Recombinant Human Alpha-synuclein (mutated E46K) protein (ab51188)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
-
Product name
Recombinant Human Alpha-synuclein (mutated E46K) protein
See all Alpha-synuclein proteins and peptides -
Purity
> 95 % SDS-PAGE.
Alpha Synuclein E46K was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques. -
Expression system
Escherichia coli -
Accession
-
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
MDVFMKGLSK/ AKEGVVAAAE/ KTKQGVAEAA/ GKTKEGVLYV/ GSKTK[K]GVVH/GVATVAEKTK/EQVTNVGGAV/VT GVTAVAQK/TVEGAGSIAA/ ATGFVKKDQL/GKNEEGAPQE/GILEDM PVDP/DNEAYEMPSE/EGYQDYEPEA -
Predicted molecular weight
14 kDa -
Amino acids
1 to 140 -
Modifications
mutated E46K
-
Preparation and Storage
-
Alternative names
- Alpha synuclein
- Alpha-synuclein
- Alpha-synuclein, isoform NACP140
see all -
Function
May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. -
Tissue specificity
Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals. -
Involvement in disease
Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.
Parkinson disease 1
Parkinson disease 4
Dementia Lewy body -
Sequence similarities
Belongs to the synuclein family. -
Domain
The 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments. -
Post-translational
modificationsPhosphorylated, 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. -
Cellular localization
Cytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons. - Information by UniProt