• Nature
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
    • Sequence
    • Molecular weight
      15 kDa
    • Amino acids
      1 to 140
    • Additional sequence information
      Produced in E. coli.


Our Abpromise guarantee covers the use of ab218819 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity

    Endogenous alpha-synuclein phosphorylation. 100 µM alpha synuclein protein monomer (ab218818) seeded with 10 nM alpha synuclein protein aggregate (ab218819) in 25 µM Thioflavin T (ab120751) (PBS pH 7.4, 100 µl reaction volume) generated a fluorescence intensity of 13,000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 24 hours. Fluorescence was measured by excitation at 450 nm and emission at 485 nm on a microplate reader.

  • Applications

    Functional Studies


  • Purity
    >95% by SDS-PAGE .
    ab218819 was purified by ion-exchange.
  • Form
  • Additional notes
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    Constituent: 100% PBS

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • Alpha synuclein
    • Alpha-synuclein
    • Alpha-synuclein, isoform NACP140
    • alphaSYN
    • MGC105443
    • MGC110988
    • MGC127560
    • MGC64356
    • NACP
    • Non A beta component of AD amyloid
    • Non A4 component of amyloid
    • Non A4 component of amyloid precursor
    • Non-A beta component of AD amyloid
    • Non-A-beta component of alzheimers disease amyloid , precursor of
    • Non-A4 component of amyloid precursor
    • Non-A4 component of amyloid, precursor of
    • OTTHUMP00000218549
    • OTTHUMP00000218551
    • OTTHUMP00000218552
    • OTTHUMP00000218553
    • OTTHUMP00000218554
    • PARK 1
    • PARK 4
    • PARK1
    • PARK4
    • Parkinson disease (autosomal dominant, Lewy body) 4
    • Parkinson disease familial 1
    • SNCA
    • Snca synuclein, alpha (non A4 component of amyloid precursor)
    • SYN
    • Synuclein alpha
    • Synuclein alpha 140
    • Synuclein, alpha (non A4 component of amyloid precursor)
    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
    Phosphorylated, 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


  • ThT emission curves show increased fluorescence (correlated to alpha-synuclein protein aggregation) over time when 10 nM of active alpha-synuclein aggregate (ab218819) is combined with 100 µM of active alpha-synuclein monomer (ab218818) (light blue), as compared to when 100 µM of active alpha-synuclein monomer is combined with 10 nM of control alpha-synuclein aggregate (purple line), or 100 µM of control alpha-synuclein monomer (ab218816) is combined with 10 nM of control alpha-synuclein aggregate (ab218817) (dark blue). ThT ex = 450 nm, em = 485 nm. View protocol.

  • Immunohistochemical analysis of primary rat hippocampal neurons showing lewy body inclusion formation when treated with active Alpha Synuclein Protein Aggregate (ab218819) at 4 µg/ml (D-F), but not when treated with control Alpha Synuclein Protein Aggregate (ab218817) at 4 µg/ml (A-C). Tissue: Primary hippocampal neurons. Species: Sprague-Dawley rat. Fixation: 4% formaldehyde from PFA. Primary antibody: Mouse anti-pSer129 Antibody at 1/1000 24 hours at 4°C. Secondary antibody: FITC Goat Anti-Mouse (green) at 1/700 for 1 hour at RT. Counterstain: Hoechst (blue) nuclear stain at 1/4000 for 1 hour at RT. Localization: Lewy body incluscions. Magnification: 20x.

  • SDS-PAGE analysis of ab218819.


ab218819 has not yet been referenced specifically in any publications.

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