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

Webinars LabRulezLCMS Week 08/2026

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

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

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

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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><strong>Premier MALS</strong></h5><p>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.</p><h5><strong>Separation First</strong></h5><p>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.</p><h5><strong>Supported by ASTRA ™ &nbsp;Software</strong></h5><p>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.</p><p><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"></p><h4><strong>Product description</strong></h4><p>The DAWN and its companion <strong>Optilab ™ &nbsp;dRI detector</strong> are the established benchmarks for MALS analysis, cited in thousands of peer-reviewed publications. Multi-angle light scattering detection is indispensable for use with <strong>GPC</strong> and <strong>HPLC-SEC </strong>in order to obtain reliable molecular mass distributions and information on molecular conformation, branching ratio, fragments and aggregates.</p><p><strong>SEC-MALS</strong> with a <strong>DAWN</strong> and <strong>Optilab</strong> characterizes conformation and branching of synthetic and natural <strong>polymers larger than 10 nm</strong> in rms radius R g . The addition of a <strong>ViscoStar ™&nbsp;</strong> 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.</p><p>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 <strong>WyattQELS ™ &nbsp;DLS module</strong> for size determination, protein conformation may be analyzed.</p><ul><li><i>M<sub>w</sub></i> &nbsp;from 200 Da to 1000 MDa</li><li><strong>Sensitivity:</strong> 10 ng/mL 100 kDa polystyrene in THF, 0.4 µg/mL BSA (66.4 kDa) in PBS</li><li><i>R<sub>g</sub></i> &nbsp;from 10 to 500 nm, up to 1000 nm with shape-specific models</li><li>Ultra-stable, high-power laser</li></ul><p><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"></p><p>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.</p><p>In conjunction with a <strong>Calypso ™ &nbsp;CG-MALS system</strong>, 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.</p><h5><strong>Ultrasonic Cleaning Included</strong></h5><p>Each DAWN instrument includes an embedded <strong>COMET ™ &nbsp;ultrasonic transducer</strong> that cleans the flow cell automatically by agitating the fluid and loosening particles from the glass surfaces.</p><h5><strong>Temperature-Controlled Models</strong></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><strong>Specifications</strong></h4><h5><strong>Measurement Capabilities</strong></h5><ul><li><strong>Molar Mass Range:</strong> From 200 Da to 1 GDa, depending on dn/dc, sample concentration, and chromatography conditions.</li><li><strong>Molecular Size (Radius of Gyration, Rg):</strong> Approximately 10 nm to 500 nm, extendable to 1000 nm with shape-specific models.</li><li><strong>Hydrodynamic Radius (Rh):</strong><ul><li><strong>Flow mode:</strong> 0.5 nm to 300 nm (depending on configuration and flow rate).</li><li><strong>Batch mode:</strong> 0.5 nm to 1 µm (requires WyattQELS™ DLS module or DynaPro™ NanoStar™ with fiber optic connection).</li></ul></li><li><strong>Sensitivity:</strong> 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><strong>Fluidics and Compatibility</strong></h5><ul><li><strong>Mobile Phase:</strong> Compatible with both aqueous and organic solvents.</li><li><strong>Wetted Materials:</strong> 316 stainless steel, fused silica or F2 glass, and Kalrez.</li></ul><h5><strong>Optical System and Detectors</strong></h5><ul><li><strong>MALS Detectors:</strong> 18 photodiodes with high gain and wide dynamic range for multi-angle light scattering.</li><li><strong>Auxiliary Detectors:</strong><ul><li>Laser monitor for stabilization</li><li>Forward transmission monitor to improve data quality and correct for sample absorption</li></ul></li><li><strong>Dynamic Range:</strong> 3,300,000:1</li><li><strong>Optional DLS Detection:</strong><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><strong>Laser Specifications</strong></h5><ul><li><strong>Wavelength:</strong> Standard 658 nm ± 4 nm; optional 785 nm for fluorescent samples</li><li><strong>Power Control:</strong> Programmable from 10% to 100%</li></ul><h5><strong>Flow Cell Options</strong></h5><ul><li><strong>Fused Silica:</strong> Ideal for solvents with refractive index &lt; 1.50</li><li><strong>F2 Glass:</strong> Recommended for solvents with refractive index &gt; 1.50</li></ul><h5><strong>Temperature Control Options</strong></h5><ul><li><strong>Ambient operation</strong></li><li><strong>Heated/Cooled (HC):</strong> -15 °C to +150 °C</li><li><strong>Ultra-High Temperature (UHT):</strong> Ambient to +210 °C</li></ul><h5><strong>Electronics and Connectivity</strong></h5><ul><li><strong>Analog Inputs:</strong> 4 differential inputs, 24-bit resolution, range -10 V to +10 V</li><li><strong>Analog Outputs:</strong> 2 outputs from selectable measurement channels, -10 V to +10 V</li><li><strong>I/O Options:</strong> Alarm in/out, auto-inject control, and Orbit™ valve integration</li><li><strong>Computer Interface:</strong> Ethernet</li><li><strong>Display:</strong> 10.1” high-resolution capacitive touchscreen with multi-touch controls</li></ul><h5><strong>Instrument Dimensions</strong></h5><ul><li><strong>Size:</strong> 58 cm (L) x 36 cm (W) x 26 cm (H)</li></ul><h4><strong>Other MALS Instruments</strong></h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1115"><strong>miniDAWN™</strong></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"><strong>microDAWN™</strong></a><strong>&nbsp;</strong> - 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><strong>ultraDAWN™</strong> &nbsp;- Measures multi-angle light scattering and reports the results – weight-average molecular weight <i>M<sub>w</sub></i> &nbsp;and rms radius <i>R<sub>g</sub></i> &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><strong>Overview</strong></h4><h5><strong>Molar Mass</strong></h5><p>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.</p><h5><strong>Superb Sensitivity</strong></h5><p>The miniDAWN not only offers superb sensitivity—it further enhances productivity thanks to greatly enhanced field serviceability and easy data analysis with <strong>One-Click </strong><i><strong>M<sub>w</sub></strong></i><strong>™</strong> .</p><h5><strong>Compatible with ASTRA™&nbsp;</strong></h5><p>The miniDAWN is accompanied by <strong>ASTRA,</strong> 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.</p><h4><strong>Product Description</strong></h4><h5><strong>Molar mass, absolutely</strong></h5><p>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.</p><h5><strong>Characterize:</strong></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><strong>Measurement Range:</strong></h5><ul><li>MW from 200 Da to 10 MDa</li><li><i>r<sub>g</sub></i> &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><p><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"></p><p>The miniDAWN's performance is exceeded only by the <strong>DAWN™</strong> which covers a wider range of size and molecular weight, with even better sensitivity and additional optional modules.</p><h5><strong>Ultrasonic Cleaning Included</strong></h5><p>Each miniDAWN includes an embedded <strong>COMET™ ultrasonic transducer</strong> that cleans the flow cell automatically by agitating the fluid and loosening particles from the glass surfaces.</p><h5><strong>Modularity = Productivity</strong></h5><p>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.</p><p>The miniDAWN is also field-upgradeable: the embedded <strong>WyattQELS™ DLS Module </strong>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.</p><h5><strong>Not just SEC-MALS...</strong></h5><p>Wyatt's miniDAWN may be used in batch (off-line) mode or in conjunction with a <strong>Calypso™ CG-MALS system</strong> for characterization of average solution properties as well as macromolecular interaction properties including protein-protein binding affinity and complex stoichiometry.</p><h5><strong>Simplicity personified</strong></h5><p>With miniDAWN and <strong>ASTRA™</strong>, 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.</p><p>The miniDAWN's System Ready monitor will even let you know when the system is fully equilibrated with low baseline noise, ready to run.</p><h4><strong>Specifications</strong></h4><h5><strong>Measurement Capabilities</strong></h5><ul><li><strong>Molar Mass Range:</strong><br>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><strong>Molecular Size (Radius of Gyration, Rg):</strong><br>Approximately 10 nm to 50 nm, extendable up to 150 nm with shape-specific modeling.</li><li><strong>Hydrodynamic Radius (Rh):</strong><ul><li><strong>Flow mode:</strong> 0.5 nm to 50 nm (optimal at flow rates ≤ 0.3 mL/min)</li><li><strong>Batch mode:</strong> 0.5 nm to 1 µm (requires WyattQELS™ module or DynaPro™ NanoStar™ with fiber optic connection)</li></ul></li><li><strong>Sensitivity:</strong><br>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><strong>Fluidics and Compatibility</strong></h5><ul><li><strong>Mobile Phase Compatibility:</strong><br>Compatible with both aqueous and organic solvents.</li><li><strong>Wetted Materials:</strong><br>316 stainless steel, fused silica, and Kalrez.</li></ul><h5><strong>Optical System and Detectors</strong></h5><ul><li><strong>MALS Detectors:</strong><br>Three high-gain, high dynamic range photodiodes at fixed angles.</li><li><strong>Auxiliary Detectors:</strong><ul><li>Laser monitor for stability control</li><li>Forward transmission monitor for absorbing samples and data quality evaluation</li></ul></li><li><strong>Dynamic Range:</strong><br>3,300,000:1</li><li><strong>Optional DLS Detection:</strong><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><strong>Laser Specifications</strong></h5><ul><li><strong>Wavelength:</strong><br>658 nm ± 4 nm</li><li><strong>Power Control:</strong><br>Programmable from 10% to 100%</li></ul><h5><strong>Temperature Control</strong></h5><ul><li><strong>Sample Temperature:</strong> Ambient</li></ul><h5><strong>Electronics and Connectivity</strong></h5><ul><li><strong>Analog Inputs:</strong><br>2 differential inputs, 24-bit resolution, ±10 V range</li><li><strong>Analog Outputs:</strong><br>1 output from a selectable measurement channel, ±10 V range</li><li><strong>I/O Ports:</strong><br>Alarm in/out, auto-inject control, Orbit™ recycle valve support</li><li><strong>Computer Interface:</strong><br>Ethernet</li><li><strong>Data Rate:</strong><br>Up to 36.6 Hz</li></ul><h5><strong>User Interface and Display</strong></h5><ul><li><strong>Front Panel:</strong><br>7” (178 mm) high-resolution multi-touch display for real-time signal viewing, diagnostics, and settings</li></ul><h5><strong>Instrument Dimensions</strong></h5><ul><li><strong>Size:</strong> 58 cm (L) x 36 cm (W) x 18 cm (H)</li></ul><h4><strong>Other MALS Instruments</strong></h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1114"><strong>DAWN™</strong></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"><strong>microDAWN™</strong></a><strong> </strong>- 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><strong>ultraDAWN™</strong> - Measures multi-angle light scattering and reports the results – weight-average molecular weight <i>M<sub>w</sub></i> &nbsp;and rms radius <i>R<sub>g</sub></i> &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><strong>Overview</strong></h4><h5><strong>UHPLC-SEC System</strong></h5><p>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 <strong>miniDAWN™</strong>.</p><h4><strong>Product Description</strong></h4><p>The <strong>microDAWN MALS detector</strong> performs absolute characterization of macromolecules eluting from UHPLC, determining molar mass and size <i>independently </i>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 <strong>miniDAWN™</strong>, a workhorse MALS instrument used in hundreds of labs around the world for characterizing proteins and other molecules smaller than 50 nm in radius.</p><p>Distinctly from the miniDAWN, the <strong>microDAWN</strong> is uniquely <strong>suitable for use in conjunction with UHPLC Size Exclusion Chromatography (SEC-MALS)</strong> 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.</p><p><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"></p><ul><li><i>M<sub>w</sub>&nbsp;</i> from 200 Da to 10 MDa</li><li><strong>Sensitivity:</strong> 1.0 µg/mL BSA (66.4 kDa) in PBS; 50 ng/mL 100 kDa polystyrene in THF.</li><li><i>R<sub>g</sub></i> &nbsp;from 10 to 50 nm</li><li>Ultra-stable laser</li></ul><p>The microDAWN and its companion<strong> microOptilab™ Refractive Index Detector</strong> interface to most standard UHPLC systems. As these detectors are based on the advanced technology of Wyatt's miniDAWN and <strong>Optilab™</strong>, respectively, users may be confident in the underlying capabilities cited in <strong>thousands of peer-reviewed publications</strong>.</p><h5><strong>Ultrasonic Cleaning Included</strong></h5><p>Each microDAWN includes a <strong>COMET™ ultrasonic transducer</strong> that cleans MALS flow cells automatically by agitating the fluid and loosening particles from the glass surfaces.</p><h4><strong>Specifications</strong></h4><h5><strong>Measurement Capabilities</strong></h5><ul><li><strong>Molar Mass Range:</strong><br>From 200 Da to 10 MDa for proteins; up to 1 MDa for linear polymers<br><i>(Typical, depending on dn/dc, sample concentration, and chromatography conditions)</i></li><li><strong>Molecular or Particle Size (Radius of Gyration, Rg):</strong><br>10 nm to 50 nm, extendable up to 150 nm with shape-specific modeling</li><li><strong>Hydrodynamic Radius (Rh):</strong><ul><li><strong>Flow mode:</strong> 0.5 nm to 30 nm</li><li><strong>Batch mode:</strong> 0.5 nm to 1 µm<br><i>(Requires WyattQELS™ DLS module or DynaPro™ NanoStar™ with fiber optic connection)</i></li></ul></li><li><strong>Sensitivity:</strong><br>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><strong>Optical System and Detectors</strong></h5><ul><li><strong>MALS Detectors:</strong><br>Three high-gain photodiodes with broad dynamic range for multi-angle light scattering</li><li><strong>Dynamic Range:</strong><br>3,300,000:1</li><li><strong>Auxiliary Detectors:</strong><ul><li>Laser monitor for stabilization feedback</li><li>Forward transmission monitor for absorbing samples and data quality assessment</li></ul></li><li><strong>Optional DLS Detection:</strong><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><strong>Laser Specifications</strong></h5><ul><li><strong>Wavelength:</strong><br>658 nm ± 4 nm</li><li><strong>Power Control:</strong><br>Programmable from 10% to 100%</li></ul><h5><strong>Sample Temperature and Flow Characteristics</strong></h5><ul><li><strong>Sample Temperature:</strong> Ambient</li><li><strong>Interdetector Band Broadening:</strong><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><strong>Material Compatibility</strong></h5><ul><li><strong>Wetted Materials:</strong><br>316 stainless steel, fused silica, PEEK, PTFE, and MP35N (iron-free alloy)</li></ul><h5><strong>Electronics and Connectivity</strong></h5><ul><li><strong>Analog Inputs:</strong><br>2 differential inputs, 24-bit resolution, ±10 V input range</li><li><strong>Analog Outputs:</strong><br>1 output from a user-selectable measurement channel, ±10 V range</li><li><strong>I/O Ports:</strong><br>Alarm in/out, auto-inject control, Orbit™ valve integration</li><li><strong>Computer Interface:</strong><br>Ethernet</li><li><strong>Data Transmission Rate:</strong><br>Up to 73 Hz</li></ul><h5><strong>User Interface</strong></h5><ul><li><strong>Display:</strong><br>7” (178 mm) high-resolution multi-touch screen for signal monitoring, instrument settings, and diagnostics</li></ul><h5><strong>Instrument Dimensions</strong></h5><ul><li><strong>Size:</strong> 58 cm (L) x 36 cm (W) x 18 cm (H)</li></ul><h4><strong>Other MALS Instruments</strong></h4><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1114"><strong>DAWN™</strong></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"><strong>miniDAWN™</strong></a><strong> -</strong> 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><strong>ultraDAWN™</strong> - Measures multi-angle light scattering and reports the results – weight-average molecular weight <i>M<sub>w</sub></i> &nbsp;and rms radius <i>R<sub>g</sub></i> &nbsp;– in real time.</li></ul>

Products from category MALS detectors from Waters - page 1

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