Abstract
The neuronal phosphoprotein α-synuclein has been increasingly implicated in the pathogenesis of Parkinson's disease (PD) and other neurodegenerative diseases; however, the exact function of α-synuclein still remains illusive. Suitable antibodies (Abs) specific for the gene of interest are indispensable for studying biological and immunological properties of the target gene. Here, we report not only the generation and characterization of monoclonal Abs, Syn-1 and Syn-17, against human α-synuclein, but also the epitope mapping by using recombinant synuclein family proteins and various GST fusion proteins of human α-synuclein domains. Syn-17 recognizes human and rodent α-synuclein, and its epitope is localized within residues 97–99 and 101 of α-synuclein. In contrast, the Syn-1 epitope is localized in residues 121 and 122 of human α-synuclein, and Syn-1 recognizes only human but not rodent α-synuclein, indicating that it can be utilized as a useful reagent for studying human α-synuclein transgenic mouse and zebrafish lines.
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