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A rapid ELISA for the detection of matrix metallopeptidase 9 using a recombinant Fab-type antibody.
Yun, Hui-Seon; Kim, Jong-Pyo; Kim, Eun-Jung; Kim, Byung-Gee; Jeong, Hee-Jin.
Afiliação
  • Yun HS; Department of Biological and Chemical Engineering, Hongik University, Sejong, 30016, Republic of Korea.
  • Kim JP; Department of Biological and Chemical Engineering, Hongik University, Sejong, 30016, Republic of Korea.
  • Kim EJ; BioMAX/N-Bio Institute, Institute of Bioengineering, Seoul National University, Seoul, 08826, Republic of Korea.
  • Kim BG; BioMAX/N-Bio Institute, Institute of Bioengineering, Seoul National University, Seoul, 08826, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
  • Jeong HJ; Department of Biological and Chemical Engineering, Hongik University, Sejong, 30016, Republic of Korea. Electronic address: heejinjeong@hongik.ac.kr.
Biochem Biophys Res Commun ; 636(Pt 1): 184-189, 2022 12 25.
Article em En | MEDLINE | ID: mdl-36334443
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fragmentos Fab das Imunoglobulinas / Escherichia coli Tipo de estudo: Diagnostic_studies Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fragmentos Fab das Imunoglobulinas / Escherichia coli Tipo de estudo: Diagnostic_studies Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2022 Tipo de documento: Article