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S1071

Sigma-Aldrich

α-Synuclein A53T human

recombinant, expressed in E. coli, N-terminal histidine tagged, ≥90% (SDS-PAGE), lyophilized powder

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MDL number:
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

assay

≥90% (SDS-PAGE)

form

lyophilized powder

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... SNCA(6622)

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This Item
S7820AG938MABN826
vibrant-m

S1071

α-Synuclein A53T human

vibrant-m

S7820

α-Synuclein human

vibrant-m

AG938

Synuclein, α, recombinant human

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

100

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

>95% (gel scan and mass spectrometry)

assay

-

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

storage temp.

−20°C

storage temp.

−20°C

storage temp.

-

storage temp.

-

form

lyophilized powder

form

lyophilized powder

form

solid

form

-

General description

α-Synuclein is mapped to human chromosome 4q22.1. It is an intrinsically disordered protein with N-terminal imperfect repeats (KTKEGV), a central NAC crucial for aggregation and an acidic rich flexible C-terminal region.α-Synuclein is present in the Lewy bodies (LBs) and Lewy neurites (LNs).

Application

α-Synuclein A53T human has been used to treat mesencephalic neuronal and stimulate microglial cells prior to reactive oxygen species (ROS) measurement, immunohistochemistry and imaging studies.

Biochem/physiol Actions

α-Synuclein (α-Syn) interacts with toll-like receptor 2 (TLR2) and mediates interleukin-1β (IL-1β) synthesis.
A point mutation in the α-synuclein gene, A53T (Ala53-Thr), is linked to familial Parkinson′s disease. Mice expressing A53T human α-synuclein, but not wild-type or the A30P variants, develop adult-onset neurodegenerative disease with a progressive motoric dysfunction leading to death.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Mehmet Ozansoy et al.
Molecular neurobiology, 47(2), 460-465 (2012-11-28)
Parkinson's disease (PD) is the second most common neurodegenerative disorder, defined by the presence of resting tremor, muscular rigidity, bradykinesia, and postural instability. PD is characterized by the progressive loss of dopaminergic neurons within the substantia nigra pars compacta of
Nathan Meyer et al.
ACS central science, 8(4), 441-448 (2022-05-05)
The detection to α-synuclein (αS) assemblies as a biomarker of synucleinopathies is an important challenge for further development of an early diagnosis tool. Here, we present proof of concept real-time fast amyloid seeding and translocation (RT-FAST) based on a nanopipette
Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53? Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice
Lee MK, et al.
Proceedings of the National Academy of Sciences, 99(13), 8968-8973 (2002)
Ciaran P A Doherty et al.
Nature structural & molecular biology, 27(3), 249-259 (2020-03-12)
Aggregation of human α-synuclein (αSyn) is linked to Parkinson's disease (PD) pathology. The central region of the αSyn sequence contains the non-amyloid β-component (NAC) crucial for aggregation. However, how NAC flanking regions modulate αSyn aggregation remains unclear. Using bioinformatics, mutation
Yan Zhou et al.
Molecular neurodegeneration, 11, 28-28 (2016-04-17)
α-Synuclein (α-Syn), a pathological hallmark of Parkinson's disease (PD), has been recognized to induce the production of interleukin-1β in a process that depends, at least in vitro, on nod-like receptor protein 3 (NLRP3) inflammasome in monocytes. However, the role of

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