SNCA 1-60 Human
Description
A-Synuclein 1-60 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 1-60 and contains the N-terminal amphipathic domain, produced in E.Coli is a single, non-glycosylated polypeptide chain of 60 amino acids having a molecular mass of 6.1kDa. The Recombinant Human a-Synuclein 1-60 is purified by proprietary chromatographic techniques.
Product Specs
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK.
Product Science Overview
Alpha-synuclein is an intrinsically disordered protein (IDP), meaning it lacks a stable secondary or tertiary structure under physiological conditions. The protein can be divided into three distinct regions based on its amino acid composition :
- N-terminal region (residues 1-60): This region adopts an amphipathic α-helical structure when associated with membranes. It is crucial for the protein’s interaction with lipid membranes and is involved in synaptic vesicle trafficking.
- Central region (residues 61-95): This hydrophobic region is essential for the aggregation of alpha-synuclein, which is a key feature in the pathogenesis of neurodegenerative diseases.
- C-terminal region (residues 96-140): This region is enriched in acidic residues and is involved in several protein-protein interactions, conferring a chaperone-like function to the protein.
Alpha-synuclein is a major component of Lewy bodies, which are pathological hallmarks of Parkinson’s disease (PD) and other synucleinopathies such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA) . The aggregation of alpha-synuclein in the brain is associated with the selective loss of dopaminergic neurons in the substantia nigra, leading to the characteristic motor symptoms of PD .
Recombinant alpha-synuclein 1-60 is a truncated form of the full-length protein, comprising the first 60 amino acids of the N-terminal region. This recombinant protein is typically expressed in Escherichia coli and purified to high levels of purity for research purposes . The truncated form retains the ability to interact with lipid membranes and is often used in studies investigating the protein’s role in membrane binding and aggregation .
Recombinant alpha-synuclein 1-60 is widely used in research to study the molecular mechanisms underlying synucleinopathies. It serves as a valuable tool for investigating the protein’s interactions with lipid membranes, its aggregation properties, and its role in neurodegeneration. Additionally, it is used in the development of potential therapeutic strategies targeting alpha-synuclein aggregation and toxicity .
