SNCA 96-140 Human
Description
A-Synuclein 96-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 96-140, produced in E.Coli is a single, non-glycosylated polypeptide chain of 46 amino acids having a molecular mass of 5.2kDa, with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 96-140 is purified by proprietary chromatographic techniques.
Product Specs
MKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Product Science Overview
Alpha-synuclein is an intrinsically disordered protein (IDP), meaning it does not adopt a fixed three-dimensional structure under physiological conditions. This characteristic allows it to interact with a variety of other proteins and cellular components . The protein is composed of 140 amino acids and can be divided into three distinct regions:
- N-terminal domain (1-60 amino acids): This region is amphipathic and is involved in membrane binding.
- Non-amyloid-β component (NAC) domain (61-95 amino acids): This hydrophobic region is prone to aggregation and is critical for the formation of fibrils.
- C-terminal domain (96-140 amino acids): This region contains abundant proline and negatively charged amino acids, forming an acidic tail without a specific structure .
The C-terminal domain (96-140) is particularly interesting because it is involved in interactions with other proteins and cellular components, influencing the aggregation properties of alpha-synuclein .
Alpha-synuclein is the major component of Lewy bodies, which are pathological aggregates found in the brains of patients with PD, DLB, and MSA . The aggregation of alpha-synuclein is a hallmark of these diseases and is believed to contribute to neuronal dysfunction and cell death .
In Parkinson’s Disease, the death of dopaminergic neurons in the substantia nigra pars compacta is a key pathological feature. The presence of alpha-synuclein aggregates in these neurons is thought to disrupt normal cellular functions, leading to the characteristic motor symptoms of PD, such as bradykinesia, tremors, and rigidity .
Recombinant alpha-synuclein 96-140 is a synthetically produced fragment of the protein, corresponding to the C-terminal domain. This recombinant protein is used in various research applications to study the structure, function, and aggregation properties of alpha-synuclein . By focusing on this specific region, researchers can gain insights into how the C-terminal domain influences the overall behavior of the protein and its role in disease processes.
Understanding the structure and function of alpha-synuclein, particularly the C-terminal domain, is crucial for developing therapeutic strategies for synucleinopathies. Research on recombinant alpha-synuclein 96-140 has provided valuable information on the mechanisms of protein aggregation and its interactions with other cellular components . This knowledge can be leveraged to design drugs or interventions that target specific regions of the protein, potentially preventing or reducing the formation of toxic aggregates.
