This study evaluates an immobilized enzyme reactor (IMER) containing peptide N-glycosidase from Rudaea cellulosilytica (PNGase Rc) for rapid online deglycosylation of intact glycoproteins. Human glycoproteins and therapeutic antibodies were used as model substrates to assess reactor performance.The PNGase Rc IMER efficiently removed complex sialylated and core-fucosylated glycans, simplifying protein characterization and glycosylation-site analysis. The approach offers a fast and effective solution for bioanalytical workflows, biopharmaceutical quality control, and stability testing of therapeutic proteins.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577">Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor</a></h4>Katarína Molnárová, Petr Novák, Jana Nováková, and Petr Pompach*ACS Omega 2026, 11, 17, 25724–25729<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acsomega.6c00577">https://doi.org/10.1021/acsomega.6c00577</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.<div>Protein glycosylation, in which monosaccharide units are attached to a protein backbone through enzymatic pathways, is involved in many important biochemical processes and is considered one of the most important post-translational modifications. <a href="javascript:void(0);">(1)</a> It affects not only the stability and secretion of proteins, cell–cell interactions, and receptor–ligand recognition mechanisms but also the biological activity, plasma half-life, immunogenicity, pharmacodynamics, and pharmacokinetics of biotherapeutics. <a href="javascript:void(0);">(2−5)</a> Therapeutical monoclonal antibodies (mAbs) are among the best known pharmaceuticals that are based on glycoproteins. <a href="javascript:void(0);">(6)</a> Over 90% of the mAbs are derived from immunoglobulin G (IgG), in which N-glycosylation occurs at Asn297 of the Fc region and is responsible for modulating immune responses and interactions with other proteins. <a href="javascript:void(0);">(7,8)</a> In cancer treatment, mAbs are used to increase the response of the immune system against the tumor cell, thus inhibiting the cancerous cell growth and helping with the destruction and elimination. <a href="javascript:void(0);">(9)</a> Among the most commonly used mAbs are trastuzumab, bevacizumab, cetuximab, or margetuximab, which are used as an additional treatment for breast, colorectal, prostate, or lung cancer. <a href="javascript:void(0);">(10)</a>Mass spectrometry (MS)-based methods have become a method of choice in the analysis of mAbs that can provide information on sequence, post-translational modifications, and glycosylation profiles. <a href="javascript:void(0);">(11)</a> The enzymatic removal of the attached glycans from the protein backbone can reduce the complexity of the MS analysis, which can lead to a better understanding of the protein structure and modifications. In glycoproteomics, peptide-N-glycosidase F (PNGase F) is most used for glycan removal. It cleaves the linkage between the Asn residue and the N-acetylglucosamine (GlcNAc). <a href="javascript:void(0);">(12)</a> Jmeian et al. developed a monolithic PNGase F enzyme reactor fabricated in fused silica using a glycidyl methacrylate-co-ethylene dimethacrylate polymer and integrated it into an LC–MS workflow. The authors demonstrated the applicability of this system for the characterization of released neutral and acidic N-glycans by LC–MS analysis. <a href="javascript:void(0);">(13)</a> In another study, oriented immobilization of PNGase F onto a methacrylate-based monolithic support via glutathione-S-transferase–glutathione affinity coupling was employed to release N-glycans from denatured ribonuclease B and fetuin, as well as from native IgG. The released glycans and the corresponding deglycosylated proteins were subsequently analyzed by MALDI-MS. <a href="javascript:void(0);">(14)</a>Gramlich et al. showed the potential of PNGase Rc for N-glycan hydrolysis from both tryptic peptides and native glycoproteins at a low pH. The favorable properties of PNGase Rc, including activity at acidic pH and compatibility with reducing agents such as tris(2-carboxyethyl)phosphine hydrochloride (TCEP) and denaturants like urea, make this enzyme well suited for online intact protein deglycosylation workflows. <a href="javascript:void(0);">(15,16)</a>In this report, we demonstrate the potential of the PNGase Rc IMER for rapid online deglycosylation of reduced monomeric glycoproteins, including human haptoglobin (Hp), human transferrin, anti-hHD6, and the therapeutic monoclonal antibodies trastuzumab and bevacizumab. The column retained its activity over more than 150 consecutive measurements, highlighting its robustness, suitability for repeated use in bioanalytical workflows, and applicability to pharmaceutical research and development.<h4>Experimental Section</h4><h5>Instrumentation and Experimental Conditions</h5>Automated sample handling and online deglycosylation were carried out using the HDX workstation (AffiPro, Czech Republic). The scheme of the system is shown on <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig1">Figure 1</a>. Samples of 50 mM ammonium bicarbonate buffer (pH 8.2) and 40 mM TCEP were placed in a sample tray at 4 °C. Ten microliters of the protein sample at a concentration of 0.03 mg/mL (0.3 μg per injection) were added to 40 μL of 50 mM ammonium bicarbonate and then transferred to 50 μL of 40 mM TCEP, pH 2.3. The disulfide bond reduction was carried at 40 °C for 5 min. The automated sample handling system injected 100 μL of the reaction mixture into the sample loop and switched the injection valve. Online deglycosylation was performed at room temperature using a PNGase Rc IMER (2.1 × 20 mm, AffiPro, Czech Republic) at a flow rate of 50 μL/min, followed by protein desalting on an OPTI-TRAP (0.5 × 2 mm) trap column (Optimize Technologies Inc., Oregon City, Oregon, USA) heated to 55 °C for 10 min with 0.2% formic acid delivered by an <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=1260+Infinity+III+isocratic+pump">Agilent 1260 Infinity III isocratic pump</a> (Agilent Technologies, Santa Clara, California, USA). By switching the trap valve, the protein was eluted by an acetonitrile gradient [(min)/% B] 0/10-9/10-16/70-16.5/90-17/90-18/10-23/10] delivered by the <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=10&amp;search=1290+Infinity+II+LC">Agilent 1290 Infinity II HPLC</a> system (Agilent Technologies, Santa Clara, California, USA) at a flow rate of 20 μL/min. The mobile phase A consisted of 5% acetonitrile with 1% propan-2-ol and 0.1% formic acid, and the mobile phase B consisted of 95% acetonitrile with 1% propan-2-ol and 0.1% formic acid. The <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=8&amp;search=maXis+Q-TOF">maXis Q-TOF mass spectrometer</a> (Bruker Daltonics, Bremen, Germany) was operated in the survey MS mode in a mass range of m/z 50–3000. The acquired data were analyzed and processed by DataAnalysis 4.4 (Bruker Daltonics) and deconvoluted by UniDec <a href="javascript:void(0);">(17)</a> with the following parameters: data processing range, m/z 500–3000; charge range, 1–80; allowed mass range, 1,000–80,000; sampling rate, 10 Da; peak detection range, 500 Da; and peak detection threshold, 0.1.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_1_Schematic_of_the_automated_sample_handling_system_for_online_protein_deglycosylation_and_desalting_d4ee48b627.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 1. Schematic of the automated sample handling system for online protein deglycosylation and desalting. Protein samples, along with 50 mM ammonium bicarbonate and 40 mM TCEP stock solutions were placed in a sample tray chilled to 4 °C, while a second tray heated to 40 °C was used for disulfide bond reduction with TCEP buffer." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_1_Schematic_of_the_automated_sample_handling_system_for_online_protein_deglycosylation_and_desalting_d4ee48b627.jpg 245w," sizes="100vw" width="1287" height="386"><h4>Results and Discussion</h4>The performance of the PNGase Rc IMER for the removal of complex N-glycans from intact proteins was tested using heavily glycosylated human Hp with four glycosylation sites (Asn184, Asn207, Asn211, and Asn241) <a href="javascript:void(0);">(18)</a> located at the β-chain and occupied by complex N-glycans terminated with sialic acid. Haptoglobin phenotype 2-1, used in this study, forms multimers consisting of β-chain and disulfide linked α1 and α2 chains. <a href="javascript:void(0);">(19)</a> The detection of glycosylated Hp β-chain requires reduction of the disulfide bonds by incubating the protein with a reducing reagent. TCEP is a common reducing reagent used for fast reduction of disulfide bonds at various pH levels. Forty degrees Celsius, the maximum temperature of the PAL tray, and 5 min of incubation were sufficient for complete reduction of Hp disulfide bonds. Individual signals corresponding to the glycosylated β-chain were observed in the m/z range of 35,800–37,400 (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig2">Figure 2</a>a). The limited resolution of the mass spectrometer did not allow assigning the different glycoforms of the haptoglobin β-chain, which is occupied by biantennary, triantennary, or tetraantennary glycans with various amounts of sialic acid and fucose. <a href="javascript:void(0);">(20,21)</a> The nonglycosylated α1 and α2 chains were observed at m/z 9190 and 15,940. When the PNGase Rc IMER was integrated into the flow system, a signal at m/z 27,270 was detected, demonstrating complete deglycosylation of the haptoglobin β-chain (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig2">Figure 2</a>b).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_2_A_Mass_spectrum_of_human_Hp_without_the_PN_Gase_Rc_IMER_implemented_in_the_system_0ecca84ed4.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 2. (A) Mass spectrum of human Hp without the PNGase Rc IMER implemented in the system. The base peak signals of the spectrum correspond to both α1 and α2 chains. The signal of the β chain is spread across its different glycoforms. (B) Mass spectrum of human Hp with the PNGase Rc IMER implemented in the system. The signal of the deglycosylated β chain is higher compared to its glycosylated form and observed only at m/z 27,270. This indicates complete removal of glycans from the Hp β chain." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_2_A_Mass_spectrum_of_human_Hp_without_the_PN_Gase_Rc_IMER_implemented_in_the_system_0ecca84ed4.jpg 245w," sizes="100vw" width="2015" height="913">In a previous study by Krenkova et al., the PNGase F IMER was used for deglycosylation of IgG, RNase B, and bovine fetuin with follow-up mass spectrometry detection of both released glycans and intact proteins using MALDI-TOF MS. <a href="javascript:void(0);">(14)</a> The authors demonstrated an effective method for rapid protein deglycosylation, which, however, requires additional sample handling prior to mass spectrometry measurement. The other study by Jmeian et al., which focused on released N-glycans, implemented a PNGase F IMER with online LC–MS detection. <a href="javascript:void(0);">(13)</a> The authors show the effectiveness of the method by identifying many different glycans released from a single protein or from a complex plasma mixture. Our approach is not directly intended for released N-glycan analysis; instead, it demonstrates the ability to measure intact proteins after rapid online deglycosylation using PNGase Rc at low pH. Samples prepared immediately prior to mass spectrometry analysis using the automated sample-handling platform can reduce variability associated with autosampler residence time, as some proteins may undergo degradation or precipitation during storage in the autosampler.Although all glycoproteins in this study were effectively deglycosylated, the method’s efficiency depends on the characteristics of the individual glycoprotein. Therefore, optimizing method parameters─including the isocratic flow rate, glycoprotein incubation time with TCEP, and/or the addition of denaturing reagent─may improve the overall efficiency of the deglycosylation process.The PNGase Rc IMER stability over a series of injections was tested by using the trastuzumab antibody. The measurements were carried out with the enzyme column kept at the laboratory temperature. As shown in <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acsomega.6c00577#fig5">Figure 5</a>, the results indicate that the column performance remained stable over the course of the 150 measurements, and no glycosylated form of the trastuzumab antibody heavy chain was detected. The activity of PNGase Rc in the presence of 5% acetonitrile and 5% propan-2-ol was evaluated using a bottom-up approach with human 2–1 haptoglobin, which was online-digested by a coimmobilized nepenthesin-2/pepsin IMER. In the absence of an organic solvent, the peptide IEKVVLHPNYSQVD remained fully deglycosylated throughout 30 injections. In contrast, in the presence of organic solvent, a marked loss of enzymatic activity was observed after only a few injections (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acsomega.6c00577/suppl_file/ao6c00577_si_001.pdf">Figure 2</a>).<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ACS_Omega_2026_11_17_25724_25729_Figure_5_Monitoring_the_stability_and_performance_of_PN_Gase_Rc_IMER_4a9b5a9c53.jpg" alt="ACS Omega 2026, 11, 17, 25724–25729: Figure 5. Monitoring the stability and performance of PNGase Rc IMER. Trastuzumab heavy chain was completely deglycosylated after 150 injections." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ACS_Omega_2026_11_17_25724_25729_Figure_5_Monitoring_the_stability_and_performance_of_PN_Gase_Rc_IMER_4a9b5a9c53.jpg 170w," sizes="100vw" width="996" height="918"><h4>Conclusions</h4>Here, we demonstrate the potential of the PNGase Rc IMER for the online removal of N-glycans from intact monomeric glycoproteins reduced with TCEP. The column showed high sensitivity toward Hp, which has multiple glycosylation sites with various glycan structures, confirming its suitability for the profiling of complex glycoproteins. Bevacizumab and trastuzumab exhibited similar glycosylation profiles, with core-fucosylated biantennary glycans being the most abundant. Online deglycosylation with the PNGase Rc column resulted in a complete removal of the glycans from the heavy chains of both antibodies, proving that the column can be used for the rapid online deglycosylation of intact therapeutic mAbs. Moreover, the column remained stable over 150 measurements without any loss of activity, even when it was maintained at laboratory temperature. The significantly reduced reaction time, together with full automation and the absence of manual handling steps, substantially improves analytical throughput compared to conventional off-line deglycosylation workflows. These findings highlight the potential of the PNGase Rc IMER in the development of glycoprotein-based biopharmaceuticals, where detailed structural characterization of the protein part is critical for quality control, monitoring batch-to-batch variability, and stability testing.</div>

Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor

In the week of June 29, 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 5 500 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. Thermo Fisher Scientific: Insights from an IC specialist: To be suppressed or not suppressed?</h5><ul><li>Tu, 30.6.2026 09:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6310">Registration</a></li></ul>Join Thermo Fisher’s Ask the Experts session to learn how suppressor technology impacts ion chromatography performance, sensitivity, reliability, maintenance, and troubleshooting.<h5>2. SCIEX: Advancing Proteomics with ZenoTOF: From Single-Cell Analysis to Plasma Biomarker Discovery</h5><ul><li>Tu, 30.6.2026 11:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6311">Registration</a></li></ul>Discover how ZenoTOF high-resolution mass spectrometry is accelerating single-cell proteomics and plasma biomarker discovery through enhanced sensitivity, throughput, and automation.<h5>3. Agilent Technologies: Measuring Diverse Samples with UV/VIS Spectrometers and Integrating Spheres</h5><ul><li>Tu, 30.6.2026 20:30 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6052">Registration</a></li></ul>This webinar will discuss diffuse transmission and reflection UV/VIS measurements, including how to perform measurements with Agilent’s Cary 60 UV/VIS Spectrometer.<h5>4. Waters Corporation: Informatics series #33 Tips, Tricks and Best Practices</h5><ul><li>Th, 2.7.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6315">Registration</a></li></ul>This interactive session revisits essential features, shortcuts, and practical techniques in Empower software that can streamline everyday laboratory work and reduce unnecessary effort.<h5>5. Waters Corporation: Unlocking Therapeutic Peptide Characterisation (GLP-1RAs) with Cyclic IMS</h5><ul><li>Th, 2.7.2026 15:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6313">Registration</a></li></ul>Discover how cyclic ion mobility spectrometry (cyclic IMS) improves characterization of GLP-1 analogues and therapeutic peptides, supporting development, quality control, and regulatory submissions.<h5>6. Agilent Technologies: Spectral Flow Cytometry Masterclass - Session 1</h5><ul><li>Fr, 3.7.2026 07:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6316">Registration</a></li></ul>Learn how full-spectrum flow cytometry enables high-dimensional cell analysis. Explore spectral flow technology, experimental design, and applications in immunology, oncology, and vaccine research.

Webinars LabRulezLCMS Week 27/2026

The international standard ISO/IEC 17025 [1] clause 7.7.2 with regards to ensuring the validity of results, requires a laboratory to participate in proficiency testing (PT) and/or to participate in interlaboratory comparisons (ILCs) other than PT. However, no guidance as to what these other ILCs might be, or indeed how they might compare in relation to PT, is provided. This leaflet aims to outline other ILCs available, pointing out some of the limitations as compared to PT.&nbsp;There are three major types of ILCs in which a group of laboratories analyses identical portions from a homogeneous, stable test sample, with each type being characterized by its intended purpose [2,3]:<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eurachem_Interlaboratory_comparisons_other_than_proficiency_testing_2_d9263807fb.jpg" alt="Eurachem: Interlaboratory comparisons other than proficiency testing" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eurachem_Interlaboratory_comparisons_other_than_proficiency_testing_2_d9263807fb.jpg 245w," sizes="100vw" width="1507" height="607">A key point is that PT is an ILC that is designed to specifically evaluate the performance of participants, providing them with an infrastructure to monitor and assess the validity of their results. This is not the key purpose of the two other ILCs, and thus depending on their intended purpose they have a number of limitations that laboratories need to be aware of when using them rather than PT. Only proficiency testing should have been conducted in full compliance to the competency standard ISO/IEC 17043 [4].&nbsp;<h4>Evaluation of measurement procedure performance&nbsp;</h4>These ILCs, are designed to assess how a particular measurement procedure performs and whether it is fit for its intended purpose. These ILCs are often referred to as a ‘method performance study’ or a ‘collaborative study’ [2]. Some limitations of using such ILCs for monitoring laboratory performance as an alternative to PT are:&nbsp;<ul><li>All participants use the same measurement procedure i.e. the measurement procedure that is being validated. Unless the measurement procedure is being routinely used by the participating laboratory such an ILC will not assess the routine performance of the laboratory using their own routine measurement procedure. Nor does it enable them to compare their performance with other laboratories using alternative measurement procedures.&nbsp;</li><li>The measurement procedure is likely to be new, so participants may not have established stable procedures and quality control, so performance may not reflect routine use.&nbsp;</li><li>The report from such an ILC would not provide information on the performance of the participant, if the statistical model used makes the assumption that all laboratories perform with equal variability.</li><li>The design of the study may require the participants to assess multiple samples and/or to undertake multiple replicate analysis on the test materials. This may not be representative of the routine measurements or tests undertaken by the laboratory.&nbsp;</li><li>The conclusion of the ILC might be that the measurement procedure being assessed is not valid.&nbsp;</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Eurachem_Interlaboratory_comparisons_other_than_proficiency_testing_3_a53ecd2f5d.jpg" alt="Eurachem: Interlaboratory comparisons other than proficiency testing" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Eurachem_Interlaboratory_comparisons_other_than_proficiency_testing_3_a53ecd2f5d.jpg 157w," sizes="100vw" width="570" height="566"><h4>Characterisation of candidate reference materials&nbsp;</h4>These are ILCs that assign a property value to a candidate reference material, usually with a stated measurement uncertainty. These are often referred to as a ‘material certification study’ [2]. Limitations of using such ILCs as an alternative to PT are:&nbsp;<ul><li>The analysis of the candidate reference material is likely to require additional care in exercising the routine measurement procedure, such as substantially more replication, and/or may require quite different reporting formats (e.g. all valid replicates instead of a mean result). Thus, such an ILC will not necessarily provide an evaluation of the performance of the laboratory based on the routine use of their measurement procedures.&nbsp;</li><li>The report from such an ILC may include the results from the participating laboratories but would not provide information on the performance of each laboratory.&nbsp;</li><li>Participating laboratories may be required to assess multiple samples and/or to undertake multiple replicate analysis on the candidate reference materials. Thus this may not be representative of the routine measurements or tests undertaken by the laboratory.&nbsp;</li></ul><h4>Other ILCs&nbsp;</h4>Some other ILCs, whilst not being conducted in full compliance of the requirements of ISO/IEC 17043, may be designed to evaluate participant performance. These would include small ILCs as defined by EA‑2/21 [5] or split sample ILCs i.e. where a portion of a single sample is sent to two or three laboratories. Whilst these ILCs are specifically designed to evaluate participant performance, they may not provide a comprehensive comparison that a PT might provide. In such cases the laboratory needs to evaluate carefully the competence of the organization managing the ILC and the suitability of the service externally provided (ISO/IEC 17025 clause 6.6).

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<h4>European Free Educational Webinar Series</h4>
Let&#39;s go back to the basics of Chromatography, Mass Spectrometry, Data Analysis and Trouble-shooting: understanding the importance of the basics will enable you to be more effective in your daily laboratory life.
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Introduction to Mass Spectrometry
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Prezenter: Antonia Wierzbicki (Principal MS Market Dev Manager, EMEA, Waters Corporation)
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Antonia Wierzbicki is a MS market development manager at Waters working in EMEA. Antonia has BSc in Pharmaceutical Science and a MSc in Cancer Pharmacology.
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Following several years working as an analytical chemist in drug development roles within both academic labs and contract research organizations, Antonia has more recently spent time working with analytical chemists to provide solutions using cutting edge technologies to meet their needs and requirements, with a specific interest in ultra-sensitive quantitation of small molecules.
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Back to Basics - Sample Preparation: Theory and Overview
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Introduction to Mass Spectrometry

Fundamentals of MS in LC/MS, LC/MS/MS & TOF Systems.

Join our upcoming webinar on the MassHunter Quant Screener Tool to discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds.This session will provide in-depth guidance on creating methods from PCDL databases, evaluating result parameters, and generating straightforward summary reports. Additionally, learn how retention time (RT) prediction can enhance your screening process by significantly accelerating and simplifying large database searches.Don’t miss this opportunity to elevate your analytical capabilities!<blockquote>Presenter: &nbsp;Jonathan Spencer (Application Specialist, Agilent Technologies)Jonathan studied BSc Natural Sciences at the University of Nottingham and later went on to Sheffield Hallam University to study a MSc in Forensic Science.Following graduation, he spent 2 years as a Confirmatory Analyst in an anti-doping and forensic toxicology lab, before joining Agilent as an LC/MS Applications Scientist. At Agilent, he focuses on small molecule applications using LC/TQ and LC/Q-TOF in fields of like food, forensic and environmental analysis.</blockquote>

Agilent Technologies: MassHunter Masterclass Months

MassHunter Quant Screener Tool

Discover how to harness the power of quantitative analysis for effective screening and identification of potential suspect compounds. 

Join us on the hunt for the needle in the haystack!This session will delve into best practices for untargeted feature finding, focusing on achieving the optimal balance between sample coverage and processing speed using Profinder and the new MassHunter Explorer. We will explore techniques to differentiate between features and noise by applying the right filters for quality checking your data. Additionally, the webinar will cover essential aspects of compound identification, including database matching, formula generation, and structure elucidation.This is a must-attend event for anyone looking to enhance their analytical capabilities and streamline their data processing workflows.<blockquote>Presenter: &nbsp;Stefan Schaebler (Application Specialist LC/MS, Agilent Technologies)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.</blockquote>

Finding the Needle in the Haystack Part I: From Complex Samples to Compounds of Interest

The best practices for untargeted feature finding, focusing on achieving the optimal balance between sample coverage and processing speed.

From Complex Samples to Compounds of Interest

The hunt goes on, let's find the needle in the haystack:Join us for an insightful webinar where we delve into the world of chemometrics to enhance your data interpretation skills. Learn how to select the appropriate statistical tools to make sense of your data and identify features of interest by visualizing trends and changes using various clustering and grouping approaches. We will also cover the construction of class prediction models to differentiate between sample cohorts effectively.Finally, gain a deeper understanding of your findings by mapping them onto relevant metabolomic pathways, providing essential context for your research.<blockquote>Presenter: Hannah Florance (Application Specialist LC/MS, Agilent Technologies)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. Presenter: Shaun Reeksting (Application Specialist LC/MS, Agilent Technologies)Shaun completed his PhD in Biochemistry, specializing in molecular parasitology a focus in metabolomics. Following his doctoral studies, he worked in accredited industry laboratories and academia core-facilities before joining Agilent Technologies as an LC/MS Application Engineer.In this role, Shaun focuses on environmental small molecule applications using LC-QTOF, with a strong emphasis on software tools and data interpretation.</blockquote>

Finding the Needle in the Haystack Part II; All Things Chemometric

Join us for an insightful webinar where we delve into the world of chemometrics to enhance your data interpretation skills.

All Things Chemometric

With the need for risk assessment and testing plans looming on the horizon, join us to learn about the challenges of low-level nitrosamine detection for both LCMS and GCMS applications.We will explore the pressing questions of coming regulation, including guidance on NDSRIs, the differing use cases of the 4 Procedures of USP &lt;1469&gt; and how Shimadzu can be your partner in creating solutions to meet these requirements.As you prepare for the August 1, 2025 deadline, whether your needs will be nitrosamine discovery with LCMS-QTOF or high-sensitivity QC monitoring with headspace GC-MS/MS, Shimadzu has the hardware and applications to help you succeed.We will host a Q&amp;A session after the presentation to address any questions or comments.<blockquote>Presenter: Brian Domanski (Strategic Collaboration Scientist, Shimadzu Scientific Instruments)Brian has over 10 years working to provide LC and SFC solutions for Pharma, as well as experience with a wide range of chromatography techniques including RP, NP, HILIC, IEX, SEC/GPC, and IC. His focus also includes scalable Informatics and Data Integrity solutions.</blockquote>

Shimadzu: Are you Nitrosamine Ready? Solutions for Nitrosamine Analysis

Are you Nitrosamine Ready? Solutions for Nitrosamine Analysis

Join us to learn about the challenges of low-level nitrosamine detection for both LCMS and GCMS applications.

Solutions for Nitrosamine Analysis by LCMS and GCMS

The technologies presented will be CE and LC-MS.The presentations will also be available on demand after the virtual event.<h3>(Day 1): Therapeutic proteins and peptides</h3><h5>10:00–10:10 Welcome and introduction</h5><ul><li>Steve Lock, SCIEX, UK</li></ul><h5>10:10–10:35 Using LC-MS for multi-attributes monitoring (MAM) of proteins</h5><ul><li>Ricardo Gomes, IBET, Portugal [NEW SPEAKER]</li></ul><h5>10:35–11:00 Lastest methods for analyzing charge variants by ciEF-MS</h5><ul><li>Whitney Smith, SCIEX, Germany</li></ul><h5>11:00–11:25 Biomarker quantitation using LC-MS</h5><ul><li>Speaker to be announced soon [NEW SPEAKERS]</li></ul><h5>11:25–11:35 Break</h5><h5>11:35–12:00 The lastest ways to screen N-glycans using CE</h5><ul><li>Gabor Jarvas, University of Pannonia, Hungary [NEW SPEAKER]</li></ul><h5>12:00–12:25 Understanding SEC and CEX coupled to LC-MS for protein intact and subunit analysis</h5><ul><li>Sarah Nguyen, LSMBO, Strasbourg University, France</li></ul><h5>12:25–12:50 Beneath the peak: mass spectrometry as a tool in ADC development</h5><ul><li>Christopher Nortcliffe, Sterling Pharma Solutions, UK</li></ul><h5>12:50–13:00 Wrap-up and Q&amp;A</h5><blockquote>Your host: Steve Lock, PhD (Senior Marketing and Market Development Manager, Biopharma, EMEAI, SCIEX) Steve obtained his PhD in Physical Organic Chemistry from the University College of Swansea in 1993 and is a chartered chemist and a member of the Royal Society of Chemistry. He has worked for SCIEX in various technical roles for over 20 years and has presented at over 80 international meetings around the world. He currently works closely with customers in the biopharmaceutical industry. Steve is also currently an Adjunct Professor at the University of Pannonia.</blockquote>

2024 SCIEX Biopharma meeting (Day 1): Therapeutic proteins and peptides

This online event has been designed for our customers and brings  together opinion leaders, top scientists and industry innovators.

2024 SCIEX Biopharma: Therapeutic proteins and peptides

The technologies presented will be CE and LC-MS.The presentations will also be available on demand after the virtual event.<h3>(Day 2): Gene therapy, vaccines and oligonucleotides</h3><h5>10:00–10:10 Welcome and introduction</h5><ul><li>Steve Lock, SCIEX, UK</li></ul><h5>10:10–10:35 The latest developments in plasmid analysis by CE</h5><ul><li>Luiza Chrojan / Ryan Hylands, Pharmaron, UK</li></ul><h5>10:35–11:00 Pure and simple: understanding LNP analytics for better mRNA-based drugs</h5><ul><li>Adam Crowe, Cytiva, Canada</li></ul><h5>11:00–11:25 Tips and tricks to speed up CE-SDS analysis</h5><ul><li>Marcus Heinl, SCIEX, Germany</li></ul><h5>11:25–11:35 Break</h5><h5>11:35–12:00 Applying CE to viral vector analysis of process samples</h5><ul><li>Juliette Laigle / Yolande Masson, Yposkesi, France [NEW SPEAKERS]</li></ul><h5>12:00–12:25 Exploring mRNA mapping and aggregation analyses for mRNA characterization</h5><ul><li>Lucia Geis Asteggiante, Phenomenex, Italy</li></ul><h5>12:25–12:50 After the experiment: electronic lab execution as standard</h5><ul><li>Marc Smith, IDBS, UK [NEW SPEAKER]</li></ul><h5>12:50–13:00 Wrap-up and Q&amp;A</h5><blockquote>Your host: Steve Lock, PhD (Senior Marketing and Market Development Manager, Biopharma, EMEAI, SCIEX) Steve obtained his PhD in Physical Organic Chemistry from the University College of Swansea in 1993 and is a chartered chemist and a member of the Royal Society of Chemistry. He has worked for SCIEX in various technical roles for over 20 years and has presented at over 80 international meetings around the world. He currently works closely with customers in the biopharmaceutical industry. Steve is also currently an Adjunct Professor at the University of Pannonia.</blockquote>

2024 SCIEX Biopharma meeting (Day 2): Gene therapy, vaccines and oligonucleotides

SCIEX Biopharma: Gene therapy, vaccines and oligonucleotides

<div>Join us for the first-ever Semicon e-Symposium, a one-day virtual event featuring expert discussions on crucial topics in the semiconductor industry, including yield improvement, sustainability, PFAS analysis, and advanced analytical techniques.Here’s why you don’t want to miss this:<ul><li>Discover how leading-edge analytical solutions are driving innovation, featuring a plenary talk by Dr. Stefanie Fingerhut from Merck KGaA on transforming semiconductor materials for mobile technology.</li><li>Explore key advancements in vacuum technology and regulatory updates.</li><li>Gain actionable insights from experts in GC-ICP-MS, UV-Vis spectroscopy, and a special talk by Inès Tendero from Technic France on the analysis of silicon in high-purity matrices.</li></ul>This is a must-attend event for anyone looking to stay informed on key trends and cutting-edge advancements in semiconductor manufacturing. Don’t miss out—register today!<h4>Agenda</h4>8:30 a.m. How Analytical Techniques Contribute to Yield Improvement and Environmental Sustainability in the Semiconductor Industry<ul><li>Gernot Hudin, Agilent Technologies</li></ul>9:00 a.m. Plenary Talk: The Hidden Connection: Merck's Advanced Analytical Techniques Transforming Semiconductor Materials for Mobile Technology<ul><li>Dr. Stefanie Fingerhut, Merck KGaA</li></ul>9:45 a.m. Agilent ICP-MS Supplies Selection Tips for the Semiconductor Industry&nbsp;<ul><li>Alain Desprez, Agilent Technologies</li></ul>10:00 a.m. PFAS 'Forever Chemicals'—Forever a Problem?<ul><li>Shifen Xu, Agilent Technologies</li></ul>10:30 a.m. Quantitative Workflow for the Analysis of PFAS in Semiconductor Lubricant with LC-MS (Q-TOF)<ul><li>Peter Kornas, Agilent Technologies</li></ul>11:00 a.m. Agilent Vacuum in Semiconductor Market<ul><li>Fabio Ardissone, Agilent Technologies</li></ul>11:30 a.m. GC, GC/MS, and GC-ICP-MS in Semiconductor: What, Why, and How?<ul><li>Stephane Decouflet, Agilent Technologies</li></ul>12:00 p.m. Lunch break1:00 p.m. Semiconductor Application of Single Particle ICP-MS<ul><li>Yoshinori Shimamura, Agilent Technologies</li></ul>1:30 p.m. Is It Possible to Identify Organic Solvents by ICP-MS?<ul><li>Katsuo Mizobuchi, Agilent Technologies</li></ul>2:00 p.m. Special talk: Analysis of Si in High-Purity Matrix for Semiconductor Application&nbsp;<ul><li>Inès Tendero, Technic France</li></ul>2:30 p.m. Measuring the Band Gap Energy Using UV-Vis Spectroscopy<ul><li>Marcus Schulz, Agilent Technologies</li></ul>2:45 p.m. Recap—closing session<ul><li>Gernot Hudin, Agilent Technologies</li></ul></div>

Semicon e-Symposium 2024

Expert discussions on crucial topics in the semiconductor industry.

Join Dr. Katie Horton, medical science liaison specialist – EXENT and Dr. Mark Perkins, senior manager, portfolio lifecycle – EXENT, The Binding Site, as they discuss the development and performance of the EXENT® System, a clinical mass spectrometry solution for monoclonal gammopathy assessment.The EXENT System is an automated solution that enables M-protein identification and measurement in serum with enhanced sensitivity beyond conventional methods.The system combines&nbsp;the EXENT&nbsp;Analyzer&nbsp;with the EXENT GAM Assay to&nbsp;provide a fully automated solution&nbsp;to isotype, quantify and track monoclonal&nbsp;proteins throughout the patient journey.​Key learning objectives<ul style="list-style-type:disc;"><li style="tab-stops:list 36.0pt;">Understand the role of mass spectrometry (MS) in monoclonal protein testing</li><li style="tab-stops:list 36.0pt;">Explore the analytical performance of the EXENT System using MALDI-ToF MS technology</li><li style="tab-stops:list 36.0pt;">Understand the potential clinical impact of mass spectrometry for patients with monoclonal gammopathies</li></ul>Who should attend?Laboratory professionals, hematologists, and primary care professionals who would like to learn more about the latest innovation for monoclonal gammopathy assessment.Certificate of attendance All webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes. The EXENT Analyser and Immunoglobulin Isotypes (GAM) for EXENT Analyser are only commercially available in Australia, New Zealand, United Kingdom, Switzerland and the EEA. The products are not commercially available in the USA or China, future commercial availability cannot be guaranteed.Product availability is subject to country specific regulatory requirements. Contact your local representative for availability in your country.<blockquote>Presenter: Dr. Mark Perkins (Senior Manager, Portfolio Lifecycle - EXENT, The Binding Site, part of Thermo Fisher Scientific)Dr. Mark Perkins has over 20 years of experience in the life science and diagnostic industry. He led the team responsible for the design and development of the EXENT solution and currently manages the team responsible for clinical and education evidence generation for the EXENT System.Presenter: Dr Katie Horton (Medical Science Liaison - EXENT, The Binding Site, part of Thermo Fisher Scientific)Dr. Katie Horton has over five years’ experience working in a UK National Health Service (NHS) diagnostic clinic. She now works as a medical science liaison specialist using her mass spectrometry and clinical diagnostics expertise to help drive forward the clinical evidence generation and educational initiatives for the EXENT System.</blockquote>

SelectScience: Transforming M-protein diagnostics with mass spectrometry using the EXENT® System

Transforming M-protein diagnostics with mass spectrometry using the EXENT® System

Join us as we discuss the development and performance of the EXENT® System, a clinical mass spectrometry solution for monoclonal gammopathy assessment.

M-protein diagnostics with MS using the EXENT®

Session 1:The fundamental unit of a living organism is the single cell. What are the benefits and issues with pushing towards single cell measurements? The overarching goal is to provide an understanding of why discovery based single cell analysis is important and achievable. Several example applications highlight single cell metabolites including amino acids, small bio-active neuropeptides and neurotransmitters. Metabolites in individual cells were characterized using capillary electrophoresis (CE) with MRM MS with the QqQ-MS. The sample preparation steps were performed in vial inserts in the CE system to reduce the solution requirements of the autosampler to ~2 µL. Other changes to the system include a nanointerface and a mechanically tapered capillary tip for optimized detectability. The CE-nanoESI-QqQ MS system demonstrated detection limits at the single attomole level for a range of amino acids and transmitters. We characterize a range of cells including Aplysia californica neurons, rodent neurons, transplant-quality islets, and individual endocrine cells. The combination of nanovial CE-nanoESI-QqQ MS, interface, auto sampler, and fast MRM measurements enables high-throughput, high-sensitivity, and robust metabolite analysis of single cells.Key learning objectives<ul style="list-style-type:disc;"><li style="tab-stops:list 36.0pt;">Why single cell assays provide key details</li><li style="tab-stops:list 36.0pt;">How to prepare single cells for measurements</li><li style="tab-stops:list 36.0pt;">Why CE/MS works well for single cell metabolomics</li><li style="tab-stops:list 36.0pt;">Benefits of a targeted QQQ approach</li><li style="tab-stops:list 36.0pt;">How to reduce sample volumes</li><li style="tab-stops:list 36.0pt;">On going optimization of CEMS interface</li><li style="tab-stops:list 36.0pt;">Quantify differences in metabolic levels between cells</li><li style="tab-stops:list 36.0pt;">Scientists in the life sciences, with a focus on discovery, or a need for large-scale analyses</li></ul>Who should attend?<ul style="list-style-type:disc;"><li style="tab-stops:list 36.0pt;">Discovery groups involved with identifying and quantifying biomarkers. Researchers who are sample limited.</li></ul>Session 2:Untargeted metabolomics and lipidomics have traditionally been seen as primarily academic pursuits, often dismissed in clinical research due to perceived challenges in scalability and reproducibility. However, the emergence of precision health, which relies on the concept of digital twins—comprehensive digital representations of the complete molecular content of biological specimens—necessitates the use of untargeted approaches. These methods, in theory, offer the potential to explore an extensive chemical space. But what does it take to implement such analyses on a large scale, aiming both for accuracy in quantification and extensive identification? This presentation will highlight the key lessons learned from the Swiss Personalized Health Initiative.Key learning objectives<ul style="list-style-type:disc;"><li style="tab-stops:list 36.0pt;">Why is QTOF technology ideally suited for untargeted analyses, both for metabolites and lipidomics</li><li style="tab-stops:list 36.0pt;">What are the critical factors to perform large scale LC-MS (LC, MS, DDA)</li><li style="tab-stops:list 36.0pt;">Harmonization of large-scale data</li></ul>Who should attend?<ul style="list-style-type:disc;"><li style="tab-stops:list 36.0pt;">Scientists in the life sciences, with a focus on discovery, or a need for large-scale analyses</li></ul>Certificate of attendance All webinar participants can request a certificate of attendance, including a learning outcomes summary, for continuing education purposes.<blockquote>Presenter: Dr. Jonathan V. SweedlerJames R. Eiszner Family Endowed Professor of Chemistry and is affiliated with the Institute of Genomic Biology and the Beckman Institute for Advanced Science and Technology at the University of Illinois Urbana-Champaign, University of Illinois Urbana-ChampaignDr. Sweedler’s research interests focus on developing new lipidomics, metabolomics and peptidomics approaches for assaying small volume samples including new sampling approaches, miniaturized separations, and mass spectrometry. He has used these tools to characterize small molecules and peptides in a range of animal models across metazoan life and in samples as small as individual cells and cellular domains. Sweedler has published more than 500 manuscripts and presented more than 600 invited lectures. &nbsp;He has received numerous awards including the Instrumentation Award from the Analytical Division of the ACS, the Pittsburgh Analytical Chemistry Award, and the ACS Award in Analytical Chemistry. He is a fellow of both the American Association for the Advancement of Science and the American Chemical Society. He is currently the Editor-in-Chief for Analytical Chemistry.Presenter: Prof. Dr. Nicola ZamboniProfessor at the Institute of Molecular Systems Biology of ETH Zurich, and head of the PHRT Clinical Metabolomics Analysis Center., ETH ZurichNicola Zamboni’s research pivots on investigating metabolism and its regulation, from cells to humans. The lab relies heavily on mass spectrometry to quantify levels and rates of conversion of metabolites. In parallel, it develops computational approaches to enable large-scale data acquisition and integration. The lab is embedded in the Swiss personalized health initiatives as main provider of metabolomics and lipidomics for clinical research.Moderator: Matilde Marques (Life Sciences Assistant Editor, SelectScience)</blockquote>

SelectScience: Metabolomics Masterclass: Cutting-Edge Techniques for Single Cell Analysis and Precision Health at Scale

Metabolomics Masterclass: Cutting-Edge Techniques for Single Cell Analysis and Precision Health at Scale

In two sessions, single-cell metabolomics and untargeted metabolomics, and lipidomics will be discussed.

LCMS webinars focusing on LC/TOF - page 12