupt bacteria’s capacity to restart proliferation, which could in the future help medicine better combat infections.</strong></p><p><strong>Every bacterium has one essential ability </strong>– when exposed to unfavourable conditions, it can slow down and survive until conditions improve. Once they do, it quickly resumes its activity. It is precisely in this process that scientists from <strong>CEITEC at Masaryk University</strong> have identified bacteria’s Achilles’ heel.</p><p>The research team focused on the bacterium <i><strong>Escherichia coli</strong></i><strong> </strong>and found that <strong>without the protein RimM, its cells recover from stress much less efficiently</strong>. Their ability to resume cell division is slow in such cases, as <strong>RimM is involved in the assembly of ribosomes</strong> – structures essential for the production of proteins required for cell survival. Without it, bacteria multiply much more slowly following stress.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_199d25ed9b.jpg" alt="CEITEC/Demo Lab: Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly: Cryo-EM micrograph of ribosomal particles dispersed in a thin layer of amorphous ice." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_199d25ed9b.jpg 207w," sizes="100vw" width="1600" height="1205"></p><p>Using <strong>cryo-electron microscopy</strong>, the scientists observed how ribosomes behave in the absence of RimM. They found that ribosomes <strong>assemble slowly and in a disordered manner</strong> – particularly in regions critical for accurate reading of genetic information – effectively placing the cell in a kind of “waiting mode.” <i>“We found that the protein RimM is much more important for bacteria than previously thought,”</i> says first author<strong> </strong><a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/ahmed-adel-ibrahim-hassona-hassan/u94046?page=publication"><strong>Ahmed H. Hassan</strong></a>. <i>“Without it, the bacterial cell struggles to return to normal function, as ribosomes mature only slowly.”</i></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_3_1e27130702.jpeg" alt="CEITEC: Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly: Ahmed H. Hassan." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_3_1e27130702.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>The study also revealed that under these conditions, bacteria activate a protective mechanism that prevents premature joining of incomplete ribosomal parts. Additional proteins are engaged to deliberately slow the process, reducing the risk of forming defective ribosomes. As a result, the bacterium eventually recovers, but much later than usual. This vulnerability – where bacteria without RimM operate in a slowed-down mode – could in the future be exploited in <strong>new therapeutic strategies against bacterial infections</strong>.</p><p><strong>RimM is commonly found in bacteria but does not occur in humans</strong>, which is a major advantage for drug development, including antibiotics. If scientists develop a drug that blocks this protein, it would affect only bacteria and not human cells. <i>“Such a treatment could significantly hinder bacterial recovery after stress caused, for example, by antibiotics, thereby limiting their further spread without causing side effects in patients,”</i> explains lead researcher<strong> </strong><a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/gabriel-demo-ph-d/u92825"><strong>Gabriel Demo</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_4_474572c812.jpeg" alt="CEITEC/Martin Indruch: Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly: Gabriel Demo." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_4_474572c812.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>The study, conducted in collaboration with scientists from <strong>Thomas Jefferson University, Columbia University, and the University of California, Riverside</strong>, was published in the journal <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41467-026-71781-6"><strong>Nature Communications</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_2_d3266ee9ec.jpg" alt="CEITEC/Ahmed H. Hassan: Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly: Model of ribosome assembly with identified factors (red and blue) that promote assembly in the absence of RimM." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Achillova_pata_bakterii_bez_klicoveho_proteinu_se_mnozi_pomalu_2_d3266ee9ec.jpg 103w," sizes="100vw" width="1600" height="2423"></p>

Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly 

<p><strong>This study investigates the impact of emitter positioning on signal intensity in nanoflow electrospray ionization mass spectrometry. By systematically varying emitter position in three dimensions, the authors demonstrate that signal robustness improves at greater distances along the z-axis, with consistent performance maintained within 1–2 mm of the optimal position.</strong></p><p>Signal behavior was consistent across the m/z range, indicating that precise repositioning for different analytes is unnecessary. These findings provide practical guidance for improving robustness and reproducibility in nanoflow LC–MS/MS proteomics workflows.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/jasms.5c00441"><strong>Regarding Emitter Positioning for Nanoflow Electrospray Ionization with a High-Capacity Inlet Capillary</strong></a></h4><p>Noah M. Lancaster, Scott T. Quarmby, Katherine A. Overmyer, and Joshua J. Coon*</p><p>J. Am. Soc. Mass Spectrom. 2026, 37, 3, 754–759</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/jasms.5c00441">https://doi.org/10.1021/jasms.5c00441</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><div><p>Owing to its high sensitivity, nanoflow electrospray liquid chromatography coupled with tandem mass spectrometry (nESI-LC-MS/MS) is widely used for protein sequence analysis. <a href="javascript:void(0);">(1,2)</a> Whereas high-flow electrospray sources typically have relatively fixed emitter alignments and are more robust to changes in emitter positioning, nESI sources frequently require manual alignment in three dimensions. <a href="javascript:void(0);">(3,4)</a> Since the number of ions reaching the MS system can vary depending on the location of the nESI emitter, positioning is a critical aspect of achieving robust and reproducible results.</p><p>Multiple reports illustrate the relationship between emitter positioning and electrospray signal intensity; <a href="javascript:void(0);">(2,4−10)</a> however, these studies typically examine a single dimension or evaluate emitters and flow regimes not typical of shotgun proteomic workflows. To understand these relationships, we investigate here the effect of emitter positioning on signal intensity when using fused-silica capillaries with integrated emitters at a flow rate of 300 nL/min, a common choice across the field. <a href="javascript:void(0);">(11−17)</a> Experiments were conducted using an Orbitrap Ascend mass spectrometer, a notable example of instruments commonly used in proteome analysis, <a href="javascript:void(0);">(18)</a> which features a nanoflow source and asymmetric inlet capillary (high-capacity transfer tube, HCTT). This work represents, to our knowledge, the first report in the literature characterizing how emitter positioning impacts signal intensity for nanoflow electrospray ionization into an inlet capillary without radial symmetry.</p><p>Since most nESI emitters are manually positioned, understanding the precision in positioning that is required could assist in reducing batch-to-batch variation that is common in larger proteomic experiments. Further, recent efforts to improve the throughput of proteome analysis feature the use of multiple columns with multiple emitters aligned with the source at the same time. <a href="javascript:void(0);">(19−23)</a> By performing measurements in all three dimensions, this report provides insight for implementing such a multiemitter setup.</p><h4><strong>Experimental Section</strong></h4><p>Emitter positioning measurements were performed by infusing BSA peptides at 300 nL/min into an <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/748"><strong>Orbitrap Ascend mass spectrometer</strong></a> (Thermo Scientific) using a fused silica capillary (360 μm O.D, 75 μm I.D.) with integrated emitter (∼10 μm opening). <a href="javascript:void(0);">(24)</a> The emitter was aligned to the inlet using the source camera and the <i>x</i>/<i>y</i>/<i>z</i> micrometer on a NanoSpray Flex source (Thermo Scientific). The origin of the coordinate system used here was defined as the center of the inlet capillary opening. In particular, the <i>z</i> = 0 plane is orthogonal to the opening of the inlet capillary, and the <i>x</i> = 0 and <i>y</i> = 0 planes are parallel to the inlet capillary axis. Top- and side-view images of the starting position are shown in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S2</a>. Code used for data analysis is available at <a target="_blank" rel="noopener noreferrer" href="https://github.com/coongroup/EmitterPositioning">https://github.com/coongroup/EmitterPositioning</a>. Raw data is available at MassIVE accession number MSV000100165. Additional experimental and data analysis details are described in the <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Supporting Information</a>.</p><h4><strong>Results and Discussion</strong></h4><p>We characterized signal intensity dependence on emitter position for nanoflow electrospray by infusing a mixture of peptides generated via trypsin digestion of purified BSA in an Orbitrap-quadrupole linear ion trap hybrid mass spectrometer (Orbitrap Ascend Tribrid). To ensure LC–MS applicability, we used an emitter size (∼10 μm orifice) and flow rate (300 nL/min) identical to those typical of capillary LC–MS. <a href="javascript:void(0);">(11−17)</a> The resulting MS1 analysis produced numerous ions across the <i>m</i>/<i>z</i> range (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S3</a>). We selected two of these ions, a doubly protonated species (LGEYGFQNALIVR at <i>m</i>/<i>z</i> 740.4) and a triply protonated species (RHPEYAVSVLLR at <i>m</i>/<i>z</i> 480.6), for their strong signal intensity and stability over the time range of the experiments here (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figures S4 and S5</a>). With the above setup, we tracked those <i>m</i>/<i>z</i> peaks as a function of emitter position in three dimensions and recorded intensity distributions (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/jasms.5c00441#fig1">Figure 1</a>). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/jasms.5c00441#fig1">Figure 1</a>C presents the ion signal across x-positions, where the <i>x</i> = 0 plane is aligned to the central axis of the inlet capillary and the dashed lines depict the MS inlet opening width in this dimension (0.6 mm, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S6</a>). <a href="javascript:void(0);">(25,26)</a> Strikingly, we observe that the signal is relatively stable and high across two millimeters of the <i>x</i>-dimension. Further, greater than 50% of the ion signal is retained at distances up to ∼five times the width of the inlet (i.e., full width half max (fwhm)). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/jasms.5c00441#fig1">Figure 1</a>D presents the same concept but in the y-dimension, where good signal stability is also observed across a similar length of two millimeters; however, the larger inlet opening in the y-dimension (1.6 mm) does not appear to proportionally impact the width of the intensity distribution. The ion plume is roughly symmetrical in both <i>x</i>- and <i>y</i>-dimensions; <a href="javascript:void(0);">(8)</a> therefore, it is expected that the smaller inlet width in the <i>x</i>-dimension would have a higher probability of being in the high density region of the plume than in the <i>y</i>-dimension. Proportional to inlet opening, the <i>x</i> position of the emitter would consequently have less of an effect on the intensity than the <i>y</i> position. We note the intensity distributions appear to be slightly off-center; however, we find the centroids of the distributions (−0.1 and 0.3 mm, <i>x</i>- and <i>y</i>-respectively, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S7</a>) were within the tolerance of the micrometer. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/jasms.5c00441#fig1">Figure 1</a>E presents the ion intensities as a function of emitter position in the <i>z</i>-dimension. Impressively, signal continues to be observed up to ∼7 mm removed from the inlet at levels close to 50% of the highest. Not surprisingly, the highest signal is observed at the closest position, but, as noted above, that signal gradually declines with increasing distance. The relative intensities of these two peptide ions remain fairly constant at all observed z positions (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S8</a>). Overall, identical trends were observed for both peptides over all dimensions. As these peptides are fairly high signal intensity, we wanted to confirm that the trends reported here were not biased by signal saturation, so we extracted signal intensities for low intensity features and compared the <i>x</i>, <i>y</i>, and <i>z</i> intensity distributions (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/jasms.5c00441/suppl_file/js5c00441_si_001.pdf">Figure S9</a>). This analysis confirms that these two peptides are representative of global trends for our tryptic peptide sample.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Am_Soc_Mass_Spectrom_2026_37_3_754_759_Figure_1_1_D_Positioning_Experiments_A_The_xyz_coordinate_system_used_for_this_study_c971dc3d2f.jpg" alt="J. Am. Soc. Mass Spectrom. 2026, 37, 3, 754–759: Figure 1. 1D Positioning Experiments. (A) The x/y/z coordinate system used for this study. (B) An x/y perspective of the inlet with coordinate definitions. (C) Intensity dependence on x-position for two selected peptides (at y = 0 and z = −0.9). Dotted lines indicate the estimated position of the inlet capillary edges. (D) Intensity dependence on y-position for two selected peptides (at x = 0 and z = −0.9). Dotted lines indicate the estimated position of the inlet capillary edges. (E) Intensity dependence on z-position for two selected peptides (at x = 0 and y = 0)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Am_Soc_Mass_Spectrom_2026_37_3_754_759_Figure_1_1_D_Positioning_Experiments_A_The_xyz_coordinate_system_used_for_this_study_c971dc3d2f.jpg 94w," sizes="100vw" width="996" height="1652"></p><h4><strong>Conclusions</strong></h4><p>We report the dependence of peptide signal intensity on emitter positioning for nanoflow electrospray. Specifically, within 1–2 mm in any dimension, one can achieve reasonably consistent and robust signal. Distinct intensity profiles we observed here for the <i>x</i>- and <i>y</i>-dimensions likely arise from the asymmetric shape of the ion capillary. We demonstrate improved robustness of signal intensity to <i>x</i>/<i>y</i> variation at increasing <i>z</i> distances, an observation that will be helpful for positioning multiple emitters, for example. <a href="javascript:void(0);">(19−23)</a></p><p>We provide evidence that the effect of the emitter position on signal intensity does not strongly depend on the analyte for bottom-up proteomics analysis. This report provides insight into the role of emitter positioning on signal intensity for bottom-up proteomics and represents the first characterization of the effect of emitter position on electrospray signal intensity on an instrument with an inlet capillary lacking radial symmetry. Future areas of interest would be an examination of how trends vary across different flow rates or emitter types, as well as assessing how the exact intensity profiles vary across instruments with differences in their atmospheric interface.</p></div>

Regarding Emitter Positioning for Nanoflow Electrospray Ionization with a High-Capacity Inlet Capillary

<p><strong>In the week of May 4, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 500 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. Merck: Recent Advances in Chromatographic Approaches in Characterizing Antibody-Drug Conjugates</strong></h5><ul><li>Tu, 5.5.2026 16:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6146">Registration</a></li></ul><p>Explore advanced LC-MS and HIC strategies for comprehensive ADC characterization, including impurity profiling, DAR analysis, and MS-compatible workflows.</p><h5><strong>2. Waters Corporation: Empower Tips: Ask Me Anything About Updates in Empower Software to Advance Your Compliance</strong></h5><ul><li>Tu, 5.5.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5975">Registration</a></li></ul><p>Discover the latest Empower CDS updates and learn how new features enhance compliance, security, USP calculations, and risk reduction in modern chromatography labs.</p><h5><strong>3. Metrohm: Electrochemiluminescence: The technique that should be on your radar for sensor development</strong></h5><ul><li>We, 6.5.2026 09:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6158">Registration</a></li></ul><p>In this webinar, we will explore what makes ECL a unique technique for sensor development providing key hints and examples.</p><h5><strong>4. Phenomenex: How To Start Up and Shut Down LC and LC-MS Instruments</strong></h5><ul><li>We, 6.5.2026 10:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6180">Registration</a></li></ul><p>Learn practical LC and LC-MS startup and shutdown procedures, column care, and system checks in this webinar. Gain system-agnostic best practices to protect instruments and maximize column lifetime.</p><h5><strong>5. Thermo Fisher Scientific: Integrated LC-MS CDS workflow for automated ADC and DAR analysis</strong></h5><ul><li>We, 6.5.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6135">Registration</a></li></ul><p>In this webinar, we’ll present an automated, high-throughput intact ADC workflow using LC-MS under native conditions on the Thermo Scientific Orbitrap Exploris 240 mass spectrometer.</p><h5><strong>6. Waters Corporation: Improving Sensitivity and Throughput in Early Drug Development with Inert LC Technologies</strong></h5><ul><li>We, 6.5.2026 16:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6152">Registration</a></li></ul><p>Discover how Waters MaxPeak Premier Columns improve LC method development with better sensitivity, peak shape, and robustness for acidic analytes in early drug research.</p><h5><strong>7. Thermo Fisher Scientific: Keeping Up with Evolving Regulatory Requirements: Addressing Analytical Challenges for Known and Unknown Nitrosamines</strong></h5><ul><li>Th, 7.5.2026 05:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6166">Registration</a></li></ul><p>Join our webinar to see how advanced LC-MS tools can help you confidently quantify known nitrosamines and uncover unknown impurities.</p><h5><strong>8. Waters Corporation: Transform Your Daily Lab Operations with Automation - Proteomics Workflows</strong></h5><ul><li>Th, 7.5.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6165">Registration</a></li></ul><p>Explore how automated liquid handling improves reproducibility, scalability, and efficiency in proteomics workflows across digestion, desalting, and peptide analysis.</p><h5><strong>9. SCIEX: Assessing biotherapeutic stability through forced degradation using intact and subunit icIEF-UV/MS workflows</strong></h5><ul><li>Th, 7.5.2026 11:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6181">Registration</a></li></ul><p>Explore icIEF-UV/MS workflows for biotherapeutic stability studies. Learn how to identify charge variants and degradation pathways in monoclonal antibodies with enhanced analytical confidence.</p><h5><strong>10. Metrohm: Environmental waters: A new generation of high-capacity IC columns makes analysis more efficient</strong></h5><ul><li>Th, 7.5.2026 15:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6155">Registration</a></li></ul><p>Learn how next-generation high-capacity IC columns enable compliant, robust analysis of environmental waters with improved detection limits and streamlined workflows.</p><h5><strong>11. Waters Corporation: Add a New Dimension - MS Imaging for Environmental Analysis</strong></h5><ul><li>Th, 7.5.2026 15:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5927">Registration</a></li></ul><p>Learn about MS imaging and discover key benefits of Desorption Electro Spray Ionisation (DESI) for environmental analysis.</p><h5><strong>12. US HUPO: Raising the Bar: Quality Assurance and Data Integrity in MALDI MSI</strong></h5><ul><li>Th, 7.5.2026 19:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6133">Registration</a></li></ul><p>Join US HUPO experts to explore quality assurance and data integrity in MALDI MSI, covering best practices for reliable imaging workflows and reproducible spatial omics data.</p><h5><strong>13. Agilent Technologies: Impurity Characterization of GLP-1 Receptor Agonists via RPLC and HILIC</strong></h5><ul><li>Th, 7.5.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5998">Registration</a></li></ul><p>Explore RPLC and HILIC strategies for GLP-1 impurity profiling. Learn method development tips to optimize separation, resolution, and regulatory-ready characterization.</p><h5><strong>14. Agilent Technologies: Accelerating LC/MS Impurity Screening Followed by ECD-Based Sequence Analysis for GLP-1 Analogs</strong></h5><ul><li>Fr, 8.5.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5945">Registration</a></li></ul><p>Episode 4 of Peptide 360 presents a staged LC/MS workflow for rapid GLP-1 impurity screening followed by ECD-based sequence analysis for precise structural confirmation and faster decisions.</p>

Webinars LabRulezLCMS Week 19/2026

Article

Webinars

Scientific article

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

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

Metrohm

Merck

Phenomenex

Thermo Fisher Scientific

SCIEX

Waters Corporation

<div><h4><strong>Unlock the Power of the Latest Empower CDS Releases</strong></h4><p><strong>Since the base release of Empower Chromatography Data System (CDS) in 2010, we have gone through 36 version updates. These updates have included new features, enhancements to existing functionality, and numerous updates across multiple areas - from instrument support to infrastructure technology.</strong></p><p>In this webinar we will focus on new features and updates in recent releases impacting compliance, an extremely important topic for many of you.</p><h5><strong>What you’ll understand by the end</strong></h5><ul><li>Risks of using outdated software</li><li>Support status of various Empower Software versions</li><li>Security enhancements to Empower CDS</li><li>Recent updates in USP calculations</li><li>Risk reduction of potential bias in the laboratory</li><li>Streamline the lab with Multi Angle Light Scattering and monitoring application</li></ul><h5><strong>Who should attend</strong></h5><ul><li>This webinar is designed for Lab Managers, Empower System Administrators, Quality, Quality IT, and Lab Personnel.</li></ul><p>Please join us for a lively discussion as we explore this topic. As always, please bring your questions for this exclusive opportunity to ask our experts anything about Empower Software.</p><blockquote><p><strong>Presenter:</strong> Neil Lander (Senior Principal Product Manager, Waters Corporation)</p><p>Neil has worked for Waters Corporation since 1994 and has held a variety of positions including Technical Support Specialist, Technical Trainer, Manager Customer Education and currently, Senior Principal Product Manager focusing on Informatics solutions.</p><p>He provides internal support for Empower Chromatography Data System and is focused on developing laboratory software solutions that help organizations achieve their scientific and operational objectives.</p></blockquote></div>

Waters Corporation: Empower Tips: Ask Me Anything About Updates in Empower Software to Advance Your Compliance

Empower Tips: Ask Me Anything About Updates in Empower Software to Advance Your Compliance

Webinar on recent Empower CDS releases, covering compliance updates, security enhancements, and laboratory risk reduction strategies.

Updates in Empower Software to Advance Compliance

<p><strong>Antibody-drug conjugates (ADCs) require robust characterization of key quality attributes—especially the drug-to-antibody ratio (DAR)—to support confident decisions in discovery, development, and manufacturing.</strong></p><p><strong>In this webinar, we’ll present an automated, high-throughput intact ADC workflow using LC-MS under native conditions on the Thermo Scientific Orbitrap Exploris 240 mass spectrometer, fully integrated within Thermo Scientific Chromeleon CDS.</strong></p><p>You’ll see how a single, unified platform can bring together data acquisition, automated intact deconvolution, DAR calculation, and reporting—reducing manual handoffs and analyst intervention while improving consistency and throughput. Whether you are scaling ADC characterization, standardizing DAR reporting, or looking to streamline intact analysis, this session will highlight a practical, end-to-end approach designed for efficient routine use.</p><h4><strong>Key learning objectives:</strong></h4><ul><li>Why intact ADC analysis (native LC–MS) is valuable for monitoring ADC heterogeneity and DAR-related attributes</li><li>How high-resolution mass spectrometry (HRMS) supports confident intact mass measurements for ADC characterization</li><li>What an end-to-end Chromeleon CDS workflow looks like—from instrument control to automated processing and reporting</li><li>How automated intact deconvolution enables rapid, consistent interpretation of intact ADC datasets</li><li>Approaches to automated DAR calculation and standardized reporting to support high-throughput workflows and data integrity</li></ul><h4><strong>Who should attend?</strong></h4><ul><li>ADC analytical characterization scientists in biopharma/biotech (discovery through late-stage)</li><li>LC-MS / HRMS users developing or running intact protein and ADC methods</li><li>CMC, process development, and QC teams interested in scalable DAR characterization workflows</li><li>Lab automation and informatics professionals focused on integrating acquisition, processing, and reporting</li><li>Chromeleon CDS users looking to expand into integrated intact deconvolution and reporting</li></ul><p><i>Cannot attend the broadcast on May 6? Please register to automatically receive the link to the recording.</i></p><blockquote><p><strong>Speaker: </strong>Dr. Ulrik H. Mistarz (Application Scientist, Thermo Fisher Scientific)</p><p>Dr. Ulrik Mistarz is a Senior Application Scientist at Thermo Fisher Scientific in Copenhagen, Denmark. He supports a broad range of LC-MS applications with a focus on developing novel workflows for characterization of oligonucleotides, therapeutic proteins, as well as different antibody formats.</p><p>He has a strong interest in improving the throughput and automation of analytical workflows through developing new LC-MS as well as software workflows.Ulrik Mistarz has a PhD from The Department of Pharmacy at the University of Copenhagen and has more than 10 years of experience with pharma/biopharma characterization and analytics. This includes positions in both pharmaceutical and biotech companies working on LC-MS and HPLC application development.</p></blockquote>

Thermo Fisher Scientific: Integrated LC-MS CDS workflow for automated ADC and DAR analysis

Integrated LC-MS CDS workflow for automated ADC and DAR analysis

Webinar, will present automated intact ADC workflow using LC-MS under native conditions on the Thermo Scientific Orbitrap Exploris 240

LC-MS CDS workflow for automated ADC and DAR analysis

<p><strong>Antibody-drug conjugates (ADCs) represent a rapidly growing class of biotherapeutics that combine the specificity of monoclonal antibodies with the cytotoxic potency of small molecule drugs. Comprehensive characterization of ADCs is critical for ensuring product quality, efficacy, and safety, requiring advanced analytical techniques capable of resolving their inherent structural complexity and heterogeneity.</strong></p><p>This webinar presents state-of-the-art liquid chromatography-mass spectrometry (LC-MS) approaches for ADC characterization. The first half focuses on recent advances in reversed-phase LC-MS analysis, highlighting improvements in separation efficiency and detection sensitivity. Application examples will demonstrate the determination of low concentration impurities and variants, the effects of mobile phase and mobile phase modifiers on chromatographic performance, and the performance gains to the method by utilizing unique column geometries (1.5 mm I.D.).</p><p>The second half explores native ADC analysis by hydrophobic interaction chromatography (HIC). Modern HIC stationary phases, combined with targeted mobile‑phase engineering, demonstrate high‑resolution, reproducible DAR separations across multiple ADC modalities, including improved resolution of high‑DAR and low‑abundance species. This state-of-the-art stationary phase was used to develop an HIC workflow using ammonium tartrate to achieve ammonium‑sulfate‑like performance and enabling rapid, MS‑compatible, and PAT‑ready ADC characterization.</p><p>Attendees will gain practical insights into selecting appropriate LC-MS methodologies for their ADC characterization needs and understanding the complementary nature of reversed-phase and hydrophobic interaction chromatography.</p><h4><strong>During this webinar, you will:</strong></h4><ul><li><strong>Discover the latest advancements in reversed-phase liquid chromatography-mass spectrometry</strong> (LC-MS) for the effective characterization of antibody-drug conjugates (ADCs), focusing on improved separation efficiency and detection sensitivity.</li><li><strong>Learn about practical applications of LC-MS </strong>in identifying low concentration impurities and variants, including the impact of mobile phase components on chromatographic performance.</li><li><strong>Explore innovative techniques in hydrophobic interaction chromatography</strong> (HIC) for native ADC analysis, emphasizing high-resolution and reproducible drug-to-antibody ratio (DAR) separations.</li><li><strong>Gain an understanding about the development of a streamlined HIC</strong> workflow utilizing ammonium tartrate, which enhances ADC characterization efficiency while maintaining compatibility with mass spectrometry and process analytical technology (PAT).</li></ul><blockquote><p><strong>Presenter: </strong>Andrea Krumm (Product Manager, Analytical Columns, Tosoh Bioscience GmbH)</p><p>Andrea Krumm studied biotechnology before gaining a PhD in Cell and Cancer Biology. After four years as an applications specialist for optical analytical devices used in academic and pharmaceutical research, she joined Tosoh Bioscience GmbH in 2020 as a product manager for analytical columns. Andrea is responsible for gathering customer requirements, application areas and addressing these with new and existing products of the analytical columns line.</p><p><strong>Presenter: </strong>Cory E. Muraco (Senior Global Product Manager, Large Molecule HPLC, MilliporeSigma, the life science business of Merck KGaA, Darmstadt, Germany)</p><p>Cory E. Muraco is the Senior Global Product Manager for Large Molecule HPLC Columns at MilliporeSigma, the life science business of Merck KGaA, Darmstadt, Germany. After finishing his graduate studies at Youngstown State University (Youngstown, Ohio, USA), Cory started his career at MilliporeSigma in 2013. After holding several roles in both R&amp;D and Marketing functions across the past decade, in 2026, Cory assumed his current role as the Large Molecule HPLC Columns Product Manager where he is tasked with designing, developing, and executing the marketing and R&amp;D strategies around MilliporeSigma’s biomolecule HPLC columns. Cory is the author of several manuscripts appearing in trade magazines and has delivered over 100 presentations at international conferences, round table symposia, and at various pharmaceutical and biopharmaceutical companies.</p></blockquote>

Tosoh Bioscience: Recent Advances in Chromatographic Approaches in Characterizing Antibody-Drug Conjugates

Recent Advances in Chromatographic Approaches in Characterizing Antibody-Drug Conjugates

Discover LC-MS and HIC methods for ADC characterization, including DAR analysis, impurity detection, and high-resolution separations for biopharma workflows.

Chromatographic Characterizing Antibody-Drug Conjugates

<p><strong>In the second webinar of the Small Molecules, Big Impact series, Ken Berthelette will demonstrate how Waters™ solutions and MaxPeak Premier Columns can be applied to improve LC discovery and early development workflows.</strong></p><p>This webinar will focus on applied case studies in early drug research development and demonstrate how enhanced surface technology can deliver improved sensitivity and peak shape for acidic analytes, helping teams generate higher-quality data earlier in development process. By focusing on specific applications of method development, this session will highlight how through intelligent column selection and process introduction, development workflows can be streamlined to generate the highest quality data possible.</p><h4><strong>Who should attend</strong></h4><ul><li>Analytical scientists who support early development workflows.</li></ul><h4><strong>Why you should attend</strong></h4><ul><li>Gain a clearer understanding of how MaxPeak Premier Columns can enhance LC workflows through improved sensitivity, peak shape, and robustness for acidic analytes.</li><li>Access resources and tools that enable independent exploration and evaluation of MaxPeak Premier technology within your own laboratory workflows.</li></ul><h4><strong>What you will walk away with</strong></h4><ul><li>A better understanding of MaxPeak Premier technology to gain the advantage in your research</li><li>Insights into how MaxPeak Premier Columns can improve their separations</li><li>Access to resources to support your own research to stay better informed.</li></ul><blockquote><p><strong>Speaker: </strong>Kenneth Berthelette (Principal Scientist, Waters Corporation)</p><p>Ken earned his Bachelor of Science in Professional Chemistry from Bridgewater State University in Bridgewater, Massachusetts in 2010.</p><p>He joined Waters Corporation in March 2012, where he contributed to multiple product launches as part of the Research and Development team. In 2021, Ken transitioned into a role supporting Chemistry Aftermarket initiatives.</p><p>With a strong focus on applications and customer education, he has delivered numerous seminars and webinars covering topics such as method development, method modernization and transfer, HILIC separation techniques, and LC system troubleshooting.</p></blockquote>

Improving Sensitivity and Throughput in Early Drug Development with Inert LC Technologies

Learn how MaxPeak Premier Columns enhance LC workflows, improving sensitivity and peak shape for acidic analytes in early drug development.

Early Drug Development with Inert LC

<p><strong>Compliance with IC methods US EPA 300.1 Parts A and B, ISO 10304 Parts 1 and 4, or US EPA 557 can make efficient monitoring of environmental waters a challenge. Selecting the right column technology is key, whether you are working with carbonate or hydroxide eluents.</strong></p><p>In our upcoming webinar, we focus on a new generation of high-capacity anion exchange columns. We will show how innovative column chemistry enables lowest detection limits and improved robustness against complex matrices for fully compliant analysis of environmental waters.</p><p>Two complementary analytical strategies for the analysis of common anions and oxyhalides are presented in the webinar: The carbonate-based eluent approach with the new Metrosep A Supp 20 column and the hydroxide-selective approach with the Metrosep A Supp 21 column. Both strategies enable performing US EPA 300.1 Parts A and B and ISO 10304 Parts 1 and 4, respectively, in one single run.</p><p>We will also show how automated hydroxide eluent production provides for highly precise and reproducible analyses with ultra‑low baselines, supporting demanding applications such as the determination of haloacetic acids (HAA) according to US EPA 557.</p><h4><strong>Key learnings of this webinar</strong></h4><ul><li>Understand how high-capacity IC columns improve robustness, accuracy, and reproducibility of your IC analysis of environmental waters</li><li>Learn how EPA 300.1 Parts A and B and ISO 10304 Parts 1 and 4, respectively, can be resolved in a single run&nbsp;</li><li>Discover the advantages of automated eluent generation combined with hydroxide-selective columns, such as the Metrosep A Supp 19 column, for haloacetic acid analysis (US EPA 557)</li><li>Explore how the right choice of columns and eluent strategies can optimize your workflows and increase laboratory efficiency and data quality</li></ul><h4><strong>Who should attend?</strong></h4><ul><li>Water utility operators who need robust and reliable analytical techniques to guarantee the safety of drinking water</li><li>Lab managers responsible for their lab’s compliance with the standards and regulations for the analysis of environmental waters</li><li>Scientists, researchers, and analytical method developers who need to stay up to date on state-of-the-art methods for ion chromatography</li><li>Laboratory staff and managers interested in a reliable, cost- and time-efficient analysis technique for their monitoring of environmental waters</li></ul><blockquote><p><strong>Presenter: </strong>Dr. Vincent Diederich (Product Manager Ion Chromatography Columns, Metrohm International Headquarters)</p><p>Vincent Diederich received his MSc in Chemical and Bioengineering at the ETH Zurich in Switzerland and stayed there for a PhD in Chemical Engineering where he gained a deep understanding of polymer reaction engineering. Since 2015, he has worked at Metrohm International Headquarters focusing on column and method development for ion chromatography, initially as a Column Production Specialist and now as Product Manager for ion chromatography columns.</p></blockquote>

Metrohm: Environmental waters: A new generation of high-capacity IC columns makes analysis more efficient

Environmental waters: A new generation of high-capacity IC columns makes analysis more efficient

Discover advanced IC column strategies for EPA and ISO water analysis, improving sensitivity, robustness, and efficiency in environmental monitoring workflows.

High-capacity IC columns for water analysis

<p><strong>Electrogenerated Chemiluminescence (ECL) has rapidly become one of the most powerful analytical techniques for applications requiring extreme sensitivity, specificity, and quantitative performance. In this webinar, we will explore what makes ECL a unique technique for sensor development providing key hints and examples.</strong></p><p>We will begin by introducing the core principles behind the ECL mechanism, including its advantages over traditional methods. We will then move on to discuss specific case studies.</p><p>To bridge science with practical implementation, we will demonstrate how advanced ECL instrumentation streamlines workflows, improves sensitivity and reproducibility, and expands the range of possible applications. This includes an overview of our instrumental solutions, highlighting their ease of use, performance benefits, and integration into routine analytical environments.</p><h4><strong>By the end of the session, participants will gain:</strong></h4><ul><li>A clear understanding of the fundamentals and advantages of ECL</li><li>Insights into cutting-edge applications in different fields driving innovation in industry and academia</li><li>Practical examples showing how ECL enables highly sensitive and selective detection</li><li>A preview of instrumental platforms designed to optimize ECL performance</li><li>Guidance on choosing the right systems and configurations for specific analytical needs</li></ul><p>This webinar is ideal for researchers in sensor development that are looking for electrochemical techniques to improve the sensitivity on their concrete application.&nbsp;</p><blockquote><p><strong>Presenter: </strong>Ibáñez Martínez, David (Spectroelectrochemistry Manager, Metrohm Dropsens)</p><p>PhD in Chemistry (2015, University of Burgos, Spain), with expertise in the development of novel devices for time-resolved Raman spectroelectrochemistry, applied to the study of various systems such as carbon nanotubes, metal nanoparticles, conducting polymers, graphene, DNA bases, and liquid–liquid interfaces. Postdoctoral researcher (2015–2017, University of Burgos, Spain), focused on the electrochemical fabrication of Janus materials and their characterization using UV/Vis and NIR spectroelectrochemistry. Product Specialist in Spectroelectrochemistry at Metrohm DropSens S.L.U. (2018–2022) for the development of new applications and spectroelectrochemical devices. Spectroelectrochemistry Manager at Metrohm DropSens S.L.U. (2023–present), leading the development and innovation of fully-integrated spectroelectrochemical and electrochemiluminescence instrumentation.</p></blockquote>

Metrohm: Electrochemiluminescence: The technique that should be on your radar for sensor development

Electrochemiluminescence: The technique that should be on your radar for sensor development

In this webinar, we will explore what makes ECL a unique technique for sensor development providing key hints and examples.

Electrochemiluminescence

<h3><strong>Bringing laboratory automation to life with Andrew+ and OneLab</strong></h3><p>This webinar series explores how Andrew+ automated liquid handling and OneLab workflow software support consistent, traceable and efficient laboratory operations. Through application‑focused episodes, you will see how automation can be successfully integrated into everyday laboratory workflows, from method development to routine and regulated environments, supported by customer experiences and testimonials.</p><h4><strong>Episode 1 – Proteomics Workflows</strong></h4><h5><strong>Overview</strong></h5><p>Automation plays a key role in modern proteomics, where reproducibility and consistency are essential. In this episode, we explore how automated liquid handling supports robust, scalable sample preparation workflows while reducing manual variability across studies, with insights shared directly from proteomics laboratories using automation in practice.</p><h5><strong>Key highlights</strong></h5><ul><li>Apply automation across proteomics workflows including digestion, desalting, peptide quantification and normalization</li><li>Reduce batch effects and improve reproducibility in long-term and large-scale studies</li><li>Support evolving proteomics methods with flexible, reliable automation<br>Speakers</li></ul><h5><strong>Customer testimonials:</strong></h5><p><strong>Imperial College London – National Phenome Centre</strong></p><ul><li>A leading UK-based academic research centre specialising in large-scale, high‑throughput proteomics and multi‑omics studies.<br>In this episode, the team shares how automated liquid handling has been integrated into routine proteomics sample preparation workflows — from protein assays and digestion to desalting, peptide quantification and sample normalisation — enabling highly reproducible results while significantly reducing batch variation across long-term studies.</li></ul><p><strong>MRC Laboratory of Medical Sciences</strong></p><ul><li>A biomedical research institute focused on understanding the molecular basis of human disease, with strong expertise in proteomics and metabolomics.<br>The laboratory provides insight into how automation supports attention‑intensive workflows such as concentration normalisation and solid phase extraction (SPE), helping to improve consistency, usability and throughput in proteomics sample preparation.</li></ul><p><strong>University of Leicester – Van Geest Multiomics Facility</strong></p><ul><li>A university-based multiomics facility supporting large‑scale clinical and translational research projects.<br>In this episode, the facility explains how automated liquid handling has transformed proteomics workflows for large cohort studies, enabling scalable, flexible sample preparation while minimising batch effects and supporting highly reproducible biomarker research.</li></ul><p><strong>Reserve Your Spot Today!</strong></p>

Transform Your Daily Lab Operations with Automation - Proteomics Workflows

Learn how automation enhances proteomics workflows, improving reproducibility, reducing batch effects, and enabling scalable sample preparation.

Transform Daily Lab Operations with Automation - Proteomics

<div><div container-id="cq-colctrl-lt0" comp-id="A1"><div><p><strong>Regulatory expectations around nitrosamines continue to evolve, placing increasing pressure on analytical workflows to deliver both accuracy and flexibility. Join our upcoming webinar with AbbVie to see how advanced LC-MS tools can help you confidently quantify known nitrosamines and uncover unknown impurities, saving valuable time and resources.</strong></p><h4><strong>What you’ll learn:</strong></h4><ul><li><strong>Confident annotation &amp; accurate quantification:</strong> Leverage the SQUAD approach to precisely identify and quantify targeted nitrosamines using authentic standards and calibration curves.</li><li><strong>Simultaneous targeted &amp; untargeted analysis:</strong> Perform comprehensive screening in a single run—detect known compounds while uncovering unexpected impurities without additional injections.</li><li><strong>Overcoming unknown nitrosamine challenges:</strong> Optimize your LC-MS methods to improve confidence in identifying unknown nitrosamines and meet regulatory expectations.</li></ul><blockquote><p><strong>Presenter: </strong>Jessica Hoskins, PhD (Principal Research Scientist I, Predictive Stability and Structure Elucidation)</p><p>Jessica is a Principal Research Scientist at AbbVie where she and her team focus on Predictive Stability and Structure Elucidation to understand degradation pathways and other potential stability limiting attributes for new synthetic molecule drug substances and drug products. She has a PhD in Organic Chemistry from Tulane University with Scott Grayson, where she first became interested in mass spectrometry for polymers. Prior to joining AbbVie, she was an Adolf Martens Postdoctoral Fellow at the Federal Institute for Materials Research and Testing (BAM) in Berlin, Germany, and worked as an analytical chemist at Stepan Company in the surfactant and polymer industry.</p><p><strong>Presenter:&nbsp;</strong>Sebastien Morin (Sr Manager, Business Development, Thermo Scientific)</p><p>Sebastien is a Senior Manager, Business Development at Thermo Fisher Scientific where he partners closely with Pharma and Biopharma Companies to address analytical challenges. He holds a M. SC. in Organic Chemistry from Universite de Montreal. Prior to joining Thermo Fisher Scientific, he was a Research Associate, Medicinal Chemistry for Boehringer Ingelheim, advancing virology research.</p></blockquote></div></div></div>

Thermo Fisher Scientific: Keeping Up with Evolving Regulatory Requirements: Addressing Analytical Challenges for Known and Unknown Nitrosamines

Keeping Up with Evolving Regulatory Requirements: Addressing Analytical Challenges for Known and Unknown Nitrosamines

Join our webinar to see how advanced LC-MS tools can help you confidently quantify known nitrosamines and uncover unknown impurities.

Analytical Challenges for Known and Unknown Nitrosamines

<h4><strong>Key Learning Points</strong></h4><ul><li>Understand how to prepare your LC/LC-MS system for startup with essential checks, solvent verification, and secure connections.</li><li>Follow clear, step-by-step guidance for LC startup and shutdown procedures (system agnostic guidance).</li><li>Learn best practices for properly cleaning and storing columns, both on and off the system, to maximize lifetime and performance.</li></ul><h4><strong>Who Should Attend</strong></h4><ul><li>The session is aimed at LC and LC‑MS users, especially those newer to the techniques, who want a clear, system‑agnostic protocol to protect columns and instruments during start‑up and shut‑down.</li></ul><blockquote><p><strong>Speaker:</strong> Duilio Romanello (Senior Technical Specialist, Phenomenex)</p><p>Duilio Romanello earned his MSc in Pharmaceutical Chemistry and Technology from the University of Bologna. He joined Phenomenex in 2008 as an Inside Technical Sales Consultant, later leading GC/SPE and Env/Food teams in Italy. Since 2016, he has been Account Manager for Southern Italy and GC Specialist. In 2023, he became Senior Technical Specialist for Phenomenex’s Technical team supporting scientists globally with method development, troubleshooting, and application support.</p></blockquote>

Phenomenex: How To Start Up and Shut Down LC and LC-MS Instruments

How To Start Up and Shut Down LC and LC-MS Instruments

Join this webinar to learn LC/LC-MS startup, shutdown, and column care best practices to improve performance, reliability, and instrument longevity.

Start Up and Shut Down LC and LC-MS Instruments

<p><strong>Biotherapeutic stability is essential for ensuring product quality, safety, and efficacy. In this webinar, discover how forced degradation studies combined with intact and subunit icIEF-UV/MS workflows provide deeper insights into charge variants and degradation pathways. Learn how integrating icIEF with UV and mass spectrometry enhances analytical confidence and supports robust biopharmaceutical characterization.</strong></p><h4><strong>Key highlights</strong></h4><ul><li>Understand how the icIEF-UV/MS method works to identify charge variants in 30 minutes</li><li>Discover how it has been applied to the analysis of an intact and the sub units of a stressed monoclonal antibody</li><li>Find out how the Biologics Explorer software aids data visualisation in both intact and subunit analysis</li></ul><blockquote><p><strong>Speaker:</strong> Dr. Stephen Lock, Senior Market Development Manager, SCIEX</p></blockquote>

SCIEX: Assessing biotherapeutic stability through forced degradation using intact and subunit icIEF-UV/MS workflows

Assessing biotherapeutic stability through forced degradation using intact and subunit icIEF-UV/MS workflows

Join this webinar to learn icIEF-UV/MS workflows for biotherapeutic stability, charge variant analysis, and monoclonal antibody characterization.

Related content

Webinars LabRulezLCMS Week 19/2026

Regarding Emitter Positioning for Nanoflow Electrospray Ionization with a High-Capacity Inlet Capillary

Bacteria’s Achilles’ Heel – Without a Key Protein, They Multiply Slowly