Recombinant Human Alpha-synuclein protein aggregate (Control) (ab218817)



  • Nature
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
    • Sequence
    • Molecular weight
      14 kDa
    • Amino acids
      1 to 140


Our Abpromise guarantee covers the use of ab218817 in the following tested applications.

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

  • Applications


    Functional Studies

  • Purity
    = 92 % SDS-PAGE.
    ab218817 is purified by ion-exchange and 0.2µm filtered.
  • Form
  • Additional notes

    ab218817 is a protein aggregate which can be used as a control in various assays. 

    Learn more.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 7.50
    Constituents: 0.24% Tris, 0.87% Sodium chloride

    0.2µm filtered solution

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


  • SDS-PAGE analysis of ab218817.

  • Immunohistochemical analysis of 4% formaldehyde fixed primary rat hippocampal neurons from Sprague-Dawley rat labeling lewy body inclusions formed when treated with active Alpha Synuclein Protein Aggregate at 4 µg/ml (D-F), but not when treated with ab218817 at 4 µg/ml (A-C). 

    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 hours at RT. Counterstain: Hoechst (blue) nuclear stain at 1/4000 for 1 hour at RT. Magnification: 20x.

  • 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.


ab218817 has not yet been referenced specifically in any publications.

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