Alpha-Synuclein is expressed predominantly in brain, where it is concentrated in presynaptic nerve terminals (1). The deposition of the abundant presynaptic brain protein alpha-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of neurodegenerative disorders. These disorders include Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, collectively referred to as synucleinopathies. Phosphorylation of alpha-synuclein at Ser 129 promoted fibril formation in vitro and these results highlight the importance of phosphorylation of filamentous proteins in the pathogenesis of neurodegenerative disorders (2). Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin. It is hypothesized that parkin and alpha-synculein interact functionally, namely, that parkin ubiquitinates alpha-synuclein normally and that this process is altered in autosomal recessive PD (3).
EGFR1 Signaling Pathway
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