| Literature DB >> 9598980 |
J M Dore1, F Morard, N Vita, J Wijdenes.
Abstract
Using a phage display peptide library, we characterized the epitope of two monoclonal antibodies reacting with syndecan-1: B-B2 and B-B4. The identified epitopes QDIT, for B-B2, and LPEV, for B-B4, were found to align with residues 36-39 and 90-93 of the mature protein, respectively. In contrast to B-B4, the B-B2 epitope is close to a potential glycosaminoglycan attachment site. Since syndecan-1 is heavily glycosylated and post-translational modifications are cell type specific, these results might explain the differences observed in the reactivity pattern of B-B2 and B-B4 and suggest that these monoclonal antibodies are useful probes to study cell surface exposed syndecan-1.Entities:
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Year: 1998 PMID: 9598980 DOI: 10.1016/s0014-5793(98)00310-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124