Detection of Phospho-Synuclein-alpha (S129) by Western Blot
Western Blot of rat cortex lysate showing specific labeling of the ~15 kDa Synuclein-alpha protein phosphorylated at S129. Immunolabeling is blocked by the phosphopeptide (peptide) used as antigen but not by the corresponding dephosphopeptide (not shown).
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
For long-term storage, ≤ -20° C is recommended. Product is stable at ≤ -20° C for at least 1 year.
Synuclein-alpha is a 14 kDa member of the synuclein family. It is found in both the neuron nucleus and the cytosol of presynaptic nerve terminals in the brain. Synuclein-alpha is 140 amino acids in length and runs anomalously at 19 kDa in SDS-page. It contains three domains; an N-terminal lipid-binding domain, a central amyloid-binding region, and a C-terminal acidic tail. The N-terminal area (aa 1 - 100) is involved with lipid (membrane) and protein binding. The C-terminus may be regulatory. There is a NAC (non-Ab component of AD amyloid) segment between aa 61 - 95. This has been thought to mediate synuclein-alpha filament formation and microtubial stabilization. Whether it exists as a stand-alone normal cleavage product of synuclein-alpha is unclear. Synuclein-alpha is phosphorylated on multiple sites. S129 undergoes constitutive phosphorylation and dephosphorylation. When phosphorylated, filament formation (and perhaps oligomerization) is promoted. Uncontrolled filament/fibril formation is suggested to be involved in Parkinson’s disease Lewy body formation. Tyrosine phosphorylation also occurs at Y125. Synuclein-alpha is known to bind to, and inhibit, PLD-1 and -2. When phosphorylated at Y125, synuclein-alpha activity is decreased and PLD activity is increased.
da Costa, C.A. (2003) Curr. Mol. Med. 3:17.
Ueda, K. et al. (1993) Proc. Natl. Acad. Sci. USA 90:11282.
alpha-Synuclein; Lewy body) 4; MGC110988; NACP; non A-beta component of AD amyloid; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; non-A4 component of amyloid; PARK1; PARK4; PD1; SNCA; synuclein, alpha (non A4 component of amyloid precursor); Synuclein-alpha
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