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An isoform of the oncogenic splice variant AIMP2-DX2 detected by a novel monoclonal antibody
- An isoform of the oncogenic splice variant AIMP2-DX2 detected by a novel monoclonal antibody
- Kim D.G.; Nguyen T.T.H.; Kwon N.H.; Sung J.; Lim S.; Kang E.-J.; Lee J.; Seo W.Y.; Kim A.; Chang Y.S.; Shim H.; Kim S.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Biomolecules vol. 10, no. 6
- AIMP2-DX2; Antibody; Diagnostic marker; Phage display; Splice variant
- MDPI AG
- SCIE; SCOPUS
- Document Type
- AIMP2-DX2, an exon 2-deleted splice variant of AIMP2 (aminoacyl-tRNA synthetase-interacting multifunctional protein 2), is highly expressed in lung cancer and involved in tumor progression in vivo. Oncogenic function of AIMP2-DX2 and its correlation with poor prognosis of cancer patients have been well established; however, the application of this potentially important biomarker to cancer research and diagnosis has been hampered by a lack of antibodies specific for the splice variant, possibly due to the poor immunogenicity and/or stability of AIMP2-DX2. In this study a monoclonal antibody, H5, that specifically recognizes AIMP2-DX2 and its isoforms was generated via rabbit immunization and phage display techniques, using a short peptide corresponding to the exon 1/3 junction sequence as an antigen. Furthermore, based on mutagenesis, limited cleavage, and mass spectrometry studies, it is also suggested that the endogenous isoform of AIMP2-DX2 recognized by H5 is produced by proteolytic cleavage of 33 amino acids from N-terminus and is capable of inducing cell proliferation similarly to the uncleaved protein. H5 monoclonal antibody is applicable to enzyme-linked immunosorbent assay, immunoblot, immunofluorescence, and immunohistochemistry, and expected to be a valuable tool for detecting AIMP2-DX2 with high sensitivity and specificity for research and diagnostic purposes. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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