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S7820

Sigma-Aldrich

α-Synuclein 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
S1071S4447AG549
vibrant-m

S7820

α-Synuclein human

vibrant-m

S1071

α-Synuclein A53T human

vibrant-m

S4447

α-Synuclein E46K human

vibrant-m

AG549

α-synuclein 61-140, human

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

>95% (SDS-PAGE)

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

powder

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

UniProt accession no.

P37840

General description

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.

Application

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.

Biochem/physiol Actions

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.

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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Customers Also Viewed

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Effects of alpha-Synuclein Monomers Administration in the Gigantocellular Reticular Nucleus on Neurotransmission in Mouse Model
Joniec MI, et al.
Neurochemical Research, 44(4), 968-977 (2019)
Structural characteristics and membrane interactions of tandem alpha-synuclein oligomers
Dong C, et al.
Scientific reports, 8(1), 6755-6755 (2018)
Tian-Yuan Wang et al.
Journal of cellular and molecular medicine, 24(24), 14247-14256 (2020-11-15)
Islet inflammation severely impairs pancreatic β-cell function, but the specific mechanisms are still unclear. Interleukin1-β (IL-1β), an essential inflammatory factor, exerts a vital role in multiple physio-pathologic processes, including diabetes. Calcium/calmodulin-dependent serine protein kinase (CASK) is an important regulator especially
Juan A Gerez et al.
Science translational medicine, 11(495) (2019-06-07)
Parkinson's disease (PD) is a neurological disorder characterized by the progressive accumulation of neuronal α-synuclein (αSyn) inclusions called Lewy bodies. It is believed that Lewy bodies spread throughout the nervous system due to the cell-to-cell propagation of αSyn via cycles
Residual structure, backbone dynamics, and interactions within the synuclein family
Sung YH and Eliezer D
Journal of Molecular Biology, 372(3), 689-689 (2007)

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