alpha-Synuclein Antibody (2A7)

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 5 applications: FLOW, ICC/IF, IHC-P, Immunocytochemistry/ Immunofluorescence, WB.

Showing Publications 1 - 9 of 9.

Publications using NBP1-05194	Applications	Species
Rueda-Gensini L, Serna JA, Rubio D et al. Three-dimensional neuroimmune co-culture system for modeling Parkinson's Disease microenvironments in vitro Biofabrication 2023-06-27 [PMID: 37369196] (Immunocytochemistry/ Immunofluorescence, Human)	Immunocytochemistry/ Immunofluorescence	Human
Amireddy N, Dulam V, Kaul S et al. The mitochondrial uncoupling effects of nitazoxanide enhances cellular autophagy and promotes the clearance of ?-synuclein: Potential role of AMPK-JNK pathway Cellular signalling 2023-06-12 [PMID: 37315747] (WB, Human)	WB	Human
Leupold L, Sigutova V, Gerasimova E et al. The Quest for Anti-?-Synuclein Antibody Specificity-Lessons Learnt From Flow Cytometry Analysis Frontiers in neurology 2022-07-15 [PMID: 35911883] (FLOW, ICC/IF, WB, Human) Details: AF488-conjugate. Flow: 2 ug per test, ICC/IF: 1:100 dilution, WB: 1:500 dilution	FLOW, ICC/IF, WB	Human
Huynh B Brainstem Neurotransmitter System Deterioration in Parkinson's Disease and Parkinson's Disease with Dementia Thesis 2023-01-01 (IHC-P, Human)	IHC-P	Human
Kim Y, Stahl MC, Huang X, Connor JR H63D variant of the homeostatic iron regulator (HFE) gene alters alpha-synuclein expression, aggregation, and toxicity J. Neurochem. 2020-06-23 [PMID: 32574378] (Human)		Human
Lv R, Du L, Liu X et al. Rosmarinic acid attenuates inflammatory responses through inhibiting HMGB1/TLR4/NF-kB signaling pathway in a mouse model of Parkinson's disease Life Sci. 2019-04-15 [PMID: 30880023] (ICC/IF, Mouse)	ICC/IF	Mouse
Lee M, Liu K, Thomas J et al. Peptide-Imprinted Poly(hydroxymethyl 3,4-ethylenedioxythiophene) Nanotubes for Detection of alpha Synuclein in Human Brain Organoids ACS Appl. Nano Mater. 2020-08-28 (WB)	WB
Wilmes P, Trezzi J, Aho V et al. An archaeal compound as a driver of Parkinson’s disease pathogenesis Research Square 2022-07-26 (ICC/IF, Human)	ICC/IF	Human
Liu X, Balaraman K, Lynch CC et al. Inhibition of Ubiquitin-Specific Protease-13 Improves Behavioral Performance in Alpha-Synuclein Expressing Mice International journal of molecular sciences 2022-07-23 [PMID: 35897705]

Array NBP1-05194

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