SNCA E46K, Human
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
Greater than 95.0% as determined by SDS-PAGE.
Description
SNCA E46K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140a.a.) and having a molecular mass of 14.4kDa.
SNCA is purified by proprietary chromatographic techniques.
Product Specs
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKKGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Product Science Overview
Alpha-Synuclein is a 140-amino acid protein that is composed of three primary regions:
- Amino Terminus: Contains apolipoprotein lipid-binding motifs, which are anticipated to form amphiphilic helices.
- Central Region: Known as the non-Aβ component (NAC), containing a hydrophobic domain that gives β-sheet potential.
- Carboxyl Terminus: Characterized by a high negative charge and remains unstructured .
Under physiological conditions, alpha-synuclein is predominantly a neuronal protein that localizes to presynaptic terminals. It plays several roles in synaptic activity, such as the regulation of synaptic vesicle trafficking and neurotransmitter release .
The E46K mutation is a specific point mutation in the alpha-synuclein protein, where the amino acid glutamic acid (E) at position 46 is replaced by lysine (K). This mutation is a result of a 188G-A transition in the gene . Among the familial mutations of alpha-synuclein, E46K has the greatest potential to aggregate, leading to the formation of fibrillary tangles, which are a hallmark of certain neurodegenerative diseases .
The deposition of alpha-synuclein aggregates is a defining characteristic of synucleinopathies. In Parkinson’s disease, for example, alpha-synuclein is the principal component of Lewy bodies, which are pathological inclusions found in the brains of affected individuals . The E46K mutation has been shown to enhance the aggregation propensity of alpha-synuclein, thereby exacerbating the pathological processes associated with these diseases .
Recombinant alpha-synuclein E46K is produced in Escherichia coli and purified to apparent homogeneity using conventional column chromatography techniques . This recombinant protein is used in various research applications, including the study of protein aggregation, interaction with metals like iron and copper, and the formation of isoaspartate protein damage .
Recombinant alpha-synuclein E46K has been used in:
- Preparation of alpha-synuclein fibrils to study amyloid-related imaging abnormalities (ARIA).
- Investigating the interaction of alpha-synuclein with metals to understand their role in proteinopathies.
- Studying the formation of isoaspartate protein damage, which triggers familial Parkinsonian phenotypes .
