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    Epitope mapping and specificity of the anti-alpha-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines. 
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    • Epitope mapping and specificity of the anti-alpha-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines.
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    • School of Biological and Chemical Sciences
    • School of Biological and Chemical Sciences
    • Epitope mapping and specificity of the anti-alpha-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines.
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    Epitope mapping and specificity of the anti-alpha-synuclein monoclonal antibody Syn-1 in mouse brain and cultured cell lines.

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    Published version
    Embargoed until: 2100-01-01
    Reason: VoR
    Volume
    349
    Pagination
    133 - 135
    Journal
    Neurosci Lett
    Issue
    2
    ISSN
    0304-3940
    Metadata
    Show full item record
    Abstract
    While alpha- and beta-synuclein largely overlap in their expression in the vertebrate brain, only alpha-synuclein accumulates in the fibrillar aggregates typical of Parkinson's disease. It is thus critical to have immunological reagents that distinguish between these two protein isoforms. The monoclonal antibody Syn-1 (Transduction Labs) has been frequently used for the specific detection of alpha-synuclein. In this report, the epitope for Syn-1 is localized within residues 91-99 of human alpha-synuclein. Sequence differences exist in this domain that account for the specificity of Syn-1 for alpha- versus beta-synuclein. However, Syn-1 also displays reactivity with additional species (approximately 45 kDa) in brain homogenates from both wild-type and alpha-synuclein null mice, indicating a potential for cross-reactivity with a protein species that is unrelated to alpha-synuclein in brain tissue or extracts.
    Authors
    Perrin, RJ; Payton, JE; Barnett, DH; Wraight, CL; Woods, WS; Ye, L; George, JM
    URI
    http://qmro.qmul.ac.uk/xmlui/handle/123456789/2819
    Collections
    • School of Biological and Chemical Sciences [1689]
    Language
    eng
    Copyright statements
    Copyright © 2003 Elsevier Ireland Ltd.
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