Anti-phospho-SNCA (Ser129)(S22-365R)

Anti-phospho-SNCA (Ser129)(S22-365R)

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Description :Rabbit Polyclonal Antibody

Species :Rabbit

Tag :

Expression System:

Sequence :

Specificity :Recognizes the SNCA protein phosphorylated at serine 129

Cited Applications :WB

Cross Reactivity :Human, Mouse, Bovine, Canine and non-Human Primate

Host :Rabbit, IgG

Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser129 of Rat SNCA conjugated to KLH

Purification :Affinity Chromatography

Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Sample Data :Western blot of rat cortex lysate showing specific labeling of the ~15kDa alpha synuclein protein phosphorylated at Ser129. Immunolabeling is blocked by the phosphopeptide (peptide) used as antigen but not by the corresponding dephosphopeptide (not shown).

Scientific Background :Alpha-synuclein is expressed in the presynaptic terminal of the neuron where it is implicated in the formation of SNARE complexes. Aggregated alpha-synuclein is one of the major components found in the Lewy bodies, which are found in the brains of patients with Parkinson’s disease (PD) and other neurodegenerative disorders (1). In fact, there is evidence to suggest that early onset Parkinson's disease may be caused by a duplication or triplication of one of the alpha synuclein genes (2). Alpha-synuclein is also found in the brains of patients with multiple system atrophy (MSA) and amyotrophic lateral sclerosis (ALS). Recent evidence suggests that phosphorylation of alpha-synuclein at Ser129 plays a role in the formation of inclusions in PD (3,4).

References :
1. Okochi, M. et al: Constitutive phosphorylation of the Parkinson’s disease associated alpha-synuclein. J Biol Chem 2000 Jan 7;275(1): 390-7.

2. Chartier-Harlin, M C. et al: Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 2004 364: 1167-1169.

3. Smith, W W. et al: Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y Cells. J Neurosci 2005 June 8; 25(23):5544-5552.

4. Masliah, E. et al: Effects of alpha-synuclein immunization in a mouse model of Parkinson’s disease. Neuron 2005 Jun 16;46(6):857-868.

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J1274-4.pdf

Research Areas :Cancer, Neurobiology, Cancer, Neurobiology