Epitope mapping of Anti-YB-1 antibodies using truncated proteins

Increased expression and nuclear localization of Y-box-binding protein-1 (YB-1) are associated with drug resistance and tumor progression. Detection of YB-1 primarily depends on the recognition of YB-1 antibody on its epitopes. To determine the epitopes binding of anti-YB-1 A-16 and 59-Q antibodies,...

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Bibliographic Details
Main Authors: Wei, T.C., Shamsuddin, S.
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2014
Online Access:http://journalarticle.ukm.my/7285/
http://journalarticle.ukm.my/7285/
http://journalarticle.ukm.my/7285/1/43_1_03.pdf
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Summary:Increased expression and nuclear localization of Y-box-binding protein-1 (YB-1) are associated with drug resistance and tumor progression. Detection of YB-1 primarily depends on the recognition of YB-1 antibody on its epitopes. To determine the epitopes binding of anti-YB-1 A-16 and 59-Q antibodies, three YB-1 truncated proteins were generated using bacterial expression system and their aberrant migration were reported. Epitope mapping analyses revealed anti-YB-1 A-16 antibody recognized epitope at 1-127 amino acid residues of YB-1, whereas 59-Q antibody was reactive with epitope at 61-127 amino acid residues. Based on our findings, 59-Q antibody was suggested used in the future study to avoid ambiguity.