alpha-Synuclein Products

Antibodies
alpha-Synuclein Antibody
alpha-Synuclein Antibody
Species: Hu, Mu, Rt, Po, Bv, Pm, Sh
Applications: WB, ICC/IF, IHC, IHC-Fr, IHC-P
Host: Rabbit Polyclonal
alpha-Synuclein Antibody
alpha-Synuclein Antibody
NBP2-25146
Species: Hu, Mu, Rt, Po, Bv, Eq
Applications: WB, ICC/IF, IHC, IHC-FrFl
Host: Chicken Polyclonal
ELISA Kits
Human alpha-Synuclein ELISA K ...
Human alpha-Synuclein ELISA Kit (C...
NBP2-62748
Species: Hu
Applications: ELISA
Human alpha-Synuclein DuoSet ...
Human alpha-Synuclein DuoSet ELISA...
DY1338-05
Species: Hu
Applications: ELISA
Mouse alpha-Synuclein ELISA K ...
Mouse alpha-Synuclein ELISA Kit (C...
NBP3-08174
Species: Mu
Applications: ELISA
Lysates
alpha-Synuclein Overexpressio ...
alpha-Synuclein Overexpression Lysate
NBL1-16274
Species: Hu
Applications: WB
alpha-Synuclein Overexpressio ...
alpha-Synuclein Overexpression Lysate
NBP2-11293
Species: Hu
Applications: WB
Proteins
Recombinant Human alpha-Synuc ...
Recombinant Human alpha-Synuclein ...
NBP2-54789
Species: Hu
Applications: WB, In vitro, In vivo, PAGE, Bioactivity
Recombinant Human alpha-Synuc ...
Recombinant Human alpha-Synuclein ...
NBP2-54788
Species: Hu
Applications: WB, In vitro, In vivo, PAGE, Bioactivity
Recombinant Human alpha-Synuc ...
Recombinant Human alpha-Synuclein ...
NBP2-54787
Species: Hu
Applications: WB, In vitro, In vivo, PAGE, Bioactivity

Description

Alpha-synuclein, a member of the synuclein family, is a protein that was first identified in 1988 whose name is derived from its localization to both the synapse and nucleus (1-3). Specifically, it is expressed primarily in the brain, including Lewy Bodies (1-6). Alpha-synuclein is encoded by the SNCA gene, located on chromosome 4p21, and is processed as a 140 amino acid (aa) protein with a theoretical molecular weight of 14 kDa (1,2,4). Structurally alpha-synuclein consists of a N-terminal binding domain (1-60 aa), a central domain core region called the non-amyloid-beta component (NAC) (61-95 aa), and a C-terminal domain (96-140 aa) (1-3). The N-terminal region contains aa repeats with a KTKEGV consensus sequence that gives the protein its alpha-helical structure that associates with lipid membranes (1-4). The hydrophobic NAC region is responsible for alpha-synuclein aggregation and fibril formation (1-4). The acidic C-terminal tail is largely unstructured but can be targeted for post-translational modifications (1-4). The function of alpha-synuclein is not entirely understood, but it is shown to have a role in suppression of apoptosis, acting as a molecular chaperone, regulating glucose, and modulating calmodulin activity (1,3).

A number of studies have revealed that alpha-synuclein aggregation is a hallmark feature in a number of neurodegenerative diseases, referred to as synucleinopathies (2-4). Alpha-synuclein protein aggregates are a large component of Lewy bodies that are present in Parkinson's disease (PD), Lewy body dementia (LBD), and multiple system atrophy (1-6). Research has shown phosphorylation of alpha-synuclein at Ser129 moves the protein from the nucleus to the cytoplasm and promotes fibril formation associated with synucleinopathies (1,2,5). Recent studies also suggest that alpha-synuclein accumulation can prevent mitochondrial import machinery causing mitochondrial dysfunction that is often observed in neurodegeneration (5). It is thought that preventing alpha-synuclein aggregation may prevent PD, thus alpha-synuclein is a target for many potential therapeutic interventions aimed at decreasing aggregate formation or increasing clearance (1,2,4-6).

References

1. Villar-Pique, A., Lopes da Fonseca, T., & Outeiro, T. F. (2016). Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies. Journal of neurochemistry. https://doi.org/10.1111/jnc.13249

2. Emamzadeh F. N. (2016). Alpha-synuclein structure, functions, and interactions. Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences. https://doi.org/10.4103/1735-1995.181989

3. Burre J. (2015). The Synaptic Function of alpha-Synuclein. Journal of Parkinson's disease. https://doi.org/10.3233/JPD-150642

4. Lashuel, H. A., Overk, C. R., Oueslati, A., & Masliah, E. (2013). The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nature reviews. Neuroscience. https://doi.org/10.1038/nrn3406

5. Rocha, E. M., De Miranda, B., & Sanders, L. H. (2018). Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson's disease. Neurobiology of disease. https://doi.org/10.1016/j.nbd.2017.04.004

6. O'Leary, E. I., & Lee, J. C. (2019). Interplay between alpha-synuclein amyloid formation and membrane structure. Biochimica et biophysica acta. Proteins and proteomics. https://doi.org/10.1016/j.bbapap.2018.09.012

Bioinformatics

Entrez Human
Mouse
Rat
Bovine
Canine
Uniprot Human
Human
Human
Human
Human
Human
Human
Human
Human
Product By Gene ID 6622
Alternate Names
  • alpha-synuclein
  • I+/--synuclein
  • NACP
  • PD1
  • SNCA
  • synuclein alpha-140
  • truncated alpha synuclein
  • PARK1
  • MGC110988
  • Non-A4 component of amyloid precursor
  • PARK4
  • Non-A beta component of AD amyloid
  • non A-beta component of AD amyloid
  • synuclein, alpha (non A4 component of amyloid precursor)

Research Areas for alpha-Synuclein

Find related products by research area and learn more about each of the different research areas below.

Alzheimers Research
Apoptosis
Cell Biology
Cytoskeleton Markers
Loading Controls
Neurodegeneration
Neuroscience
Phospho-Specific
Stem Cell Markers

Bioinformatics Tool for alpha-Synuclein

Discover related pathways, diseases and genes to alpha-Synuclein. Need help? Read the Bioinformatics Tool Guide for instructions on using this tool.
 
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Related alpha-Synuclein Blog Posts

Check out the latest blog posts on alpha-Synuclein.
Mechanisms of neurodegeneration: Mitochondrial dysfunction and oxidative stress
By Michalina Hanzel, PhDIn this second installment of our three blog-posts series on major cellular mechanisms responsible for neurodegenerative disorders, we will explore the processes of mitochondrial dysfunction an...    Read more.
Mechanisms of Neurodegeneration: Protein aggregation and failure of autophagy
By Michalina Hanzel, PhDIn a series of three blog posts I will briefly explore the major cellular mechanisms responsible for many neurodegenerative disorders. The first, and perhaps the most apparent, is the accumulat...    Read more.
The role of Parkin and autophagy in retinal pigment epithelial cell (RPE) degradation
The root of Parkinson’s disease (PD) points to a poorly regulated electron transport chain leading to mitochondrial damage, where many proteins need to work cohesively to ensure proper function.  The two key players of this pathway are PINK1,...    Read more.
Read more alpha-Synuclein related blogs.