Synuclein cDNA was isolated from Torpedo californica and found to encode a 143 amino acid neuron-specific protein. In addition, a rat brain cDNA library yielded several clones that encode different proteins with homology to Torpedo Synuclein. A 140 amino acid protein in rat is referred to as Synuclein-1. In situ hybridization shows synuclein mRNAs in discrete areas of rat brain, notably the hippocampus. In humans, two synuclein proteins of 140 and 134 amino acids were sequenced that exhibit a high degree of homology with each other (61% identity) and with previously described Synuclein proteins. The 140 amino acid protein (α-Synuclein) is the human homologue of rat Synuclein-1 and is identical to the non-amyloid-β component precursor (NACP), a presynaptic protein involved in amyloidogenesis in Alzheimer's disease (AD). The 134 amino acid protein (β-Synuclein) is the human homologue of bovine phosphoneuroprotein. These proteins are expressed in brain, primarily in presynaptic nerve terminals. Although the exact function of the Synucleins has not been determined, they have been linked to the prominent neurodegenerative disorders AD and Parkinson's disease.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.