Specifications
- Pk:1 mg
- Protein/peptide type:Recombinant
- Source:E. coli
- Species:Human
- Storage conditions:Store at 4 °C short term. Aliquot and store at −20 °C long term. Avoid freeze-thaw cycles.
- Endotoxin content:<1,0 EU per 1 µg of protein (determined by LAL method)
- Amino acid number:1 to 140
- Reconstitution instructions:Reconstitute with sterilised distilled water to a final concentration of less than 1,0 mg/ml
- Protein synonyms:PARK1|synuclein alpha-140|SNCA|PARK4|I+/--synuclein|Non-A beta component of AD amyloid|Synuclein-alpha|Non-A4 component of amyloid precursor|MGC110988|NACP|PD1|synuclein, alpha (non A4 component of amyloid precursor)|non A-beta component of AD amyloid|truncated alpha synuclein
- Protein/peptide name:alpha-Synuclein
- Purity:>95%, by SDS-PAGE
- Molecular weight:14,4 kDa (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)
- Sequence:MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
- Concentration:LYOPH
- Tested applications:PAGE
Specifications
About this item
Alpha-synuclein, a member of the synuclein family, is a protein that was first identified in 1988 whose name is derived from its localisation 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).
Buffer: Lyophilised from 0,2 µm filtered 20 mM Tris-HCl buffer (pH 7,5), 100 mM NaCl, 1 mM MgCl₂
Gene: SNCA
Dilutions: SDS-Page
Structurally alpha-synuclein consists of a N-terminal binding domain (1 to 60 aa), a central domain core region called the non-amyloid-beta component (NAC) (61 to 95 aa), and a C-terminal domain (96 to 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).