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

Webinars LabRulezLCMS Week 08/2026

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

<p><strong>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.</strong></p><p>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.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.est.5c11233"><strong>Unlocking Phytoplankton Metallomes with Comparative Analysis of Metal Quotas, Quantitative Proteomics, and Inferred Metalloproteomes</strong></a></h4><p>Qiong Zhang*, Jiayou Ge, Fengjie Liu, Shabaz Mohammed, Kedong Yin, and Rosalind E. M. Rickaby</p><p>Environ. Sci. Technol. 2025, 59, 50, 27367–27377</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.est.5c11233">https://doi.org/10.1021/acs.est.5c11233</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><p>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.</p><p>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 <i>in situ</i> 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 (<i>e.g.,</i> by ICP-MS) and the protein sequence (<i>e.g.,</i> 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></p><p>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.</p><h3><strong>Materials and Methods</strong></h3><h4><strong>ICP-MS Analysis</strong></h4><p>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 <i>G. huxleyi</i> (OA1, OA4, OA8, OA15, OA16, OA23, and RCC 1242) and <i>Synechocystis</i> (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></p><h4><strong>Protein Mass Spectrometry</strong></h4><p>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"><strong>Ultimate 3000 UHPLC </strong></a>system (Thermo Fisher Scientific) and electrosprayed directly into a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559"><strong>Q-Exactive Mass Spectrometer</strong></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 <i>m</i>/<i>z</i>, 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 <i>m</i>/<i>z</i>) with the first fixed mass at 180 <i>m</i>/<i>z</i>. Charge exclusion was selected for unassigned and 1+ ions. The dynamic exclusion was set to 20 s.</p><h3><strong>Results and Discussion</strong></h3><h4><strong>Trace Elements Determined from the Expressed Proteomes of Different Phytoplankton</strong></h4><p>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 <i>G. huxleyi</i>, 31 different metals in <i>C. reinhardtii</i>, and 30 different metals in <i>Synechocystis</i>. Although only 6 different metals were identified in <i>O. tauri</i> proteins, it has to be noted that the analysis for <i>O. tauri</i> 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.</p><p><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"></p><p>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 (Mg<sup>2+</sup> and Ca<sup>2+</sup> [weakest binding] &lt; Mn<sup>2+</sup> &lt; Fe<sup>2+</sup> &lt; Co<sup>2+</sup> &lt; Ni<sup>2+</sup> &lt; Cu<sup>2+</sup> &gt; Zn<sup>2+</sup>). <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>).</p><p>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 <i>G. huxleyi</i> and <i>Synechocystis</i>. <a href="javascript:void(0);">(22,24)</a> The essential roles of Mg in plants have been reported in various studies. Mg<sup>2+</sup> 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></p><h4><strong>Comparison Between Metallome Measured Directly and Reconstructed from Proteins</strong></h4><p>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.</p><p>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 (<i>r</i><sup>2</sup> = 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 <i>r</i><sup>2</sup> = 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.</p><p><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"></p><p>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 <i>G. huxleyi</i> and <i>Synechocystis</i> (<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. Ca<sup>2+</sup> 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<sup>+</sup> 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 Mg<sup>2+</sup> and K<sup>+</sup> abundances should also be higher than those determined from the protein structures. Free Mg<sup>2+</sup> and K<sup>+</sup> 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>).</p>

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

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<p><strong>In this part of the course we will deal with sample preparation: why, how and which sample preparation is the most suitable for the target analyte?</strong></p><p>SPE, LLSE, or syringe filter?&nbsp;</p><blockquote><p><strong>Presenter:</strong> Shaun Pritchard (Product Specialist Liquid Phase Separations, Agilent Technologies)</p><p>Shaun Pritchard is a Product Specialist for separation products at Agilent Technologies covering the UK and Ireland. He started his career in 1989 working at a large Pharmaceutical company holding a number of roles, this is where he became passionate about HPLC finally in 1998 he took the leap to leave the lab and move to the commercial side of things and has had a number of roles within the industry until 2017 he joined Agilent.</p></blockquote>

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<p><strong>Join us for an insightful webinar where we will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results. From screening to quantification, discover the value of targeted data analysis workflows using non-targeted data with our innovative software and hardware.</strong></p><p>Find by Formula algorithm. Learn to identify the most suitable MS/MS approach for your experiments, initiate quantitation for your compounds of interest, and incorporate retention times (RTs) and MS/MS spectra into a custom database and library.</p><p>This session is designed to enhance your understanding and application of Q-TOF data analysis, ensuring robust and reliable outcomes.</p><blockquote><p><strong>Presenter:</strong> Hannah Florance (Agilent Technologies)</p><p>Hannah has had multiple roles in the life sciences, starting as a protein chemist, before moving into proteomics and then metabolomics. A major part of her time working in academia involved running LC and GCMS core facilities supporting projects ranging from synthetic biology to cancer research. She is currently an LCMS applications specialist for Agilent.<br><br><strong>Presenter:</strong> Stefan Schaebler (Application Specialist LC/MS, Agilent Technologies)</p><p>Stefan completed his PhD in Biology, specializing in LC-MS-based lipidomics and metabolomics. Following his doctoral studies, he joined Agilent Technologies as an LC/MS Application Specialist. In this role, Stefan focuses on small molecule applications using LC-QTOF, with a strong emphasis on software tools and data interpretation.</p></blockquote>

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MassHunter Qual – The Solid Pillar in Q-TOF Data Analysis

We will explore the critical aspects of differentiating good from bad data and how this distinction can significantly influence your results.

<div><p><strong>To unravel the functions of the vast universe of small molecules in human biology it is essential to first detect and quantify these molecules—a task carried out by the field of metabolomics. In traditional liquid chromatography-mass spectrometry (LC-MS)-based metabolomics, quantitative analysis is divided across two categories: relative or absolute.&nbsp;&nbsp;&nbsp;</strong></p><p>In this webinar we will explore the importance of metabolomics in disease research, and the challenges associated with LC-MS based metabolomics studies. We will also introduce Pyxis, a scalable, machine learning-based approach to absolute quantitation of metabolites across various matrices, and potential applications in research and the clinic.&nbsp;</p><p><strong>Learning Objectives</strong></p><ul><li><strong>The application of quantitation in understanding metabolite functions in biological systems.</strong></li><li><strong>The experimental requirements of absolute and relative quantitation of metabolites along with their benefits and limitations.</strong></li><li><strong>Introduction of Pyxis, a method that enables scalable absolute quantitation of metabolites without relying on isotopically labeled standards.</strong></li></ul><blockquote><p><strong>Presenter:</strong> Naama Kanarek, PhD (Assistant Professor, Pathology Department at Boston Children’s Hospital and Harvard Medical School)</p><p>A native of Jerusalem, Israel, Dr. Naama Kanarek trained at the Hebrew University, where she earned a BSc in medical science, an MSc in proteomics and microbiology, and a PhD in immunology and cancer research (including one year at Columbia University Medical Center, NY). Dr. Kanarek’s postdoctoral research was performed under the supervision of Prof. David M. Sabatini at MIT’s Whitehead Institute.</p><p>Dr. Kanarek is the recipient of a number of awards and honors, including the Margaret and Herman Sokol Postdoctoral Award, the Leukemia and Lymphoma Society New Idea Award, the Hebrew University Women in Science Postdoctoral Award, the Weizmann Institute Postdoctoral Award for Advancing Women in Science and a Revson Fellow of that program, and the James Sivarsten Prize in Pediatric Cancer Research. Her postdoctoral work was supported by fellowships from the American Association for Cancer Research and the European Molecular Biology Organization.</p><p>Dr. Kanarek’s laboratory is interested in folate metabolism, and the metabolic adaptations of cells as they move around and migrate to new sites. They apply genetic perturbations, biochemical assays, molecular biology, functional genomic screens, and metabolite profiling by mass spectrometry in cell-culture systems and in vivo. They study basic folate biology including folate metabolism, folate-related signal transduction, the oncogenic role of folate and folate homeostasis in normal physiology and pathological conditions.</p><p><strong>Presenter:</strong> Jennifer M. Campbell, PhD (Chief Scientific Officer, Matterworks, Inc.)</p><p>Jennifer M. Campbell, PhD is currently Chief Scientific Officer at Matterworks, a multidisciplinary startup focused on using the power of deep learning on raw mass spectrometric data. Their first product, Pyxis, enables scalable quantitative metabolomics through the use of AI. Prior to Matterworks, Dr. Campbell worked at Novartis Institutes of Biomedical Research, heading up MS and separations within the Cambridge (MA) chemistry department. Dr. Campbell served as technical lead of NeoBase2, an FDA 510K approved assay for newborn screening at Perkin Elmer and Director of Proteomics at BG Medicine. Her career started in instrument development - she obtained her PhD, which focused on the development of a linear ion trap-TOFMS at the University of British Columbia under Don Douglas and she worked for eight years at Applied Biosystems, aiding in the development of all aspects of the MALDI TOF/TOF product line (4700, 4800, and 5800). She has authored numerous papers, patents, and book chapters.</p></blockquote></div>

The Analytical Scientist: A scalable approach to absolute quantitation in metabolomics

A scalable approach to absolute quantitation in metabolomics

We will explore the importance of metabolomics in disease research, and the challenges associated with LC-MS based metabolomics studies.

<div><div id="inner_content_body_text" data-content-id="391110"><p><strong>Per- and polyfluoroalkyl substances (PFAS) are synthetic chemicals prevalent across numerous industries and used in many everyday products, but their persistent and bioaccumulative nature raises critical health and environmental concerns. Join us for our upcoming Ask Me Anything (AMA) Q&amp;A session, where you can explore the latest research, regulatory challenges and advancements in the field.</strong></p><p>During this hour-long virtual session, you’ll have the unique opportunity to ask your most pressing questions directly to our expert speaker, Dr. Ian Ross, in real time.</p><h4><strong>About Our Expert</strong></h4><p>We are honored to host Dr. Ian Ross, Global PFAS Practice Lead at CDM Smith and visiting professor at Manchester Metropolitan University. Dr. Ross is a distinguished biochemist specializing in contaminated land assessment and PFAS decontamination. His extensive expertise is reflected in over 100 publications, including a comprehensive 204-page chapter on PFAS in the Emerging Contaminants Handbook.</p><h4><strong>What to Expect</strong></h4><p>Ian will connect with our live audience to address a broad spectrum of topics related to PFAS. While the spontaneous nature of an AMA session makes it impossible to predict every question, we anticipate discussions will focus on:</p><ul><li><strong>PFAS contamination:</strong> Latest research and case studies</li><li><strong>Environmental and health impacts:</strong> Emerging evidence and implications</li><li><strong>Regulatory challenges: </strong>Current frameworks and future directions</li><li><strong>Applications and concerns:</strong> Industrial uses and associated risks</li></ul><div><div><h4><strong>Why Attend?</strong></h4></div></div><ul><li><strong>Expert insights:</strong> Gain knowledge directly from a leading authority in PFAS.</li><li><strong>Live interaction:</strong> Have your questions addressed in real time for personalized answers.</li><li><strong>Exclusive content:</strong> Access in-depth discussions that you won't find anywhere else.</li></ul><p><strong>Space is limited! Register now to secure your spot for this exclusive AMA session.</strong></p><p><span><strong>Presenter:</strong> Ian Ross, PhD </span>(CDM Smith / Global PFAS Practice Lead, Manchester Metropolitan University)</p></div></div>

Technology Networks: Ask Me Anything: PFAS

Ask Me Anything: PFAS

Ian will connect with our live audience to address a broad spectrum of topics related to PFAS.

<div><div><div><p><strong>Alithea Biotechnology was founded in 2019 by Fanny Giannou and Tim Fugmann to support Biopharma globally on the development of innovative therapies targeting HLA-presented peptides. Alithea has a significant track record in the absolute quantification of HLA peptides, off-target toxicity predictions and target discovery.</strong></p><p>In addition, HLA-Compass is Alithea's cloud-accessible HLA peptide database featuring the measurement of a total of 1.4 Million HLA peptides in 4160 healthy tissue, tumor tissue and cancer cell line samples for target validation and off-target toxicity prediction.</p><h5><strong>Why to join this webinar:</strong></h5><ul><li><strong>The timsTOF Ultra can lead to high quality immunopeptidomes from limited sample</strong></li><li><strong>Extensive HLA databases can significantly speed up the T-Cell-Receptor therapy development process</strong></li><li><strong>The time is ripe to bring immunopeptidomics into clinical routine</strong></li></ul><blockquote><p><strong>Presenter:</strong> Tim Fugmann, Ph.D. (Chief Scientific Officer and Co-Founder, Alithea Biotechnology GmbH, Berlin, Germany)</p><p>Tim Fugmann got his Ph.D. from ETH Zurich, on mass-spectrometric discovery of antibody targets and disease biomarkers. Later, he was leading the target discovery efforts at Philochem, before moving to the Max-Delbrueck-Centrum for Molecular Medicine in Berlin. He was later appointed professor for MS-based proteomics at JLU Giessen. In 2019 he co-founded Alithea Bio UG, which is focusing on immunopeptidomics, a topic which Tim Fugmann studied since 2012.</p></blockquote></div></div></div>

Bruker: Unlocking the full potential of immunopeptidomics with the timsTOF Ultra

Unlocking the full potential of immunopeptidomics with the timsTOF Ultra

Alithea has a significant track record in the absolute quantification of HLA peptides, off-target toxicity predictions and target discovery.

The potential of immunopeptidomics with the timsTOF Ultra

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 1 – October 30</strong></h4><h5><strong>15:00 – 15:50 GMT: The Human Protein Atlas – Creating a Pan-Disease Resource Based on Next Generation Blood Profiling</strong></h5><ul><li>Mathias Uhlén, PhD (KTH Royal Institute of Technology)</li></ul><h5><strong>15:50 – 15:55 GMT:</strong> Networking Break</h5><h5><strong>15:55 – 16:15GMT: Mitigating Sorter-Induced Cellular Stress with Cartridge, Microfuildics-Based Sorting</strong></h5><ul><li>Crystal Montoya (Miltenyi Biotec)</li></ul><h5><strong>16:15 – 16:20 GMT:</strong> Networking Break</h5><h5><strong>16:20 – 16:40 GMT: Speaker to be announced</strong></h5><h5><strong>16:40 – 16:45 GMT</strong>: Networking Break</h5><h5><strong>16:45 – 17:35 GMT: Spatial Tissue Proteomics to Assess Health and Disease</strong></h5><ul><li>Fabian Coscia, PhD (Max Delbrück Center)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:00 GMT: The Sulpho-Phospho-Vanillin Assay: Accurate Lipid Normalization in Quantitative Lipidomics</strong></h5><ul><li>Karri Basso, PhD (University of Florida)</li></ul><h5><strong>18:00 – 18:05 GMT:</strong> Networking Break</h5><h5><strong>18:05 – 18:55 GMT: Proteomics for Cancer Precision Medicine</strong></h5><ul><li>Janne Lehtiö, PhD (Karolinska Instutet)</li></ul><h5><strong>18:55 – 19:00 GMT: </strong>Networking Break</h5><h5><strong>19:00 – 19:20 GMT: How Breakthroughs in Depth, Scale and Speed are Unlocking New Proteomic Discovery</strong></h5><ul><li>Aaron Gajadhar, PhD (Seer Bio)</li></ul><h5><strong>19:20 – 19:25 GMT: </strong>Networking Break</h5><h5><strong>19:25 – 19:55 GMT:</strong> Phantom Metabolites: Unraveling Metabolic Shadows</h5><ul><li>Gary Siuzdak, PhD (Scripps Research Institute)</li></ul><h5><strong>19:55 GMT:</strong> End of Day 1</h5><div><div><div><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote></div></div></div>

Technology Networks: Advances in Proteomics & Metabolomics 2024

Advances in Proteomics & Metabolomics 2024 (Day 1)

Hear about the latest advancements in translational proteomics and metabolomics. 

Advances in Proteomics & Metabolomics 2024  (Day 1)

<p><strong>Hear about the latest advancements in translational proteomics and metabolomics. From the molecular mechanisms of disease pathology to the latest technological developments in diagnostics and treatment.</strong></p><h5><strong>Key Learning Objectives:</strong></h5><ul><li>Spatial proteomics to assess health and diseases</li><li>Absolute quantitation of human proteins</li><li>The latest innovations in proteomics and metabolomics instrumentation and data analysis</li><li>Biomarker-guided precision medicine</li></ul><h4><strong>Day 2 – October 31</strong></h4><h5><strong>15:00 – 15:50 GMT: A Novel Strategy for the Absolute Quantification of Human Proteins</strong></h5><ul><li>Christoph Borchers, PhD (McGill University)</li></ul><h5><strong>15:50 – 15:55 GMT: </strong>Networking Break</h5><h5><strong>15:55 – 16:15 GMT: From Single Cells to the Metaproteome: Latest Developments in timsTOF Technology for Proteomics</strong></h5><ul><li>Matt Willetts, PhD (Bruker)</li></ul><h5><strong>16:15 – 16:20 GMT: </strong>Networking Break</h5><h5><strong>16:20 – 17:10 GMT: Single-Cell Chromatin Proteomics to Investigate the Biology of Exceptional Longevity</strong></h5><ul><li>Simone Sidoli, PhD (Albert Einstein College of Medicine)</li></ul><h5><strong>17:10 – 17:15 GMT: </strong>Networking Break</h5><h5><strong>17:15 – 17:35 GMT: Optimizing Metabolomics Workflows: From Sample Preparation to Multi-omics Integration</strong></h5><ul><li>Hagen Magnus Gegner, PhD (CTC Analytics)</li></ul><h5><strong>17:35 – 17:40 GMT:</strong> Networking Break</h5><h5><strong>17:40 – 18:10 GMT: Analyzing Metabolic Responses to a Standardized Meal Challenge Using Exhaled Breath</strong></h5><ul><li>Matteo Tardelli, PhD (Owlstone Medical)</li></ul><h5><strong>18:10 GMT: </strong>Event Close</h5><h5><strong>Who Should Attend:</strong></h5><ul><li>Scientists and researchers seeking to expand their knowledge</li><li>Pharmaceutical and biotech professionals driving drug development</li><li>Clinicians looking to improve patient care</li><li>Academicians exploring new research avenues</li><li>Graduate students and postdoctoral fellows building their careers</li></ul><blockquote><p><strong>Presenter: </strong>Mathias Uhlén, PhD (Professor, KTH - Royal Institute of Technology)</p><p><strong>Presenter:&nbsp;</strong>Christoph Borchers, PhD (Professor, McGill University)</p><p><strong>Presenter:</strong>&nbsp;Janne Lehtiö, PhD (Professor, Karolinska Institutet)</p><p><strong>Presenter:</strong>&nbsp;Crystal Montoya (Senior Marketing Product Manager, Miltenyi Biotec)</p><p><strong>Presenter:</strong>&nbsp;Kari Basso, PhD (Director of Mass Spectrometry Research and Education, University of Florida)</p><p><strong>Presenter:&nbsp;</strong>Fabian Coscia, PhD (Group Leader, Max Delbrück Center)</p><p><strong>Presenter:</strong>&nbsp;Simone Sidoli, PhD (Assistant Professor, Albert Einstein College of Medicine)</p><p><strong>Presenter:</strong>&nbsp;Hagen Magnus Gegner, PhD (Content and Digital Marketing, CTC Analytics)</p><p><strong>Presenter:</strong>&nbsp;Matt Willetts, PhD (Proteomics Applications Manager, Bruker Daltonics)</p><p><strong>Presenter:&nbsp;</strong>Matteo Tardelli, PhD (Senior Biomarker Scientist, Owlstone Medical)</p><p><strong>Presenter:&nbsp;</strong>Aaron Gajadhar, PhD (Director, Strategic Applications, Seer)</p><p><strong>Presenter:&nbsp;</strong>Gary Siuzdak, PhD (Professor and Senior Director, Scripps Research Institute)</p></blockquote>

Advances in Proteomics & Metabolomics 2024 (Day 2)

<div id="inner_content_body_text" data-content-id="391734"><p><strong>Join us for an exclusive, extended webinar spotlighting the cutting-edge innovations propelling the future of battery research and development. This immersive webinar features multiple talks, offering a comprehensive exploration of the groundbreaking advancements in materials and technologies that will transform energy storage.</strong><br><br>Led by industry experts, sessions will provide deep insights into the latest breakthroughs, showcasing how these innovations are shaping the future of battery technology and driving transformative change in energy solutions.<br><br><strong>Attend this webinar to:</strong></p><ul><li>Understand the challenges of using silicon in lithium-ion batteries</li><li>Explore the role of conductive polymer binding in battery performance</li><li>Discover how hyphenating technologies can provide deeper insights into complex materials for battery research</li></ul><blockquote><p><strong>Presenter:</strong> Krystelle Mafina, PhD (Applied Products Leader, PerkinElmer)</p><p><strong>Presenter:</strong> Gao Liu, PhD (Senior Scientist and Group Leader, Lawrence Berkeley National Laboratory)</p></blockquote></div>

Technology Networks: Innovative Technologies and Materials Advancing Battery Research

Innovative Technologies and Materials Advancing Battery Research

A comprehensive exploration of the groundbreaking advancements in materials and technologies that will transform energy storage.

Technologies and Materials Advancing Battery Research

<div><div><div><p><strong>Targeted protein degradation (TPD) is a powerful therapeutic modality to eliminate disease-causing proteins that are resistant to conventional drugs. In this webinar, we present a high-throughput scalable proteomics approach that utilizes label-free, single-shot dia-PASEF<sup>®</sup> mass spectrometry to identify novel degrader targets on a large scale with unmatched coverage, accuracy, and speed. A combination of DIA-NN software and advanced statistical tools guarantees rapid, automated analysis of large proteomics datasets with highest precision of quantification, data completeness and sensitivity. A slice-PASEF-based global ubiquitinomics approach will be presented that verifies degrader-induced modifications with an unprecedented depth of 50,000 ubiquitination sites. In addition, a data analysis suite designed for user-friendly evaluation and in-depth meta-analysis will be shown, making proteomics data easily accessible for target identification, SAR optimization, library expansion and strategic drug discovery decisions.</strong></p></div></div></div><div><div><div><p><strong>About NEOsphere Biotechnologies:</strong></p><p>NEOsphere Biotechnologies is a leading partner in TPD (Targeted Protein Degradation) proteomics, collaborating with pharmaceutical and biotechnology companies to advance drug discovery and develop innovative degrader pipelines. The platform combines cutting-edge mass spectrometry technologies with advanced biostatistical data analysis, enabling high-throughput proteomic screening of entire degrader libraries and mechanistic target validation, including global ubiquitinomics. NEOsphere Biotechnologies offers unmatched sensitivity, precision, and turnaround times, facilitating the large-scale identification of novel degrader targets and the systematic exploration of previously undruggable therapeutic targets.<br><br><strong>You will learn about:&nbsp;</strong></p><ul><li>A high-throughput proteomics approach that utilizes label-free, single-shot dia-PASEF to identify novel degrader targets on a large scale with unmatched coverage, accuracy, and speed</li><li>The verification of degrader-induced modifications using an optimized acquisition strategy based on slice-PASEF-based global ubiquitinomics</li><li>The benefit of combining the capabilities of a timsTOF HT and a timsTOF Ultra 2</li></ul><blockquote><p><strong>Presenter: </strong>Uli Ohmayer, Ph.D. (Head of Mass Spectrometry and Founder, NEOsphere Biotechnologies GmbH, Munich, Germany)</p></blockquote></div></div></div>

Bruker: Unlock the therapeutic potential of targeted protein degradation with deep proteomic screening

Unlock the therapeutic potential of targeted protein degradation with deep proteomic screening

High-throughput scalable proteomics approach that utilizes label-free, single-shot dia-PASEF® mass spectrometry

Targeted protein degradation with deep proteomic screening

<div><div><div><p><strong>Pure MHC, a pioneer in immunopeptidomics, has partnered with Bruker, a leader in state-of-the-art mass spectrometry, to demonstrate one of Pure MHC’s immunopeptidomics workflows. In this Live from the Lab webinar, tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis will be reviewed as tools for the development and validation of HLA peptide targets for immunopeptidomic development.</strong></p><p><strong>Key Learning Objectives:</strong></p><ul><li>Get insights into Pure MHC's sample preparation strategies to maximize the yield of immunopeptides from tissue samples</li><li>Discover how the unparalleled sensitivity and robustness of the Bruker timsTOF Ultra empowers users to maximize the potential of their immunopeptide samples</li><li>Understand data processing workflows for both DDA and DIA data processing</li></ul><blockquote><p><strong>Presenter:</strong> Curtis McMurtrey, Ph.D. (Director of Immunoproteomics, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. McMurtrey earned his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2010. He currently serves as the Director of Immuno-Proteomics at Pure MHC, LLC.</p><p>Dr. McMurtrey has studied HLA and its role in immunity since 2005. He is a member of American Society for Histocompatibility and Immunogenetics (ASHI) and holds the distinction of having won four ASHI Top Scholar Awards, more than any other scientist in the history of ASHI. Dr. McMurtrey is most notable for his work on West Nile virus epitope discovery and validation with HLA-A*02:01 and B*07:02; epitopes he discovered have been successfully tested in a WNV vaccine (collaboration with Drs. Hansen and Diamond at Washington University). His most recent accolades come from discovery of MR1 ligands from Mycobacterium tuberculosis (Mtb) as well as over 200 novel ligands from Toxoplasma gondii utilizing Deep Ligand Sequencing (DLS).</p><p>Dr. McMurtrey has expertise in BSL-3 containment techniques, protein purification, HLA ligand isolation, HPLC separation, mass spectrometric analysis, ELISPOT, and multicolor flow cytometry as well as provides bioinformatics expertise. To date, he has directed mass spectrometry (both IDA and SWATH) acquisition as well as comparative analysis and interpretation for a wide variety of MHC ligands including those from tuberculosis, toxoplasmosis, influenza, WNV, HIV and multiple cancers. Dr. Curtis McMurtrey oversees DLS acquisition and analyses and also manages database library collection.</p><p><strong>Presenter: </strong>Jason R. Krawic, Ph.D. (Business Development Manager, Pure MHC, LLC, Oklahoma City, OK, USA)</p><p>Dr. Krawic earned his Master’s degree in Biomolecular Sciences from Central Connecticut State University in 2012 before returning to academia and earning his Ph.D. in Microbiology and Immunology from the University of Oklahoma Health Sciences Center in 2024. He currently serves as the Director of Business Development at Pure MHC, LLC.</p><p>Dr. Krawic began his scientific career teaching Microbiology, Biology, and Chemistry to community college students in Connecticut and Oklahoma. He has studied HLA and non-classical MHC molecules since 2018. He is most recognized for discovering multiple isomeric conformations of MR1 ligands, as well as his work in MHC Class I and Class II ligands and cancer immunotherapies.</p><p>Dr. Krawic’s expertise ranges from classical microbiology and bacteriology to HPLC separation, protein purification, negative ion mode small molecule mass spectrometry, DDA, DIA and MRM acquisition and a variety of bioinformatics tools. In addition to his scientific career, Dr. Krawic has more than a decade of experience in sales and retail management. With this skill set he combines his science and sales backgrounds to serve Pure MHC’s customer base.</p><p><strong>Presenter: </strong>Kris Looney, MBA (President, Pure MHC, LLC, Austin, TX, USA)</p><p>As President of Emergent Technologies, the manager of Pure MHC, Kris Looney is responsible for conceiving and executing key business initiatives, developing strategic plans, and managing business processes including accounting, marketing, intellectual property, and business development. Kris has more than two decades of experience as a business generalist with a background in start-ups, management, accounting, marketing, negotiation, and sales.</p><p>Before joining Emergent, Kris served as the COO and Interim CEO of the American Red Cross of Central Texas, where he balanced multiple stakeholder needs with service responsibilities in a competitive philanthropic environment. Prior to that, he was the CFO of Transformation Enzyme Corporation, where his financial management and business development helped a bootstrapped entrepreneurial start-up become a leader in the nutritional supplement market. Kris has a B.A. in marketing and an M.B.A. from the University of Texas at Austin.</p><p><strong>Presenter: </strong>Matt Willetts, Ph.D. (Proteomics Applications Manager, Bruker Scientific LLC, Billerica, MA, USA)</p><p>Matt received his Ph.D. in mass spectrometry with Prof. Malcolm Clench at Sheffield Hallam University in the UK. He then joined Waters as the Technical Marketing Specialist for LCMS and MALDI products, focusing on application development for proteomics-based workflows. Matt joined Bruker in 2010 and is responsible for proteomics applications and support in North America.</p></blockquote><p>&nbsp;</p></div></div></div>

Bruker: Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Pure MHC's immunopeptidomics workflow with the timsTOF Ultra

Tissue sample processing, data acquisition with a Bruker timsTOF Ultra, and data analysis for immunopeptidomic development.