SNCA 61-140 Human
Description
A-Synuclein 61-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 61-140 , produced in E.Coli is a single, non-glycosylated polypeptide chain of 81 amino acids having a molecular mass of 8.4kDa (molecular size on SDS-PAGE will appear higher), with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 61-140 is purified by proprietary chromatographic techniques.
Product Specs
Recombinant Human A-Synuclein 61-140, produced in E. coli, is a truncated form of the alpha-synuclein protein, encompassing amino acids 61-140. This non-glycosylated polypeptide chain consists of 81 amino acids, resulting in a molecular weight of 8.4 kDa. However, its apparent size on SDS-PAGE may appear larger due to an additional methionine residue at the N-terminus. Purification of this recombinant protein is achieved through proprietary chromatographic techniques.
MEQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Product Science Overview
Alpha-synuclein is a small, soluble protein composed of 140 amino acids. It is natively unfolded, meaning it does not adopt a fixed three-dimensional structure under physiological conditions. This intrinsic disorder allows alpha-synuclein to interact with a variety of other proteins and cellular components. The 61-140 segment of alpha-synuclein retains many of the protein’s functional properties and is often used in research to study its behavior in isolation.
Alpha-synuclein is primarily found in the brain, particularly in the presynaptic terminals of neurons, where it is believed to play a role in synaptic vesicle regulation and neurotransmitter release. It is also involved in the maintenance of synaptic plasticity and the regulation of dopamine neurotransmission .
The pathological aggregation of alpha-synuclein is a hallmark of several neurodegenerative diseases collectively known as synucleinopathies. These include Parkinson’s disease, dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). In these conditions, alpha-synuclein aggregates to form insoluble fibrils that are deposited in the brain, leading to neuronal dysfunction and cell death .
In Parkinson’s disease, alpha-synuclein aggregates are found in Lewy bodies and Lewy neurites, which are characteristic pathological features of the disease. The presence of these aggregates is associated with the loss of dopaminergic neurons in the substantia nigra, a brain region critical for motor control. This neuronal loss leads to the motor symptoms of Parkinson’s disease, such as tremors, rigidity, and bradykinesia .
The study of recombinant alpha-synuclein, including the 61-140 segment, has provided valuable insights into the mechanisms of protein aggregation and its role in disease. Researchers use recombinant alpha-synuclein to investigate how mutations, post-translational modifications, and environmental factors influence its aggregation propensity and toxicity .
Understanding the behavior of alpha-synuclein is crucial for developing therapeutic strategies aimed at preventing or reversing its aggregation. Potential therapeutic approaches include small molecules that inhibit aggregation, immunotherapies that target alpha-synuclein, and gene therapies that modulate its expression .
