Anti-alpha-Synuclein Antibody, oligomer-specific Syn33 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 a membrane-bound protein in dopaminergic neurons that is involved in the regulation of dopamine release and transport. It is also reported to induce fibrillization of microtubule-associated protein tau and reduces neuronal responsiveness to various apoptotic stimuli. Aggregation of alpha-synuclein is known to be a causative factor in the development of Parkinson's disease (PD), which leads to the degeneration of dopaminergic neurons in the substantia nigra (SN) in the midbrain region. Aggregates of alpha-synuclein are present in Lewy bodies. Alpha-synuclein can be phosphorylated, predominantly on serine residues by casein kinase 1. Phosphorylation of Ser129 is reported to be selective and extensive in synucleinopathy lesions and promotes insoluble fibril formation. Mutations in the SNCA gene produce defective alpha-synuclein that induces conformational changes making it more prone to self-aggregation and deposition in Lewy bodies. Mutant forms of alpha-synuclein impair synaptic vesicle formation, elevate cytoplasmic levels of dopamine, and increases superoxide radicals, which lead to oxidative stress and misfolding of alpha-synuclein.