α-Synuclein has emerged as a biomarker for Parkinson’s disease (PD) and a number of other α-Synuclein related disorders collectively termed as Synucleinopathies. α-Synuclein serves as a common link between inherited and sporadic forms of PD, as this protein and its post-translationally modified (PTM) forms are found in large and insoluble proteinaceous deposits known as Lewy bodies (LBs) and Lewy neurites. These PTMs, including phosphorylation and truncation, have been shown to promote aggregation and oligomerization of α-Synuclein, and play an important role in the pathogenesis of PD.
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Phosphorylated α-Synuclein at serine residue 129 (pS129) was shown to make up the majority of this protein in inclusions isolated from the postmortem tissues derived from patients with PD and other Synucleinopathies. Therefore, pS129 has emerged as a hallmark of pathology in these disorders. Clone P-syn/81A can be used to detect pS129 by IHC.
Studies from PD-like animal and cell culture models, as well as further investigations into the constituents within LBs, have shown additional α-Synuclein phospho-species such as phosphorylated residues tyrosine 39 and serine 87. Clone A15119B can be used to detect α-Synuclein Phospho (Tyr39).
Clone A15115A detects the native and phosphorylated serine 87 forms, and can be used for both IHC and western blotting.
Biochemical and mass spectrometry analyses of α-Synuclein derived from LBs have also detected C-terminal truncated forms of this protein including a species that terminates at asparagine 122. Clone A15127A detects this truncated form and can be used for IHC.
Clone A15126D also detects truncated α-Synuclein at residue 122, and can be used for both IHC and western blotting.


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