Antibody Camelization (Convert to Single Domain Ab) Service

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Currently, we are able to provide the antibody camelization service for our customers all over the world. </p> <h2 class="h2_tit page_tab_margin" id="tab1"> Introduction of Antibody Camelization </h2> <p> Single domain antibodies (sdAbs) are antibody fragments derived from camelids’ heavy-chain antibody (V<sub>H</sub>H) or cartilaginous fishes’ IgNAR (V<sub>NAR</sub>). However, the non-human nature of V<sub>H</sub>Hs results in immunogenicity issues so that limits their use in human immunotherapy. </p> <p> In the meantime, human V<sub>H</sub> is an ideal candidate for therapeutic applications because of the least immunogenicity. However, monomeric human V<sub>H</sub> derived from conventional antibody is tend to aggregation and thus difficult to generate. </p> <p> Camelization refers to the approach that key solubilizing residues from camelid sdAb are introduced into human V<sub>H</sub> to generate monomeric human V<sub>H</sub>. Furthermore, the CDR3 codons of such a ‘camelized’ V<sub>H</sub> are then randomized to obtain a synthetic library from which to retrieve binders. </p> <p class="ServiceShowPic"> <img src="static/img/2-9-Antibody-Camelization-fig1.png" width="699" alt="Ribbon drawings of the human Pot VH (left) and the camelid VHH, cAb-HUL06" /> Fig.1 Ribbon drawings of the human Pot V<sub>H</sub> (left) and the camelid V<sub>H</sub>H, cAb-HUL06 (right). </p> <h2 class="h2_tit page_tab_margin" id="tab2"> Sites Mutation for Camelization </h2> <p> Antibody gene structure and sequence analysis showed that there are several amino acid residues in antibody framework region 2 involved in the interaction of V<sub>H</sub>/VL interface, while these residues are changed in sdAbs for better characterizations. Using this feature, the hydrophobic amino acid residues at positions of human VH FR2 region can be replaced with corresponding hydrophilic amino acids in sdAbs. Studies have shown that the ‘camelized’ V<sub>H</sub> not only maintains the specificity and affinity of the original antibody but also has greatly improved stability and solubility. In addition, the introduction of an additional disulfide bridge between CDR1 and CDR3 also increases thermal stability. </p> <h2 class="h2_tit page_tab_margin" id="tab3"> Synthetic Library for Camelization </h2> <p> CDR3 is the major contributor to most antigen-binding sites and the stability and solubility of antibody domains are dependent on CDR3 partly. According to the site mutation, a human VH can be reshaped in its framework 2 region to mimic the V<sub>H</sub>H. Meanwhile, the synthetic library based on randomized CDR3 codons is constructed to retrieve binders. While the exclusion of CDR1 and CDR2 randomization compromises library complexity, the design simplicity of CDR3 randomization remains an attractive choice.<strong></strong> </p> <h2 class="h2_tit page_tab_margin" id="tab4"> Features of Camelized Antibodies </h2> <ul class="ullist"> <li> Immunization is avoided </li> <li> High expression yield </li> <li> High refoldability </li> <li> Resistance to aggregation </li> <li> Maintained specificity and affinity </li> <li> Improved stability and solubilit </li> </ul> <p class="ServiceShowPic"> <img src="static/img/Antibody Camelization Service.jpg" alt="(Human) Antibody Camelization Services" /> Fig.2 (A) From left to right the composition of a classical antibody (left), a heavy-chain antibody (middle) and a single domain antigen-binding entity derived from a heavy-chain antibody, the V<sub>H</sub>H or single domain antibody (right). (B) The sequence organization of the V<sub>H</sub> and V<sub>H</sub>H with framework and CDR’s is schematically represented at the top of this panel. Below is the folded structure of the V<sub>H</sub> (left) and V<sub>H</sub>H domain (right with its four β-stranded sheets (back) and the five β-stranded sheets in front). </p> <p> Besides the common residues mutation and library construction, our service is built to meet the customer’s project and assay-specific requirements for antibody camelization. If you are interested in our service, please do not hesitate to <a class="inquiry-button">contact us</a> for more details. </p><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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