Purified, stabilized, and native full-length proteins without mutation and truncation play a crucial role in antibody development by serving as high-quality antigens. Their high quality ensures that the antibodies generated in response to these antigens have high specificity and affinity for the target protein, which is essential for the accuracy and reliability of subsequent antibody-based assays and applications. Besides, as antigens for immunization, the full-length and unmodified structure of the protein ensures that the antibodies recognize the natural conformation and epitopes present in the native protein. These antibodies are instrumental in various research, diagnostic, and therapeutic applications, making them essential tools in the field of life sciences and biotechnology.
Purified A2AR protein or a receptor, can be used as antigens to initiate the generation of antibodies, which are specific to A2AR by animal immunization. Eurofins CALIXAR’s Adenosine receptor A2A, with maintained native structure, is able to bind to agonists, antagonists, as well as allosteric modulators. Wild-type, full-length A2AR in CALX condition were evaluated with immunization of 3 mice using ELISA assay. Our purified A2AR exhibits a higher immunogenicity than mutated stabilized protein, which has 8 mutations and C-ter truncation.
STD-NMR reveals that adenosine's ribose moiety undergoes solvent exposure changes upon binding to the A2A receptor (A2AR), in the presence or in the absence of agonists (CGS-21680), with the buried ribose proton structure aligning with the crystal structure from PDB ID: 2YDO (Igonet S et al. 2018).
Eurofins CALIXAR’s Adenosine receptor A2A facilitates reliable fragment-based drug design (FBDD), structure-based drug discovery (SBDD) and antibody discovery corresponding to this specific target. Explore our case studies and discover how Eurofins CALIXAR can contribute to your next scientific breakthrough. For custom inquiries or collaborations, please contact us.
References :
Igonet S et al. 2018
Desuzinges Mandon E. et al. 2017
