alpha-Synuclein Antibody (5C2) - BSA Free

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

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.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 2 applications: DB, WB.

Showing Publications 1 - 5 of 5.

Publications using NBP1-04321	Applications	Species
Desai AA, Zupancic JM, Trzeciakiewicz H et al. Flow cytometric isolation of drug-like conformational antibodies specific for amyloid fibrils bioRxiv : the preprint server for biology 2023-07-04 [PMID: 37461643] (DB, Mouse)	DB	Mouse
De Luca CMG, Elia AE, Portaleone SM et al. Efficient RT-QuIC seeding activity for alpha-synuclein in olfactory mucosa samples of patients with Parkinson's disease and multiple system atrophy Transl Neurodegener 2019-08-08 [PMID: 31406572] (WB, Human)	WB	Human
Julian M C, Rabia L A et al. Nature-inspired design and evolution of anti-amyloid antibodies. J Biol Chem 2019-05-24 [PMID: 30918024] (WB, Mouse)	WB	Mouse
Zunke F, Moise AC, Belur NR et al. Reversible Conformational Conversion of a-Synuclein into Toxic Assemblies by Glucosylceramide. Neuron 2017-12-20 [PMID: 29290548] (Human)		Human
Herva ME, Zibaee S, Fraser G et al. Anti-amyloid compounds inhibit alpha-synuclein aggregation induced by Protein Misfolding Cyclic Amplification (PMCA). J. Biol. Chem. 2014-03-03 [PMID: 24584936] (WB, Human)	WB	Human

Array NBP1-04321

• alpha-Synuclein Antibodies
• alpha-Synuclein ELISA Kits
• alpha-Synuclein Lysates
• alpha-Synuclein Proteins
• alpha-Synuclein Proteins and Enzymes
• alpha-Synuclein ELISA