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Published on: July 14, 2023
Data about performances of whole and monovalent half-fragments antibodies in immunosorbent assays
Vanessa Susini1, Laura Caponi1, Veronica Lucia Rossi2
1Department of Translational Research and of New Surgical and Medical Technologies, University of Pisa, via Savi 10, Pisa, Italy.
The data here presented are related to the research article entitled "Sensitivity and reproducibility enhancement in enzyme immunosorbent assays based on half fragment antibodies" [1] aimed to compare the performance in ELISA of whole antibodies and their corresponding monovalent half-fragments obtained by reduction. Half-fragment antibodies represent an interesting method to orient antibodies in high-sensitive immunoassays taking advantage of the free sulfhydryl groups of the hinge region [2], [3], [4] that allow their oriented binding on maleimide functionalized microplates. Data here presented describe the contribution of both chemical reduction and orientation on the antigen binding capacity of whole and half-fragments antibodies. For this purpose, monoclonal anti-horseradish peroxidase (anti-HRP) or monoclonal anti-fPSA antibodies, and their respective half-fragments, were coated on polystyrene or maleimide functionalized microplates. The antigen binding capability was analyzed by in-house enzyme linked immunosorbent assays. These data would be used for further studies on the development of oriented immunoassays based on half fragment antibodies.
The data here presented are related to the research article entitled "Sensitivity and reproducibility enhancement in enzyme immunosorbent assays based on half fragment antibodies" [1] aimed to compare the performance in ELISA of whole antibodies and their corresponding monovalent half-fragments obtained by reduction. Half-fragment antibodies represent an interesting method to orient antibodies in high-sensitive immunoassays taking advantage of the free sulfhydryl groups of the hinge region [2], [3], [4] that allow their oriented binding on maleimide functionalized microplates. Data here presented describe the contribution of both chemical reduction and orientation on the antigen binding capacity of whole and half-fragments antibodies. For this purpose, monoclonal anti-horseradish peroxidase (anti-HRP) or monoclonal anti-fPSA antibodies, and their respective half-fragments, were coated on polystyrene or maleimide functionalized microplates. The antigen binding capability was analyzed by in-house enzyme linked immunosorbent assays. These data would be used for further studies on the development of oriented immunoassays based on half fragment antibodies.
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