Product nameRecombinant Human Alpha-synuclein protein
See all Alpha-synuclein proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
SequenceMDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVH GVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Molecular weight14 kDa
Amino acids1 to 140
Our Abpromise guarantee covers the use of ab51189 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity> 95 % SDS-PAGE.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.0095% Magnesium chloride, 0.316% Tris HCl, 0.58% Sodium chloride
- Alpha synuclein
- Alpha-synuclein, isoform NACP140
FunctionMay 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 specificityExpressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
Involvement in diseaseGenetic 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 similaritiesBelongs to the synuclein family.
DomainThe '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.
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 localizationCytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
- Information by UniProt
Anti-Alpha-synuclein antibody [LB 509] (ab27766) at 1/1000 dilution +
Recombinant Human Alpha-synuclein protein (ab51189) at 0.1 µg
Goat Anti-Mouse IgG H&L (HRP) preadsorbed (ab97040) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Exposure time: 8 minutes
ab51189 (3 µg) in 14% SDS-PAGE.
This product has been referenced in:
- Tyson T et al. Novel animal model defines genetic contributions for neuron-to-neuron transfer of a-synuclein. Sci Rep 7:7506 (2017). Read more (PubMed: 28790319) »
- Brudek T et al. Autoimmune antibody decline in Parkinson's disease and Multiple System Atrophy; a step towards immunotherapeutic strategies. Mol Neurodegener 12:44 (2017). Read more (PubMed: 28592329) »