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A rapid ELISA for the detection of matrix metallopeptidase 9 using a recombinant Fab-type antibody
- Authors
- Yun, H.-S.; Kim, J.-P.; Kim, E.-J.; Kim, B.-G.; Jeong, H.-J.
- Issue Date
- 25-Dec-2022
- Publisher
- NLM (Medline)
- Keywords
- Enzyme-linked immunosorbent assay; Escherichia coli expression; Matrix metalloproteinase 9; Point-of-care testing; Recombinant fragment antigen-binding
- Citation
- Biochemical and biophysical research communications, v.636, pp.184 - 189
- Journal Title
- Biochemical and biophysical research communications
- Volume
- 636
- Start Page
- 184
- End Page
- 189
- ISSN
- 0006-291X
- Abstract
- Matrix metalloproteinase 9 (MMP9) contributes to several aspects of inflammation and cancer pathology, including invasion, metastasis, and angiogenesis. In this study, we expressed a recombinant fragment antigen-binding (Fab)-type anti-MMP9 antibody in Escherichia coli with high purity within five days and confirmed the nanomolar order of antigen-binding efficiency of the recombinant Fab. Moreover, we optimized the experimental time for performing enzyme-linked immunosorbent assay (ELISA), and decreased the reaction time from the conventional 20.5 h to 3.5 h. The rapid and sensitive MMP9 detection system developed in this study can be applied to a range of applications, including the diagnosis of diseases with MMP9 overexpression including inflammatory and cancer-related diseases. Copyright © 2022 Elsevier Inc. All rights reserved.
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Related Researcher
- Jeong, Hee-Jin
- Science & Technology (Biological and Chemical Engineering)