|Application ||WB, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||14460 Da|
|Other Names||Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, SNCA, NACP, PARK1|
|Target/Specificity||A synthetic peptide corresponding to residues on the N-terminus of human Alpha-synuclein was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SNCA Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cytoplasm, cytosol Membrane. Nucleus. Cell junction, synapse. Secreted. Note=Membrane-bound in dopaminergic neurons.|
|Tissue Location||Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals|
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Provided below are standard protocols that you may find useful for product applications.
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).
1. Jakes R, et al. FEBS Lett. 345(1):27-32, 1994.
2. Fujiwara H, et al. Nat Cell Biol 4(2):160-4, 2002.
3. Shimura H, et al. Science 293(5528):263-9, 2001.
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