alpha-Synuclein Antibody (017)


Western Blot: alpha-Synuclein Antibody (017) [NBP2-90051] - Lane A: 293T Whole Cell LysateLysates/proteins at 30 ug per lane.SecondaryGoat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey more

Product Details

Reactivity HuSpecies Glossary
Applications WB, IHC, IHC-P, IP

alpha-Synuclein Antibody (017) Summary

Additional Information
Recombinant Monoclonal Antibody
This alpha-Synuclein Antibody (017) was developed against rabbit immunized with purified, recombinant human alpha-Synuclein (P37840-1; Met1-Ala140).
Protein A purified
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  • Immunohistochemistry 1:10-1:500
  • Immunohistochemistry-Paraffin 1:100
  • Immunoprecipitation 2-5 ug/mg lysate
  • Western Blot 1:500-1:2000

Packaging, Storage & Formulations

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
0.2 um filtered solution in PBS
No Preservative
Protein A purified


This antibody can be stored at 2C-8C for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20C to -80C. Avoid repeated freeze-thaw cycles.

Alternate Names for alpha-Synuclein Antibody (017)

  • alpha-Synuclein
  • I+/--synuclein
  • MGC110988
  • NACP
  • non A-beta component of AD amyloid
  • Non-A beta component of AD amyloid
  • Non-A4 component of amyloid precursor
  • PARK1
  • PARK4
  • PD1
  • SNCA
  • synuclein alpha-140
  • synuclein, alpha (non A4 component of amyloid precursor)
  • Synuclein-alpha
  • truncated alpha synuclein


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).


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.

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.

3. Burre J. (2015). The Synaptic Function of alpha-Synuclein. Journal of Parkinson's disease.

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.

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.

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.


This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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FAQs for alpha-Synuclein Antibody (NBP2-90051). (Showing 1 - 1 of 1 FAQ).

  1. I'm looking for an alpha-Synuclein antibody with an epitope located in the first half (N-terminus) of the protein - preferably a monoclonal antibody. Can you help me with that?
    • Please take a look at NB110-57475. It has been validated for human, rat and mouse and the applications ICC and WB and the epitope it detects is in the N terminal.

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Gene Symbol SNCA