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Data about performances of whole and monovalent half-fragments antibodies in immunosorbent assays.


ABSTRACT: 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.

SUBMITTER: Susini V 

PROVIDER: S-EPMC7841312 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Data about performances of whole and monovalent half-fragments antibodies in immunosorbent assays.

Susini Vanessa V   Caponi Laura L   Rossi Veronica Lucia VL   Sanesi Antonio A   Romiti Nadia N   Paolicchi Aldo A   Franzini Maria M  

Data in brief 20210120


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],  ...[more]

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