Anti-alpha-synuclein N103 fragment from rabbit

Alpha-synuclein (UniProt: P37840; also known as Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP) is encoded by the SNCA (also known as NACP, PARK1) gene (Gene ID 6622) in human. Alpha-synuclein is abundantly expressed in the brain and is found in a classic amyloid fibril form within the intra-neuronal Lewy body deposits of Parkinson's disease brains. The physiological function of synucleins is not well understood, but appears to involve membrane interactions, and in particular reversible binding to synaptic vesicle membranes. It may also be involved in the regulation of dopamine release and transport. It is also reported to reduce neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. Genetic alterations of SNCA gene is reported to result in aberrant polymerization into fibrils, which is associated with several neurodegenerative diseases (synucleinopathies). Alpha-synuclein is also sown to serve as a substrate for asparagine endopeptidase (AEP) that cleaves it at N103 in an age-dependent manner. This cleavage triggers alpha-synuclein aggregation and neurotoxicity, which leads to the loss of dopaminergic neurons. Higher activity of AEP has been shown in subjects with Parkinson s disease and knockout of AEP is reported to ameliorate pathological effects of alpha-synuclein in animal models. Mutations in SNCA gene are also known to Parkinson's disease characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. The pathology of Parkinson s disease involves progressive loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies in surviving neurons in various areas of the brain. (Ref.: Zhang, Z et al., (2017), Nat. Struct. Mol. Biol. 24(8); 632-6420).