In the week of February 16, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 000 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. Agilent Technologies: From Complex to Simplicity – Get More Peace of Mind on Your HPLC Workflows with InfinityLab Assist</h5><ul><li>Mo, 16.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5908">Registration</a></li></ul>Discover how Agilent InfinityLab Assist simplifies LC system control with intuitive multitouch operation, guided troubleshooting, and smart monitoring to boost efficiency and reduce downtime.<h5>2. Thermo Fisher Scientific: Driving the Process Development of Recombinant Therapeutic Products with Automated MS-Based Target Peptide Mapping</h5><ul><li>Tu, 17.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5931">Registration</a></li></ul>Explore automated MS-based MAM workflows for peptide mapping, enabling faster CMC decisions and scalable analytics from development to QC readiness.<h5>3. Thermo Fisher Scientific: PFAS Analysis Solutions – Innovations for Today’s Labs</h5><ul><li>Tu, 17.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5818">Registration</a></li></ul>Explore the latest challenges and solutions in PFAS analysis for environmental and food testing, including advanced workflows that improve sensitivity, accuracy, and lab efficiency.<h5>4. Phenomenex: Understanding and Applying USP Chapter 621 for Generic Pharmaceutical Applications</h5><ul><li>We, 18.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5794">Registration</a></li></ul>Learn the key guidelines defined in USP &lt;621&gt; and practical examples of how to apply them in generic pharmaceutical method development.<h5>5. SCIEX: Genome Integrity Analysis of Adeno-Associated Viruses (AAV) by Genome Sizing Using a SCIEX Capillary Electrophoresis System</h5><ul><li>We, 18.2.2026 11:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5935">Registration</a></li></ul>Join this webinar to learn how capillary electrophoresis enables reliable genome integrity analysis of AAV for gene therapy applications.<h5>6. Waters Corporation: The Gold Standard – Achieving Optimal Peptide Purification with Reversed-Phase Chromatography</h5><ul><li>We, 18.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5917">Registration</a></li></ul>Discover why reversed-phase chromatography remains the gold standard for peptide purification and analytical performance.<h5>7. Axcend: Understanding Capillary LC – Part 5: Detectors, Sensitivity, and MS/UV</h5><ul><li>We, 18.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5829">Registration</a></li></ul>Join experts to explore MS, UV, and electrochemical detectors at the capillary scale and learn how to achieve reliable sensitivity in capillary LC workflows.<h5>8. Thermo Fisher Scientific: Single Cell and Immunopeptidomics Explorations on Orbitrap Astral MS</h5><ul><li>Th, 19.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5932">Registration</a></li></ul>Discover how Orbitrap Astral MS and Vanquish Neo HPLC enable deep single-cell proteomics and immunopeptidomics from ultra-low-input clinical samples.<h5>9. Evosep Biosystems: Experimental Design Considerations for Scalable Proteomics</h5><ul><li>Th, 19.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5836">Registration</a></li></ul>Explore best practices for experimental design in LC-MS–based proteomics to build robust, reproducible, and scalable analytical workflows.<h5>10. Waters Corporation: Ask Me Anything About Managing Computerized System Risks to Data Integrity</h5><ul><li>Th, 19.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5809">Registration</a></li></ul>Learn practical strategies to manage computerized system risks in regulated laboratories and protect data integrity while ensuring compliance.<h5>11. Shimadzu Corporation: Automating a Comprehensive Amino Acid Panel for Inborn Errors of Metabolism</h5><ul><li>Th, 19.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5936">Registration</a></li></ul>Discover how Shimadzu’s CLAM-2040 automates LC-MS/MS sample preparation to standardize workflows, reduce manual handling, and improve consistency in clinical labs.

Webinars LabRulezLCMS Week 08/2026

Imaging of Protein Assemblies up to 231 kDa in Tissues with Nano-DESI Mass Spectrometry

Metalloproteins play essential roles in marine phytoplankton, yet their metalloproteomes remain poorly characterized. This study combines protein modeling, quantitative proteomics, and ICP-MS measurements to assess metal requirements across several phytoplankton species, including chlorophytes, a haptophyte, and a cyanobacterium.Results show strong agreement between proteome-inferred metal demands and measured cellular metal quotas, while providing deeper insight into biological functions. Mg-containing proteins were most abundant overall, with Zn, Fe, and Mn as dominant trace cofactors. Distinct differences between prokaryotic and eukaryotic phytoplankton were observed, and strain-level analysis demonstrated how metalloproteomes reflect environmental adaptation and metal limitation strategies.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233">Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes</a></h4>Qiong Zhang*, Jiayou Ge, Fengjie Liu, Shabaz Mohammed, Kedong Yin, and Rosalind E. M. RickabyEnviron. Sci. Technol. 2025, 59, 50, 27367–27377<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.est.5c11233">https://doi.org/10.1021/acs.est.5c11233</a><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.Many important biological processes of phytoplankton, including photosynthesis, carbon fixation, and nitrogen reduction, rely on enzymes that have metals as cofactors. <a href="javascript:void(0);">(1)</a> It has been estimated that half of all enzymes must be associated with a particular metal to function. <a href="javascript:void(0);">(2)</a> The availability of metals in the environment has changed over geological time and, given imperfections in the selectivity of metal transport systems, proteins have evolved to make the best use of metals that are more available. <a href="javascript:void(0);">(3−5)</a> Depending on their evolutionary histories, different groups of marine phytoplankton may have differences in their metalloprotein compositions and metal transport strategies. The evolving trace metal availability in the environment, thus, may provide a selective pressure to promote the proliferation of different phytoplankton groups in the oceanic environment, affecting the phytoplankton community structure with knock-on effects on the marine food web and carbon sequestration. <a href="javascript:void(0);">(5)</a> It is crucial to understand the utilization of trace metals by different groups of marine phytoplankton that inhabit contrasting niches in the modern ocean, not only by assessing the accumulation of trace metals in cells but also examining the functions of trace metals in different biological pathways.In previous studies, the utilization or requirements of trace metals by marine phytoplankton were mostly determined by measuring the elemental stoichiometry in cells (metallome or quota of trace metals). <a href="javascript:void(0);">(6−8)</a> In the field, attempts have also been made to investigate the elements in phytoplankton <a href="javascript:void(0);">(9,10)</a> which have then been compared with profiles in the abiotic environment to understand their relationships. <a href="javascript:void(0);">(11)</a> The discovery of various metal storage proteins and the plasticity in elemental quotas under different environmental conditions raise the question of whether intracellular trace metal quotas reflect true differences in trace metal usage by phytoplankton. <a href="javascript:void(0);">(12,13)</a> In the past few decades, more and more studies have focused on metal–protein partnerships, using approaches such as genome-wide analysis to identify homologues of known metalloproteins and other deduced metal-binding motifs encoded within sequenced genomes. <a href="javascript:void(0);">(5,14)</a> However, this approach has limitations in estimating metal abundance in cells because not all genes predicted in the genome would be translated and expressed as proteins under all environments, and a single gene for a metalloprotein could be highly expressed, such that a translation from genetic presence to a required concentration is not linear and could be environment-dependent. To obtain in situ metal abundance in metalloproteins in cells, native separation of proteins by HPLC or PAGE followed by the detection of metals using ICP-MS <a href="javascript:void(0);">(15,16)</a> has been used. This approach also has limitations in that, without bioinformatics, it cannot identify the function of proteins within which the metals are found, and it may also depend on the composition of the media to which the organism has been exposed and in which it has been growing. An ideal way to solve the problem would be to separate and purify each of the proteins and then identify both the associated metal (e.g., by ICP-MS) and the protein sequence (e.g., by mass spectrometry). However, this approach is constrained by the resolution of chromatographic or electrophoretic techniques, making it challenging to establish the metal–protein associations unambiguously; many proteins often co-occur in metal-containing fractions. Additionally, this method requires huge volumes of biomass and is both time-consuming and complex, complicating the reconstruction of the expressed metalloproteome in cells. The techniques and challenges for metalloproteomics have been discussed in detail in previously published review articles (and the references therein). <a href="javascript:void(0);">(17)</a>In this study, we determined the trace metal utilization (the metallome) of different phytoplankton from their expressed proteome via a protein modeling and homologue identification approach, and then compared the resulting metallome with the metal quota data measured by the traditional inductively coupled plasma mass spectrometry (ICP-MS). This approach allows the building of a link between the truly used trace elements and their biological functions in phytoplankton. We aim to fill the gap between an estimation of metals encoded in the genome and metal analysis by ICP-MS in phytoplankton, which may be more broadly applicable to infer cellular metallomes.<h3>Materials and Methods</h3><h4>ICP-MS Analysis</h4>All preparation of samples for ICP-MS measurement was undertaken using trace metal clean methods. All plasticware used in this study, including culture flasks, pipette tips, and centrifuge tubes, was precleaned in 10% quartz-distilled HCl and thoroughly rinsed with 18 MΩ cm water in a clean laboratory. Trace elements in the filtered lysates of G. huxleyi (OA1, OA4, OA8, OA15, OA16, OA23, and RCC 1242) and Synechocystis (FACHB898) strains were measured using an ICP-MS. The detailed ICP-MS method and instrumental settings are described in Zhang et al. (2018). <a href="javascript:void(0);">(31)</a><h4>Protein Mass Spectrometry</h4>The peptides were resuspended in 5% formic acid and 5% DMSO prior to mass spectrometry. They were separated on an <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=3&amp;search=Ultimate+3000+UHPLC">Ultimate 3000 UHPLC </a>system (Thermo Fisher Scientific) and electrosprayed directly into a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559">Q-Exactive Mass Spectrometer</a> (Thermo Fisher Scientific) through an EASY-Spray nanoelectrospray ion source (Thermo Fisher Scientific). The peptides were trapped on a C18 PepMap100 precolumn (300 μm i.d. × 5 mm, 100 Å, Thermo Fisher Scientific) using solvent A (0.1% formic acid in water) at a pressure of 500 bar. The peptides were separated on an in-house packed analytical column (75 μm i.d. × 50 cm packed with ReproSil-Pur 120 C18-AQ, 1.9 μm, 120 Å, Dr. Maisch GmbH) using a linear gradient (length: 65 min, 15% to 35% solvent B [0.1% formic acid in acetonitrile], flow rate: 200 nL/min). The raw data were acquired on the mass spectrometer in a data-dependent mode (DDA). Full scan MS spectra were acquired in the Orbitrap (scan range 350–1500 m/z, resolution 70000, AGC target 3e6, maximum injection time 50 ms). After the MS scans, the 10 most intense peaks were selected for HCD fragmentation at 30% of normalized collision energy. HCD spectra were also acquired in the Orbitrap (resolution 17500, AGC target 5e4, maximum injection time 120 ms, isolation window 1.5 m/z) with the first fixed mass at 180 m/z. Charge exclusion was selected for unassigned and 1+ ions. The dynamic exclusion was set to 20 s.<h3>Results and Discussion</h3><h4>Trace Elements Determined from the Expressed Proteomes of Different Phytoplankton</h4>Based on the expressed proteome sequences, we predicted metal-binding proteins and compared their distribution among various phytoplankton species (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig2">Figure 2</a>). The inference revealed 28 different metals in G. huxleyi, 31 different metals in C. reinhardtii, and 30 different metals in Synechocystis. Although only 6 different metals were identified in O. tauri proteins, it has to be noted that the analysis for O. tauri was only based on the 40 most abundant proteins reported in this organism <a href="javascript:void(0);">(21)</a> and, hence, the listed elements, including Mg, Fe, Mn, Ca, Zn, and Cu, may represent the most essential metals for the species.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Environ_Sci_Technol_2025_59_50_27367_27377_Figure_2_The_number_of_metal_binding_proteins_identified_in_the_expressed_proteome_of_the_haptophyte_G_9b8ac0f004.jpeg" alt="Environ. Sci. Technol. 2025, 59, 50, 27367–27377: Figure 2. The number of metal-binding proteins identified in the expressed proteome of the haptophyte G. huxleyi (a), the chlorophyte C. reinhardtii (b) and O. tauri(c), and the cyanobacteria Synechocystis (d). Pie charts show the percentages of metalloproteins containing specific metals. Original proteome data for G. huxleyi are from Mckew et al. (2013) (24) for C. reinhardtii are from Hsieh et al. (2013) (77) for O.tauriare from Martin et al. (2012) (21) for Synechocystisare from Chen et al. (2018). (22) *Noted that for O. tauri, only the 40 most abundant proteins were included in this analysis. ND: no metal binding was found in the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Environ_Sci_Technol_2025_59_50_27367_27377_Figure_2_The_number_of_metal_binding_proteins_identified_in_the_expressed_proteome_of_the_haptophyte_G_9b8ac0f004.jpeg 123w," sizes="100vw" width="934" height="1181">The number of proteins that bind with different metals varies dramatically in phytoplankton. For metalloproteins, there are variations in the binding affinities of different metals to organic molecules. For example, the affinities of divalent metals to proteins have a tendency to follow a universal order of preference, namely the Irving-Williams series (Mg2+ and Ca2+ [weakest binding] &lt; Mn2+ &lt; Fe2+ &lt; Co2+ &lt; Ni2+ &lt; Cu2+ &gt; Zn2+). <a href="javascript:void(0);">(43)</a> Cells can simultaneously contain proteins having high-affinity-binding metals, such as Cu and Zn, and others that require uncompetitive metals, such as Mg and Ca. One of the least competitive metals for binding with biological chelators, Mg, is even found to be the most widely distributed metal in the metalloproteomes of various phytoplankton species in this study, supporting the observations of high concentrations in the protein fraction of cells (at millimolar concentrations <a href="javascript:void(0);">(31)</a>).In all phytoplankton species in our analysis, the Mg-containing proteins are found to have the highest proportion in all metalloproteins identified. About 30% of the metalloproteins in different strains of phytoplankton are found to contain Mg or depend on it for function (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig2">Figure 2</a>), suggesting the important role of Mg in phytoplankton cells. It is generally coordinated in protein complexes by ATP or ADP and has also been found to be largely distributed in the chloroplasts or thylakoids in G. huxleyi and Synechocystis. <a href="javascript:void(0);">(22,24)</a> The essential roles of Mg in plants have been reported in various studies. Mg2+ is known to be the central atom of the chlorophyll molecule, and its levels in the chloroplast regulate the activity of key photosynthetic enzymes. <a href="javascript:void(0);">(44)</a> It was reported that approximately 15–35% of total Mg is in the chloroplasts of a plant, <a href="javascript:void(0);">(45)</a> and it also serves as an osmotically active ion in the regulation of cells <a href="javascript:void(0);">(46)</a><h4>Comparison Between Metallome Measured Directly and Reconstructed from Proteins</h4>A large proportion of metals, such as Fe, Mn, and Cu, are found in membrane proteins,and may contribute significantly to total cellular quotas. <a href="javascript:void(0);">(54,55)</a> However, for method development purpose, we endeavored to remove the cell membranes from our samples to focus mostly on the analysis of intracellular metal quotas and metalloproteins in the cytosol fraction in this study. We note that our analysis includes some membrane-bound proteins likely derived from organelles or surface membranes disrupted during sonication.The derivation of cellular metal composition, as determined by two different methods, is compared in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>. The abundance of metal in the proteins is determined as the relative abundance of the protein multiplied by the number of metal ions needed for the specific protein. The abundance of the proteins was normalized to ensure that the total intensities from each replicate measurement for the same species were similar. Since the proteomic data used here were generated from different studies using different instruments, we cannot quantify or compare the absolute biomass of proteins used for each species. Therefore, we cannot compare the absolute trace metal abundance between species solely from metal inferences of expressed proteomes. Nevertheless, we can estimate the relative abundance of different metals in the same species. For the elements that are both measured by the ICP-MS and identified in the proteome, there are generally good correlations (r2 = 0.81 in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>a and r2 = 0.74 in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>b) between the two approaches. This indicates that the metal compositions determined from the protein modeling may be reliable and, therefore, can reflect the metal usage in different phytoplankton. This would provide a level of assurance to further investigate the metal binding associated with various proteins, thereby deepening our understanding of the roles that different metals play in phytoplankton.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Environ_Sci_Technol_2025_59_50_27367_27377_Figure_3_Relationship_between_the_abundance_of_metals_determined_by_ICP_MS_analysis_e7b259e376.jpeg" alt="Environ. Sci. Technol. 2025, 59, 50, 27367–27377: Figure 3. Relationship between the abundance of metals determined by ICP-MS analysis (normalized to C, mmol/mol C) and metal abundance determined from the metalloproteome analysis (the unit is arbitrary). To account for strain variations, the ICP-MS data for the cellular metal content of G. huxleyi are average values from 7 G. huxleyi strains isolated from different areas of the ocean, and the proteome-derived metal composition data are average values calculated from 2 of those G. huxleyi strains (OA1 and OA16) isolated previously, and data from Mckew et al., 2013. (24) The ICP-MS data for Synechocystis are from Synechocystis sp. FACHB898 measured in this study, and the proteome data are calculated from Chen et al., 2018. (22) Noted that the abundance of metals from each proteome was calculated by using the metal stoichiometry multiplied by the relative abundance of proteins, which provides only a relative relationship of different trace metals, not absolute abundance. The symbols represent the mean values, and the error bars indicate standard deviations." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Environ_Sci_Technol_2025_59_50_27367_27377_Figure_3_Relationship_between_the_abundance_of_metals_determined_by_ICP_MS_analysis_e7b259e376.jpeg 245w," sizes="100vw" width="1384" height="641">Compared to the other metals investigated in this study, Ca and Mg appear to have a much higher relative abundance in the ICP-MS analysis than in the proteomic analysis of G. huxleyi and Synechocystis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>). These two elements are essential macronutrients for phytoplankton and plants. Ca is the most prominent secondary messenger that plays a crucial role in response to extracellular stimuli in all eukaryotes. Ca2+ fluxes are transported via Ca channels and transporters, such as Ca-ATPase, regulating a series of important biological functions, including mineral uptake and utilization, K+ homeostasis adjustment, and regulatory network activity in response to P or N deficiency. <a href="javascript:void(0);">(56)</a> Ca is not always incorporated into protein structures. The Ca abundance determined from the proteins in this study, therefore, is much lower than the actual Ca needed intracellularly. Similarly, the intracellular Mg2+ and K+ abundances should also be higher than those determined from the protein structures. Free Mg2+ and K+ are known to regulate cation–anion balance and serve as osmotically active ions in the regulation of cells <a href="javascript:void(0);">(46)</a> but free metal ion concentrations cannot be determined through the approach used in this study. Thus, it is not surprising to see much higher relative abundances of Ca and Mg in ICP-MS analysis than in proteomic analysis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233#fig3">Figure 3</a>).

Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes

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<ul>
<li>Discuss what GC-MS/MS is and what applicaitons it is used for (Dioxins, POPs, etc.)
</li>
<li>Transition into an overview of APGC as a solution
</li>
<li>Discuss challenges or limitations of the current GC/MS/MS technology
</li>
<li>Share why using nitrogen as a carrier gas for GC/MS/MS analysis is optimal
</li>
</ul>
Webinar Learning Objectives:
<ul>
<li>Understanding GC-MS/MS and Its Applications:- Discuss the principles of gas chromatography-mass spectrometry (GC-MS/MS) and its role in analytical chemistry.- Explore specific applications of GC-MS/MS, including its use in detecting dioxins, persistent organic pollutants (POPs), and other environmental contaminants.
</li>
<li>Introduction to APGC (Atmospheric Pressure Gas Chromatography):-. Provide an overview of Atmospheric Pressure Gas Chromatography (APGC) as an alternative solution to traditional GC-MS/MS.- Highlight the advantages and unique features of APGC, such as improved sensitivity, reduced matrix effects, and enhanced selectivity.
</li>
<li>Challenges and Innovations in GC-MS/MS Technology:- Identify the current challenges and limitations faced by GC-MS/MS technology.- Discuss recent innovations and advancements aimed at overcoming these challenges.- Emphasize the importance of using nitrogen as a carrier gas for GC-MS/MS analysis, considering its inertness, availability, and compatibility with various detectors.
</li>
</ul>
<blockquote>
Prtesenter: Frank Dorman (Senior Principal Market Development Mgr, Waters Corporation)
</blockquote>
<blockquote>
Frank Dorman is currently Senior Principal Market Development Manager for Waters focusing on their global environmental business and, concurrently, a Resident Scholar in the Chemistry Department at Dartmouth College in Hanover, NH where he is active in teaching analytical chemistry to undergraduates and graduate students.
</blockquote>
<blockquote>
In his role at Waters, Frank manages the research-focused environmental market, external collaborations, and interfaces with R&amp;D for new product development. Prior to this, Frank was an Associate Professor in the Department of Biochemistry and Molecular Biology (BMB) sat Penn State University in University Park, PA. At Penn State, Frank served as a member of the Graduate Faculty in: Biochemistry, Microbiology and Molecular Biology (BMMB), Chemistry (CHEM), Biogeochemistry (BGC) and the Forensic Science Program (FRNSC) and the Center for Molecular Toxicology and Carcinogenesis. Franks scientific interests are in gas and liquid chromatography and fundamental characterization, instrumentation and column development, as well as mass spectrometry and atomic spectroscopy as applied to trace analysis in complex sample matrices.
</blockquote>
<blockquote>
Presenter: Sarah Dowd (Principal Mass Spectrometry Applications Specialist, Waters Corporation)
</blockquote>
<blockquote>
Sarah Dowd joined Waters as a mass spectrometry application specialist in 2015 after earning her PhD in analytical chemistry from the University of Illinois at Urbana Champaign.
</blockquote>
<blockquote>
In her eight years at Waters in the Americas application lab, Sarah has collaborated with many customers looking to expand the MS capabilities of their laboratories with Water&#39;s instruments and software. Specializing in analyses in food, environmental, and polymeric materials characterization, she has done extensive work looking at environmental contaminants with tandem quadrupole and high resolution mass spectrometers.
</blockquote>
<blockquote>
One of the hot topics for the past couple of years is the analysis of per- and polyfluoroalkyl substances (PFAS) and Sarah has collaborated with customers and other scientists within Waters to guide the next phase of PFAS testing with Waters mass spectrometry systems.
</blockquote>

Waters Corporation: APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evolution

APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evolution

Discuss what GC-MS/MS is and what applicaitons it is used for (Dioxins, POPs, etc.)

APGC Roundtable: Unveiling the Pathways of GC-MS/MS Evo

When developing an LC method, there are various factors that can be tested to achieve the desired resolution and symmetry of the analytes.In this webinar we will discuss the various factors and give tips on developing a robust method.<blockquote>Presenter: Laura Montis (Product Specialist Liquid Phase Separations, Agilent)Laura began her carrier in the Liquid Chromatography over 15 years ago. After experiencing the pharmaceutical world in an analytical development lab, she went on to work with preparative chromatography and gained experience with Supercritical Fluid Chromatography prior to moving onto special HPLC applications, like 2DLC and Online LC.Throughout her career, Laura has held several positions, including application chemist, trainer, sales specialist, and marketing business development. She is currently Product Specialist for liquid phase chromatography systems within the International Distributor Organization in EMEA at Agilent Technologies.Laura studied analytical chemistry and holds a master’s degree from University of Lyon in France.</blockquote>

Agilent Technologies: HPLC Beginner Webinar Series

Method Development in HPLC

In this webinar we will discuss the various factors and give tips on developing a robust HPLC method.

Manual sample preparation has its limitations. As sample throughput increases, so does fatigue, leading to a decline in data quality. This issue is significant across various markets but is especially critical in drug development and the production of therapeutics in biotechnology.However, employing automation can enhance data consistency and improve reproducibility. Additionally, automation reduces the need for costly sample reruns and frees up users’ time for other tasks.Attend this webinar to:<ul><li>Discover the benefits of automation and identify who should consider adopting it</li><li>Explore comprehensive workflow solutions that guide you from sample preparation to data-driven decisions, tailored to biopharma and proteomics applications</li><li>Learn how the updated AssayMAP Citation Index assists users in finding published methods that utilize the AssayMAP Bravo for biopharma applications</li><li>See how compliant software can facilitate the transition of methods from non-compliant to compliant labs, such as moving from early to late stages of drug discovery</li></ul><blockquote>Presenter: Kenda LJ Evans, PhD (Automation Workflow Specialist, Agilent Technologies)Kenda received her Ph.D. from The University of Texas Health Science Center in San Antonio in the field of Pharmacology with a focus on the signal transduction pathway for the Serotonin 1A (5-HT1A) receptor. Kenda’s post-doctoral work occurred at the University of Houston.</blockquote>

Technology Networks: Automation Answers to Your Liquid Handling Challenges

Automation Answers to Your Liquid Handling Challenges

Discover the benefits of automation and identify who should consider adopting it

While much effort has been invested in process analytics for upstream bioprocess, downstream operations still suffer from a lack of technologies suitable for inline/online monitoring of product attributes with rapid response times. Such a technology is real-time multi-angle light scattering (RT-MALS), which can be integrated inline with chromatographic purification or online with UF/DF and homogenization equipment.RT-MALS determines biophysical attributes such as molecular weight and size of proteins, nucleic acids and polysaccharides, as well as size and particle concentration of lipid nanoparticles or viral vectors. Molecular weight and size discriminate product from impurities such as residual DNA or aggregates. For small vectors such as AAV, RT-MALS also determines empty and full titers and the full:total capsid ratio.This webinar will cover the technology and implementation of RT-MALS in process development and process control, with case studies from the realm of monoclonal antibodies, proteins and viral vectors.Key Learning Objectives:<ul><li>How RT-MALS accelerates bioprocess DSP development</li><li>How RT-MALS controls downstream bioprocesses to enhance yield and lot consistency</li><li>How RT-MALS integrates with continuous manufacturing of monoclonal antibodies</li></ul>Who Should Attend:<ul><li>PAT experts for biologics, vaccines and gene therapies</li><li>Biopharm process development scientists</li><li>Downstream bioprocess engineers</li><li>Biopharm MSAT leaders &nbsp;</li></ul>

Waters: RT-MALS: Real-Time PAT for biologics, gene vectors and vaccines in downstream processing

RT-MALS: Real-Time PAT for biologics, gene vectors and vaccines in downstream processing

Implementation of RT-MALS in process development and process control, with case studies from the realm of monoclonal antibodies, proteins and viral vectors.

RT-MALS PAT for biologics, gene vectors and vaccines

The complexity of biological systems and diseases, such as Alzheimer’s disease, necessitates spatial multiomics techniques to gain a holistic understanding of cell-cell interactions and communication. A singular approach to spatial multiomics is possible with MALDI Imaging, including label-free imaging of small molecules, lipids, drugs, and glycans. Additionally, with technology developed by AmberGen, Inc., photocleavable mass-tag (PCMT) conjugated affinity probes are available for antibodies, oligos, and lectins.Key Learning Objectives:<ul><li>Learn the spatial biology utility of MALDI Imaging</li><li>Understand multiomics workflows and the applications to disease-based research</li></ul>Who Should Attend:<ul><li>Researchers interested in multiomics brain analysis</li><li>Investigators researching Alzheimer’s disease</li></ul><blockquote>Presenter: Mark Lim, Ph.D. (Chief Scientific Officer and Executive VP, AmberGen Inc., Billerica, MA, USA)Mark Lim Ph.D. is the Chief Scientific Officer and Executive VP at AmberGen Inc. He has over 23 years’ experience in the biotechnology industry and has been awarded over 20 patents which underlie key technologies in the biotechnology industry, including in the fields of proteomics, genomics/transcriptomics, and diagnostics. His early work at AmberGen on photocleavable linkers and protein engineering contributed to the commercialization of a variety of novel reagents including PC-Biotin, PC-Phosphoramidites and fluorescent suppressor tRNAs. Dr. Lim now leads the application of these core AmberGen technologies to multiomic biomarker discovery and biomarker-driven diagnostics.Presenter: Kate Stumpo, Ph.D. (Senior Market Manager, Bruker Scientific, Billerica, MA, USA)Dr. Kate Stumpo is a Market Manager which entails messaging and marketing for MALDI Imaging. Dr. Stumpo completed her Ph.D. at Texas A&amp;M University, and is an expert in MALDI applications, including MALDI Imaging.</blockquote>

Bruker: Advancing understanding of Alzheimer’s disease using multiomics spatial biology

Advancing understanding of Alzheimer’s disease using multiomics spatial biology

Learn the spatial biology utility of MALDI Imaging. Understand multiomics workflows and the applications to disease-based research.

Understanding of Alzheimer’s with multiomics spatial biology

Efficient technology transfer is crucial in biotherapy manufacturing to ensure consistent product quality across multiple sites, regulatory compliance and timely market entry.In this webinar, you will discover the best practices for handing over protocols and data to contract development and manufacturing organizations (CDMOs) or other partners.You will also learn about the challenges faced during technology transfer and how leveraging easy-to-follow protocols and ready-to-use kits can significantly streamline the process.In this webinar, you will:<ul><li>Explore the core principles and importance of technology transfer in biotherapy manufacturing</li><li>Gain insights into best practices for comprehensive documentation, effective data management and techniques to maintain data integrity</li><li>Discover how ready-to-use kits and standardized protocols can simplify your supply chain and accelerate technology transfer</li></ul><blockquote>Presenter: Srinath Kashi Ranganath (Staff Scientist, Field Applications, Thermo Fisher Scientific)Srinath is a Staff Scientist – Field Applications with the Pharma Analytics group at Thermo Fisher Scientific, supporting customers in implementing, optimizing and validating the Pharma Analytics workflows for biomanufacturing processes across various therapeutic&nbsp;</blockquote>&nbsp;

Technology Networks: Streamlining Analytical Method Transfer in Biotherapy Manufacturing

Streamlining Analytical Method Transfer in Biotherapy Manufacturing

Discover the best practices for handing over protocols and data to contract development and manufacturing organizations (CDMOs) or other partners.

Analytical Method Transfer in Biotherapy Manufacturing

We’ll work through a topic of the week 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 dn/dc values and why dn/dc is important, and see how stable RI baselines are achievable.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.The live interactive web series are 100% live sessions, with anonymous Q&amp;A welcome during and after the discussion. Free for all Wyatt customers.Session Topics<ul><li>Methods for branching characterization</li><li>Abnormal SEC elution of branched polymers</li><li>Average branching characteristics</li></ul><blockquote>Presenter: Dr. Christian AckerschottDr. Christian Ackerschott studied Chemistry at the University of Cologne and finished with his diploma thesis in Biochemistry. He completed his studies with the PhD thesis “Characterization of Recombinant Flagelliform Spider Silk Proteins” at the Technische Universität München, where AF4-MALS was used as an essential characterization method.Since 2007, Christian works at Wyatt Technology as Application Scientist and is now Head of Customer Service. His tasks also include customer trainings in Dernbach and onsite as well as education and training of the local Field Application Scientists. &nbsp;</blockquote>

Analysis of Biopolymers

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 dn/dc values.

In today’s fast-paced research environment, optimizing lab workflows is crucial to maintaining productivity and ensuring high-quality results. Sample preparation is a critical step in chromatography and mass spectrometry, yet it often involves time-consuming and error-prone manual processes.Join us for an exclusive webinar with Dr. Jens Lättig, Senior Scientist at Tecan and Dr. Cassandra Rusher, European Technical Support Specialist at Eprep, where they’ll reveal how the Resolvex® Prep revolutionizes sample preparation for chromatography and mass spectrometry.Key learning objectives:<ul><li>Slash prep time: Discover how you can reduce your setup to just 5–15 minutes, freeing you to focus on critical tasks while Resolvex® Prep works autonomously.</li><li>Enhance accuracy: Learn how analytical syringes and specialized tools deliver consistent, reliable results – minimizing human error.</li><li>Achieve consistency: Find out how you can achieve repeatable results across various sample types and workflows, streamlining your processes.</li><li>Unlock versatility: Explore Resolvex® Prep’s built-in wash station, RFID deck scan, and seamless sample transfer, all designed to meet your research needs.</li></ul>Who should attend?<ul><li>Laboratory scientists and managers from analytical laboratories in: pharma, biopharma, biotech, the food industry, the environmental sector, agriculture, drug screening, proteomics, and metabolomics.</li></ul>Certificate of attendanceAll webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes.<blockquote>Presenter: Jens Lattig, PhD (Sales Development Manager Proteomics &amp; MS Sample Prep, Tecan)Dr. Jens Lättig is a Sales Development Manager Proteomics &amp; MS Sample Preparation at Tecan. He has a PhD in biochemistry, and has worked in drug research projects in Germany and France. At Tecan, he is responsible for the Resolvex™ instruments and consumables portfolio in Europe.Presenter: Cassandra Rusher, PhD (European Technical Support Specialist, Eprep)Dr. Cassandra Rusher is a technical support specialist for the Resolvex Prep. at Eprep. She has a PhD in chemistry and a background specializing in chromatography including sample preparation. Her previous roles have included technical support and product management in the analytical chromatography sector. Her focus now is on supporting the automation of sample preparation methods across a range of industries that are utilizing analytical chromatography techniques.Moderator: Carrie Haslam (Associate Editor, SelectScience)</blockquote>

SelectScience: Efficient sample prep for expert mass spectrometry and chromatography

Efficient sample prep for expert mass spectrometry and chromatography

Join us for a webinar where we will reveal how the Resolvex® Prep revolutionizes sample preparation for chromatography and mass spectrometry.

Efficient sample prep for MS and chromatography

As CHO-based processes for recombinant proteins continue to have increased cell densities and titers, the need for advancement in clarification technologies is of importance to enable manufacturing scalability. A novel technology, anion exchange (AEX) fiber chromatography, aims to address this challenge and has proven to be scalable up to large commercial manufacturing. This approach combines the ease of filter-like flowthrough operation and scalability, as well as the separation precision of chromatography.Join Dr. Masa Nakamura, Senior Application Development Specialist, Solventum, as he showcases a new clarification platform strategy that can offer seamless implementation and deployment from discovery to clinical and commercial manufacturing. It can also provide consistent and high-quality clarified fluid to enhance commercialization productivity.Key learning objectives<ul><li>Learn about the application of synthetic fiber chromatography to the clarification unit operation</li><li>Explore a novel approach to harvest and clarification in CHO processes</li><li>Understand options to overcome scale up challenges and to reduce soluble impurities during clarification</li></ul>Who should attend?Scientists, Engineers, and Heads of process development, manufacturing, MSAT, and CMC from biopharmaceutical organizations focused on recombinant protein production in CHO expression systems.Certificate of attendanceAll webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes<blockquote>Presenter: Masa Nakamura, PhD (Senior Application Development Specialist, Solventum, Bioprocessing Filtration)</blockquote><div><blockquote>Dr. Masa Nakamura, Senior Application Development Specialist for Solventum, is responsible for developing new products and applications for biopharmaceutical clarification and purification processes, including the development of fiber chromatography products. He has over 25 years of bioseparation and bioengineering experience in academic and industry. He received his BS in Chemical Engineering and PhD in Biochemical Engineering from the University of Tokyo, Japan.Moderator: Matilde Marques (Life Sciences Assistant Editor, SelectScience)</blockquote></div>

SelectScience: Scalable chromatographic clarification platform for mAb manufacturing in CHO systems 

Scalable chromatographic clarification platform for mAb manufacturing in CHO systems 

A new clarification platform strategy that can offer seamless implementation and deployment from discovery to clinical and commercial manufacturing.

Chromatographic platform for mAb manufacturing in CHO

Are you ready to transform your pharmaceutical operations? Don’t miss our exclusive session on Shimadzu Digital Classrooms and begin your journey towards Pharma digital transformation (DX). Discover how Shimadzu’s pioneering AI technologies and digital solutions are ushering in a new era of pharma innovation.In this informative session, explore how Shimadzu is reshaping the drug development landscape. Learn how our innovative tools effectively streamline workflows, enhance lab efficiency, and maintain strict compliance with regulatory standards.Whether you’re a forward-thinking researcher, a quality assurance professional, or a strategic decision-maker, this session is your gateway to mastering AI and digital transformation. Equip yourself with the expertise and resources to stay ahead in the industry.This is an opportunity not to be missed – Register Now!Learning Objectives:&nbsp;<ul><li>Understand how to stay conforming to the Pharma regulations and USP 621 changes with Shimadzu Living Laboratory</li><li>Explore Shimadzu AI and Automation to elevate your lab workflows effectively</li><li>Learn about the AI features of Shimadzu Ai-series and Nexera series</li><li>Gain insights into efficient quality control strategies with Shimadzu Data Management and Software</li></ul><blockquote>Presenter: Liw Wan Tung (Assistant Market Manager (Pharma) Shimadzu (Asia Pacific) Pte Ltd)Wan Tung is the LC Product Manager and Pharmaceutical market in-charge at Shimadzu Asia Pacific Pte Ltd. She is the LC expert with more than 15 years of working experience in analytical science, specializing in method development of various LC and LCMS applications. In 2012, she joined Shimadzu to develop end-to-end workflow solutions for the customers. She has supported a multitude of applications from impurity analysis to drug discovery and biopharmaceutical applications. Prior to joining Shimadzu, Wan Tung started her professional career as a QAQC chemist in Pharmaceutical multinational company. Wan Tung earned her bachelor’s honour's degree in chemistry back in 2009.Presenter: Kanimozhi Sivarajan (Informatics Manager Shimadzu (Asia Pacific) Pte Ltd)Dr. Kani is having 10 years of experince in Laboratory Management and Informatics &nbsp;Systems. She is serving as Informatics Manager at Shimadzu Asia Pacific, Singapore, &nbsp;providing Lab Informatics Solutions such as LabSolutions CS, LIMS and other QMS applications. She is supporting customers from various segments on implementing laboratory automation and responsible for providing consultation on streamlining Lab Workflows, Regulatory Compliance requirements for Electronic Data Management and Lab Practices/Analysis.&nbsp;</blockquote>

Shimadzu:  Realizing Pharma DX: Discover Shimadzu’s AI-Driven Solutions And Automation

 Realizing Pharma DX: Discover Shimadzu’s AI-Driven Solutions And Automation

Discover how Shimadzu’s pioneering AI technologies and digital solutions are ushering in a new era of pharma innovation.