Synphilin-1 (synuclein a-interacting protein 1, SNCAIP), is a cytoplasmic protein that interacts with α-synuclein in neurons. Synphilin-1 contains several protein-protein interaction domains, including six ankyrin-like repeats, coiled-coil domain, and an ATP/GTP binding domain. The synphilin gene produces at least nine transcript variants encoding seven distinct proteins. Synphilin transcripts are widely expressed in many tissues with highest levels found in the brain, heart and placenta. Synphilin-1 is highly enriched in presynaptic nerve terminals.

synthetic peptide corresponding to amino acids 829-847 of human synphilin, conjugated to KLH. This sequence is identical in dog synphilin-1 and highly conserved (84% identity) in mouse, rat, and bovine synphilin-1.

Anti-Synphilin-1 antibody produced in rabbit has been used in co-immunoprecipitation and western blotting.

Synphilin-1 associates with and is ubiquitinated by several proteins, including α -synuclein, parkin, dorfin and siah E3 ubiquitin protein ligase 1 (SIAH1), and is a major component of Lewy bodies in Parkinson′s disease (PD). It is associated with synaptic vesicles and is modulated by α-synuclein. The central domain of synphilin-1 has been suggested to be required for the formation of aggregates and cytotoxicity. Synphilin-1 association with α -synuclein promotes the formation of cytosolic inclusions. Mutation of synphilin-1 in PD patients at amino acid R621C, is implicated in these sequestration, ubiquitination and proteasomal inhibition leading to increased accumulation of toxic intermediates. Cells with this mutation are more prone to staurosporine-induced cell death highlighting its cytoprotective functionality. In human postmortem brain tissue, synphilin-1, like a-synuclein is present in neurophil.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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