α-Synuclein human

α-Synuclein is an intrinsically disordered protein predominantly expressed in the dopaminergic neurons. It is localized to the presynaptic nerve terminals and is highly conserved in vertebrates.

α-Synuclein human has been used to study the α-syn monomers and its aggregates on paraformaldehyde (PFA)-fixed membrane. It has also been used to study its effect on neurotransmitter levels (monoamines and amino acid concentration) tyrosine hydroxylase (TH) and transglutaminase-2 (TG2) mRNA expression in the mouse striata (ST).

Human α-synuclein has been used to study the immunodetection of α-syn monomers and its aggregates. It has also been used in microscale thermophoresis to study protein-protein interactions.

140-amino acid protein (apparent molecular weight 19-20 kDa) encoded by a simple gene consisting of six exons on human chromosome 4. Induces polymerization of tubulin into microtubules and functions in the modulation of dopamine transporter function, regulating the synaptic tone of dopamine. Disruption of this function can ultimately lead to neurodegeneration of nerve terminals. Highly abundant in presynaptic terminals, a major component of Lewy bodies, the neuronal cytoplasmic inclusions that are a hallmark of diverse neurodegenerative disorders such as Parkinson′s disease (PD), dementia with Lewy bodies (filamentous inclusions), Lewy body variant of Alzheimer′s disease, and multiple system atrophy. Pathogenic point mutations in the α-synuclein gene are linked to familial Parkinson′s disease.

140-amino acid protein (apparent molecular weight 19-20 kDa) that induces polymerization of tubulin into microtubules and functions in the modulation of dopamine.