AI Article Synopsis
- Researchers aimed to create a reliable detection method for S100A8, a protein linked to inflammation and cancer, by developing a high-affinity monoclonal antibody.
- They produced a soluble and pure recombinant S100A8 protein using E. coli and then immunized mice to generate antibodies through hybridoma technology.
- The successful identification of the antibody's sequence will facilitate the creation of hybridoma cell lines and recombinant antibodies for research and clinical uses.
Article Abstract
Objectives: S100A8 is highly expressed in several inflammatory and oncological conditions. To address the current lack of a reliable and sensitive detection method for S100A8, we generated a monoclonal antibody with a high binding affinity to human S100A8 to enable early disease diagnosis.
Results: A soluble recombinant S100A8 protein with a high yield and purity was produced using Escherichia coli. Next, mice were immunized with recombinant S100A8 to obtain anti-human S100A8 monoclonal antibodies using hybridoma technology. Lastly, the high binding activity of the antibody was confirmed and its sequence was identified.
Conclusions: This method, including the production of antigens and antibodies, will be useful for the generation of hybridoma cell lines that produce anti-S100A8 monoclonal antibodies. Moreover, the sequence information of the antibody can be used to develop a recombinant antibody for use in various research and clinical applications.
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| http://dx.doi.org/10.1007/s10529-023-03364-0 | DOI Listing |
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