<div><p><strong>Purifying the target protein is crucial for investigating its specific properties and interactions with biomolecules like DNA, RNA, and other proteins. A range of purification strategies is available, and the optimal approach depends on factors such as the required scale, throughput, and downstream application. In many cases, the process must be fine-tuned through empirical optimization to achieve the desired purity and yield.</strong></p></div><div><div><div><div><h3><strong>What is Protein Purification?</strong></h3><p>Protein purification is a critical process in biotechnology and life sciences, aimed at isolating a specific protein from complex biological mixtures such as cell lysates or tissue extracts. The goal is to obtain a highly purified protein sample, free from contaminants like other proteins, nucleic acids, and lipids, to enable accurate analysis of its structure, function, and interactions.</p><p>This process is especially vital in biotechnological areas inside immunology and microbiology. In <strong>immunology</strong>, it underpins the production of vaccines, therapeutic antibodies, and diagnostic assays by enabling the isolation of key immune proteins and antibodies. It also supports the investigation of cell signaling and immune response mechanisms. In <strong>microbiology</strong>, purified proteins are essential for studying pathogens, identifying disease-related antigens, and driving drug discovery efforts. Ultimately, protein purification is fundamental to the development of targeted vaccines, innovative diagnostics, and effective therapeutic strategies.</p></div></div></div></div><div><div><div><div><h3><strong>Types of Protein Purification Methods</strong></h3></div></div></div></div><div><p>There are several types of protein purification methods, each chosen based on the protein’s characteristics such as size, charge, solubility, and binding affinity. Below are some commonly used methods:</p></div><div><div><div><div><h4><strong>Non-Chromatographic Approaches</strong></h4></div></div><div><p>Non-chromatographic approaches use simpler physicochemical principles—such as solubility, molecular size, or diffusional properties—to separate and purify proteins. These techniques are often employed as initial purification or concentration steps before further refinement.</p><h5><strong>Precipitation Techniques</strong></h5><p>Protein precipitation is a widely used approach in purification workflows, typically relying on one of three main methods:</p><ul><li><strong>Organic solvent precipitation</strong> involves adding solvents like ethanol or acetone to lower the solution's dielectric constant. This promotes protein–protein interactions, reducing solubility and leading to aggregation and precipitation.</li><li><strong>Isoelectric point precipitation </strong>exploits the pH at which a protein carries no net charge. At this point, solubility is minimized, causing the protein to precipitate from solution.</li><li><strong>Nonionic polymer precipitation</strong> uses polymers such as dextran, polyethylene glycol (PEG), or NPEP to alter the solution’s physical properties. These agents create crowding effects that promote protein aggregation without directly binding to the proteins.</li></ul><h5><strong>Dialysis</strong></h5><p>Dialysis involves placing a protein solution inside a semi-permeable membrane that allows water and ions to pass while the protein remains inside, facilitating buffer exchange.This method is commonly used during protein expression and purification workflows for buffer exchange, desalting, and removal of unwanted small molecules such as imidazole, urea, or ammonium sulfate. The process helps maintain protein stability and activity by gradually equilibrating the sample with the desired buffer conditions.</p><h5><strong>Immunocapture (Magnetic Bead-Based Purification</strong></h5><p>Immunocapture uses antibodies immobilized on solid supports like magnetic beads to selectively bind and isolate a target protein. This method is highly specific and particularly useful for low-abundance targets or small-scale prep, such as:</p><ul><li>Pulling down proteins from complex mixtures</li><li>Capturing tagged recombinant proteins (e.g., FLAG, HA, or His tags)</li><li>Enrichment before western blotting, MS, or ELISA</li></ul><p>Magnetic beads offer speed, ease of use, and minimal sample loss, making them ideal for lab-scale workflows.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/products/biozenspe-sample-preparation-products/biozen-magbeads">Biozen MagBeads</a> provide a fast and efficient method for purifying, isolating, and cleaning up monoclonal antibodies (mAbs), proteins, and peptides. These paramagnetic beads feature a streptavidin-coated surface, enabling high-affinity binding in immuno-based workflows. Compared to traditional sample preparation techniques, magnetic bead-based immunocapture offers greater speed and consistency by delivering high binding capacity with uniform particle size, ensuring accurate and reproducible results in significantly less time.</p><h5><strong>Centrifugation</strong></h5><p>Centrifugation of crude protein mixtures is an essential step in the investigation of protein purification and aggregation. Outlined below are the various types of centrifugations employed in protein purification.</p><p><strong>Preparative Ultracentrifugation</strong><br>Ultracentrifugation is an effective method of purifying proteins from aggregates based on their size, shape and density. Centrifugation, widely recognized as a robust and versatile method, is commonly used to separate complex mixtures of cellular components. Ultracentrifuges separate small particles by spinning at high speeds, utilizing centrifugal force based on size and density.</p><p><strong>Differential Centrifugation</strong><br>Differential centrifugation operates by separating components based on differences in size and density, using varying speeds of centrifugation to achieve this. Its resolving power ranges from low to medium. A key advantage of this technique is its convenience for processing multiple samples simultaneously, making it effective for purifying crude samples. Additionally, it preserves cell viability and maintains the natural distribution of hematopoietic cell populations.</p><p><strong>Rate-zonal Gradient Centrifugation</strong><br>This technique separates components based on their sedimentation rate within a medium that contains a density gradient. It offers medium resolving power and is particularly effective for separating multiple components in complex mixtures with high precision. It is also considered a cost-effective and widely used technique in molecular biology and biochemistry.</p><p><strong>Isopycnic Centrifugation (Equilibrium Centrifugation)</strong><br>Isopycnic centrifugation is an advanced protein purification method that relies on the principle of separating particles according to their intrinsic buoyant density, irrespective of their size or morphology. During the process, proteins migrate through a density gradient until they equilibrate at a position where their density matches that of the surrounding medium, resulting in precise separation without further sedimentation.</p></div></div></div><div><div><div><div><h4><strong>Chromatographic Approaches</strong></h4><p>Chromatography is a common method of protein purification and is based on the separation of molecules in a mixture as they move through a stationary phase and a mobile phase. Outlined below are the various types of chromatography employed in protein purification.</p><h5><strong>Ion Exchange Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-ion-exchange">Ion exchange chromatography</a> relies on the interaction between a charged stationary phase and oppositely charged analytes, with cation exchange chromatography attracting positively charged molecules to a negatively charged stationary phase. Successful application of this technique requires careful selection of the appropriate ion exchange column, buffer pH, and salt concentration. This approach is often used in the biopharmaceutical industries as mAb polishing steps, viral clearance and charge variant analyses as part of the product quality control.</p><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/">Phenomenex</a> offers a range of protein purification columns. Their ion exchange chromatography solutions include:&nbsp;</p><ul><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1526"><strong>Luna SCX </strong></a>for strong selectivity of positively charged compounds, such as peptides</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1540"><strong>Biozen WCX</strong></a> for efficient separation of proteins such as monoclonal antibodies charged variants</li><li><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/part/00g-3151-e0">PhenoSphere SAX</a>, a strong anion-exchanger with fully porous 80Å particles, particularly useful for small molecules such as nucleotides</li></ul><h5><strong>Size Exclusion Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-sec">Size exclusion chromatography (SEC)</a> separates molecules based on their size, with larger analytes eluting first due to their exclusion from the pores in the column packing material, while smaller molecules are able to enter the pores, facing a longer travelling path, and hence, eluting later. This method can be categorized into aqueous SEC (gel filtration chromatography, GFC) for analyzing biomolecules such as proteins and antibodies. This type of chromatography is widely used as an analytical tool for quality control in the biopharmaceutical industry and can also be an approach of choice for polishing steps.</p><p>Phenomenex offers a range of <strong>Biozen columns for SEC</strong> separations. In the case of mAbs, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1534"><strong>Biozen dSEC-2</strong></a> and<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1537"><strong> Biozen dSEC-7 </strong></a>columns are the top choices for monoclonal antibody (mAb) analysis, delivering high-resolution separation of monomers, aggregates, and fragments formed during mAb manufacturing, processing, or storage. The dSEC-7 column, featuring a larger pore size and optimized particle design, extends the dynamic range to accommodate larger biomolecules and complex biotherapeutics.</p><p>For more general applications, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1533"><strong>Biozen SEC-2</strong></a><strong> </strong>and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1532"><strong>Biozen SEC-3</strong></a> phases cover different MW ranges for high-efficiency separation of biomolecules (e.g., proteins and antibodies). Additionally, the BioSep and Yarra lines become top choices when looking for preparative scale columns.</p><h5><strong>Reversed-Phase Chromatography</strong></h5><p><a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/hplc-reversed-phase">Reversed-phase chromatography</a>, the most common mode in high-performance liquid chromatography/ ultra-high-performance liquid chromatography (HPLC/UHPLC), separates compounds based on hydrophobic and van der Waals interactions using alkyl (C18, C8, C4) stationary phases or other hydrophobic polymers. For large biomolecules such as proteins and peptides, <a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/resources/blog/wider-pore-biozen-column">wide-pore</a> (typically 300 Å) C4, C8 and C18 columns are ideal, as the larger pore size allows better accessibility of the protein molecules to the stationary phase surface, improving mass transfer and peak shape during separation.</p><p>The Biozen line from Phenomenex offers a wide range of HPLC/UHPLC columns for the analysis of biomolecules.These include phases optimized for high-resolution analysis of intact proteins (Native-RP, Widepore C4, Intact XB-C8) and peptides (Peptide PS-C18, Peptide XB-C18 and Peptide Polar-C18). Kinetex could also be an option when looking for more selectivities for the analysis of peptides and small proteins. Additionally, when aiming to preparative scale processes, several of these media are also available in Phenomenex Axia formats to easily up-scale your separations.</p><h5><strong>Hydroxyapatite Chromatography</strong></h5><p>Hydroxyapatite chromatography (HAC) is a sophisticated mixed-mode chromatographic technique that exploits the unique properties of hydroxyapatite (Ca10(PO4)6(OH)2), utilizing both cation-exchange interactions via its phosphate groups and metal affinity through its calcium sites to achieve highly selective protein separations.</p><p>Renowned for its efficacy in resolving complex biomolecular separations, HAC excels in tasks like aggregate removal from monoclonal antibodies, surpassing the capabilities of traditional single-mode chromatographic methods such as ion-exchange or hydrophobic interaction chromatography.</p><h5><strong>Hydrophobic Interaction Chromatography</strong></h5><p>Hydrophobic interaction chromatography (HIC) is a method of protein purification that separates molecules based on their hydrophobicity, using high-salt buffers to promote protein-ligand interactions while maintaining the protein's biological activity. The process involves gradually reducing the salt concentration to elute proteins in order to increase hydrophobicity, making it effective for purifying target molecules and removing impurities or aggregates, making it a valuable approach for intermediate and polishing steps during purification processes.</p><h5><strong>Affinity Chromatography</strong></h5><p>Affinity chromatography is a powerful and highly selective technique used to purify biomolecules based on specific, reversible interactions between a target molecule and an immobilized ligand. In many cases, recombinant proteins are engineered with affinity tags—such as His-tags or GST-tags—that facilitate binding to complementary ligands on the chromatography matrix.</p><p>This method offers the advantage of achieving several thousand-fold purifications in a single step while preserving the biological activity of the protein. It is widely employed for purifying enzymes, antibodies, and antigens, using a variety of ligands including specific antibodies, enzymes, and multifunctional compounds like concanavalin A and triazine dyes.</p></div></div></div></div>

Exploring Protein Purification Methods: Essential Techniques for Accurate Results

<h3><span><strong>A Practical Guide to Getting the Most from Syringe Filters: Tips, Tricks, and Common Pitfalls</strong></span></h3><p><span><strong>Syringe filters play a crucial role in chromatography and many other laboratory applications by removing particulate matter before analysis. Proper sample filtration helps protect analytical instruments, extends column lifetime, and improves data quality. However, selecting an unsuitable filter—or using one incorrectly—can introduce contamination, reduce filtration efficiency, or even compromise analytical results. The following recommendations will help you avoid common mistakes and ensure reliable filtration every time.</strong></span></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_3_150e8c1c2b.webp" alt="KNAUER: Avoiding Common Syringe Filter Mistakes" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_3_150e8c1c2b.webp 133w," sizes="100vw" width="1276" height="1496"></p><h4><span><strong>1. Improper Filter Handling</strong></span></h4><p><span>Using excessive force during filtration or attempting to reuse disposable syringe filters can damage the membrane and increase the risk of sample contamination.</span></p><ul><li><span><strong>Solution:</strong> Apply slow, even pressure throughout the filtration process and always dispose of single-use filters after one use. If the flow rate decreases noticeably, replace the filter instead of applying additional force.</span></li></ul><h4><span><strong>2. Selecting an Inappropriate Pore Size</strong></span></h4><p><span>Using the wrong pore size may either fail to remove unwanted particles or cause the membrane to clog prematurely, reducing filtration efficiency.</span></p><ul><li><span><strong>Solution:</strong> A 0.45 µm membrane is generally suitable for routine particulate removal, while a 0.22 µm membrane is recommended for finer filtration and bacterial removal. Samples with higher viscosity may require a pre-filter to prevent rapid clogging. It is also important to consider the intended analytical technique. For example, 0.22 µm filters are typically preferred for UHPLC and LC-MS applications, whereas 0.45 µm filters are often sufficient for conventional HPLC analyses.</span></li></ul><h4><span><strong>3. Choosing the Wrong Membrane Material</strong></span></h4><p><span>Different membrane materials exhibit different chemical resistance. Using an incompatible membrane may lead to degradation of the filter, sample contamination, or complete filtration failure.</span></p><ul><li><span><strong>Solution:</strong> Always verify solvent compatibility before filtration. PTFE membranes are an excellent choice for organic solvents, while PES and nylon membranes are better suited to aqueous samples. If compatibility is uncertain, perform a small-scale trial before filtering valuable samples.</span></li><li><span><strong>Pro Tip:</strong> For additional guidance, see our blog article <strong>"How to Choose the Right Membrane for your Syringe Filter"</strong>, which provides a detailed comparison of membrane materials and their recommended applications.</span></li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_2_e47021fb11.jpg" alt="KNAUER Sepapure® Syringe Filters are available with multiple membrane materials, each identified by a dedicated color code for quick and reliable selection." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_2_e47021fb11.jpg 245w," sizes="100vw" width="1580" height="902"></p><h4><span><strong>4. Ignoring Filter Capacity</strong></span></h4><p><span>Using a filter with insufficient capacity can result in rapid membrane blockage, increasing filtration time and reducing laboratory productivity.</span></p><ul><li><span><strong>Solution:</strong> When filtering larger sample volumes, choose high-capacity syringe filters or introduce a pre-filtration step. Never force liquid through a clogged membrane, as doing so may damage the filter and negatively affect sample quality.</span></li></ul><h4><span><strong>5. Overlooking Sample Adsorption</strong></span></h4><p><span>Certain membrane materials may adsorb analytes of interest, leading to lower recoveries and potentially affecting quantitative results.</span></p><ul><li><span><strong>Solution:</strong> For protein samples or other adsorption-sensitive analytes, select membranes with low binding characteristics, such as nylon or glass fiber, whenever appropriate. Performing a small recovery test before routine analysis can help identify potential analyte losses.</span></li></ul><h4><span><strong>6. Failing to Optimize Filtration Performance</strong></span></h4><p><span>Slow filtration is more than just an inconvenience—it often indicates that the filtration conditions are not optimal.</span></p><ul><li><span><strong>Solution:</strong> If filtration becomes unusually slow, investigate possible causes such as membrane clogging, excessive sample viscosity, or an unnecessarily small pore size. Depending on the sample, dilution or sequential filtration using progressively finer filters may significantly improve performance.</span></li></ul><h4><span><strong>Final Thoughts</strong></span></h4><p><span>Selecting the appropriate syringe filter is a straightforward process, but overlooking small details can have a significant impact on analytical performance. Choosing the correct membrane material, pore size, and filtration strategy helps improve laboratory efficiency, protects chromatography systems and columns, and contributes to accurate, reproducible analytical results.</span></p><p><span>With the right syringe filter and proper filtration technique, you can minimize sample preparation problems and maximize confidence in every analysis.</span></p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_4_983a15e289.jpg" alt="KNAUER: Sepapure® Syringe Filter Selection" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_KNAUER_Avoiding_Common_Syringe_Filter_Mistakes_4_983a15e289.jpg 245w," sizes="100vw" width="1160" height="627"></p><p><span><strong>Happy filtering!</strong></span></p>

Avoiding Common Syringe Filter Mistakes

News from LabRulezLCMS Library - Week 27, 2026

Article

Product

Application

Academy

Poster

Everything from the world of analytical chemistry in one place. We connect people in solving their problems. At Labrulez you will find all the necessary information easily, quickly and clearly. Stop searching and start finding.

LabRulez

Phenomenex is a global technology leader committed to developing novel analytical chemistry solutions that solve the separation and purification challenges of researchers in industrial, government and academic laboratories.

Phenomenex

Based in Berlin, KNAUER is a medium-sized, owner-managed company that has been serving the sciences since 1962. We develop and manufacture scientific instruments of superior quality for liquid chromatography, including: Analytical HPLC/UHPLC, Preparative HPLC, Fast protein liquid chromatography (FPLC), Multi-column chromatography/Simulated moving bed (SMB) chromatography. High pressure dosing, in-line detection systems, and osmometry are additional business areas.

KNAUER

Agilent Technologies

Shimadzu Corporation

<p><strong>A UV-VIS spectrometer is a powerful and versatile tool for material analysis.  It is capable of providing very quick information of sample composition and concentration for quality control in addition to indicating how samples change versus time or temperature.</strong></p>
<p>In this webinar, we will go over what is happening when we take a UV-VIS measurement, discuss how measurement parameters can improve our data collection, and look at applications like concentration and kinetics.</p>
<blockquote>
<p><strong>Presenter: Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p>
</blockquote>


Agilent Technologies: Understanding Your UV-Vis Measurements

Understanding Your UV-Vis Measurements

What is happening when we take a UV-VIS measurement, how measurement parameters can improve our data collection, and look at applications.

<p><strong>Join us to become familiar with performing UV-Vis measurements and how instrumental parameters, solvents, and cuvettes selection, etc. can affect your results. The discussion will cover basic instrument design, instrumental parameters and how they can affect the data. Cuvette selection, solvents choices, and steps involved in setting-up both qualitative and quantitative analysis will be discussed.</strong></p>
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<p><strong>Presenter: Mark Fisher, PhD (Application Engineer, Molecular Spectroscopy, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Mark, an Application Scientist for Agilent Technologies, has over 30 years of experience in molecular spectroscopy. He has held roles in Agilent&#39;s UV-Vis-NIR, fluorescence, and atomic absorption product portfolios. In addition to identifying industry trends and new business needs, Mark&#39;s responsibilities include application development, pre and post-sales support, as well as acting as a customer advocate for new product and technology opportunities. Mark received his doctorate in analytical chemistry from the University of Nebraska-Lincoln.</p>
</blockquote>


Agilent Technologies: Back to Basics Workshop for UV-Vis

Back to Basics Workshop for UV-Vis

Join us to become familiar with performing UV-Vis measurements and how instrumental parameters, solvents, and cuvettes selection, etc. can affect your results. 

<p><strong>Sample throughput can be one of the most challenging aspects of using a UV-VIS Spectrometer.  Scanning spectrometers are capable of collecting data extremely quickly but overall, certain measurements, like kinetics and thermal melts, can still be bottlenecked by the need to measure one sample at a time.</strong></p>
<p>We will discuss in this webinar what to do in these scenarios - and how simultaneous data collection can speed up sample throughput and improve workflows.</p>
<blockquote>
<p><strong>Presenter: Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p>
</blockquote>


Agilent Technologies: Improving UV-Vis Efficiency with Simultaneous Data Collection

Improving UV-Vis Efficiency with Simultaneous Data Collection

We will discuss in this webinar what to do in these scenarios - and how simultaneous data collection can speed up sample throughput and improve workflows.

Improving UV-Vis Efficiency with Data Collection

<p><strong>21 CFR Part 11 regulations and requirements for UV-VIS spectrometers can seem intimidating. Agilent&#39;s Cary 60 and Cary 3500 UV-VIS spectrometers are capable of meeting these requirements and are here to help.</strong></p>
<blockquote>
<p><strong>Presenter: Scott Melis, PhD (Application Scientist, Agilent Technologies, Inc.)</strong></p>
</blockquote>
<blockquote>
<p>Scott Melis has a PHD in Physics from Georgetown University in Washington, DC and started with Agilent in 2021 as a Molecular Spectroscopy Application Scientist. In his graduate work, Scott studied nanoparticle formation and growth for a variety of applications. Projects that he worked with include developing processes to deposit and characterize semiconducting molecular nano-cocrystals for use in optoelectronic devices as well as controlling polymer nanoparticle size through rapid mixing conditions.</p>
</blockquote>


Agilent Technologies: Meeting 21 CFR Part 11 Compliance With UV-Vis Spectrometers

Meeting 21 CFR Part 11 Compliance With UV-Vis Spectrometers

Agilent's Cary 60 and Cary 3500 UV-VIS spectrometers are capable of meeting 21 CFR Part 11 regulations and requirements  and are here to help.

<p><strong>We are interested in the growth of new materials and investigate physical properties affected by size, chemical doping, interface, heterostructure, and external tuning parameters (light, magnetic field, etc.).</strong></p>
<p>We are particularly interested in understanding the optical and dielectric properties of novel electronic materials that are fabricated in our lab in thin film form. Since the discovery of graphene, Transition metal dichalcogenides (TMDs) have merged as one of the most exciting systems to investigate properties at the nanoscale.  In our lab, we have developed few-layer large-area MoS2 thin-films using a PVD-CVD growth process that can produce films with tunable properties [1]. For this talk, I will specifically focus on their broadband dielectric properties measured using Shimadzu UV3600 Plus [2].   Next, I will discuss our work on the influence finite-size in Topological insulator Bi2Se3 thin-films. Through a combination of quantum confinement and Burstein-Moss effect, we discovered a large optical blue-shift in Bi2Se3 as it approaches the 2D limit [3].</p>
<p>References</p>
<ol>
<li><p><strong>Viable route towards large-area two dimensional MoS2 using magnetron sputtering, H. Samassekou, A. Alkabsh, M. Wasala, M. Eaton, A. Walber, A. Walker, O. Pitkänen, K. Kordas, S. Talapatra, T.Jayasekera, Dipanjan Mazumdar, 2D Materials 4 021002 (2017).</strong></p>
</li>
<li><p><strong>Broadband optical properties and electronic band structure of few-layer MoS2, Asma Alkabsh and Dipanjan Mazumdar, (unpublished) 2020.</strong></p>
</li>
<li><p><strong>Optical evidence for blue shift in Topological insulator Bismuth selenide in the few-layer limit , Yub Raj Sapkota, Asma Alkabsh, Aaron Walber, Hassana Samassekou, Dipanjan Mazumdar, Applied Physics Letters, 110, 181901 (2017).</strong></p>
</li>
</ol>


Shimadzu: Optical and dielectric properties of novel electronic materials using Shimadzu UV-3600 Plus

Optical and dielectric properties of novel electronic materials using Shimadzu UV-3600 Plus

Broadband dielectric properties measured using Shimadzu UV3600 Plus.

Optical and dielectric properties of electronic materials

<p><strong>The integrating sphere accessory is the most frequently used accessory on UV/Vis/NIR instruments.</strong></p>
<p>With an integrating sphere, one can measure just about any sample type including, solids, liquids, gels, creams, films, particle suspensions, skin, and other biologicals. In addition, samples that are turbid, cloudy, semi-transparent, or opaque can be easily measured as well. Integrating spheres are the Swiss Army Knife of spectroscopy. The ability to understand the measurement techniques of spheres is key to the evaluation of spectrophotometric materials characterization data.</p>
<p>The most common question materials characterization spectroscopists ask themselves is, “How do I measure this sample?” They ponder this as they are looking some unusual sample, like a rock or even a cockroach. And yes, they can both be measured with an integrating sphere accessory!</p>
<p>This webcast will consist entirely of spectra from a series of example samples that cover the range of specular and diffuse reflectance/transmission characteristics. We will concentrate on the decision-making process of how to measure these different sample types with both the stand-alone instrument and integrating sphere accessary. Included will be a detailed discussion of how to evaluate spectral data from the various sphere measurement formats. This webinar will also cover all the basic measurement configurations of integrating spheres and how to properly evaluate the sample’s material properties from collected spectra.</p>
<blockquote>
<p><strong>Presenter:</strong> Jeffrey L. Taylor, Ph.D. (Molecular Spectroscopy Guru, Industry Expert With Over 35 Years of Experience)</p>
</blockquote>
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<p>Dr. Jeffrey L. Taylor received his Bachelor of Science degree from Georgia College and State University with dual majors in Physiology and Organic Chemistry. He obtained a Master of Science degree from the University of Georgia in Toxicology and later a Doctor of Philosophy degree from the same school in Biochemistry and Spectroscopy.</p>
</blockquote>
<blockquote>
<p>He has spent his career of over 35 years with major spectroscopy instruments manufacturers, mainly working as Field Product Specialist and Senior Staff Scientist. Areas of expertise include technical support of sales, customer support/training, applications design and development, software specification/evaluation, and instrumental design and evaluation. He is the author of numerous application notes, conference presentations and webcasts, and holder of several patents.</p>
</blockquote>
<blockquote>
<p>Dr. Taylor, although retired, maintains his desire to contribute to the field. He is currently a consultant for Shimadzu Scientific Instruments to assist with sales support, application support and development of web-based educational resources.</p>
</blockquote>
<blockquote>
<p><strong>Presenter:</strong> Sudhir Dahal, Ph.D. (Product Manager - Molecular Spectroscopy, Shimadzu Scientific Instruments)</p>
</blockquote>
<blockquote>
<p>Sudhir Dahal is Product Manager of Molecular Spectroscopy group at Shimadzu Scientific Instruments, USA. He joined the company after obtaining his PhD from University of Maryland Baltimore County (UMBC), where he researched and collaborated on developing novel spectroscopy-based technique for brain tumor cell detection. At Shimadzu Scientific Instruments, he and his group are responsible for overall sales support of molecular spectroscopy products in North America, Central America and parts of South America. The products include UV-Vis-NIR, FTIR, Fluorescence spectrophotometers and accessories.</p>
</blockquote>
<blockquote>
<p>,His everyday responsibilities include, but are not limited to, teaching classes to sales/technical support engineers and customers, producing scientific literatures, researching new products and applications, representing Shimadzu at conferences and promoting the products through various marketing campaigns.</p>
</blockquote>


Shimadzu: Measuring Diverse Samples With UV-Vis-NIR Spectrophotometer: An Example Workflow and Evaluation Methodology for Integrating Spheres

Measuring Diverse Samples With UV-Vis-NIR Spectrophotometer: An Example Workflow and Evaluation Methodology for Integrating Spheres

Spectra from a series of example samples that cover the range of specular and diffuse reflectance/transmission characteristics.

LCMS webinars focusing on UV-Vis - page 11