A team from CEITEC Masaryk University (MUNI) in collaboration with researchers from two research institutes in Norway has, for the first time, captured how echovirus 18, a member of the enterovirus genus, releases its genetic material into cells to initiate infection. The study provides a structural view of an early stage of viral infection under near-native conditions. Using cryo-electron microscopy, the researchers discovered that the virus does not release its RNA through a small pore in its capsid, as had long been assumed. Instead, its protein shell partially disassembles, creating a large opening through which the viral genetic material escapes into the host cell. A detailed understanding of this genome release mechanism could eventually help develop compounds preventing enteroviruses from infecting cells.Enteroviruses are common human pathogens causing diseases ranging from the common cold and gastrointestinal infections to severe neurological disorders. Echovirus 18, the virus investigated in this study, is known primarily as a cause of meningitis and encephalitis in children. It belongs to the picornaviruses, a family of small, non-enveloped viruses whose genetic material is protected by a protein shell, the capsid, organized with icosahedral symmetry.To replicate within a cell, the enteroviruses must release their RNA – the molecule that carries viral genetic information – from the capsid, into the cell cytoplasm. Although this step is crucial for initiating infection, it has never been observed in infected cells.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: View into a cell infected by echovirus 18. Echovirus 18 is shown in green and yellow, ribosomes in violet, and actin filaments in cyan. Scale 50 nm. " srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg 221w," sizes="100vw" width="1600" height="1128">“For a long time, two main theories existed about how picornaviruses deliver their RNA genomes into cells. One proposed that the genome leaves the capsid through a small opening. The other, supported by earlier work from our laboratory, suggested that the genome escapes from partially disassembled capsids missing pentamers of capsid proteins. However, both models were based on experiments with virus particles outside cells. We wanted to go one step further and see what really happens during infection inside a cell,” says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/liya-mukhamedova-ph-d/u89248?page=publication">Liya Mukhamedova</a>, the study’s first author from CEITEC MUNI.Using cryo-electron microscopy, which allows scientists to visualize biological structures at exceptionally high resolution, the researchers observed individual echovirus 18 particles directly within infected cells. They discovered that empty virus particles in infected cells lack parts of their capsids. It is through these openings that the virus releases its RNA.The study also revealed the role of the FcRn receptor, a cell-surface molecule that enteroviruses use to enter cells. The binding of the virus to the receptor triggers structural changes in the viral particle that prime it for subsequent genome release. The team showed that receptor binding causes the loss of the so-called pocket factor, a small molecule that normally helps stabilize the virus particle. The virus otherwise remains largely intact, suggesting that receptor binding is only the first step toward uncoating, while additional factors within the cell are required to complete the process and trigger genome release.“Infection is a complex process, during which enterovirus particles sense various interactions with cell components. The binding of echovirus 18 to the FcRn host-cell receptor triggers conformational changes in the virus, priming it for genome release.” – explains <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavel-plevka-ph-d/u26854">Pavel Plevka</a>, head of the Structural Virology Research Group.The researchers did not observe the so-called activated particles that are key intermediates in the enterovirus uncoating process. This suggests that genome release in cells occurs much faster than previous experiments had suggested.By combining structural data obtained from studies of virus particles outside living cells with observations of infected cells, the study offers a picture of how enterovirus infection begins. Moving beyond simplified experiments with isolated virus particles, it brings scientists closer to understanding the earliest stages of enterovirus infection as they occur in living cells. The study, was published in the <a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">PNAS journal</a>.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: Reconstructions of E18 particles from infected cells. The particles are rainbow-colored based on the distance from the particle center. Scale 10 nm." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg 245w," sizes="100vw" width="1600" height="906"><blockquote><h4>Article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://www.pnas.org/doi/10.1073/pnas.2601182123">Particles of echovirus 18 open to release their genomes in vivo</a></h4>Liya Mukhamedova, David Buchta, Zuzana Trebichalská, Yevgen Levdansky, Jana Moravcová, David Potěšil, Zbyněk Zdráhal, Dominik Hřebík, Lucie Nepovímová, Torleif Tollefsrud Gjølberg, Jan Terje Andersen, Jiří Nováček, Tibor Füzik, and Pavel PlevkaProc. Natl. Acad. Sci. U.S.A., 2026, 123, e2601182123<div>&nbsp;</div><div><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">https://doi.org/10.1073/pnas.2601182123</a></div><h6>licenced under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote><h4>Abstract</h4>Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. Enterovirus cell entry involves receptor-mediated endocytosis followed by destabilizing rearrangements of the virus capsid that enable genome release. However, the mechanism of enterovirus genome release has not been visualized in infected cells. Here, we used cryoelectron tomography and microscopy to image echovirus 18 (E18) entry into host cells and its interaction with the neonatal Fc receptor (FcRn). 30 min postinfection, endosomes and cytoplasm contained empty capsids missing one or several pentamers of capsid proteins, providing evidence that in vivo E18 releases its genome through capsid opening. In vitro, FcRn binding induced the expulsion of pocket factors from hydrophobic pockets in VP1, priming the virus for uncoating. The cryoelectron microscopy reconstruction of genome-containing particles of E18 inside infected cells did not reveal pocket factors, indicating that receptor binding triggers the same priming process during infection. We did not detect activated particles in infected cells, suggesting that these intermediates are short-lived and rapidly release their genomes in vivo. Our results identify capsid opening as the in vivo mechanism of echovirus 18 genome release, providing structural evidence for a process previously only inferred from in vitro experiments.

CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection 

Gas chromatography (GC) is a powerful analytical technique used to separate and analyze compounds in a mixture. Whether you're working in pharmaceuticals, environmental testing, or food safety, understanding the key components of a gas chromatograph is essential for accurate and efficient results.In this article, we will delve into the primary components of gas chromatography, including the injector, column, detector, and carrier gas—and explain how each plays a critical role in the separation and analysis process.By mastering these elements, you can optimize your GC setup for precise and reliable outcomes. Let's explore each component in detail:<h3>Sample Injector</h3>The injector is the starting point in the <a target="_blank" rel="noopener noreferrer" href="https://www.phenomenex.com/techniques/gc">gas chromatography process</a>, where the sample is introduced into the system. In GC, the sample must be vaporized into a gas before it enters the column. The injector serves this purpose by heating the sample to its gaseous state. There are many types of injectors, Split/Splitless, PTV, on column.The most common injector is the Split/Splitless injector that can be used in split mode or in splitless mode:<ul><li>Split Injection: This mode allows a portion of the sample to be sent to the column while the remainder is vented. It is useful for high-concentration samples to prevent system overload.</li><li>Splitless Injection: In this mode, the entire sample is introduced into the column, making it ideal for trace analysis where even minute quantities need detection.</li></ul>Proper choice of injector type and proper control of injection conditions, such as temperature, sample size, injection mode are crucial for achieving reproducible and reliable results.<h3>Carrier Gas</h3>In gas chromatography, the mobile phase is represented by carrier gas, which transports the vaporized sample through the column. The carrier gas is an inert gas, such as helium, nitrogen, or hydrogen. The choice of carrier gas can influence the efficiency of the separation process.<ul><li>Helium is the most used carrier gas due to its inertness and high flow rate.</li><li>Hydrogen offers faster analysis times but requires careful handling due to its flammability.</li><li>Nitrogen provides a cheaper solution compared to Helium, although it's slower than helium or hydrogen.</li></ul>The flow rate and pressure of the carrier gas need to be carefully controlled to ensure that the sample moves smoothly through the system and adequate efficiency is generated.<h3>Column/Stationary Phase</h3>The column is the heart of the gas chromatograph, where the actual separation of compounds occurs. <a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/gcms/products?category=7&amp;manufacturerItems=50">GC columns</a> are typically long, thin tubes made from stainless steel or fused silica. They are coated with a stationary phase, which interacts with the components of the sample as they pass through.<ul><li>Packed Columns: These contain small particles of stationary phase material and generally have a larger volume. While they are less efficient than capillary columns, they can be suitable for specific applications.</li><li>Capillary Columns: These thin tubes are coated with a stationary phase, offering higher resolution and faster analysis times due to their smaller diameter.</li></ul>The length, diameter, and type of stationary phase of the column are important factors that affect the efficiency and selectivity of the separation. The choice of stationary phase (polar or non-polar; liquid-coated or solid) affects how different compounds interact with it.As the sample moves through the column, compounds separate based on volatility and their affinity for the stationary phase, resulting in distinct peaks in the chromatogram.<h3>Detector</h3>Once the sample has passed through the column, it reaches the detector, where individual components are identified and measured. There are several types of detectors, each suited to different applications:<ul><li>Flame Ionization Detector (FID): One of the most commonly used detectors in GC. It measures ions produced when organic compounds are burned in a hydrogen-air flame. FID is highly sensitive to a wide range of organic compounds and offers a broad linear dynamic range.</li><li>Thermal Conductivity Detector (TCD): Detects changes in the thermal conductivity of the gas stream as analytes elute from the column. It is a universal, non-destructive detector, but is generally less sensitive than FID.</li><li>Electron capture detector (ECD): A very sensitive and selective detector used to detect chlorinated compounds it is easily contaminated and requires very pure and dry carrier and makeup gases and difficult maintenance.</li><li>Mass Spectrometer (MS): Provides structural information, aiding in both identification and quantification. Requires advanced and trained users and it’s difficult to maintain.</li></ul>The choice of detector depends on the type of analysis being performed and the sensitivity required. Each detector converts physical or chemical changes associated with the analytes into a measurable signal, producing a chromatogram that reflects concentration and retention time.<h3>Data System</h3>Although not a physical part of the chromatograph, the data system plays an integral role in processing and interpreting the signals generated by the detector. Modern gas chromatographs are equipped with software that converts detector signals into chromatograms—visual representations of the separation process. The software allows users to quantify and identify the components of the sample based on retention times and peak areas.<h3>How to Read a Gas Chromatogram?</h3>Interpreting a gas chromatogram involves understanding its essential elements, such as peaks, retention times, and the overall data for qualitative and quantitative analysis.<h4>The Nature of the Sample</h4>Begin by considering the sample's characteristics; different samples, such as environmental pollutants or food components, may exhibit distinct peak patterns. Recognizing the baseline (the flat line representing the signal without analytes) is crucial for identifying peaks accurately. While well-defined peaks indicate successful separation of components, poorly shaped or broad peaks may suggest issues with the separation process. For instance, if a mixture is injected and three peaks are observed, it indicates the presence of three different compounds in the sample. Conversely, when evaluating the purity of a sample, one would anticipate observing a single peak. Ideally, the chromatogram should reflect this expectation, confirming the sample's purity.<h4>The Identity of the Sample</h4>Retention time (Rt) is a critical factor in identifying the compounds present in the sample. Each analyte has a characteristic retention time that can be compared to known standards or literature. To confirm identities, a standard mixture should run alongside the sample; this allows to correlate retention times with specific compounds. If available, utilizing MS in conjunction with gas chromatography (GC-MS) can provide additional structural information, enhancing identification accuracy. With HR-MS or MS-MS detectors, unknown compounds can be identified by matching perfectly the Molecular weight or by matching the fragmentation pattern.<h4>The Amount of Sample</h4>Quantifying analytes involves analyzing peak area or height, which is directly proportional to the concentration of the analyte in the sample. A calibration curve constructed from known concentrations can help relate peak areas to actual concentrations. It is essential to consider the detector’s sensitivity and the limits of detection, as peaks below a certain threshold may not provide reliable quantification.

Basic Principles of Gas Chromatography - Separation and Analysis

ISC 2026 - Day 2

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Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

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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

The International Symposium on Chromatography (ISC) represents the oldest conference series focussing on separation science. ISC symposia have been organised since 1956 in each even year. ISC is internationally recognised as one of the premier meeting series for discussion of all modes of chromatography and separation science with a broad coverage of techniques and applications.

International Symposium on Chromatography - (ISC)

Quantitative analysis of proteins (Bioanalytic) 

In our laboratory, proteomic analyses, including quantitative analysis of proteins, are performed by HPLC-MS or HPLC-MS/MS methods on a ZenoTOF 7600 high-resolution mass spectrometer (SCIEX).

Quantitative analysis of proteins is important in many industries and applications. Proteins include a diverse group of compounds that participate in virtually every biological process. Proteins are building blocks, hormones, transport molecules, cell receptors, cell growth and differentiation factors. Because of this, the analysis of protein interactions is crucial in drug design and production.Proteins are macromolecules - the basis of their structure are polypeptide chains containing from 100 to more than 10000 amino acids (10 - 100 kDa). Proteins are found in simple and complex forms. Complex proteins contain a non-protein component (sugar, lipids, metal ions or dyes) in their structure.In our laboratory, proteomic analyses, including quantitative analysis of proteins, are performed by HPLC-MS or HPLC-MS/MS methods on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=ZenoTOF+7600">ZenoTOF 7600</a> high-resolution mass spectrometer (SCIEX). We process the obtained results using Sciex OS, Spectronaut, Skyline software.<h4>MS vs MS/MS</h4>Quantitative analysis of intact protein (whole protein in intact form) leads to the concentration (determined from a prepared curve from a standard (with or without matrix) and confirmation of the identification by superimposing (on a mirrored basis) the MS spectrum of the protein determined in the sample to the MS spectrum of the standard. For your needs, we can generate a list of protein-structured compounds (impurities) that were identified in the sample and determine the ratio of their signal area to the signal area of the analyzed protein.The result of proteomic quantitative peptide analysis allows precise and much more sensitive determination of protein concentration. The analysis is based on MS/MS data obtained for peptides obtained by digestion with proteolytic enzymes. The reported result consists of the concentration of the protein under study and confirmation of its presence based on the determined amino acid sequence. For such analyses, it is recommended to add standards internal standards.<blockquote>Our offer:<ul><li>For proteins and peptides with low masses - intact analysis with MS detection;</li><li>Proteins with masses &gt;20kDa require optimization of the digestion method and MS/MS detection. This results in specific signals from the analyzed protein in the mixture/matrix;</li><li>From complex matrices (including serum, cell culture, fungal suspension), sample analysis involves several steps:&nbsp;<ul><li>Sample purification;</li><li>Digestion to obtain unique peptides to distinguish the analyzed proteins from other proteins in the sample;</li><li>Sample preparation requires appropriate method optimization and validation (let's set validation criteria individually);</li></ul></li><li>Reported quantitative result includes confirmation of the presence of the protein in native form or a peptide derived from it (usually confirmation includes at least two peptide sequences);</li><li>Statistical analysis using tools: MarkerView (PCA), GraphPad Prism, Trends, Sciex OS.</li></ul>To optimize and validate the method, it is necessary to provide a standard, in the case of proteins with high masses - it is recommended to add an internal standard.See also:<ul><li><a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/">Protein identification</a>,</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296">Analysis and characterization of monoclonal antibodies</a>.</li></ul></blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Quantitative_analysis_of_proteins_1_de494646f2.jpg" alt="Bioanalytic: Quantitative analysis of proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Quantitative_analysis_of_proteins_1_de494646f2.jpg 200w," sizes="100vw" width="777" height="606">

Identification of the substance – what is in your sample? (Bioanalytic)

We are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.

<h4>Substance Identification - Looking for answers to what's in your sample? - we can help you.</h4>Substance identification based on LC-MS/MS techniques can involve single compounds or mixtures of substances. In our analyses, we rely primarily on the knowledge and skills we have acquired after many years of work. For analysis, we use full laboratory facilities for sample preparation and high-resolution mass spectrometry (<a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/o-nas/">equipment</a>).We use different work algorithms depending on the material we are dealing with and the analytical task to be solved. We use DDA (IDA) or DIA (SWATH) methods or targeted approaches (e.g. MRMhr) if we know what to expect. Thus, we are able to identify metabolites and products of chemical reactions, contaminants of biological and chemical substances and preparations, and perform profiling of a series of samples to study the kinetics of transformations.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_2_0f425a648b.jpg 245w," sizes="100vw" width="1881" height="1156"><h4>COST OF SERVICE</h4>We determine the cost of the service individually. The final cost is influenced by many factors related to the nature of the sample itself and the client's expectations. Thus, the price depends, among other things, on the complexity of the sample preparation procedure, the scope and number of analyses, etc.The service includes (depending on individual arrangements):<h5>Development of sample preparation procedure</h5><ul><li>Depending on the matrix and test substances.</li></ul><h5>Development of analytical methods</h5><ul><li>Application of high-resolution LC-MS/MS analyses using DDA (IDA) or DIA (SWATH) experiments and software to support the development of targeted screening methods.</li></ul><h5>Analysis of results includes:</h5><ul><li>finding and identifying the substances of interest, interpreting MS/MS spectra and proposing a structural formula.</li><li>Comparative analysis of sample series, e.g. PCA,</li><li>profiling of analytes in sample series</li></ul><h5>Reporting of results</h5><ul><li>Compile results into easy-to-read reports.</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg" alt="Bioanalytic: Identification of the substance – what is in your sample" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Identification_of_the_substance_what_is_in_your_sample_3_c1b8adc1d0.jpg 245w," sizes="100vw" width="1919" height="1208">

Characteristics of monoclonal antibodies (Bioanalytic)

At LabExperts, proteomic analyses are performed on a ZenoTOF 7600 high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation.

Antibodies are molecules made up of 4 polypeptide chains: two heavy (H - high-chain) linked to each other by a specific type of chemical bond - a disulfide bridge, and two light (L - light-chain) linked by an identical bond to the heavy chains. Monoclonal antibodies (mABs) are used in various forms - as free molecules, in the form of a drug-antibody combination, and in the form of an immunoconjugate, a drug-antibody-biopolymer combination.Their main use is in highly specific targeted therapy for cancer, cardiovascular, autoimmune and nervous system diseases. They are also used in the treatment of osteoporosis, Alzheimer's disease or transplantation. The range of applications of monoclonal antibodies is systematically expanded. The introduction of a new antibody to the market requires complex product characterization, which involves numerous proteomic analyses, which are performed by LC-MS/MS techniques, among others.<h4>LC-MS/MS</h4>The characterization of monoclonal antibodies involves many aspects, including, but not limited to, a suite of analyses related to confirmation of the structure, chain sequence and degree of modification of the antibody. Post-translational modifications (PTMs) are chemical changes that occur after the translation process. These changes generally result in an increase in the immunogenicity of the drug. For this reason, it is essential to monitor modifications as critical quality attributes (CQAs) during both the production and storage of the drug. To ensure monitoring of CQA points, the primary structure of the protein is characterized based on peptide mapping (peptide mapping) analysis. The protein under study is subjected to proteolytic digestion using enzymes such as trypsin, chymotrypsin, Lys-C, Glu-C. As a result of various proteolytic enzymes, a wide range of peptides is obtained. Ultimately, coverage of the entire sequence of the protein under study is obtained.<figure class="image"><img style="aspect-ratio:1536/947;" src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg" alt="Bioanalytic: Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_3_d94fa1623b.jpg 245w," sizes="100vw" width="1536" height="947"></figure>At LabExperts, proteomic analyses are performed on a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=ZenoTOF+7600">ZenoTOF 7600</a> high-resolution LC-MS/MS system (SCIEX). For MS/MS analyses, we use Collision induced dissociation (CID) and Electron-Activated Dissociation (EAD) fragmentation. This provides us with data for unambiguous identification of protein-building amino acids. We process the results using Sciex OS, Skyline and Spectronaut software.<blockquote>We perform:<ul><li>Whole protein analyses - Intact - to determine the exact mass and confirm the theoretical mass;</li><li>N-glycosylation profile determination (based on MS spectrum reconstruction):<ul><li>Glycosylated form;</li><li>Deglycosylated;</li><li>Glycosylated with reduced disulfide bridges;</li><li>Deglycosylated with reduced disulfide bridges.</li></ul></li><li>Peptide maps:<ul><li>Protein digestion with various proteases so that sequence coverage is close to 100%<ul><li>Analysis of PTMs:</li><li>Location of modifications</li></ul></li><li>[%] of modifications compared to the unmodified sequence</li></ul></li><li>TiPOS testing - (technical proof of similarity) - technical confirmation of the similarity of the protein synthesized by the customer (from several LOTs) with the target protein (provided as a template).</li></ul>In order to maintain the highest possible analytical standards, we perform monoclonal antibody analyses under the regime of an internally developed and implemented laboratory quality system based on GLP principles.See also our other proteomics services: <a target="_blank" rel="noopener noreferrer" href="https://labexperts.com.pl/service/identyfikacja-bialek/">Protein identification</a>, <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294">Protein quantitative analysis</a></blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_2_cb93143fe6.jpg 245w," sizes="100vw" width="1536" height="908"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg" alt="Bioanalytic: Bioanalytic Characteristics of monoclonal antibodies." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Bioanalytic_Characteristics_of_monoclonal_antibodies_1_0e8ab7cdfa.jpg 245w," sizes="100vw" width="1536" height="858">

Analysis of Anabolic steroids (Bioanalytic)

We offer a highly specific and sensitive qualitative analysis of a wide profile of anabolics by LC-HR-MS/MS technique (detection limits range from 0.01 to 5 ng/ml, depending on the substance).

<h4>Anabolic substances in urine</h4>The effect of anabolic steroids (<a target="_blank" rel="noopener noreferrer" href="https://en.wikipedia.org/wiki/Anabolic_steroid">more information</a>) is to stimulate the growth of muscle mass and sometimes also bone mass by stimulating protein synthesis or altering calcium metabolism. This effect is often used in sports doping. However, anabolic steroids also have many side effects, as they strongly affect the body's overall hormonal balance.Anabolic steroids used by purely recreational athletes are still not banned in most countries, including Poland. Nevertheless, their amateur use during adolescence often results in the inability to continue a professional sports career into adulthood or leads to hormonal imbalances in the body.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_1_46fa2f41ca.jpg" alt="Bioanalytic: Analysis of Anabolic steroids." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_1_46fa2f41ca.jpg 245w," sizes="100vw" width="1200" height="740">If you want to know whether and which anabolic substances are present in the samples of athletes, or you want to exclude doping in this area - use the offer carried out by us together with the company <a target="_blank" rel="noopener noreferrer" href="http://www.lab4tox.pl/">Lab4Tox</a>. We offer a highly specific and sensitive qualitative analysis of a wide profile of anabolics by LC-HR-MS/MS technique (detection limits range from 0.01 to 5 ng/ml, depending on the substance). The use of high-resolution mass spectrometry (HR-MS and HR-MS/MS) in the analysis of anabolic steroids makes it possible to unequivocally confirm or exclude the presence of a given compound. The list of compounds at present includes:<ul><li>Boldenone undecylenate</li><li>Turinabol</li><li>Drostanolone enanthate</li><li>Drostanolone propionate</li><li>Methandienone</li><li>Methenolone acetate</li><li>Methenolone enanthate</li><li>Nandrolone phenylpropionate</li><li>Oxandrolone</li><li>Oxymetholone</li><li>Stanozolol</li><li>5-alpha-DHT</li><li>6-beta-hydroxymethandienone</li><li>19-norandrosterone</li><li>3'-hydroxystanazolol</li><li>4-beta-hydrozystanazolol</li><li>17-alpha-trenbolone</li><li>Testosterone caproate</li><li>Testosterone cypionate</li><li>Testosterone decanoate</li><li>Testosterone enanthate</li><li>Testosterone isocaproate</li><li>Testosterone phenylpropionate</li><li>Testosterone propionate</li><li>Testosterone undecanoate</li><li>Trenbolone acetate</li><li>Testosterone</li><li>Epitestosterone</li></ul>The list of compounds is not complete and will be systematically expanded according to customer needs.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg" alt="Bioanalytic: Analysis of Anabolic steroids is carried out by us together with the company Lab4Tox." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg 245w," sizes="100vw" width="625" height="100"><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=54&amp;distributorItems=315">Other analytical methods we offer</a>.

Analysis of Synthetic Peptide Hormones (Bioanalytic)

We offer highly specific and sensitive quantitative analysis of peptides by LC-MS/MS technique (LOQ < 1 ng/ml).

<h4>Synthetic peptide hormones - a study of the purity of formulations and composition of dietary supplements.</h4>In sports doping, small synthetic peptide hormones represent an increasingly attractive class of supplements for improving physical performance in amateur and professional athletes. Their use, depending on the type of peptide, is aimed primarily at building muscle tissue while intensifying fat reduction processes combined with the induction of the body's regenerative processes.Do you want to be sure that the peptide you are using is in the product in the amount declared by the manufacturer? Or do you have doubts that the supplement you are using is contaminated with these compounds? If you are troubled by these or similar questions - feel free to contact us. We perform tests in cooperation with <a target="_blank" rel="noopener noreferrer" href="http://www.lab4tox.pl">Lab4Tox</a>. We offer highly specific and sensitive quantitative analysis of peptides by LC-MS/MS technique (LOQ &lt; 1 ng/ml). At the moment, we analyze the following peptides:<ul><li>GHRP-2</li><li>GHRP-6</li><li>BPC-157</li><li>Melanotan-2</li></ul>The list of compounds is not complete and will be systematically expanded according to customer needs.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg" alt="Bioanalytic: Analysis of Synthetic Peptide Hormones. We perform tests in cooperation withLab4Tox." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Analysis_of_Anabolic_steroids_Bioanalytic_2_78729119b0.jpg 245w," sizes="100vw" width="625" height="100"><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=54&amp;distributorItems=315">Other analytical methods we offer</a>.

Determination of nitrosamine content (Bioanalytic)

Our offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products. We perform the work according to the criteria and needs of the client based on the EMA note.

Determination of nitrosamines is one of the pharmaceutical industry's top priorities. After the presence of N-nitrosodimethylamine (NDMA) was first reported in an active pharmaceutical ingredient (API), the U.S. Food and Drug Administration (FDA) and the European Medicines Agency (EMA) mandated the identification and control of all APIs and finished products in which there is a risk of nitrosamines.The content of nitrosamines in drug products can be controlled primarily by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) analysis. More than that, a reliable analysis result in our offer consists of a well-chosen sample preparation procedure, a selective and sensitive analytical method, and the experience of the analyst, who selects the best method parameters at the optimization stage.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_2_ce4f440837.jpg 234w," sizes="100vw" width="1536" height="1024">We have gained experience working with leading pharmaceutical companies. As part of our ongoing work, we have developed analytical methods for small-molecule nitrosamines of 70-150 g/mol. These compounds are mainly formed during manufacturing processes and depend on the presence and type of excipients (e.g. NDBA - N-nitroso-dibutylamine). We have also developed methods for determining molecules with higher nitrosamine drug substance related impurities (NDSRIs). In our work, we focus on achieving the highest possible sensitivity, selectivity and precision. To this end, we individually select the parameters of the methods depending on the composition of the drug and the expected nitrosamines. Due to the above criteria and the required detection limits, we perform nitrosamine impurity determinations using LC-MS/MS kits based on <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+5500%2B">QTRAP 5500+</a> and <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=QTRAP+6500%2B">QTRAP 6500+</a> mass spectrometers (<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?mainauthorItems=55">SCIEX</a>).<blockquote>Our offerOur offer includes comprehensive development and validation of methods for determination of nitrosamines in pharmaceutical products. We perform the work according to the criteria and needs of the client based on the EMA note.At the stage of sample preparation, we focus on:<ul><li>obtaining the highest possible recovery of nitrosamines (matrix purification);</li><li>limiting additional synthesis of impurities (selection of appropriate equipment and reagents);</li><li>ensuring the stability of the sample prepared for LC-MS/MS analysis.</li></ul>During the optimization of the LC-MS/MS method, we solve such problems as:<ul><li>selection of an appropriate internal standard;</li><li>separation of the impurity from the API;</li><li>obtaining the expected sensitivity of the analytical method.</li></ul>Quantitative analysis of nitrosamines requires sensitivity, precision and accuracy, which we provide to our customers.</blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg" alt="Bioanalytic: Determination of nitrosamine content." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Determination_of_nitrosamine_content_Bioanalytic_1_d629e00e62.jpg 103w," sizes="100vw" width="1130" height="1710">

Identification of the proteins (Bioanalytic)

We perform proteomic analyses on a state-of-the-art high-resolution ZenoTOF 7600 (SCIEX), in which the Zeno ion trap and EAD (Electron-Activated Dissociation) technology together make a powerful combination.

Protein identification is based on experimental measurement of peptide molecular weights and matching the amino acid sequence of the protein under study with protein sequences deposited in libraries (databases). Two approaches are most commonly used in proteomic studies: top-down and bottom-up. The top-down method involves analyzing full protein sequences. Bottom-up analyses, on the other hand, use digestion of proteins with proteolytic enzymes. The peptides obtained by digestion are analyzed using a mass spectrometer. Each analysis leads to a comparison of experimental data with data obtained by theoretical digestion of proteins described in the database.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_2_6231b73f0d.jpg 245w," sizes="100vw" width="1536" height="766"><h4>LC-MS/MS</h4>Tandem mass spectrometers are commonly used to determine protein sequences. They allow ion selection of pseudomolecular peptides and then fragmentation and measurement of the masses of the resulting fragments. Fragmentation using collision induced dissociation(CID ) is an invaluable tool in targeted and untargeted MS/MS analysis of small molecules. It is important to note that in proteomic analysis, data obtained using the aforementioned fragmentation method may leave gaps. For example, spectra obtained by CID fragmentation do not allow unambiguous differentiation of some amino acids: leucine from isoleucine (identical molar masses and CID fragmentation) and lysine from glutamine (very similar masses). For this reason, we perform proteomic analyses on a state-of-the-art high-resolution <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/library?manufacturerItems=52&amp;search=+ZenoTOF+7600">ZenoTOF 7600</a> (SCIEX), in which the Zeno ion trap and EAD (Electron-Activated Dissociation) technology together make a powerful combination. It enables the creation of unique fragments to differentiate problematic amino acids and increase the sensitivity and specificity of the analysis.<blockquote>We perform analyses of:<ul><li>samples from solution;</li><li>samples from a gel;</li><li>samples from a complex matrix (by prior arrangement);</li><li>samples from lyophilizer;</li><li>samples previously prepared by the client.</li></ul>Qualitative analysis of proteins includes:<ul><li>To confirm the presence of a protein, the sample is subjected to digestion and the result obtained from experimental data is compared with theoretical data;</li><li>Comparison of experimental data on the masses of peptides included in the analyzed protein with the protein sequences described in the database;</li><li>Analysis and identification of the protein mixture;</li><li>Identification of post translational modifications (PTMs) (we use the tools: Skyline, Spectronaut).</li><li>Reporting of the result including, but not limited to, confirmation of the coverage of the protein sequence obtained in the test sample with the theoretical protein and the list of modified peptides, location and % of modifications.</li></ul>Comparative analyses include:<ul><li>Determining the composition of mixtures;</li><li>Comparison and profiling of sample series - protein identification and trend analysis.</li></ul>Our offer also includes:<ul><li>Support in the planning and execution of studies (the scope is determined individually);</li><li>Assistance in the development of extraction methods from complex matrices - biological fluids, plant tissue, animal tissues (the scope is determined individually);</li><li>Statistical analysis using tools: MarkerView (PCA), GraphPad Prism, Trends, Sciex OS;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1294">Quantitative analysis of proteins</a>;</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/1296">Analysis and characterization of monoclonal antibodies</a>.</li></ul></blockquote><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg" alt="Bioanalytic: Identification of the proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Bioanalytic_Identification_of_the_proteins_Bioanalytic_1_97cf8c94b3.jpg 117w," sizes="100vw" width="1500" height="2000">

Analysis of peptides in supplements (Bioanalytic)

Verify peptides in dietary supplements with sensitive LC-MS/MS analysis. Identify declared peptides, detect impurities, and support reliable product quality control.

<h3>LC-MS/MS analysis of peptides in dietary supplements – precise quality control and compliance with the declaration</h3>Looking for reliable analysis of peptides in dietary supplements? We offer specialized LC-MS/MS (liquid chromatography coupled mass spectrometry) testing to accurately identify peptides used in health promoting products and nutritional supplements.<h4>Why perform LC-MS/MS analysis of peptides?</h4>Peptides are increasingly common ingredients in dietary supplements – both for athletes and those concerned with health, regeneration or skin appearance. Due to their specific action, it is extremely important to precisely analyze the composition of the preparations used and confirm the composition of the declared substances. Our research allows to:<ul><li>Verify the compliance of the supplement with the manufacturer’s declaration,</li><li>Detect contaminants or prohibited substances,</li><li>Ensure the safety and effectiveness of the product’s use,</li><li>Meet the requirements of the sanitary inspection and EU regulations.</li></ul><h4>Our offer – analysis of peptides in supplements by LC-MS/MS method</h4>As part of our service, we offer comprehensive peptide testing by LC-MS/MS, including:<ul><li>Consultation and selection of an analytical method tailored to the type of peptides and the client’s needs,</li><li>Qualitative analysis of peptides (upon request) – aimed at the accurate determination of the mass and isotopic distribution of the peptide under study in the sample in order to unambiguously confirm the identification of the peptide. Indication of impurities and determination of the relative percentage concentration of impurities,</li><li>The ability to identify new or non-standard compounds,</li><li>Fast turnaround time (results as low as 5 working days),</li></ul><h4>Who uses our services?</h4>Our research is aimed at:<ul><li>Manufacturers and importers of dietary supplements,</li><li>Supplement packaging companies,</li><li>Quality control laboratories,</li><li>Distributors and nutritional stores,</li><li>Organizations that test supplements for athletes.</li></ul><h4>Why us?</h4>We have modern technological facilities and a team of experienced analysts. We guarantee full confidentiality, flexibility and individual approach to each order. Our LC-MS/MS analyses meet the highest quality standards.<h4>Have your peptide analysis done today!</h4>Contact us for a free quote and tailor the scope of testing to meet your needs. Ensure the quality, safety and reliability of your dietary supplement with professional laboratory analysis. We offer highly specific and sensitive qualitative analysis of peptides by LC-MS/MS technique. At the moment, we analyze the following peptides:<ul><li>GHRP-2</li><li>GHRP-6</li><li>BPC-157</li><li>Melanotan-2</li><li>Semaglutide</li><li>Tirzepatide</li><li>Retatrutide</li><li>Ipamorelin</li><li>PT-141</li><li>TB-500</li><li>Tesamorelin</li><li>Epitalon</li><li>Fragment 176-191</li><li>GKH-Cu</li><li>Ostarine</li><li>Rad 140</li><li>Kisspeptin</li></ul>The list of compounds is not closed and will be systematically expanded according to customer needs.<a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products?category=54&amp;distributorItems=315">Other analytical methods we offer</a>.

Products from category Laboratory analyses distributed by Bioanalytic - page 1

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