α-Synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-Synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-Synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-Synuclein-126, lacking residues 41-54; and α-Synuclein-112, which lacks residues 103-130. α-Synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-Synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. α-Synuclein is phosphorylated at low levels under normal physiological conditions whereas the majority of the protein is phosphorylated in Lewy bodies at S129. Phosphorylation of α-Synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson’s disease. In addition, cleavage of α-Synuclein at amino acid 122 was shown to generate a truncated, aggregation-prone fragment, similar to what has been observed in PD and DLB brains. The α-Synuclein Antibody Sampler Kit provides flexibility for sampling and detection of total, truncated and phosho-specific species of α-Synuclein in human tissue.
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