Join us for a fascinating conversation with Dr. Subhoja Chakraborty from the University of Central Florida, whose cutting-edge research targets the global challenge of malaria drug resistance. Dr. Chakraborty shares her journey from structure-based drug design during her PhD to her recent collaborative work repurposing human kinase inhibitors as rapid, selective antimalarials against drug-resistant Plasmodium falciparum strains.<h4>In this episode, you'll learn:</h4><ul><li>How structure-guided approaches reveal potential drug targets, including cysteine proteases like falcipain-2, and kinases implicated in malaria's complex life cycle.</li><li>The power of repurposing kinase inhibitors originally developed for cancer and other diseases, focusing on compound 12, which blocks hemozoin formation and protein kinase 6—key steps in parasite survival.</li><li>Lab techniques such as affinity, gel filtration, and size exclusion chromatography for recombinant protein purification—and how troubleshooting is crucial for high-yield, stable complexes.</li><li>Advances in mass spectrometry for characterizing protein interactions, validating drug targets, and mapping molecular pathways pivotal to malaria therapeutics.</li><li>Tips and lessons for new researchers facing the challenges of sample preparation, complex protocols, and working as part of a collaborative team.</li></ul>Dr. Chakraborty’s insights bridge the gap between basic science and translational drug discovery, offering hope for more effective, targeted malaria treatments in a world where resistance to frontline therapies threatens millions.<h4>Referenced Papers:</h4><ul><li>"Plasmodium falciparum protein kinase 6 and hemozoin formation are inhibited by a type II human kinase inhibitor exhibiting antimalarial activity" (Cell Chemical Biology, 2025)</li><li>"New insights of falcipain 2 structure from Plasmodium falciparum 3D7 strain" (BBRC, 2022)</li><li>"Structure-Based Optimization of Protease−Inhibitor Interactions to Enhance Specificity of Human Stefin‑A against Falcipain‑2 from the Plasmodium falciparum 3D7 Strain" (Biochemistry, 2023)</li></ul>If you’re a student, scientist, or simply passionate about advances in infectious disease research, this episode offers actionable insights, inspiring advice, and a front-row seat to innovation in combating malaria.<h3>Video Transcription</h3><h4>From Structural Biology to Drug Discovery: Chromatography and Mass Spectrometry in Malaria Research</h4><h5>Introduction</h5>In this discussion, Subhoja shares insights into her research journey, focusing on malaria drug discovery and the role of modern analytical techniques in biological and biomedical research. The conversation is aimed primarily at undergraduate students and early-career researchers interested in chemistry, biotechnology, and life sciences.<h5>Research Focus: Malaria Drug Discovery and Kinase Targets</h5>Subhoja is currently involved in malaria drug discovery research at the University of Central Florida, where she has been working since beginning her postdoctoral position two years ago. Her earlier PhD research focused on structure-based drug design in malaria, using a combination of in silico approaches, recombinant protein expression, and X-ray crystallography to determine precise three-dimensional structures of target proteins and their inhibitors.This structural perspective provided a foundation for her current work, which centers on drug discovery through compound screening and repurposing. A recent publication from her laboratory explores the use of repurposed mammalian CDK-like kinase inhibitors as potential antimalarial agents. While such kinase inhibitors are well known in cancer and cardiovascular research, their application to malaria targets represents a novel and promising approach.Kinases are attractive drug targets because of their central role in cell signaling and growth pathways. By targeting specific kinases involved in different stages of the malaria parasite life cycle—whether asexual growth, gametocytogenesis, or differentiation—it may be possible to significantly inhibit parasite growth and progression.<h5>Chromatography in Protein Expression and Purification Workflows</h5>Chromatography plays a critical role throughout Subhoja’s research. Her experience spans from basic chromatography techniques during her early training to advanced protein purification workflows using affinity chromatography, gel filtration (size exclusion chromatography), and ion exchange chromatography.Recombinant proteins are routinely purified using affinity resins such as nickel or cobalt, followed by further purification to remove contaminants. Fast Protein Liquid Chromatography (FPLC) enables compact, stepwise purification workflows suitable for producing proteins for in vitro assays.A recurring challenge in this process is the expression of high-molecular-weight proteins, which often accumulate in insoluble fractions or inclusion bodies. Careful selection of expression vectors, host systems, and induction conditions is therefore essential to maximize yield and solubility.<h5>Integrating Size Exclusion Chromatography into the Workflow</h5>Size exclusion chromatography (SEC) is typically used after affinity purification to further improve protein purity. Following elution with imidazole or glutathione, desalting is required to prevent buffer components from interfering with downstream assays. This is often achieved using desalting columns such as G-25 or PD-10.To remove lower-molecular-weight contaminants, finer SEC media—such as Superdex or Sephacryl columns—are employed. Concentration steps using molecular-weight cut-off filters are then applied to obtain the desired protein concentration for functional studies.These iterative purification and troubleshooting steps are a routine part of protein biochemistry and reflect the importance of methodical optimization and careful validation.<h5>The Role of Mass Spectrometry in Biomolecular Characterization</h5>Mass spectrometry is a key analytical tool in Subhoja’s research pipeline, particularly for target identification and validation. In both malaria and cancer research, MS is used alongside chromatography, immunoprecipitation, and pull-down assays to study protein interactions and molecular recognition events.Affinity-based mass spectrometry enables the identification of binding partners and interactors, whether studying proteins, long non-coding RNAs, or protein complexes. Techniques such as native MS, tandem affinity purification, and proximity labeling (e.g., TurboID-based workflows) provide deeper insights into molecular networks and signaling pathways.These approaches are essential for understanding how candidate drug targets function within complex biological systems.<h5>Sample Preparation Challenges in Biological Research</h5>Sample preparation remains one of the most challenging aspects of biological experimentation. Whole-cell lysates contain proteases, nucleases, and other components that can rapidly degrade target molecules. Preventing degradation requires minimizing preparation time, maintaining low temperatures, and using appropriate inhibitor cocktails.Reproducibility is also critical: biological experiments require multiple replicates, and variability is often unavoidable. Careful handling, protocol optimization, and continuous troubleshooting are essential to ensure reliable results, whether preparing samples for chromatography, mass spectrometry, sequencing, or immunoprecipitation.<h5>Advances in Chromatography and MS for Malaria Research</h5>Modern advances in chromatography and mass spectrometry significantly enhance malaria research by enabling precise target identification, quantification, and functional characterization. Drug discovery workflows begin with construct design and recombinant expression, followed by purification and interaction studies.In malaria research, stage-specific parasite biology requires careful extraction and analysis of proteins from different life cycle stages. Tandem affinity MS, immunoprecipitation, and in vivo validation studies help confirm target relevance and therapeutic potential.Recent work on repurposed kinase inhibitors has shown promising results, including inhibition of hemozoin formation—a key detoxification pathway for the malaria parasite—highlighting the potential of such compounds for further development.<h5>Malaria, Drug Resistance, and Global Impact</h5>Malaria remains a major global health burden, with over 600,000 deaths annually and widespread drug resistance complicating treatment. Artemisinin resistance, particularly associated with mutations in the K13 propeller domain, has driven the search for new targets and therapies.During her PhD, Subhoja focused on falcipain-2, a cysteine protease involved in hemoglobin degradation within the parasite. This pathway is critical for parasite survival and has emerged as a promising drug target. Her work revealed that falcipain-2 operates within a larger protein complex responsible for hemoglobin processing and amino acid release.Understanding these molecular mechanisms is essential for developing robust, stage-specific antimalarial strategies.<h5>Advice for Early-Career Researchers</h5>For researchers just starting out, Subhoja emphasizes the importance of hands-on experience. Working directly with cells, lysates, and analytical tools is essential for truly understanding experimental systems. Failure is an inherent part of research, and perseverance is key.Motivation, teamwork, careful sample handling, and thorough preparation all contribute to long-term success. Reading extensively, critically evaluating one’s own work, and appreciating incremental progress are vital aspects of a sustainable research career.Every successful experiment—no matter how small—represents meaningful progress and contributes to the broader goals of science and medicine.<h5>Closing Remarks</h5>The discussion highlights how interdisciplinary approaches combining chromatography, mass spectrometry, structural biology, and biochemistry are driving advances in malaria drug discovery. Through careful experimental design, analytical rigor, and collaborative teamwork, researchers can address complex biological challenges and contribute to global health solutions.<blockquote>This text has been automatically transcribed from a video presentation using AI technology. It may contain inaccuracies and is not guaranteed to be 100% correct.</blockquote><blockquote><h4>Concentrating on Chromatography Podcast</h4>Dive into the frontiers of chromatography, mass spectrometry, and sample preparation with host David Oliva. Each episode features candid conversations with leading researchers, industry innovators, and passionate scientists who are shaping the future of analytical chemistry. From decoding PFAS detection challenges to exploring the latest in AI-assisted liquid chromatography, this show uncovers practical workflows, sustainability breakthroughs, and the real-world impact of separation science. Whether you’re a chromatographer, lab professional, or researcher you'll discover inspiring content!You can find Concentrating on Chromatography Podcast in podcast apps:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://open.spotify.com/show/1wZg67rCjoGju4yhqxI3tL">Spotify</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podcasts.apple.com/tz/podcast/concentrating-on-chromatography/id1788429185">Apple podcast</a></li><li><a target="_blank" rel="noopener noreferrer" href="https://podscan.fm/podcasts/concentrating-on-chromatography">podscan</a></li></ul>and on <a target="_blank" rel="noopener noreferrer" href="https://www.youtube.com/@ChromatographyTalk/videos">YouTube channel</a></blockquote>

Affinity, Gel Filtration, Size Exclusion Chromatography: Repurposing Kinase Inhibitors for Malaria

In the week of February 9, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.<blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars">👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</a></h4>👉 Search and filter in the largest global database with over 5 000 GC, LC, MS and spectroscopy webinars.</blockquote><h5>1. SelectScience: High-Throughput Stability Screening Strategies for Antibody Formulation</h5><ul><li>Tu, 10.2.2026 17:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5807">Registration</a></li></ul>Learn how high-throughput DLS/SLS and rapid-screening DSC accelerate stability assessment of high-concentration antibody formulations, enabling faster, data-driven biologics development.<h5>2. Phenomenex: Big Scale, Big Wins – Prep Chromatography Explained</h5><ul><li>We, 11.2.2026 10:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5793">Registration</a></li></ul>Learn how to scale analytical methods to preparative HPLC, optimize loading capacity, and understand the limits of preparative columns for pharmaceutical applications.<h5>3. ALS Czech Republic: PFAS in Food &amp; Food Contact Material</h5><ul><li>We, 11.2.2026 15:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5816">Registration</a></li></ul>Get a practical overview of PFAS in food and food contact materials, including EU and US regulations, key analytical challenges, and reliable PFAS testing strategies.<h5>4. New Food Magazine: The Science of Next-Gen Ingredients – Fermentation, Formulation and Function</h5><ul><li>We, 11.2.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5720">Registration</a></li></ul>Explore how fermentation-driven innovation is transforming functional food ingredients and how advanced analytics optimize flavour, functionality, and stability.<h5>5. SCIEX: Accurate Mass Fundamentals – Interpreting and Applying Your Data</h5><ul><li>We, 11.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5772">Registration</a></li></ul>Session 3 focuses on interpreting and applying accurate mass data to confirm compound identity, move beyond basic quantitation, and troubleshoot results for confident reporting.<h5>6. Agilent Technologies: Process Analytical Techniques – Online HPLC for Real-Time Monitoring and Control of Bioprocesses</h5><ul><li>Th, 12.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5834">Registration</a></li></ul>Discover how PAT HPLC enables near-real-time monitoring of critical quality attributes in bioprocessing, with a case study on charge-variant control by cation-exchange chromatography.<h5>7. Thermo Fisher Scientific: Introducing the Orbitrap Excedion Pro Hybrid MS</h5><ul><li>Th, 12.2.2026 11:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5889">Registration</a></li></ul>Discover the new Orbitrap Exploris Pro with expanded ETD/EThcD capabilities for confident biopharmaceutical characterization, including intact proteins, PTMs, ADCs, and large biomolecules.<h5>8. Waters Corporation: Planning Your NuGenesis Upgrade – Insights and Best Practices for a Smooth Transition</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5833">Registration</a></li></ul>Learn how to plan a successful NuGenesis upgrade, transition to Windows 11, and unlock new capabilities such as dashboards for real-time operational insights.<h5>9. Thermo Fisher Scientific: Comprehensive Analytical Strategies for Peptide Therapeutics and GLP-1 Agonists with Agilent</h5><ul><li>Th, 12.2.2026 19:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5814">Registration</a></li></ul>Explore analytical workflows for peptide therapeutics, including method development, peptide mapping, GLP-1 QC, and LC-MS strategies across Agilent platforms.<h5>10. Agilent Technologies: Moving from R&amp;D and Limited QC on a UV-Vis-NIR Instrument to Large-Scale QC Using an Autosampler</h5><ul><li>Th, 12.2.2026 20:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/2104">Registration</a></li></ul>This webinar covers practical aspects of adding and using an autosampler to maximize UV-Vis-NIR QC workflows at scale.<h5>11. Agilent Technologies: LC Method Transfer – Hidden Challenges &amp; Absolute Solution</h5><ul><li>Fr, 13.2.2026 06:30 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5787">Registration</a></li></ul>Discover why LC method transfer between legacy and modern systems is challenging, which hidden parameters affect retention and peak shape, and how to achieve robust, reliable results.

Webinars LabRulezLCMS Week 07/2026

Charge detection mass spectrometry (CDMS) allows direct mass determination of individual ions and is increasingly used to study heterogeneous biological samples. This work demonstrates the use of Orbitrap-based CDMS/Direct Mass Technology (DMT) for quantitative analysis of transthyretin (TTR) tetramer samples below 100 kDa, extending CDMS beyond its traditional qualitative role.DMT resolved wild-type and C-terminally modified TTR homotetramers, as well as hybrid tetramers, enabling kinetic analysis of subunit exchange and stability. The approach also quantified thyroxine binding to TTR variants, revealing differences in binding affinity linked to C-terminal modification. By separating overlapping m/z signals through charge measurement, CDMS enables accurate mass and abundance determination, highlighting its potential for quantitative analysis of complex protein systems.<blockquote><h4>The original article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771">Dissecting Heterogeneous Populations of Protein-Complex Samples Using Direct Mass Technology</a></h4>Robert L. Rider, Jared Hampton, Zhenyu Xi, Carter Lantz, Sangho D. Yun, Weijing Liu, Rosa Viner, Arthur Laganowsky, and David H. Russell*Anal. Chem. 2025, 97, 49, 27057–27063<a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.analchem.5c05771">https://doi.org/10.1021/acs.analchem.5c05771</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.Transthyretin (TTR) is a homotetrameric transport protein that circulates in plasma and cerebrospinal fluid, delivering thyroxine (T4) and retinol-binding protein–vitamin A complexes. <a href="javascript:void(0);">(1)</a> The stability of the TTR tetramer is central to its physiological role because dissociation into monomers can initiate misfolding and amyloid formation, leading to systemic or hereditary transthyretin amyloidosis. <a href="javascript:void(0);">(2)</a> Subunit exchange between wild-type (WT) and variant TTR proteoforms, including disease-associated mutations such as V30M and V122I, have been implicated in amyloid progression by generating hybrid tetramers (tetramers containing WT and mutant subunits) with altered stabilities. <a href="javascript:void(0);">(3,4)</a> Ligand binding, particularly at the two thyroxine-binding sites located at the dimer–dimer interface, can kinetically stabilize the tetramer and modulate amyloidogenicity. <a href="javascript:void(0);">(5,6)</a> Accurate measurement of both subunit exchange kinetics and ligand binding stoichiometry is therefore critical for elucidating the TTR dynamics and stability.Affinity or sequence tags are widely employed in protein expression, purification, or detection. <a href="javascript:void(0);">(7,8)</a> While these tags are often assumed to be inert, their influence on protein structure and dynamics are rarely examined in detail. <a href="javascript:void(0);">(9,10)</a> Protein tags at the N- and C-terminus of TTR have been shown to have differing gas phase stabilities from those of WT-TTR. <a href="javascript:void(0);">(11)</a> The C-terminus is of particular interest because this region participates in the dimer–dimer interface that governs tetramer stability. <a href="javascript:void(0);">(11,12)</a> Characterizing how the C-terminal tag (CT) (-ASGENLFYQ) affects TTR’s solution stability and ligand binding is not only relevant for understanding TTR dynamics but also provides an example of how expression tags can alter protein dynamics. <a href="javascript:void(0);">(13)</a>Native mass spectrometry (nMS) has been invaluable for characterizing protein complexes, <a href="javascript:void(0);">(14)</a> yet conventional nMS often struggles with heterogeneous samples where overlapping charge state distributions and adduct heterogeneity limit resolution and quantitation. <a href="javascript:void(0);">(15)</a> Charge detection mass spectrometry (CDMS) addresses these limitations by independently measuring the charge and m/z of individual ions, enabling the direct determination of molecular mass and abundance. Development of CDMS has largely focused on achieving higher mass resolution <a href="javascript:void(0);">(16)</a> and extending measurements toward assemblies into the GDa range. <a href="javascript:void(0);">(17,18)</a> However, there is untapped utility for CDMS experiments other than mass and proteoform determination. Jordan et al. showed the capability to assess conformational heterogeneity of mAb aggregates using the added charge dimension that CDMS provides. <a href="javascript:void(0);">(19)</a> The current work demonstrates that CDMS can separate proteoforms with overlapping m/z values based on charge and quantify their relative abundances in complex mixtures. While nMS is already a highly quantitative technique, our results establish CDMS as an equally powerful tool for quantitative analysis in heterogeneous systems. <a href="javascript:void(0);">(20,21)</a>Here, we apply Orbitrap-based CDMS/Direct Mass Technology (DMT) using the selective temporal overview of resonant ions (STORI) approach <a href="javascript:void(0);">(22,23)</a> to quantitatively compare WT-TTR and CT-TTR, focusing on two biologically relevant properties: tetramer stability assessed via subunit exchange kinetics and ligand-binding affinity. Conventional nMS cannot fully resolve the overlapping charge states of WT- and CT-TTR or their ligand-bound states. However, DMT can resolve these species by directly measuring the mass (m/z × charge), enabling quantitation of all proteoforms. The data reveal that the CT tag alters tetramer stability and thyroxine-binding affinity, demonstrating the structural sensitivity of TTR to modifications at its C-terminus. More broadly, this work demonstrates the impact that protein tags can have on native protein interactions and highlights the broader utility of quantitative CDMS for probing heterogeneous biological samples.<h4>Experimental Section</h4><h5>Data Collection</h5>All experiments were conducted on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/560">Thermo Scientific Q-Exactive UHMR</a> with added DMT capabilities (Bremen, Germany). Before DMT, mass spectra were collected at various resolving powers (6–200k) for each sample, with the instrument parameters reported in the Supporting Information (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Table S1</a>). For DMT experiments, the trapping gas pressure in the HCD cell was reduced to 0.3–0.8 to attenuate the signal intensity to a single ion level, as well as decreasing the UHV pressure to assist ion retention through the entire transient of Orbitrap analysis. We observed no significant difference between mass spectra collected at various HCD cell pressures (Supporting Information, <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S1</a>). For DMT collection, automated ion control (AIC) and 100% target density were used with 200k resolving power.<h4>Results and Discussion</h4>CDMS has emerged as a powerful tool for analyzing heterogeneous biomolecular samples, enabling accurate, direct mass determination by simultaneously measuring the charge and m/z for individual ions. While CDMS has been widely applied for qualitative analyses, its potential for quantitative and less than MDa applications remains underexplored. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>A shows the theoretical mass spectrum of WT-TTR (14+ to 16+) and CT-TTR (15+ to 17+) homotetramers, where the two proteoforms become increasingly resolved as the charge states increase (&lt;3900 m/z). <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>B zooms in on the 14+ (WT) and 15+ (CT) charge states, highlighting their strong overlap, which prevents accurate deconvolution of the proteoforms by conventional methods. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>C displays theoretical distributions for 0, 1, and 2 T4 bound states of both WT- and CT-TTR tetramers, where &lt;3900 m/z has observable separation between all proteoforms. However, for the 14+ and 15+ charge states of WT- and CT-TTR, respectively, the 0 T4- and 1 T4-bound populations overlap (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig1">Figure 1</a>D). Furthermore, commonly adducted species (Na+, K+, and Zn2+) observed in experimental spectra broaden these distributions, making it increasingly difficult to distinguish and deconvolute the proteoforms (see <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figure S2</a>). Here, we employ Orbitrap-based CDMS/DMT to overcome this m/z overlap to resolve and quantify hybrid tetramer formation and T4 binding.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 1. (A) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers. (B) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions to show the large overlap of the proteoforms. (C) Theoretical mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine (T4) binding. (D) Zoomed-in view of the 14+ WT-TTR and 15+ CT-TTR distributions where the 0 and 1 T4 have overlapping distributions. These theoretical distributions do not contain any commonly adducted species (Na+, K+, Zn2+), which broaden the distributions and create more overlap even for the proteoforms in the range 3300–3900 m/z (see Figure S2)." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_1_A_Theoretical_mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_47232849d9.jpg 187w," sizes="100vw" width="1417" height="1182"><h5>Thyroxine Binding to TTR Homotetramers</h5>Thyroxine is the less active form of a thyroid hormone important for metabolism that binds to TTR for transport throughout plasma and cerebral spinal fluid. <a href="javascript:void(0);">(31)</a> Turnover of T4 into T3 (active) occurs after dissociation, where it can then modulate gene expression via binding to nuclear receptors. <a href="javascript:void(0);">(32)</a> The TTR tetramer gains substantial stability as it binds up to 2 T4 at the tetramer interface, decreasing tetramer dissociation and SUE. <a href="javascript:void(0);">(33)</a> This has been shown previously to decrease the amyloidogenic rate of TTR, which led to tafamidis (similar in structure to T4) to be designed and is currently the only drug that is approved for clinical treatment of TTR amyloidosis. <a href="javascript:void(0);">(34)</a> Measuring the difference in binding affinity between TTR proteoforms may provide insight into regions of TTR or TTR intermolecular/intramolecular interactions that are important for binding of small molecules such as tafamidis and T4.DMT was further applied to quantify T4 binding to WT- and CT-TTR homotetramers, highlighting the technique’s utility in probing protein–ligand interactions. <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>A shows a representative mass spectrum of TTR homotetramers in the presence of T4. While ligand-bound species can be observed, homotetramers cannot be confidently resolved across the entire 3000–5000 m/z range. By leveraging the charge-resolving capabilities of DMT, we achieve separation of the homotetramers (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.analchem.5c05771#fig3">Figure 3</a>B,C) and the 0, 1, and 2 ligand-bound states. The 2D plot clearly shows the gain in resolution achieved when charge is simultaneously measured with m/z by separating the 14+ and 15+ charge states for WT and CT, respectively, in the range 3900–4200 m/z. Additionally, using ion mobility does not provide the same kind of 2D resolution due to the similarity in arrival times for the homotetramer proteoforms, as evidenced by <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.analchem.5c05771/suppl_file/ac5c05771_si_001.pdf">Figures S4 and S5</a> (see the Supporting Information). These data provide evidence that when ion mobility is able to separate out species that overlap in m/z yet differ in mobility, CDMS could be an alternative or used complementarily since the species likely also differ in charge.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg" alt="Anal. Chem. 2025, 97, 49, 27057–27063: Figure 3. (A) Mass spectra of WT-TTR and CT-TTR homotetramers with thyroxine binding. Ligand binding can be resolved, but homotetramers cannot be confidently identified. Charge states labeled are for WT; CT is always one charge state higher at the same m/z range. (B) DMT heatmap resolving WT-TTR and CT-TTR homotetramers with the additional measurement of charge. (C) Deconvoluted mass spectrum from DMT analysis. Both homotetramers and their ligand binding are resolved, and fit for analysis is shown in red. (D) Mole fraction of each homotetramer and their thyroxine binding species. Error bars represent the standard deviation of replicates (n = 3). The significance for each ligand state is in respect to the left adjacent state. *p &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Anal_Chem_2025_97_49_27057_27063_Figure_3_A_Mass_spectra_of_WT_TTR_and_CT_TTR_homotetramers_with_thyroxine_binding_61b1e98a94.jpg 181w," sizes="100vw" width="1266" height="1094"><h4>Conclusion</h4>This work demonstrates that quantitatively, Orbitrap-based CDMS/DMT can determine differences in protein-complex stability and ligand binding. By directly comparing WT- with CT-TTR, we show that the CT tag accelerates tetramer dissociation while enhancing T4 binding affinity. These results indicate that the C-terminus, located at the dimer–dimer interface, plays a more significant role in TTR stability and ligand recognition than previously appreciated. <a href="javascript:void(0);">(12)</a> Even the addition of a short peptide sequence perturbs noncovalent interactions at the interface, likely altering solvent accessibility, and the dynamics of the thyroxine binding channel. <a href="javascript:void(0);">(37,54)</a> Such findings underscore the importance of evaluating how seemingly minor sequence modifications, such as affinity tags, can influence fundamental biophysical properties.Beyond TTR, this work positions quantitative CDMS as a broadly applicable strategy for analyzing heterogeneous protein systems, where charge domain separation overcomes the resolution limits of m/z domain measurements in traditional nMS experiments. While much of the field has emphasized extending CDMS to ultrahigh masses and maximal resolution, <a href="javascript:void(0);">(16,18)</a> our results highlight the underexplored potential of applying the method in the 1000–10,000 m/z range common to nMS experiments. This capability is directly relevant to heterogeneous membrane protein complexes, which often display broad distributions of oligomeric states, PTMs, lipid, and ligand adducts that complicate spectra. <a href="javascript:void(0);">(48,55)</a> Similarly, mAbs can oligomerize and exhibit mass heterogeneity from variable glycosylation, affecting pharmacokinetics, effector function, and stability. <a href="javascript:void(0);">(19)</a> CDMS may resolve and quantify such proteoforms in a single experiment without the need for charge reduction or chemical derivatization. <a href="javascript:void(0);">(48,56,57)</a>

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Waters/Wyatt DAWN™ Multi Angle Light Scattering (MALS) Detector

The world's most advanced light scattering instrument for absolute characterization of proteins, conjugates, macromolecules, and nanoparticles.

<h5>Premier MALS</h5>The DAWN instrument is the premier Multi-Angle static Light Scattering (MALS) detector for absolute characterization of the molar mass and size of macromolecules and nanoparticles in solution. It offers the highest sensitivity, the widest range of molecular weight, size, and concentration, and the largest selection of configurations and optional modules for enhanced capabilities.<h5>Separation First</h5>MALS is most often used in conjunction with a separation system such as Gel Permeation Chromatography (GPC-MALS), Size Exclusion Chromatography (SEC-MALS), or Field-Flow Fractionation (FFF-MALS) to determine distributions of mass, size, and composition, independent of column calibration by reference standards.<h5>Supported by ASTRA ™ &nbsp;Software</h5>ASTRA Software and its built-in analysis modules support the DAWN MALS instrument, providing the most versatile analysis available for online multi-angle and dynamic light scattering measurements.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_DAWN_MALS_HPLC_detektor_konfigurace_d5b83e46b2.jpg" alt="Waters DAWN™ Multi Angle Light Scattering (MALS) Instrument: ASTRA Software" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_DAWN_MALS_HPLC_detektor_konfigurace_d5b83e46b2.jpg 245w," sizes="100vw" width="1500" height="807"><h4>Product description</h4>The DAWN and its companion Optilab ™ &nbsp;dRI detector are the established benchmarks for MALS analysis, cited in thousands of peer-reviewed publications. Multi-angle light scattering detection is indispensable for use with GPC and HPLC-SEC in order to obtain reliable molecular mass distributions and information on molecular conformation, branching ratio, fragments and aggregates.SEC-MALS with a DAWN and Optilab characterizes conformation and branching of synthetic and natural polymers larger than 10 nm in rms radius R g . The addition of a ViscoStar ™&nbsp; differential viscometer creates a GPC triple-detection system that can analyze molecular conformation and size below the R g &nbsp;limit of 10 nm and determine Mark-Houwink Sakurada coefficients.The combination of a UV/Vis absorbance detector with a DAWN instrument and Optilab refractive index detector creates a UV-MALS-RI triple-detection system, for analysis of copolymers and protein conjugates (glycoproteins, PEGylated proteins, surfactant-bound membrane proteins, etc.). With the addition of a WyattQELS ™ &nbsp;DLS module for size determination, protein conformation may be analyzed.<ul><li>Mw &nbsp;from 200 Da to 1000 MDa</li><li>Sensitivity: 10 ng/mL 100 kDa polystyrene in THF, 0.4 µg/mL BSA (66.4 kDa) in PBS</li><li>Rg &nbsp;from 10 to 500 nm, up to 1000 nm with shape-specific models</li><li>Ultra-stable, high-power laser</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_DAWN_MALS_HPLC_detektor_konfigurace_1_98811a1e87.jpg" alt="Waters DAWN™ Multi Angle Light Scattering (MALS) Instrument: Accessories" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_DAWN_MALS_HPLC_detektor_konfigurace_1_98811a1e87.jpg 213w," sizes="100vw" width="1000" height="733">The DAWN may also be used in batch (off-line) mode to characterize the weight-average molar mass, z-average size and second virial coefficient of unfractionated samples.In conjunction with a Calypso ™ &nbsp;CG-MALS system, the DAWN characterizes macromolecular interactions, label-free and immobilization-free: affinity and absolute stoichiometry of self- and hetero-association of simple or complex molecular systems. The Calypso system also automates the determination of second virial coefficients, cross virial coefficients, average molar masses and sizes.<h5>Ultrasonic Cleaning Included</h5>Each DAWN instrument includes an embedded COMET ™ &nbsp;ultrasonic transducer that cleans the flow cell automatically by agitating the fluid and loosening particles from the glass surfaces.<h5>Temperature-Controlled Models</h5><ul><li>Ambient model</li><li>Ultra-High-Temperature (UHT) model, from ambient up to +210 °C</li><li>Standard Peltier heated/cooled (H/C) model, temperature control from -15 °C to +150 °C</li></ul><h4>Specifications</h4><h5>Measurement Capabilities</h5><ul><li>Molar Mass Range: From 200 Da to 1 GDa, depending on dn/dc, sample concentration, and chromatography conditions.</li><li>Molecular Size (Radius of Gyration, Rg): Approximately 10 nm to 500 nm, extendable to 1000 nm with shape-specific models.</li><li>Hydrodynamic Radius (Rh):<ul><li>Flow mode: 0.5 nm to 300 nm (depending on configuration and flow rate).</li><li>Batch mode: 0.5 nm to 1 µm (requires WyattQELS™ DLS module or DynaPro™ NanoStar™ with fiber optic connection).</li></ul></li><li>Sensitivity: Detects as little as 10 ng of 100 kDa polystyrene in THF or 200 ng of BSA in PBS, using a standard 7.8 mm x 300 mm SEC column and no post-column filter.</li></ul><h5>Fluidics and Compatibility</h5><ul><li>Mobile Phase: Compatible with both aqueous and organic solvents.</li><li>Wetted Materials: 316 stainless steel, fused silica or F2 glass, and Kalrez.</li></ul><h5>Optical System and Detectors</h5><ul><li>MALS Detectors: 18 photodiodes with high gain and wide dynamic range for multi-angle light scattering.</li><li>Auxiliary Detectors:<ul><li>Laser monitor for stabilization</li><li>Forward transmission monitor to improve data quality and correct for sample absorption</li></ul></li><li>Dynamic Range: 3,300,000:1</li><li>Optional DLS Detection:<ul><li>Integrated WyattQELS™ module inside the DAWN</li><li>External fiber optic connection with DynaPro NanoStar or Mobius DLS-ELS instruments</li></ul></li></ul><h5>Laser Specifications</h5><ul><li>Wavelength: Standard 658 nm ± 4 nm; optional 785 nm for fluorescent samples</li><li>Power Control: Programmable from 10% to 100%</li></ul><h5>Flow Cell Options</h5><ul><li>Fused Silica: Ideal for solvents with refractive index &lt; 1.50</li><li>F2 Glass: Recommended for solvents with refractive index &gt; 1.50</li></ul><h5>Temperature Control Options</h5><ul><li>Ambient operation</li><li>Heated/Cooled (HC): -15 °C to +150 °C</li><li>Ultra-High Temperature (UHT): Ambient to +210 °C</li></ul><h5>Electronics and Connectivity</h5><ul><li>Analog Inputs: 4 differential inputs, 24-bit resolution, range -10 V to +10 V</li><li>Analog Outputs: 2 outputs from selectable measurement channels, -10 V to +10 V</li><li>I/O Options: Alarm in/out, auto-inject control, and Orbit™ valve integration</li><li>Computer Interface: Ethernet</li><li>Display: 10.1” high-resolution capacitive touchscreen with multi-touch controls</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 58 cm (L) x 36 cm (W) x 26 cm (H)</li></ul><h4>Other MALS Instruments</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1115">miniDAWN™</a> &nbsp;- Second only to the DAWN in sensitivity. Incorporates detectors at 3 angles to determine molar masses from 200 Da to 10 MDa and radii from 10 – 50 nm. Ambient only.</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1116">microDAWN™</a>&nbsp; - The first MALS detector for UHPLC, with interdetector dispersion as low as 1.5 µL. Incorporates detectors at 3 angles to determine molar masses from 200 Da to 20 MDa and radii from 10 – 50 nm. Ambient only.</li><li>ultraDAWN™ &nbsp;- Measures multi-angle light scattering and reports the results – weight-average molecular weight Mw &nbsp;and rms radius Rg &nbsp;– in real time.</li></ul>

Waters/Wyatt miniDAWN™ Multi Angle Light Scattering (MALS) Detector

The Best in Basic Multi-Angle Light Scattering for Absolute Macromolecular Analysis.

<h4>Overview</h4><h5>Molar Mass</h5>The miniDAWN determines absolute molar mass and size to characterize proteins, peptides, small polymers and nanoparticles in solution. Coupled to size exclusion chromatography (SEC or GPC), it eliminates the uncertainty and hassle of column calibration, for true confidence in macromolecular characterization.<h5>Superb Sensitivity</h5>The miniDAWN not only offers superb sensitivity—it further enhances productivity thanks to greatly enhanced field serviceability and easy data analysis with One-Click Mw™ .<h5>Compatible with ASTRA™&nbsp;</h5>The miniDAWN is accompanied by ASTRA, the most versatile software package available for analysis of online multi-angle and dynamic light scattering. ASTRA and the miniDAWN incorporate advanced ease-of-use features that help guarantee excellent measurements with a single click.<h4>Product Description</h4><h5>Molar mass, absolutely</h5>Wyatt's miniDAWN is most often used in conjunction with size exclusion chromatography (SEC-MALS) or field-flow fractionation (FFF-MALS) to determine distributions of molecular weight, size and composition. No need to make assumptions about molecular conformation or ideal column interactions.<h5>Characterize:</h5><ul><li>Proteins, small peptides and oligonucleotides</li><li>Synthetic and natural polymers</li><li>Nanoparticles, virus-like particles and vesicles</li></ul><h5>Measurement Range:</h5><ul><li>MW from 200 Da to 10 MDa</li><li>rg &nbsp;from 10 to 50 nm, up to 150 nm with shape-specific models</li><li>sensitivity down to 25 ng of 100 kDa polystyrene in THF, injected on a standard GPC column</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Mini_DAWN_urcuje_molekulovou_hmotnost_nezavisle_na_kalibraci_kolony_Zde_MALS_ukazuje_ze_nejdrive_eluujici_molekula_nema_nejvyssi_molarni_hmotnost_509e5530ea.jpg" alt="Waters: The miniDAWN determines molecular weight independently of column calibration. Here MALS shows that the earliest-eluting molecule does not have the highest molar mass." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Mini_DAWN_urcuje_molekulovou_hmotnost_nezavisle_na_kalibraci_kolony_Zde_MALS_ukazuje_ze_nejdrive_eluujici_molekula_nema_nejvyssi_molarni_hmotnost_509e5530ea.jpg 245w," sizes="100vw" width="820" height="438">The miniDAWN's performance is exceeded only by the DAWN™ which covers a wider range of size and molecular weight, with even better sensitivity and additional optional modules.<h5>Ultrasonic Cleaning Included</h5>Each miniDAWN includes an embedded COMET™ ultrasonic transducer that cleans the flow cell automatically by agitating the fluid and loosening particles from the glass surfaces.<h5>Modularity = Productivity</h5>The miniDAWN incorporates a fully modular design. Each module can be tested independently by the software to verify that it is functioning correctly. This imparts nearly complete field serviceability, since malfunctioning modules can be replaced and validated on-site by service engineers with no further calibration or alignment.The miniDAWN is also field-upgradeable: the embedded WyattQELS™ DLS Module for measuring hydrodynamic radii from 0.5 to 50 nm can be installed on-site as well as in new units shipped from the factory.<h5>Not just SEC-MALS...</h5>Wyatt's miniDAWN may be used in batch (off-line) mode or in conjunction with a Calypso™ CG-MALS system for characterization of average solution properties as well as macromolecular interaction properties including protein-protein binding affinity and complex stoichiometry.<h5>Simplicity personified</h5>With miniDAWN and ASTRA™, SEC-MALS became a whole lot easier. Sample-specific methods are set up in three short steps with ASTRA's Method Wizard, and new capabilities for automatic data processing mean that it takes just one click from your sample to a full report of the molecular weight and size results.The miniDAWN's System Ready monitor will even let you know when the system is fully equilibrated with low baseline noise, ready to run.<h4>Specifications</h4><h5>Measurement Capabilities</h5><ul><li>Molar Mass Range: 200 Da to 10 MDa for proteins; up to 1 MDa for linear polymers (depending on dn/dc, sample concentration, and chromatography conditions).</li><li>Molecular Size (Radius of Gyration, Rg): Approximately 10 nm to 50 nm, extendable up to 150 nm with shape-specific modeling.</li><li>Hydrodynamic Radius (Rh):<ul><li>Flow mode: 0.5 nm to 50 nm (optimal at flow rates ≤ 0.3 mL/min)</li><li>Batch mode: 0.5 nm to 1 µm (requires WyattQELS™ module or DynaPro™ NanoStar™ with fiber optic connection)</li></ul></li><li>Sensitivity: Detects as little as 25 ng of 100 kDa polystyrene in THF or 500 ng of BSA in PBS using a standard 7.8 mm x 300 mm SEC column with no post-column filter.</li></ul><h5>Fluidics and Compatibility</h5><ul><li>Mobile Phase Compatibility: Compatible with both aqueous and organic solvents.</li><li>Wetted Materials: 316 stainless steel, fused silica, and Kalrez.</li></ul><h5>Optical System and Detectors</h5><ul><li>MALS Detectors: Three high-gain, high dynamic range photodiodes at fixed angles.</li><li>Auxiliary Detectors:<ul><li>Laser monitor for stability control</li><li>Forward transmission monitor for absorbing samples and data quality evaluation</li></ul></li><li>Dynamic Range: 3,300,000:1</li><li>Optional DLS Detection:<ul><li>Integrated WyattQELS™ module within the miniDAWN chassis</li><li>External fiber optic connection from DynaPro™ NanoStar or Mobius™ DLS-ELS instruments</li></ul></li></ul><h5>Laser Specifications</h5><ul><li>Wavelength: 658 nm ± 4 nm</li><li>Power Control: Programmable from 10% to 100%</li></ul><h5>Temperature Control</h5><ul><li>Sample Temperature: Ambient</li></ul><h5>Electronics and Connectivity</h5><ul><li>Analog Inputs: 2 differential inputs, 24-bit resolution, ±10 V range</li><li>Analog Outputs: 1 output from a selectable measurement channel, ±10 V range</li><li>I/O Ports: Alarm in/out, auto-inject control, Orbit™ recycle valve support</li><li>Computer Interface: Ethernet</li><li>Data Rate: Up to 36.6 Hz</li></ul><h5>User Interface and Display</h5><ul><li>Front Panel: 7” (178 mm) high-resolution multi-touch display for real-time signal viewing, diagnostics, and settings</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 58 cm (L) x 36 cm (W) x 18 cm (H)</li></ul><h4>Other MALS Instruments</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1114">DAWN™</a> - The most sensitive MALS detector available, anywhere. Incorporates detectors at 18 angles to determine molar masses from 200 Da to 1 GDa and radii from 10 – 500 nm.<ul><li>Standard option: ambient temperature</li><li>Heated/cooled option: -15 °C to +150 °C</li><li>High-temperature option: ambient to +210 °C</li><li>The DAWN offers special options to handle fluorescent samples: fluorescence-blocking filters and an infrared, 785 nm laser.</li></ul></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1116">microDAWN™</a> - The first MALS detector for UHPLC, with interdetector dispersion as low as 1.5 µL. Incorporates detectors at 3 angles to determine molar masses from 200 Da to 20 MDa and radii from 10 – 50 nm. Ambient only.</li><li>ultraDAWN™ - Measures multi-angle light scattering and reports the results – weight-average molecular weight Mw &nbsp;and rms radius Rg &nbsp;– in real time.</li></ul>

Waters/Wyatt microDAWN™ Multi Angle Light Scattering (MALS) Detector

The microDAWN can be coupled to any UHPLC-SEC system to determine absolute molecular weights and sizes of polymers, peptides, or proteins directly, without resorting to column calibration or reference standards.

<h4>Overview</h4><h5>UHPLC-SEC System</h5>The microDAWN can be coupled to any UHPLC-SEC system to determine absolute molecular weights and sizes of polymers, peptides, or proteins directly, without resorting to column calibration or reference standards. The microDAWN produces minimal band broadening in order to maintain the narrow peaks typical of UHPLC, while meeting or exceeding the sensitivity of the miniDAWN™.<h4>Product Description</h4>The microDAWN MALS detector performs absolute characterization of macromolecules eluting from UHPLC, determining molar mass and size independently of retention time and molecular reference standards. This instrument offers superb sensitivity over a wide range of molar mass, size and concentrations. In most respects the microDAWN is similar to the well-established miniDAWN™, a workhorse MALS instrument used in hundreds of labs around the world for characterizing proteins and other molecules smaller than 50 nm in radius.Distinctly from the miniDAWN, the microDAWN is uniquely suitable for use in conjunction with UHPLC Size Exclusion Chromatography (SEC-MALS) thanks to its small interdetector dispersion. In some cases it may be used with ion-exchange or other types of chromatography. Regardless of the specifics, the microDAWN produces minimal band broadening in order to maintain the narrow peaks typical of UHPLC.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_micro_DAWN_MALS_HPLC_detektor_konfigurace_1_4e888650cf.jpg" alt="Waters microDAWN™ Multi Angle Light Scattering (MALS) Instrument: Experimental setup" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_micro_DAWN_MALS_HPLC_detektor_konfigurace_1_4e888650cf.jpg 229w," sizes="100vw" width="894" height="609"><ul><li>Mw&nbsp; from 200 Da to 10 MDa</li><li>Sensitivity: 1.0 µg/mL BSA (66.4 kDa) in PBS; 50 ng/mL 100 kDa polystyrene in THF.</li><li>Rg &nbsp;from 10 to 50 nm</li><li>Ultra-stable laser</li></ul>The microDAWN and its companion microOptilab™ Refractive Index Detector interface to most standard UHPLC systems. As these detectors are based on the advanced technology of Wyatt's miniDAWN and Optilab™, respectively, users may be confident in the underlying capabilities cited in thousands of peer-reviewed publications.<h5>Ultrasonic Cleaning Included</h5>Each microDAWN includes a COMET™ ultrasonic transducer that cleans MALS flow cells automatically by agitating the fluid and loosening particles from the glass surfaces.<h4>Specifications</h4><h5>Measurement Capabilities</h5><ul><li>Molar Mass Range: From 200 Da to 10 MDa for proteins; up to 1 MDa for linear polymers (Typical, depending on dn/dc, sample concentration, and chromatography conditions)</li><li>Molecular or Particle Size (Radius of Gyration, Rg): 10 nm to 50 nm, extendable up to 150 nm with shape-specific modeling</li><li>Hydrodynamic Radius (Rh):<ul><li>Flow mode: 0.5 nm to 30 nm</li><li>Batch mode: 0.5 nm to 1 µm (Requires WyattQELS™ DLS module or DynaPro™ NanoStar™ with fiber optic connection)</li></ul></li><li>Sensitivity: Detects as little as 3.5 ng of 100 kDa polystyrene in THF or 70 ng of BSA in PBS, assuming use of a 15 cm UHPLC-SEC column with no post-column filter</li></ul><h5>Optical System and Detectors</h5><ul><li>MALS Detectors: Three high-gain photodiodes with broad dynamic range for multi-angle light scattering</li><li>Dynamic Range: 3,300,000:1</li><li>Auxiliary Detectors:<ul><li>Laser monitor for stabilization feedback</li><li>Forward transmission monitor for absorbing samples and data quality assessment</li></ul></li><li>Optional DLS Detection:<ul><li>Integrated WyattQELS™ module within the microDAWN chassis</li><li>External DLS connection via fiber optic from DynaPro™ NanoStar or Mobius™ DLS-ELS instruments</li></ul></li></ul><h5>Laser Specifications</h5><ul><li>Wavelength: 658 nm ± 4 nm</li><li>Power Control: Programmable from 10% to 100%</li></ul><h5>Sample Temperature and Flow Characteristics</h5><ul><li>Sample Temperature: Ambient</li><li>Interdetector Band Broadening:<ul><li>Upstream detector to microDAWN: &lt; 1.5 µL</li><li>Upstream to downstream detector: &lt; 1.6 µL</li></ul></li></ul><h5>Material Compatibility</h5><ul><li>Wetted Materials: 316 stainless steel, fused silica, PEEK, PTFE, and MP35N (iron-free alloy)</li></ul><h5>Electronics and Connectivity</h5><ul><li>Analog Inputs: 2 differential inputs, 24-bit resolution, ±10 V input range</li><li>Analog Outputs: 1 output from a user-selectable measurement channel, ±10 V range</li><li>I/O Ports: Alarm in/out, auto-inject control, Orbit™ valve integration</li><li>Computer Interface: Ethernet</li><li>Data Transmission Rate: Up to 73 Hz</li></ul><h5>User Interface</h5><ul><li>Display: 7” (178 mm) high-resolution multi-touch screen for signal monitoring, instrument settings, and diagnostics</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 58 cm (L) x 36 cm (W) x 18 cm (H)</li></ul><h4>Other MALS Instruments</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1114">DAWN™</a> - The most sensitive MALS detector available, anywhere. Incorporates detectors at 18 angles to determine molar masses from 200 Da to 1 GDa and radii from 10 – 500 nm.<ul><li>Standard option: ambient temperature</li><li>Heated/cooled option: -15 °C to +150 °C</li><li>High-temperature option: ambient to +210 °C</li><li>The DAWN offers special options to handle fluorescent samples: fluorescence-blocking filters and an infrared, 785 nm laser.</li></ul></li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1115">miniDAWN™</a> - Second only to the DAWN in sensitivity. Incorporates detectors at 3 angles to determine molar masses from 200 Da to 10 MDa and radii from 10 – 50 nm. Ambient only.</li><li>ultraDAWN™ - Measures multi-angle light scattering and reports the results – weight-average molecular weight Mw &nbsp;and rms radius Rg &nbsp;– in real time.</li></ul>

Waters/Wyatt ViscoStar HPLC viscometer

Waters ViscoStar is a highly sensitive, on-line differential viscometer used in conjunction with SEC-MALS-IV to determine the size and conformation of all types of biopolymers, synthetic polymers and even proteins and peptides.

<h4>Highly Sensitive</h4>A highly sensitive, on-line differential viscometer used in conjunction with SEC-MALS-IV to determine the size and conformation of all types of biopolymers, synthetic polymers and even proteins and peptides.<h4>Multiple Novel Technologies</h4>The ViscoStar incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for GPC. Its ease-of-use and serviceability make it the perfect companion for Wyatt's DAWN™ light scattering and Optilab™ refractive index detectors.<h4>Another path to polymer and protein characterization: SEC-MALS-IV</h4>When coupled with size-exclusion chromatography and a concentration detector such as the Optilab™ , the ViscoStar derives the intrinsic viscosity (IV) of polymers. An inherently valuable physico-chemical property in itself, IV is best utilized together with molar mass information from multi-angle light scattering (SEC-MALS-IV) to derive the hydrodynamic radius, conformation, and branching ratio of a macromolecule in solution.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg" alt="Waters ViscoStar: Patented pulse compensation technology in the ViscoStar eliminates pump fluctuations. At the hardware level, the bridge is impedance matched for dynamic balance, greatly reducing the effect of pump pulses. An additional layer of software filtering eliminates residual pump pulses." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg 233w," sizes="100vw" width="348" height="233"><h5>Key benefits of the ViscoStar</h5><ul><li>High sensitivity, equivalent to 100 ng of 100 kDa polystyrene in THF at 1.0 mL/min injected onto a standard GPC column</li><li>High dynamic range of over 135,000:1. The full measurement range corresponds to over 13 mg/mL of 100 kDa polystyrene in THF</li><li>Extended solvent compatibility with all-316 stainless steel transducers</li><li>Temperature range from 4 °C to 70 °C for polymers or proteins that require a range of temperatures</li><li>Minimal band broadening thanks to fast pressure transducers</li><li>Pump pulse suppression to below 4 Pa (hardware alone) or 1 Pa (hardware + software) without loss of chromatographic resolution</li><li>Automated capillary bridge tuning with no moving parts, to guarantee a perfectly balanced bridge, every run</li><li>Enhanced thermal stability with drift of &lt;2.5 Pa/hour</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Visco_Star_cmc_plga_intrinsic_viscosity_graphs_be99c5d115.jpg" alt="Waters ViscoStar: The ViscoStar provides the highest available dynamic range and sensitivity in online viscometry. This graph shows the intrinsic viscosities of 1) poly(lactic co-glycolic acid), or PLGA, in THF and 2) carboxymethyl cellulose, or CMC, in aqueous mobile phase, both measured with a ViscoStar and Optilab, spanning a range from tens to thousands of mL/g. The same instruments readily measure intrinsic viscosity values in the low single digits with excellent signal-to-noise, even at very low concentrations." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Visco_Star_cmc_plga_intrinsic_viscosity_graphs_be99c5d115.jpg 236w," sizes="100vw" width="406" height="268"><h5>SEC-IV without MALS?</h5>Yes, as much as we love MALS for optimal polymer analysis, it's true that there are occasions when it just won't fit the bill.Universal calibration is a parallel technique to SEC-MALS for determining molecular weight, commonly used to characterize linear polymers. While universal calibration overcomes some of the problematic issues associated with column calibration by reference molecules, it does not account for non-ideal column behavior caused by chemical solute-column interactions or hyperbranching.Universal calibration is particularly-well suited to replace MALS for:<ul><li>Strongly fluorescent polymers, in particular those not adequately addressed by a DAWN™ with long-wavelength (785 nm) laser or a standard DAWN (685 nm) with fluorescence-blocking filters.</li><li>Weakly-scattering polymer/solvent systems with very low dn/dc values</li></ul>The Mark-Houwink-Sakurada relationship makes use of empirical relationships between intrinsic viscosity and molar mass, specific to each polymer and solvent, to estimate molar mass from SEC-IV measurements. Of course, the best way to determine MHS coefficients is to measure them using SEC-MALS-IV and ASTRA™!<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Visco_Star_v3_protein_rh_measurements_0951d3769a.jpg" alt="Waters ViscoStar: Three IgG proteins with similar MWs eluted at different elution volumes. To understand their different elution properties, online DLS is typically used to measure the hydrodynamic radius, R h , of a protein. However, online DLS did not provide reliable insights, in this case due to the relatively high experimental uncertainty of the DLS. The precise Rh values obtained with a MALS detector and the ViscoStar III, on the other hand, clearly revealed the causes. IgG B eluted later than IgG A due to its more compact structure; IgG C had a slight interaction with the SEC column." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Visco_Star_v3_protein_rh_measurements_0951d3769a.jpg 237w," sizes="100vw" width="401" height="264"><h4>Specifications</h4><h5>Measurement Capabilities – Differential Viscosity</h5><ul><li>Sensitivity: Detects as little as 0.1 µg of 100 kDa polystyrene in THF at 1 mL/min under typical GPC conditions.</li><li>Differential Pressure Performance:<ul><li>Noise: &lt; 0.05 Pa</li><li>Range: 6.9 kPa, with built-in overpressure protection</li><li>Drift: &lt; 2.5 Pa/hr</li><li>Linearity: Within 0.5% of full scale</li><li>Dynamic Range: 135,000:1</li></ul></li><li>Capillary Bridge Autobalance: Thermally regulated, leak-free mechanism ensures stable baseline and precision.</li><li>Sample Shear Rate: Up to 5000 Hz with water at 1 mL/min</li></ul><h5>Fluidics and Flow Compatibility</h5><ul><li>Maximum Flow Rate:<ul><li>Aqueous: 1.5 mL/min</li><li>THF: 3 mL/min</li></ul></li><li>Delay Volume Options: Configurable at 16.2, 10.8, or 5.4 mL; optional factory-installed upgrade to 32.4 mL (Note: actual column fluid volume is approx. half the listed value)</li><li>Maximum Inlet-to-Outlet Pressure: 690 kPa</li><li>Wetted Materials: 316 stainless steel, PTFE, zirconium silicate, Kalrez, Inconel, and 26-1 stainless steel – all selected for chemical resistance and long-term durability</li></ul><h5>Temperature Control</h5><ul><li>Operating Range: 4 °C to 70 °C</li><li>Stability: Maintains temperature within &lt; 0.005 °C for precise measurements</li><li>Ambient Conditions: 0 °C to 40 °C; relative humidity 20% to 70%</li></ul><h5>Electronics and Connectivity</h5><ul><li>Digital Output: 20-bit resolution at 10 Hz for high-fidelity data</li><li>Auxiliary I/O:<ul><li>Inputs: Autoinject contact closure, Alarm In, and 2 analog inputs (18-bit, ±10 V)</li><li>Outputs: Autoinject retransmit, Alarm Out, Recycle Out</li></ul></li><li>Communication Interface: Ethernet for seamless integration into lab networks and data systems</li></ul><h5>User Interface</h5><ul><li>Front Panel Display: 7” (178 mm) high-resolution capacitive touchscreen for monitoring signals, diagnostics, and adjusting settings with ease</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 58 cm (L) × 36 cm (W) × 18 cm (H)</li></ul><h4>Other Viscometers</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1267">microViscoStar™ </a>- Similar to the ViscoStar but designed specifically for use with UHPLC/APC.</li></ul>

Waters/Wyatt microViscoStar viscometer

The Waters microViscoStar incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for UHPLC. 

<h4>Highly Sensitive</h4>A highly sensitive, on-line differential viscometer used with SEC-MALS-IV to determine the size and conformation of polymers, proteins and peptides separated by UHPLC.<h4>Multiple Novel Technologies</h4>The microViscoStar™ incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for UHPLC. Its ease-of-use and serviceability make it the perfect companion for Wyatt's microDAWN™ light scattering and microOptilab™ refractive index detectors for UHPLC.<h4>Another path to polymer and protein characterization: SEC-MALS-IV</h4>When coupled with size-exclusion chromatography and a concentration detector such as the Optilab™ , the microViscoStar derives the intrinsic viscosity (IV) of polymers. An inherently valuable physico-chemical property in itself, IV is best utilized together with molar mass information from multi-angle light scattering (SEC-MALS-IV) to derive the hydrodynamic radius, conformation, and branching ratio of a macromolecule in solution.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg" alt="Waters microViscoStar: Patented pulse compensation technology in the microViscoStar eliminates pump fluctuations. At the hardware level, the bridge is impedance-matched for dynamic balance, greatly reducing the effect of pump pulses. An additional layer of software filtering eliminates residual pump pulses." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Waters_Visco_Star_pump_pulse_suppression_with_inset_e8c2fbfc18.jpg 233w," sizes="100vw" width="348" height="233"><h5>Key benefits of the ViscoStar</h5><ul><li>High sensitivity, equivalent to 5 ng of 100 kDa polystyrene in THF at 1.0 mL/min injected onto a standard GPC column</li><li>High dynamic range of over 135,000:1. The full measurement range corresponds to over 13 mg/mL of 100 kDa polystyrene in THF</li><li>Extended solvent compatibility with all-316 stainless steel transducers</li><li>Temperature range from 4 °C to 70 °C for polymers or proteins that require a range of temperatures</li><li>Minimal band broadening thanks to fast pressure transducers</li><li>Pump pulse suppression to below 4 Pa (hardware alone) or 1 Pa (hardware + software) without loss of chromatographic resolution</li><li>Automated capillary bridge tuning with no moving parts, to guarantee a perfectly balanced bridge, every run</li><li>Enhanced thermal stability with drift of &lt;1.25 Pa/hour</li></ul><h4>SEC-IV without MALS?</h4>Yes, as much as we love MALS for optimal polymer analysis, it's true that there are occasions when it just won't fit the bill.Universal calibration is a parallel technique to SEC-MALS for determining molecular weight, commonly used to characterize linear polymers. While universal calibration overcomes some of the problematic issues associated with column calibration by reference molecules, it does not account for non-ideal column behavior caused by chemical solute-column interactions or hyperbranching.Universal calibration is particularly-well suited to replace MALS for:<ul><li>Strongly fluorescent polymers</li><li>Weakly-scattering polymer/solvent systems with very low dn/dc values</li></ul>The Mark-Houwink-Sakurada relationship makes use of empirical relationships between intrinsic viscosity and molar mass, specific to each polymer and solvent, to estimate molar mass from SEC-IV measurements. Of course, the best way to determine MHS coefficients is to measure them using SEC-MALS-IV and ASTRA™<h4>Specifications</h4><h5>Measurement Capabilities – Differential Viscosity</h5><ul><li>Sensitivity: Detects as little as 5 ng of 100 kDa polystyrene in THF at 1 mL/min under typical UHPLC-SEC conditions.</li><li>Differential Pressure Performance:<ul><li>Noise: &lt; 0.05 Pa</li><li>Range: Up to 6.9 kPa, with overpressure protection</li><li>Drift: &lt; 1.25 Pa/hr</li><li>Linearity: Within 0.5% of full scale</li><li>Dynamic Range: 135,000:1</li></ul></li><li>Capillary Bridge Autobalance: Thermal, leak-free mechanism ensures stable baseline performance.</li><li>Sample Shear Rate: Up to 15,000 Hz with water at 1 mL/min for high-resolution viscosity profiling.</li></ul><h5>Fluidics and Compatibility</h5><ul><li>Maximum Flow Rate: Aqueous and THF: up to 1 mL/min (Note: Using an inline UV detector may reduce allowable flow rate.)</li><li>Delay Volume: 5.4 mL</li><li>Maximum Inlet-to-Outlet Pressure: 3000 kPa (435 psi)</li><li>Wetted Materials: 316 stainless steel, PTFE, zirconium silicate, Kalrez®, Inconel, 26-1 stainless steel, and nickel</li></ul><blockquote>Note: Due to the location of wetted components, this instrument is primarily recommended for use with organic solvents. High-ionic-strength buffers may cause corrosion.</blockquote><h5>Temperature Control</h5><ul><li>Operating Range: 4 °C to 70 °C</li><li>Stability: Maintains temperature within &lt; 0.005 °C</li><li>Ambient Conditions: 0 °C to 40 °C; 20% to 70% relative humidity</li></ul><h5>Electronics and Connectivity</h5><ul><li>Digital Output: 20-bit resolution at 10 Hz</li><li>Auxiliary I/O:<ul><li>Inputs: Autoinject contact closure, Alarm In, and 2 analog inputs (16-bit, ±10 V)</li><li>Outputs: Autoinject retransmit, Alarm Out, Recycle Out</li></ul></li><li>Communication Interface: Ethernet</li></ul><h5>User Interface</h5><ul><li>Front Panel Display: 7” (178 mm) high-resolution, capacitive multi-touch screen for real-time monitoring, configuration, and diagnostics</li></ul><h5>Instrument Dimensions</h5><ul><li>Size: 60 cm (L) × 36 cm (W) × 17 cm (H)</li></ul><h4>Other Viscometers</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1117">ViscoStar™</a> - A highly sensitive, on-line differential viscometer used in conjunction with SEC-MALS to determine the size and conformation of all types of biopolymers, synthetic polymers and even proteins and peptides.</li><li>The ViscoStar incorporates multiple novel technologies to provide the highest sensitivity, stability and solvent compatibility of any available viscometer for GPC. Its ease-of-use and serviceability make it the perfect companion for Wyatt's DAWN® light scattering and Optilab® refractive index detectors. Temperature-controlled from 4 °C to 70 °C .</li></ul>

Waters/Wyatt Optilab On-line Differential Refractometer

The Waters Optilab is a unique dRI detector for standard HPLC/GPC with 256 times the detection power and 50 times the dynamic range of every other RI detector for chromatography in existence today, making it a valuable addition to any MALS setup.

<h4>Independent of Chromaphores</h4>Independent of chromaphores or fluorophores, differential Refractive Index (dRI) detectors serve as accurate and versatile concentration detectors in all types of solvents. dRI is part of standard instrumentation for a variety of macromolecular characterization techniques including standard chromatography, SEC-MALS, FFF-MALS and CG-MALS.<h4>Unique dRI Detector</h4>The Optilab is a unique dRI detector for standard HPLC/GPC with 256 times the detection power and 50 times the dynamic range of every other RI detector for chromatography in existence today, making it a valuable addition to any MALS setup.<h4>Product Description</h4>Using a combination of cutting-edge semiconductor photodiode technology and proprietary computer algorithms, the Optilab achieves an unprecedented combination of sensitivity and range. These features mean that it addresses both standard chromatographic applications and some challenges unique to light scattering measurements such as high concentrations, determination of sample refractive increments (dn/dc) and solvent refractive index.<h5>Key Benefits</h5><ul><li>Extraordinary dRI measurement range, -0.0047 to +0.0047 RIU (comparable to 25 mg/mL protein in PBS)</li><li>Highly sensitive, ±7.5 x 10 -10 &nbsp;RIU across the entire measurement range</li><li>Measures solvent absolute refractive index, required for MALS calculations</li><li>Measures at the same wavelength as the MALS detector, for maximum accuracy in MALS calculations</li><li>Band broadening &lt; 20 µL preserves SEC resolution</li><li>Temperature range 4 °C to 65 °C for proteins and polymers that require a range of temperatures</li><li>High-resolution, touch-screen front panel displays data graphs and diagnostics, even with the host computer turned off</li></ul><h5>Unparalleled Features</h5>Even though the Optilab offers a dRI measurement range orders of magnitude beyond that of other dRI detectors, unlike other detectors there are no range or gain settings in the Optilab. The full range of instrument detection is always present, and the full sensitivity exists over the entire range.The Optilab can also do something no other on-line refractive index detector can: it can measure the absolute refractive index of a solution. In addition, it can measure the dn/dc of a solvent at the same wavelength of light as the light scattering instrument. And just to make sure it can't be matched, you can replace the light source in the Optilab for other wavelengths (e.g., 690, 633, 488, etc.) in just minutes!The Optilab can go below ambient temperatures as easily as above ambient. No hassle temperature control can be programmed from 4 °C to 65 °C. Compatible with all HPLC systems.<h4>Specifications</h4><h5>Measurement Capabilities – Differential Refractive Index</h5>Standard Optilab Configuration<ul><li>Measurement Range: –0.0047 to +0.0047 RIU</li><li>Peak-to-Peak Noise: ±7.5 × 10⁻¹⁰ RIU (Measured per ASTM-E1303-95 at 25 °C)</li></ul>High Concentration (HC) Option<ul><li>Measurement Range: –0.0026 to +0.034 RIU</li><li>Peak-to-Peak Noise: ±1.5 × 10⁻⁹ RIU (Optimized for higher concentration samples)</li><li>Response Time: User-selectable from 0.1 to 5 seconds</li><li>Absolute Refractive Index Measurement Range: 1.2 to 1.8 RIU</li><li>Absolute RI Sensitivity: ±0.002 RIU</li></ul>Fluidics and Flow Properties<ul><li>Band Broadening: &lt;12 µL</li><li>Fill Volume (Inlet Tubing + Flow Cell): 51.4 µL</li><li>Outlet Tubing Volume (0.030" ID): 370 µL</li></ul>Pressure Ratings<ul><li>Inlet Back Pressure (0.5 mL/min H₂O @ 20 °C): &lt;22 psi (1.5 bar)</li><li>Max Outlet Back Pressure: 30 psi (2 bar)</li></ul>Temperature Control<ul><li>Sample Temperature Control Range: 4 °C to 65 °C</li><li>Regulation Stability: ±0.005 °C</li></ul>Light Source Options<ul><li>Standard: 660 nm</li><li>HC Model (Optional): 488 nm, 785 nm, or 940 nm</li></ul>Safety Features<ul><li>Built-in vapor and liquid leak sensors for enhanced lab safety</li></ul>Electronics and Connectivity<ul><li>Digital Output: 22+ bit resolution @ 10 Hz</li><li>Analog Output: ±10 V or ±1 V, 18-bit resolution</li><li>Computer Interface: Ethernet</li></ul>Auxiliary I/O Ports<ul><li>Inputs:<ul><li>Analog In (16-bit, ±10 V A/D)</li><li>Zero dRI</li><li>Purge</li><li>Recycle In</li><li>Autoinject In</li><li>Alarm In</li></ul></li><li>Outputs:<ul><li>Autoinject Retransmit</li><li>Alarm Out</li><li>Recycle Out (controls Orbit™ valve switching)</li></ul></li></ul>User Interface<ul><li>Front Panel Display: 7” (178 mm) high-resolution multi-touch screen for viewing signals, diagnostics, and adjusting instrument settings</li></ul>Instrument Dimensions<ul><li>Size: 58 cm (L) × 36 cm (W) × 18 cm (H)</li></ul><h4>Other Refractive Index Detectors</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1269">microOptilab™</a> - The first RI detector specifically designed for use with all UHPLC systems.</li></ul>

Waters/Wyatt microOptilab On-line Differential Refractometer

The Waters microOptilab brings the universal detection capabilities, unsurpassed concentration range, and superb sensitivity and linearity

<h4>Independent of Chromaphores</h4>Independent of chromaphores or fluorophores, differential Refractive Index (dRI) detectors measure concentrations of all types of samples in almost all solvents. The microOptilab brings the universal detection capabilities, unsurpassed concentration range, and superb sensitivity and linearity – familiar from the Optilab™ – to the domain of UHPLC.<h4>SEC-MALS with UHPLC</h4>Like standard SEC, UHPLC-SEC analysis relying on column calibration with molecular standards is unreliable when the standards do not accurately reflect your samples in terms of conformation, non-ideal (e.g., hydrophobic) column interactions or reversible association. SEC-MALS employs a microDAWN™ MALS detector downstream of the SEC column and UV detector, to determine molar mass / molecular weight distributions of macromolecules independently of column calibration.Refractive index detection is an important component of any SEC-MALS system, and necessary for analyzing conjugated proteins or polymers devoid of chromaphores. The microOptilab connects with the microDAWN MALS detector for a complete UHP-SEC-MALS setup that transfers the many benefits of SEC-MALS analysis to the realm of UHPLC.<h5>Key benefits</h5><ul><li>Very low band broadening, &lt; 4 µL, to maintain the resolution of very narrow UHPLC peaks</li><li>Extraordinary dRI measurement range, -4.7 x 10 -3 &nbsp;to +4.7 x 10 -3 &nbsp;RIU (comparable to 25 mg/mL protein in PBS)</li><li>Highly sensitive, ± 1.5 x 10 -9 &nbsp;RIU across the entire measurement range</li><li>Measures solvent refractive index, require for MALS calculations</li><li>Measures at the same wavelength as the MALS detector, for maximum accuracy in MALS calculations</li><li>Temperature range 4 °C to 65 °C for proteins and polymers that require a range of temperatures</li><li>High-resolution, touch-screen front panel displays data graphs and instrument diagnostics, even with the host computer turned off</li></ul><h5>Unparalleled features</h5><ul><li>Considering the extremely small peak volumes of UHPLC, band broadening in the microOptilab is kept to the absolute minimum, at less than 4 µL, as compared to 20 - 40 µL or more for standard RI detectors. As a result, the superior resolution from UHPLC columns and instruments will not be compromised with the microOptilab RI detector.</li><li>Even though the microOptilab offers a dRI measurement range orders of magnitude beyond that of other UHPLC dRI detectors, unlike other detectors there are no range or gain settings in the microOptilab. The full range of instrument detection is always present, and the full sensitivity exists over the entire range. The small flow cell and proprietary temperature regulation enable stable RI baselines and signals which further enhance the detector's sensitivity.</li><li>Unlike all other dRI detectors, the microOptilab also measures absolute refractive index in order to determine solvent RI, necessary in light scattering calculations and useful in assessing the accuracy of mixing of solvent gradients.</li><li>The microOptilab can be operated below ambient temperatures as easily as above ambient. No hassle temperature control can be programmed down to 4 °C or as high as 65 °C.</li><li>The microOptilab is compatible with all UHPLC systems.</li></ul><h4>Specifications</h4><h5>Measurement Capabilities – Differential Refractive Index</h5><ul><li>Differential RI Measurement Range: –0.0047 to +0.0047 RIU</li><li>Peak-to-Peak Noise: ±1.5 × 10⁻⁹ RIU (Measured per ASTM-E1303-95 at 25 °C with a 0.5 sec collection interval)</li><li>Response Time: User-selectable from 0.04 to 5 seconds</li><li>Absolute Refractive Index Range: 1.2 to 1.8 RIU</li><li>Absolute RI Sensitivity: ±0.002 RIU</li></ul>Fluidics and Flow Properties<ul><li>Band Broadening: &lt;4 µL (at 0.3 mL/min)</li><li>Fill Volume (Inlet Tubing + Flow Cell): 13.7 µL</li><li>Outlet Tubing Volume (0.030” ID): 228 µL</li></ul>Pressure Ratings<ul><li>Inlet Back Pressure (0.5 mL/min H₂O @ 20 °C): &lt;320 psi (22 bar)</li><li>Maximum Permissible Outlet Pressure: 30 psi (2 bar)</li></ul>Temperature Control<ul><li>Control Range: 4 °C to 65 °C</li><li>Stability: ±0.005 °C for precise thermal regulation</li></ul>Optical Source and Safety<ul><li>Light Source: 660 nm wavelength</li><li>Safety Sensors: Integrated vapor and liquid leak detection</li></ul>Electronics and Connectivity<ul><li>Digital Output Rate: 25 Hz</li><li>Analog Output: ±10 V or ±1 V, 18-bit resolution</li><li>Computer Interface: Ethernet for seamless data connectivity</li></ul>Auxiliary I/O Ports<ul><li>Inputs:<ul><li>Analog In (16-bit, ±10 V A/D)</li><li>Zero dRI</li><li>Purge</li><li>Recycle In</li><li>Autoinject In</li><li>Alarm In</li></ul></li><li>Outputs:<ul><li>Autoinject Retransmit</li><li>Alarm Out</li><li>Recycle Out (Orbit™ valve switching)</li></ul></li></ul>User Interface<ul><li>Display: 7” (178 mm) high-resolution multi-touch screen for viewing live signals, diagnostics, and configuring instrument settings</li></ul>Instrument Dimensions<ul><li>Size: 58 cm (L) × 36 cm (W) × 18 cm (H)</li></ul><h4>Other Refractive Index Detectors</h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1268">Optilab™</a> - A unique on-line differential refractometer for measuring concentration of any macromolecule, regardless of chromophores. Temperature controlled from 4 °C to 65 °C. The high-concentration option accommodates protein concentration up to 180 mg/mL.</li></ul>

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