SNCA A30P Human
Description
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
Product Specs
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Product Science Overview
Alpha-synuclein is a presynaptic neuronal protein that has been extensively studied due to its significant role in the pathogenesis of Parkinson’s disease and other neurodegenerative disorders known as synucleinopathies. The A30P mutation in alpha-synuclein is one of several mutations associated with familial forms of Parkinson’s disease. This article delves into the background, structure, function, and implications of the Alpha Synuclein A30P mutation, particularly in its recombinant human form.
Alpha-synuclein is an intrinsically disordered protein, meaning it lacks a stable secondary or tertiary structure under physiological conditions. It is composed of three distinct regions:
- N-terminal region (residues 1-60): This region adopts an amphipathic α-helical structure when associated with membranes.
- Central region (residues 61-95): This highly hydrophobic region is essential for the protein’s aggregation.
- C-terminal region (residues 96-140): Enriched in acidic residues, this region is involved in several protein-protein interactions, conferring a chaperone-like function to the protein .
Alpha-synuclein is predominantly found in the brain, particularly in presynaptic terminals, where it is thought to play a role in synaptic vesicle trafficking and neurotransmitter release.
The A30P mutation involves the substitution of alanine with proline at position 30 of the alpha-synuclein protein. This mutation is associated with early-onset familial Parkinson’s disease. Patients carrying the A30P mutation typically exhibit symptoms similar to those of sporadic Parkinson’s disease, including bradykinesia, rigidity, and tremors .
The A30P mutation affects the protein’s ability to bind to membranes and its propensity to aggregate. Studies have shown that the A30P mutant form of alpha-synuclein has a reduced affinity for lipid membranes compared to the wild-type protein. This reduced binding affinity is thought to contribute to the protein’s increased propensity to form aggregates, which are a hallmark of Parkinson’s disease .
In cellular models, the A30P mutation has been shown to affect the internalization and trafficking of alpha-synuclein. The mutant protein can enter cells and form high molecular weight species, accumulating in intracellular inclusions. This accumulation is thought to contribute to the progressive nature of synucleinopathies .
Recombinant human alpha-synuclein A30P is produced using recombinant DNA technology, allowing for the study of this specific mutant form in various experimental settings. This recombinant protein is used in research to investigate the molecular mechanisms underlying the aggregation and toxicity of alpha-synuclein, as well as to screen potential therapeutic compounds that may inhibit its aggregation or promote its clearance .
