Recombinant Human Alpha-synuclein (mutated E46K) protein (Tag Free)

Specifications

Form

Liquid

Additional notes

Alpha Synuclein E46K was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques.

General info

Function

The protein expressed by the SNCA gene is involved in various synaptic activities, including the regulation of synaptic vesicle trafficking and neurotransmitter release. As a monomer, it enhances synaptic vesicle exocytosis through vesicle priming, fusion, and dilation of exocytotic fusion pores. Mechanistically, it increases local Ca(2+) release, which is crucial for ATP-induced exocytosis. In its multimeric membrane-bound form, SNCA acts as a molecular chaperone, assisting in the folding of synaptic fusion components known as SNAREs at the presynaptic plasma membrane, in conjunction with cysteine string protein-alpha/DNAJC5, a function that is vital for maintaining normal SNARE-complex assembly during aging. Additionally, SNCA plays a role in dopamine neurotransmission regulation by associating with the dopamine transporter (DAT1) and modulating its activity. This supplementary information is collated from multiple sources and compiled automatically.

Sequence similarities

Belongs to the synuclein family.

Post-translational modifications

Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.. Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.