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α-Synuclein is a 140-amino acid intracellular protein encoded by the SNCA gene in humans.1 It is primarily localized to the synaptic terminal of neurons in both the central and peripheral nervous systems where it has a role in regulation of synaptic vesicle docking and neurotransmitter release.2 α-Synuclein is an intrinsically disordered, multi-domain protein composed of a negatively charged C-terminal domain that provides structural flexibility, a central hydrophobic region with a high propensity to aggregate, and a positively charged N-terminal domain containing a repeated consensus sequence KTKEGV.1,3 It exists as a monomer in the cytoplasm, however, mutations, posttranslational modifications, and changes in cellular environmental conditions can induce oligomerization and aggregate formation. Aggregated α-synuclein is found in Lewy bodies that occur in Parkinson’s disease and diffuse Lewy body disease, as well as in glial cells in postmortem brains from patients with multiple system atrophy (MSA) and amyotrophic lateral sclerosis (ALS). Cayman's α-Synuclein Rabbit Monoclonal Antibody (Clone RM492) can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes α-synuclein at approximately 15 kDa from human, mouse, and rat samples.
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1. Structure, function and toxicity of alpha-
2. Alpha-
3. The function of α-