Phospho alpha-Synuclein (S129) Antibody

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PPS091
Detection of Phospho-Synuclein-alpha  (S129) by Western Blot
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Phospho alpha-Synuclein (S129) Antibody Summary

Species Reactivity
Human, Mouse, Rat, Bovine, Canine, Primate
Specificity
Human, mouse, rat, bovine, canine, and non-human primate Synuclein-alpha phosphorylated at S129
Source
Polyclonal Rabbit IgG
Purification
Antigen Affinity-purified
Immunogen
Phosphopeptide corresponding to amino acid residues surrounding the phospho-S129 of Synuclein-alpha
Formulation
100 μL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 μg/mL BSA, and 50% glycerol.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
1:1000 dilution
See below

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

Western Blot Detection of Phospho-Synuclein-a (S129) antibody by Western Blot View Larger

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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Preparation and Storage

Shipping
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.

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.

References
  1. da Costa, C.A. (2003) Curr. Mol. Med. 3:17.
  2. Ueda, K. et al. (1993) Proc. Natl. Acad. Sci. USA 90:11282.
  3. Okochi, M. et al. (2000) J. Biol. Chem. 275:390.
  4. Goers, J. et al. (2003) Biochemistry 42:8465.
  5. Ahn, B-H. et al. (2002) J. Biol. Chem. 277:12334.
Entrez Gene IDs
6622 (Human); 20617 (Mouse); 29219 (Rat); 641350 (Porcine); 282857 (Bovine)
Alternate Names
alpha-Synuclein; I+/--synuclein; MGC110988; NACP; non A-beta component of AD amyloid; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; PARK1; PARK4; PD1; SNCA; synuclein alpha-140; synuclein, alpha (non A4 component of amyloid precursor); Synuclein-alpha; truncated alpha synuclein

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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

  1. 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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