Anti-Synphilin-1 (C-terminal) antibody produced in rabbit

Synphilin-1 (synuclein a-interacting protein 1, SNCAIP), is a cytoplasmic protein with six ankyrin-like repeats, coiled-coil domain, and an ATP/GTP binding domain. It is highly expressed in brain, heart, placenta and presynaptic nerve terminals. The synphilin gene produces at least nine transcript variants encoding seven distinct proteins.

synthetic peptide corresponding to amino acids 911-919 of human synphilin-1, conjugated to KLH. This sequence is identical in several species including mouse, rat, and dog synphilin-1.

Anti-Synphilin-1 (C-terminal) antibody produced in rabbit has been used in immunoblotting.

Cells with this mutation are more prone to staurosporine-induced cell death highlighting its cytoprotective functionality. 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). In synaptic vesicles it 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. In human postmortem brain tissue, synphilin-1, like a-synuclein is present in neurophil. Mutation of synphilin-1 in PD patients at amino acid R621C, is implicated in the sequestration, ubiquitination and proteasomal inhibition leading to increased accumulation of toxic intermediates.

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

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