alpha-Synuclein Antibody

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 8 applications: ELISA, ICC/IF, IF/IHC, Immunocytochemistry/ Immunofluorescence, Immunohistochemistry-Frozen, S-ELISA, WB, Western Blot.

Showing Publications 1 - 10 of 12. Show All 12 Publications. Collapse Publications.

Publications using NBP2-15365	Applications	Species
Lee JY, Castelli V, Sanberg PR, Borlongan CV. Probing Gut Participation in Parkinson's Disease Pathology and Treatment via Stem Cell Therapy International Journal of Molecular Sciences 2023-06-25 [PMID: 37445778] (Immunohistochemistry-Frozen, Immunocytochemistry/ Immunofluorescence)	Immunohistochemistry-Frozen, Immunocytochemistry/ Immunofluorescence
Lee JY, Wang ZJ, Moscatello A et al. Inflammatory gut as a pathologic and therapeutic target in Parkinson's disease Cell Death Discovery 2022-09-24 [PMID: 36153318] (Immunocytochemistry/ Immunofluorescence)	Immunocytochemistry/ Immunofluorescence
Han S, Lim S, Yeo S. Association between Decreased ITGA7 Levels and Increased Muscle ?-Synuclein in an MPTP-Induced Mouse Model of Parkinson's Disease International Journal of Molecular Sciences 2022-05-18 [PMID: 35628462] (Western Blot)	Western Blot
D'Antongiovanni V, Pellegrini C, Antonioli L et al. Palmitoylethanolamide Counteracts Enteric Inflammation and Bowel Motor Dysfunctions in a Mouse Model of Alzheimer's Disease Frontiers in Pharmacology 2021-09-29 [PMID: 34658885] (ELISA)	ELISA
Lin L, Petralia RS, Lake R et al. A novel structure associated with aging is augmented in the DPP6-KO mouse brain Acta Neuropathol Commun 2020-11-23 [PMID: 33225987] (IF/IHC, Mouse) Details: DPP6-KO and wild type mice hippocampi were analyzed via immunohistochemistry	IF/IHC	Mouse
Wang H, Dou S, Zhu J et al. Ghrelin protects dopaminergic neurons against MPTP neurotoxicity through promoting autophagy and inhibiting endoplasmic reticulum mediated apoptosis Brain Res 2020-07-26 [PMID: 32710901] (ICC/IF, WB)	ICC/IF, WB
Zhu J, Dou S, Wang C et al. Apelin-36 mitigates MPTP/MPP+-induced neurotoxicity: involvement of alpha-synuclein and endoplasmic reticulum stress Brain Res. 2019-07-12 [PMID: 31306618] (WB, ICC/IF, Human, Mouse)	WB, ICC/IF	Human, Mouse
Akerman, SC;Hossain, S;Shobo, A;Zhong, Y;Jourdain, R;Hancock, MA;George, K;Breton, L;Multhaup, G; Neurodegenerative Disease-Related Proteins within the Epidermal Layer of the Human Skin J. Alzheimers Dis. 2019-04-15 [PMID: 31006686] (ICC/IF, Human)	ICC/IF	Human
Akerman S Early biomarker detection & potential novel pathogenic pathways of Alzheimer disease involving A beta and Tau Thesis 2022-01-01
Lin L, Petralia RS, Holtzclaw L et al. Alzheimer's disease/dementia-associated brain pathology in aging DPP6-KO mice Neurobiology of disease 2022-11-01 [PMID: 36209950] (WB)	WB
Zappelli E, Daniele S, Ceccarelli L et al. Alpha-glyceryl-phosphoryl-ethanolamine protects human hippocampal neurons from aging-induced cellular alterations The European journal of neuroscience 2022-07-28 [PMID: 35902984] (S-ELISA, Human) Details: NBP2-15365 used as coating antibody, sc-12767, Santa Cruz detection antibody	S-ELISA	Human
Plaksina D, Ekimova I Age-Related Features of alpha-Synuclein Pathology in the Brain on Modeling the Preclinical Stage of Parkinson's Disease in Rats Zh Nevrol Psikhiatr Im S S Korsakova 2020-10-20 [PMID: 33076642]
Show All 12 Publications. Collapse Publications.

Images	Ratings	Applications	Species	Date	Details
Enlarge	5 reviewed by: Verified Customer	WB	Human and Mouse	12/18/2017	View Summary Application Western Blot Sample Tested Mouse forebrain lysate Species Human and Mouse Lot 42837

Array NBP2-15365

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