The Immunogen: Alpha synuclein is a member of the synuclein family, the other two proteins being beta and gamma synuclein. Alpha synuclein was originally isolated as a major synaptic vesicle associated protein from the electric organ of the fish Torpedo (1). Direct homologues of alpha-synuclein are found in all vertebrates. Later work connected alpha-synuclein with human brain pathology, when a protein originally identified as a component of NAC, the "Non-Amyloid beta Component of Alzheimer's disease amyloid" proved to be a peptide derived from alpha-synuclein (2). The alpha-synuclein protein is therefore sometimes known as NAC precursor or NACP. Further work showed that alpha-synuclein is a major component of the Lewy bodies of Parkinson's disease and point mutations of alpha-synuclein proved to be causative of some forms of familial Parkinson's disease (3, 4, 5). Early onset Parkinson's disease may be caused by a duplication or triplication of one of the Alphasynuclein genes (6, 7). However, despite being discovered as as component of amyloid preparations, alpha-synuclein is apparently not a major component of the senile plaques of Alzheimer's disease (6). Early onset Parkinson's disease may be caused by a duplication or triplication of one of the alpha synuclein genes (7, 8). Alpha-synuclein is also found in the Lewy bodies of patients with diffuse Lewy body disease and inclusions in glial cells in the brains of patients with multiple system atrophy (MSA) and amyotrophic lateral sclerosis (ALS). Alpha-synuclein is heavily expressed in brain and appears to be localized primarily to presynaptic regions, though not with a typical synaptic vesicle distribution pattern. The synuclein proteins appear to have little 3D structure in solution, and probably belong to the family of "intrinsically unstructured proteins" which only adopt a well-defined conformation when bound to other proteins or membrane lipids (9). An excellent recent review of the role of alpha-synuclein in health and disease was recently published by Mark Cookson (10).

Figures: Left: Blots of MCA-3H9 on recombinant alpha-synuclein (left lane) and crude extract of mouse brain (right lane, courtesy Rogan Tinsley, Howard Florey Institute, University of Melbourne). Right: Mixed neuron-glial cultures stained with MCA-3H9, our monoclonal antibody to alpha-synuclein (red) and chicken polylclonal antibody to MAP2 CPCA-MAP2 (green). The alpha-synuclein antibody stains vesicular structures the perikarya and processes of the neurons in this image.

Antibody characteristics: MCA-3H9 is a mouse IgG1 class antibody. MCA-3H9 recognizes full length human and rodent alpha-synuclein specifically both in western blots and in immunocytochemical experiments. The epitope for MCA-3H9 is in the region 61-95 which correspond to the "Non-Amyloid beta Component of Alzheimer's disease amyloid" (NAC, see above also see here). MCA-3H9 will also bind human alpha-synuclein containing the A30P and A53T mutations.

Suggestions for use: Try at dilutions of 1:1,000 and higher for immunofluorescence.

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References:

1. Maroteaux, L., J.T. Campanelli, and R.H. Scheller. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8:2804-2815 (1988).

2. Lavedan, C. The Synuclein Family. Genome Research 8:871-880 (1998).

3. Polymeropoulos, MH et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276: 2045-2047 (1997).

4. Kruger, R et al. Ala30-to-Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature Genet. 18: 106-108 (1998).

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

6. Singleton, AB.et al. Alpha-synuclein locus triplication causes Parkinson's disease. Science 302: 841 (2003).

7. Culvenor, J.G. et al. Non-Abeta component of Alzheimer's disease amyloid (NAC) revisited: NAC and alpha-synuclein are not associated with Abeta amyloid. Am. J. Pathol. 155:1173-1181 (1999).

8. Ibanez, P. et al. Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease. Lancet 364:1169-1171 (2004).

9. Dyson, HJ. and Wright, PE. Intrinsically unstructured proteins and their functions. Nature Reviews of Molecular and Cellular Biology 6:197-208 (2005).

10. Cookson MR. Alpha-Synuclein and neuronal cell death. Mol Neurodeg 4:9 (2009).

Limitations: This product is for research use only and is not approved for use in humans or in clinical diagnosis.

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