Phospho alpha-Synuclein (S129) Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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).
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Background: alpha-Synuclein
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.
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- Goers, J. et al. (2003) Biochemistry 42:8465.
- Ahn, B-H. et al. (2002) J. Biol. Chem. 277:12334.
Product Datasheets
Citation for Phospho alpha-Synuclein (S129) Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Chronic Mild Gut Inflammation Accelerates Brain Neuropathology and Motor Dysfunction in alpha -Synuclein Mutant Mice
Authors: Yuki Kishimoto, Wandi Zhu, Waki Hosoda, Jyoti M. Sen, Mark P. Mattson
NeuroMolecular Medicine
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