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,...

Full description

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/7285/1/43_1_03.pdf
_version_ 1796930510932410368
author Wei, T.C.
Shamsuddin, S.
author_facet Wei, T.C.
Shamsuddin, S.
author_sort Wei, T.C.
collection UKM
description 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.
first_indexed 2024-03-06T04:04:07Z
format Article
id ukm.eprints-7285
institution Universiti Kebangsaan Malaysia
language English
last_indexed 2024-03-06T04:04:07Z
publishDate 2014
publisher Penerbit Universiti Kebangsaan Malaysia
record_format dspace
spelling ukm.eprints-72852016-12-14T06:43:38Z http://journalarticle.ukm.my/7285/ Epitope mapping of Anti-YB-1 antibodies using truncated proteins Wei, T.C. Shamsuddin, S. 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. Penerbit Universiti Kebangsaan Malaysia 2014-06 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/7285/1/43_1_03.pdf Wei, T.C. and Shamsuddin, S. (2014) Epitope mapping of Anti-YB-1 antibodies using truncated proteins. Malaysian Applied Biology, 43 (1). pp. 21-30. ISSN 0126-8643 http://mabjournal.com/
spellingShingle Wei, T.C.
Shamsuddin, S.
Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title_full Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title_fullStr Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title_full_unstemmed Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title_short Epitope mapping of Anti-YB-1 antibodies using truncated proteins
title_sort epitope mapping of anti yb 1 antibodies using truncated proteins
url http://journalarticle.ukm.my/7285/1/43_1_03.pdf
work_keys_str_mv AT weitc epitopemappingofantiyb1antibodiesusingtruncatedproteins
AT shamsuddins epitopemappingofantiyb1antibodiesusingtruncatedproteins