Immunohistochemistry-Frozen: alpha-Synuclein Antibody [NBP2-15365] - Frozen-sectioned adult mouse hippocampus. Green: alpha Synuclein protein stained by alpha Synuclein antibody diluted at 1:250. Red: NeuN, stained by ...read more
Independent Antibodies: Western Blot: alpha-Synuclein Antibody [NBP2-15365] - Various tissue extracts (50 ug) were separated by 15% SDS-PAGE, and the membranes were blotted with alpha Synuclein antibody diluted ...read more
Immunohistochemistry-Frozen: alpha-Synuclein Antibody [NBP2-15365] - Frozen-sectioned adult mouse cerebellum. Green: alpha Synuclein protein stained by alpha Synuclein antibody diluted at 1:250. Red: beta Tubulin 3/ ...read more
Immunocytochemistry/ Immunofluorescence: alpha-Synuclein Antibody [NBP2-15365] - DIV14 rat E18 primary cortical neurons were fixed in 4% paraformaldehyde at RT for 15 min. Green: alpha Synuclein protein stained by alpha ...read more
Immunohistochemistry-Frozen: alpha-Synuclein Antibody [NBP2-15365] - Frozen sectioned E13.5 Rat brain. Green: alpha Synuclein protein stained by alpha Synuclein antibody diluted at 1:250. Blue: Fluoroshield with DAPI.
Immunohistochemistry-Paraffin: alpha-Synuclein Antibody [NBP2-15365] - Synuclein-alpha Antibody [NBP2-15365] - Paraffin-embedded Rat brain diluted at 1:500.
Western Blot: alpha-Synuclein Antibody [NBP2-15365] - Various whole cell extracts (30 ug) were separated by 15% SDS-PAGE, and the membrane was blotted with alpha Synuclein antibody diluted at 1:1000. The HRP-conjugated ...read more
Western Blot: alpha-Synuclein Antibody [NBP2-15365] - Various tissue extracts (50 ug) were separated by 15% SDS-PAGE, and the membrane was blotted with alpha Synuclein antibody diluted at 1:2000. The HRP-conjugated ...read more
Immunohistochemistry-Paraffin: Synuclein-alpha Antibody [NBP2-15365] - Paraffin-embedded Colon ca, using antibody at 1:250 dilution.
Immunohistochemistry-Paraffin: Synuclein-alpha Antibody [NBP2-15365] - Paraffin-embedded rat brain. Green: alpha Synuclein antibody diluted at 1:200. The signal was developed using goat anti-rabbit IgG antibody ...read more
14 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read 1 Review rated 5 using NBP2-15365 in the following applications:
Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
PBS, 20% Glycerol (pH7)
0.025% Proclin 300
Immunogen affinity purified
Alternate Names for alpha-Synuclein Antibody
non A-beta component of AD amyloid
Non-A beta component of AD amyloid
Non-A4 component of amyloid precursor
synuclein, alpha (non A4 component of amyloid precursor)
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. 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.
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