Skip to Content
Merck
All Photos(1)

Key Documents

S7820

Sigma-Aldrich

α-Synuclein human

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

Synonym(s):

α-Synuclein protein, Synuclein protein

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352200
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)

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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
Structural characteristics and membrane interactions of tandem alpha-synuclein oligomers
Dong C, et al.
Scientific reports, 8(1), 6755-6755 (2018)
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
Prolyl Oligopeptidase Enhances a-Synuclein Dimerization via Direct Protein-Protein Interaction*
Mari H. Savolainen
The Journal of Biological Chemistry (2015)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service