alpha-Synuclein Antibody (017) [DyLight 488]


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Product Details

Reactivity HuSpecies Glossary
Applications WB, ELISA
DyLight 488

alpha-Synuclein Antibody (017) [DyLight 488] 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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  • Western Blot
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Packaging, Storage & Formulations

Store at 4C in the dark.
50mM Sodium Borate
0.05% Sodium Azide
Protein A purified


DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.

Alternate Names for alpha-Synuclein Antibody (017) [DyLight 488]

  • 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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Product General Protocols

Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.

Video Protocols

WB Video Protocol

FAQs for alpha-Synuclein Antibody (NBP2-90051G). (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.

Secondary Antibodies


Isotype Controls

Other Available Formats

Alexa Fluor 350 NBP2-90051AF350
Alexa Fluor 405 NBP2-90051AF405
Alexa Fluor 488 NBP2-90051AF488
Alexa Fluor 532 NBP2-90051AF532
Alexa Fluor 594 NBP2-90051AF594
Alexa Fluor 647 NBP2-90051AF647
Alexa Fluor 700 NBP2-90051AF700
Alexa Fluor 750 NBP2-90051AF750
Biotin NBP2-90051B
DyLight 350 NBP2-90051UV
DyLight 405 NBP2-90051V
DyLight 488 NBP2-90051G
DyLight 550 NBP2-90051R
DyLight 594 NBP2-90051DL594
DyLight 650 NBP2-90051C
DyLight 680 NBP2-90051FR
DyLight 755 NBP2-90051IR
FITC NBP2-90051F
HRP NBP2-90051H

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Gene Symbol SNCA