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S7820

Sigma-Aldrich

α-Synuclein human

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

Synonyme(s) :

α-Synuclein protein, Synuclein protein

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About This Item

Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

Pureté

≥90% (SDS-PAGE)

Forme

lyophilized powder

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

human ... SNCA(6622)

Description générale

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.

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

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
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)
Prolyl Oligopeptidase Enhances a-Synuclein Dimerization via Direct Protein-Protein Interaction*
Mari H. Savolainen
The Journal of Biological Chemistry (2015)
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

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