Phospho-Synuclein-α (S129) Polyclonal Antibody, 100µg, (ATB-P0258)

Description

Background:

Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer’s disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene. [provided by RefSeq, Mar 2009]

May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.

Product datasheet:

Overview
Product Description	Phospho-Synuclein-α (S129) Polyclonal Antibody, 100µg, (ATB-P0258)
Image
Species Reactivities	Human,Mouse,Rat
Immunogen	Synthesized peptide derived from human Synuclein-α around the phosphorylation site of S129.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. Membrane interactions and fibrillization of α-synuclein play an essential role in membrane disruption. Chaudhary H, et al. FEBS Lett, 2014 Nov 28. PMID 25448986
2. Early and persistent expression of phosphorylated α-synuclein in the enteric nervous system of A53T mutant human α-synuclein transgenic mice. Bencsik A, et al. J Neuropathol Exp Neurol, 2014 Dec. PMID 25383638
3. The newly discovered Parkinson’s disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding. Ghosh D, et al. Biochemistry, 2014 Oct 21. PMID 25268550
4. Besides fibrillization: putative role of the peptide fragment 71-82 on the structural and assembly behavior of α-synuclein. Bédard L, et al. Biochemistry, 2014 Oct 21. PMID 25255476
5. Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions. Shahpasandzadeh H, et al. J Biol Chem, 2014 Nov 7. PMID 25231978
6. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
   Ueda K., Fukushima H., Masliah E., Xia Y., Iwai A., Yoshimoto M., Otero D.A., Kondo J., Ihara Y., Saitoh T.
   Proc. Natl. Acad. Sci. U.S.A. 90:11282-11286(1993) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 61-95. Tissue: Brain.
7. The NACP/synuclein gene: chromosomal assignment and screening for alterations in Alzheimer disease.
   Campion D., Martin C., Heilig R., Charbonnier F., Moreau V., Flaman J.-M., Petit J.-L., Hannequin D., Brice A., Frebourg T.
   Genomics 26:254-257(1995) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2-4 AND 2-5).
8. Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer’s disease amyloid.
   Ueda K., Saitoh T., Mori H.
   Biochem. Biophys. Res. Commun. 205:1366-1372(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2-4). Tissue: Brain.
9. Xia Y., Silva R.D., Chen X.H., Saitoh T.
   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
10. Human and mouse alpha-synuclein genes: comparative genomic sequence analysis and identification of a novel gene regulatory element.
    Touchman J.W., Dehejia A., Chiba-Falek O., Cabin D.E., Schwartz J.R., Orrison B.M., Polymeropoulos M.H., Nussbaum R.L.
    Genome Res. 11:78-86(2001) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2-4).