Cysteine Modification Service

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Advantages include quality, stability, purity, rapidly delivery as well as reduced production and development cost. This service has a wide application including but not limited to molecular imaging, antibody-drug conjugations (ADCs) and diagnostics. </p> <h2 class="h2_tit page_tab_margin" id="tab1"> Background </h2> <p> Modification of proteins by the covalent attachment of payloads has gained prominence in the development of therapeutic proteins. In the past decade, many novel site-specific, bio-orthogonal reactions that enable precise and controlled modification of proteins have been reported. Comparing with the primary amines of lysines, it takes more advantages to choose sulfhydryls of cysteines serve as conjugation sites. Because this amino acid is less abundant and forms conserved disulfide bridges in antibodies to eliminate the risk of leading to steric hindrance of target recognition, we use both conventional modification methods and novel precise modification at engineered C- or N-terminal free cysteines of antibodies, such as site-specific mutagenesis and traceless cleavable linkers. </p> <p class="ServiceShowPic"> <img loading="lazy" width="560" height="195" src="static/img/Custom Cysteine Modification in Antibody for website_Chen_baiyw-1.jpg" alt="Custom Cysteine Modification in Antibody" /><b>Fig. 1</b> Construction of a traceless chemically defined tumor-vascular targeting antibody-drug conjugate based on disulfide linkage. (Bernardes <i>et al</i>. 2013) </p> <p class="ServiceShowPic"> <img loading="lazy" width="480" height="212" src="static/img/Custom Cysteine Modification in Antibody for website_Chen_baiyw-2.jpg" alt="Custom Cysteine Modification in Antibody" /><b>Fig. 2</b> Massa <i>et al</i>. (2014) </p> <h2 class="h2_tit page_tab_margin" id="tab2"> Guarantees </h2> <p> We guarantee any antibody cysteine modification (over 95% purity) with excellent homogeneity and antigen-binding properties. </p> <h2 class="h2_tit page_tab_margin" id="tab3"> Competitive advantages </h2> <p> Expertise knowledge and rich experience in site-specific modification and conjugation; <br /> A comprehensive system of both conventional and modern novel methods and technologies for biomodification and conjugation; <br /> Professional computational modelling and computer analysis design for site-specific modification residues selection. </p> <h2 class="h2_tit page_tab_margin" id="tab4"> Quality Controls Measures </h2> <p> The following quality control measures are employed to create the highest quality monoclonal antibodies commercially available: ELISA against the antigen, HPLC. </p> <p> Other optional <a href="/antibody-engineering-services.html">antibody engineering services</a>: </p> <ul class="ullist"> <li> <a href="/antibody-affinity-maturation.html">Antibody Affinity Maturation</a> </li> <li> <a href="/Antibody-Stability-Improvement.html">Antibody Stability Improvement</a> </li> <li> <a href="/Simianization-of-Non-monkey-Antibodies.html">Simianization of Non-monkey Antibodies</a> </li> <li> <a href="/Antibody-Caninization-Service.html">Monoclonal Antibody Caninization Service</a> </li> <li> <a href="/Antibody-Murinization-Service.html">Monoclonal Antibody Murinization Service</a> </li> </ul> <div class="reference"> <strong>References</strong> <ol class="ollist decimal"> <li> Bernardes, G. J., Steiner, M., Hartmann, I., Neri, D. and Casi, G. (2013) 'Site-specific chemical modification of antibody fragments using traceless cleavable linkers', <i>Nature protocols,</i> 8(11), 2079-2089. </li> <li> Massa, S., Xavier, C., De Vos, J., Caveliers, V., Lahoutte, T., Muyldermans, S. and Devoogdt, N. (2014) 'Site-specific labeling of cysteine-tagged camelid single-domain antibody-fragments for use in molecular imaging', <i>Bioconjugate chemistry,</i> 25(5), 979-988. </li> </ol> </div> <script type="text/javascript"> window.addEventListener('load',function(){ faqlist(4); }); </script> <h2 class="h2_tit page_tab_margin" id="tab5"> FAQ </h2> <ol class="ollist faqlist"> <li> <span class="sFAQTit">What is antibody cysteine modification?</span> <p> Antibody cysteine modification refers to the process of chemically altering cysteine residues within an antibody. This is typically done to enhance the antibody's properties, such as improving its stability, solubility, or therapeutic efficacy. Modifications can include the attachment of drugs, toxins, or other functional groups to the antibody, enabling it to target and interact with specific cells or molecules more effectively. </p> </li> <li> <span class="sFAQTit">Why is cysteine used for antibody modification?</span> <p> Cysteine residues are chosen for modification because they contain a thiol group, which is reactive and can form disulfide bonds. This makes cysteine ideal for conjugation with other molecules. Modifying cysteine residues can help in creating antibody-drug conjugates (ADCs) or enhancing antibody binding affinity and specificity without significantly altering the antibody's overall structure. </p> </li> <li> <span class="sFAQTit">How does cysteine modification affect antibody function?</span> <p> Cysteine modification can significantly enhance an antibody's function in several ways. For instance, by attaching therapeutic drugs to cysteine residues through stable linkers, antibodies can be transformed into highly specific drug delivery systems known as ADCs. These conjugates are designed to deliver cytotoxic drugs directly to tumor cells, minimizing the impact on normal cells and reducing side effects. </p> </li> <li> <span class="sFAQTit">How is the specificity of cysteine modification ensured in antibodies?</span> <p> To ensure specificity in cysteine modification, antibodies may be engineered to include free cysteine residues at specific sites. This engineering allows precise control over where modifications occur, minimizing unwanted alterations in other parts of the antibody. Additionally, protective groups can be used to temporarily block other reactive groups during the modification process, further enhancing specificity. </p> </li> <li> <span class="sFAQTit">What are the applications of antibody cysteine modification in medical research?</span> <p> Modified cysteine residues in antibodies are particularly useful in the development of targeted therapies, such as antibody-drug conjugates (ADCs) used in cancer treatment. These modifications also facilitate the creation of bispecific antibodies, where modification can help in linking two different antibodies or fragments to target multiple antigens or pathways simultaneously. Moreover, cysteine-modified antibodies are used in diagnostic applications, where they may carry labels or probes that enhance detection capabilities. </p> </li> </ol> <h2 class="h2_tit page_tab_margin" id="tab6"> 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>Podcasts</span><span>Infographic</span><span>Flyer</span><span>Case study</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/introduction-of-recombinant-antibody.jpg" alt="" /> </div> <a href="https://youtu.be/0-yZ9dTGg18" target="_blank">Introduction of Recombinant Antibody</a> </div> <div class="col-md-4"> <div class="pagerow_pt_unit"> <img loading="lazy" src="../static/img/development-of-monoclonal-antibodies.jpg" alt="" 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