The use of monoclonal antibodies for the treatment of diseases has increased in recent years. The pre-clinical and clinical development of antibody drugs requires intensive pharmacokinetic and immune response testing in non-human and human subjects.
This usually involves the use of anti-idiotypic antibodies, which are basically antibodies that bind to specific regions of other antibodies. To know more about antibodies, you can also check out the Boster Bio featured products online.
To be effective, these anti-idiotypic antibodies must have high affinity and specificity. In addition, they must be easy to manufacture and available in constant quality throughout the drug development process to avoid the need for new sources of reagents.
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Phage display from a large library of recombinant antibodies can be used to rapidly generate anti-idiotypic antibodies against any paratope antibody. However, the affinity of the antibody to its target antigen is an important aspect that determines the effectiveness of these anti-idiotypic antibodies in pharmacokinetic assays and immune responses.
Thus, antibody selection based on binding strength can significantly increase the sensitivity of the assay. This is a challenge in antibody manufacturing projects because several unique antibody candidates are created after initial screening.
Only a small proportion of these antibodies were brought in for further characterization, and because they were selected on the basis of specific binding in the ELISA and not on other properties such as binding strength, high-affinity antibodies, which might perform better in certain analyses, were negligible.
A similar procedure was performed with an anti-trastuzumab antibody and one of the resulting anti-trastuzumab antibodies underwent an affinity maturation process that increased the affinity range to 65 m – 4 nM. In this case, the addition of a secondary screening step also allows detection of the antibody with the lowest Koff coefficient.