CreMap™ B Cell Epitope Mapping Services

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This method is fast and relatively inexpensive, and specifically suited to the epitope profiling for a large number of candidate antibodies against a defined target. <a href="/cremap-peptide-protein-microarray-service.html" rel="nofollow">Read more…</a> </p> <p> <strong>Limited Proteolysis Coupled With Mass Spectrometry</strong> </p> <p> Limited proteolysis method was invented several decades ago. Coupling with mass spectrometry ensures the high efficacy and precision Proteases with different restriction sites are applied to the antigen-antibody complex and the native antigen is treated in the same condition. The proteolytically robust paratope on the antibody protects the epitope from proteolysis. Fragments released from the different cleavage sites in the presence and absence of the antibody are detected by MS to reveal the bound fragments to the antibody. <a href="/cremap-epitope-mapping-by-limited-proteolysis-coupled-with-mass-spectrometry.html" rel="nofollow">Read more…</a> </p> <p> <strong>Amide Hydrogen/Deuterium Exchange</strong> </p> <p> Derived from the limited proteolysis method, amide hydrogen/deuterium exchange method takes advantage of the fact that a covalently bonded hydrogen atom would be replaced by a deuterium atom. When the antigen is diluted into a solution of D<sub>2</sub>O, Labile protons, such as those on primary amines, exchange nearly instantaneously. Meanwhile, the amides buried in the protein core or located interaction surfaces are protected against hydrogen exchange due to the limited solvent exposure and shows slower exchange kinetics. The antigen is mixed a deuterium buffer in solution, and the mixture was incubated for a series of time points before the exchange reaction is quenched by eluting out in a low pH buffer and digested by pepsin. The fragments would, therefore, be measured by HPLC and MS. <a href="/cremap-epitope-mapping-service-by-hydrogen-deuterium-exchange.html" rel="nofollow">Read more…</a> </p> <p> <strong>Nuclear Magnetic Resonance (NMR) Analysis</strong> </p> <p> NMR emerges as a useful tool for epitope mapping analysis. Through NMR, the 3D-structure of the target protein could be constructed by measuring distances and angles between amino acids residues. For identifying epitopes, NMR analysis provides a detailed structure analysis for epitope-Fab interaction, therefore the nature of epitope recognition could be accurately explained. The NMR chemical shift map was developed to describe and determine the epitope residues by comparing changes in the NMR spectral signals before and after the formation of the antigen-antibody complex. <a href="/cremap-epitope-mapping-by-nuclear-magnetic-resonance-analysis.html" rel="nofollow">Read more…</a> </p> <p> <strong>Surface Plasmon Resonance (SPR)</strong> </p> <p> Monitored in real time, SPR is a powerful method for characterizing antigen-antibody interactions. The basic Surface plasmon resonance (SPR) analysis involves immobilizing the antigen on the sensor chip surface of a flow-cell, and then an antibody solution flows over the antigen and the sensor detects the changes in refractive index of the surface layer of a solution in contact with the sensor chip that is caused by a variation of the mass on the sensor chip surface. Real-time measurements allow for the calculation of the association and dissociation kinetic rate constants, <em>k<sub>a</sub></em> and <em>k<sub>d</sub></em> of the interaction. A small amount of reagent is required for SPR and no labeling or modification is needed before analysis. <a href="/cremap-epitope-mapping-by-surface-plasmon-resonance.html" rel="nofollow">Read more…</a> </p> <p> <strong>Crystallography-based Methods</strong> </p> <p> X-ray crystallography is the gold standard among all the epitope mapping methods. In this technique, the highly purified antigens are obtained and allowed to co-crystallize with their corresponding antibodies. Then, the atomic structure of the complex is solved using X-ray diffraction analysis. The amino acids that are within a distance of 4 Å of each other are considered to be counteracting. Accordingly, epitope regions of an antigen that contact with the antibody molecule could be identified. Obviously, this co-crystallization method is able to detect continuous linear epitopes as well. <a href="/cremap-epitope-mapping-service-by-x-ray-crystallography.html" rel="nofollow">Read more…</a> </p> <p> <strong>Alanine Scanning Mutagenesis</strong> </p> <p> High-throughput Mutagenesis Mapping is based on a comprehensive mutation library, in which residues of a target protein are substituted for a certain kind of amino acid (often alanine substitution) at selected positions by site-directed mutagenesis. All the plasmid clones from the mutation library are individually arrayed in microplates, expressed in mammalian cells and tested for their antibody binding capacity. <a href="/cremap-alanine-scanning-mutagenesis-mapping-service.html" rel="nofollow">Read more…</a> </p> <p> <strong>Microfluidic Peptide Microarray</strong> </p> <p> Creative Biolabs has developed an advanced microfluidic microarray technology service for epitope mapping and other immunoassays, which utilizes the microfluidics during the process of synthesis of the arrays as well as the binding assay reactions. This technology could achieve high throughput peptide screening on a comprehensive scale. <a href="/epitope-mapping-on-a-microfluidic-peptide-microarray.html" rel="nofollow">Read more…</a> </p> <p> <strong>Surface Display Methods</strong> </p> <p> This technique is based on testing the binding capacity of a variety of peptides displayed on the surface of a bacteriophage to the monoclonal antibody of interest. The foreign DNA is inserted into the genome of bacteriophage. Viral peptides including the foreign DNA are then synthesized and displayed on the amino-terminal portion of the viral coat protein. After that, the binding ability of the peptide displayed on the phage surface to the antibody would be tested and the epitope mapping performed. <a href="/cremap-epitope-mapping-by-surface-display-technique.html" rel="nofollow">Read more…</a> </p> <p> <strong>Linear B-Cell Epitopes </strong> </p> <p> B-cell epitopes play an important role in vaccine discovery, high-affinity antibodies design as well as protein-peptide interaction analysis. In recent years, many attempts have been made by Creative Biolabs to predict linear B-cell epitopes. We offer a wide variety of structural and functional analysis of B cells, such as sequential residues, peptides. In general, linear peptide fragments from antigenic proteins have been widely used to screen Ag-Ab reactivity of mutants. <a href="/linear-b-cell-epitopes.html" rel="nofollow">Read more…</a> </p> <p> <strong>Conformational B-Cell Epitopes </strong> </p> <p> Conformational B-cell epitope mapping has been considered as a common strategy for immunologic analysis of drug candidates. Creative Biolabs has been generated to provide an array of peptide-based and protein-based B-cell epitope mapping services for our clients all over the world. The peptide or protein fragments can be analyzed by a number of advanced technologies to obtain meaningful results that support the safety and Immunogenicity evaluation of specific therapeutic molecules. <a href="/conformational-b-cell-epitopes.html" rel="nofollow">Read more…</a> </p> <p> <strong>Creative Biolabs</strong> offers comprehensive as well as professional technologies for your epitope discovery and we are so honored to provide a customized schedule to help you with your research. If you are interested in our CreMap™ B cell epitope mapping, please <a class="inquiry-button">contact us</a> for more information and a detailed quote. </p> <p> Learn more about CreMap™ B cell epitope mapping services: </p> <ul class="ullist"> <li> <a href="/cremap-peptide-protein-microarray-service.html">CreMap™ Epitope Mapping by Peptide Microarray</a> </li> <li> <a href="/cremap-epitope-mapping-by-limited-proteolysis-coupled-with-mass-spectrometry.html">CreMap™ Epitope Mapping by Limited Proteolysis coupled with Mass Spectrometry</a> </li> <li> <a href="/cremap-epitope-mapping-service-by-hydrogen-deuterium-exchange.html">CreMap™ Epitope Mapping by Hydrogen/Deuterium Exchange</a> </li> <li> <a href="/cremap-epitope-mapping-by-nuclear-magnetic-resonance-analysis.html">CreMap™ Epitope Mapping by Nuclear Magnetic Resonance (NMR) Analysis</a> </li> <li> <a href="/cremap-epitope-mapping-by-surface-plasmon-resonance.html">CreMap™ Epitope Mapping by Surface Plasmon Resonance</a> </li> <li> <a href="/cremap-epitope-mapping-service-by-x-ray-crystallography.html">CreMap™ Epitope Mapping by X-ray Crystallography</a> </li> <li> <a href="/CreMap-Alanine-Scanning-Mutagenesis-Mapping-Service.html">CreMap™ Epitope Mapping by Alanine Scanning Mutagenesis</a> </li> <li> <a href="/epitope-mapping-on-a-microfluidic-peptide-microarray.html">CreMap™ Epitope Mapping by Microfluidic Peptide Microarray</a> </li> <li> <a href="/cremap-epitope-mapping-by-surface-display-technique.html">CreMap™ Epitope Mapping by Surface Display Technique</a> </li> <li> <a href="/linear-b-cell-epitopes.html">Linear B-Cell Epitopes</a> </li> <li> <a href="/conformational-b-cell-epitopes.html">Conformational B-Cell Epitopes</a> </li> </ul> <h2 class="h2_tit page_tab_margin" id="tab3"> Published Data </h2> <ul class="ullist"> <li> <strong>Using B-cell Epitope Mapping to Identify of Immune-Reactive Regions of <em>Vibrio Cholerae</em> Toxins</strong> </li> </ul> <p class="show-center"> <img loading="lazy" src="static/img/1-2-8-3-1-b-cell-epitope-mapping-service-1.jpg" width="353" height="413" alt="" />Fig. 1 Epitope localization in three-dimensional structures of <em>V. cholerae</em> toxins A (A), B (B), and P (C). (Salvatore G. De-Simone, 2023) </p> <p> The research described in the article highlights the use of B-cell epitope mapping to identify immune-reactive regions of <em>Vibrio cholerae</em> toxins, which is significant for enhancing cholera vaccine development and diagnostic assays. The study used a comprehensive SPOT synthesis approach to map linear B-cell epitopes across the cholera toxin proteins A, B, and P. A total of 18 epitopes were identified, and specific epitopes were used to develop an ELISA that accurately detected immune responses in vaccinated mice. This method of epitope mapping allows for the precise identification of immunogenic regions on pathogens, facilitating the creation of more targeted and effective vaccines and diagnostic tools. </p> <div class="reference"> <strong>Reference</strong> <ol class="ollist decimal"> <li> De-Simone, Salvatore G., et al. "B-Cell Epitope Mapping of the Vibrio cholera Toxins A, B, and P and an ELISA Assay." <em>International Journal of Molecular Sciences</em> 24.1 (2022): 531. </li> </ol> </div> <script type="text/javascript"> window.addEventListener('load',function(){ faqlist(4); }); </script> <h2 class="h2_tit page_tab_margin" id="tab4"> FAQ </h2> <ol class="ollist faqlist"> <li> <span class="sFAQTit">What is B cell epitope mapping?</span> <p> B cell epitope mapping is a technique used to identify the specific regions of an antigen that are recognized by B cell receptors or antibodies. This process helps to determine which parts of an antigen stimulate an immune response, aiding in the development of vaccines, therapeutic antibodies, and diagnostic tests. </p> </li> <li> <span class="sFAQTit">What techniques are commonly used in B cell epitope mapping?</span> <p> Common techniques include peptide scanning (using synthetic peptides), phage display libraries, ELISA-based methods, and computational modeling. These techniques can identify linear (continuous) and conformational (discontinuous) epitopes by testing how well peptides or modified proteins bind to specific antibodies. </p> </li> <li> <span class="sFAQTit">How does B cell epitope mapping contribute to vaccine development?</span> <p> By identifying the precise parts of an antigen that an antibody recognizes, B cell epitope mapping enables researchers to design vaccines that specifically target these regions. This targeted approach can lead to more effective and efficient vaccines, as it focuses the immune response on the critical parts of the pathogen. </p> </li> <li> <span class="sFAQTit">Can B cell epitope mapping predict allergic reactions?</span> <p> B cell epitope mapping can be used to identify potential allergenic epitopes in foods, drugs, or environmental substances. By recognizing which molecular structures trigger allergic responses, it's possible to reformulate products or develop desensitization therapies that minimize these reactions. </p> </li> <li> <span class="sFAQTit">What is the difference between linear and conformational B cell epitopes?</span> <p> Linear epitopes consist of a continuous sequence of amino acids in a protein, while conformational epitopes are formed by amino acids that are brought together in the three-dimensional structure of the protein but are not necessarily sequential in the linear sequence. Both types of epitopes can be recognized by B cells and are important in different immunological contexts. </p> </li> <li> <span class="sFAQTit">How do computational methods enhance B cell epitope mapping?</span> <p> Computational methods predict B cell epitopes based on protein structure and sequence information, reducing the need for extensive laboratory experiments. These methods use algorithms to analyze protein sequences for epitope prediction, increasing the speed and lowering the cost of epitope mapping projects. </p> </li> <li> <span class="sFAQTit">How is B cell epitope mapping used in therapeutic antibody development?</span> <p> In therapeutic antibody development, B cell epitope mapping is used to identify and engineer specific regions on target antigens that are most effective for antibody binding. This ensures that therapeutic antibodies can effectively target and neutralize disease-causing agents or pathological cells. </p> </li> </ol> <h2 class="h2_tit page_tab_margin" id="tab5"> Resources </h2> <p> Use the resources in our library to help you understand your options and make critical decisions for your study. </p> <div class="tab_nav"> <span class="tab_choosebg">Videos</span><span>Articles</span> </div>  <div class="tab_cont" style="display:block;"> <div class="row pagerow_pt"> <div class="col-md-4"> <div class="pagerow_pt_unit"> <img loading="lazy" src="../static/img/immunogenicity-overview-of-therapeutic-biologics.jpg" alt="" /> </div> <a href="https://youtu.be/J430752_dTo" target="_blank">Immunogenicity overview of therapeutic biologics</a> </div> </div> </div>  <div class="tab_cont"> <div class="row pagerow_pt"> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-immune-monitoring-for-immunogenicity-assessment-1.jpg" alt="" /> </div> <a href="/immune-monitoring-for-immunogenicity-assessment.html">Immune Monitoring for Immunogenicity Assessment</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-current-immunogenicity-evaluation-systems-a-deep-dive-by-creative-biolabs-1.jpg" alt="" /> </div> <a href="/current-immunogenicity-evaluation-systems.html">Current Immunogenicity Evaluation Systems: A Deep Dive by Creative Biolabs</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-1-in-silico-immunogenicity-assessment-the-leading-edge-approach-to-drug-development-1.jpg" alt="" /> </div> <a href="/in-silico-immunogenicity-assessment-the-leading-edge-approach-to-drug-development.html"><i>In Silico</i> Immunogenicity Assessment: The Leading-edge Approach to Drug Development</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-4-how-to-evaluate-the-immunogenicity-of-therapeutic-protein-drugs-in-vivo-1.jpg" alt="" /> </div> <a href="/how-to-evaluate-the-immunogenicity-of-therapeutic-protein-drugs-in-vivo.html">How to Evaluate the Immunogenicity of Therapeutic Protein Drugs <i>In Vivo</i></a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-5-the-origin-and-detection-methods-of-anti-drug-antibodies-1.jpg" alt="" /> </div> <a href="/the-origin-and-detection-methods-of-anti-drug-antibodies.html">The Origin and Detection Methods of Anti-Drug Antibodies</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/4-2-14-1-8-immunogenic-risk-assessment-of-therapeutic-proteins-1.jpg" alt="" /> </div> <a href="/immunogenic-risk-assessment-of-therapeutic-proteins.html">Immunogenic Risk Assessment of Therapeutic Proteins</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit_2"> <img loading="lazy" src="static/img/anti-drug-antibody-introduction-1.jpg" alt="" /> </div> <a href="/anti-drug-antibody-introduction.html">Anti-Drug Antibody Introduction</a> </div> </div> </div> <script> window.addEventListener('load',function(){ // $(function () { $(".tab_nav span").click(function(){ var eqindex=$(this).index(); $(this).addClass("tab_choosebg"); $(this).siblings("span").removeClass("tab_choosebg"); $(".tab_cont").hide().eq(eqindex).show(); }) // }) }); </script><br> <p class="pronote"><i class="fa fa-exclamation-triangle"></i>All listed services and products are For Research Use Only. 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