• Product name

    Recombinant Human Alpha-synuclein protein monomer (Active)
    See all Alpha-synuclein proteins and peptides
  • Biological activity

    100 µM alpha synuclein protein monomer (ab218818), seeded with 10 nM alpha synuclein protein aggregate 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 Molecular Devices Gemini XPS microplate reader.

  • Purity

    > 95 % SDS-PAGE.
    ab218818 is purified by ion exchange.
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

  • Nature

    • Species

    • Sequence

    • Predicted molecular weight

      14 kDa
    • Amino acids

      1 to 140
    • Additional sequence information

      (NP_000336.1) (GeneID 6622)
  • Description

    Recombinant human Alpha-synuclein protein (Active)


Our Abpromise guarantee covers the use of ab218818 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

    Western blot


  • Form

  • Additional notes

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.40
    Constituent: 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
    • 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 of ~14 kDa Human Recombinant Alpha Synuclein Protein Monomer (SPR-321). Lane 1: Molecular Weight Ladder (MW). Lane 2: Alpha Synuclein Protein Monomer (2 µg) (SPR-321).
  • 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 (ab218819) (dark blue).

    ThT ex = 450 nm, em = 485 nm. View protocol.

  • Arrow indicating SDS-PAGE of ab218818 at ~14 kDa.

    Lane 1: 5 µg BSA Control.

    Lane 2: 2.5 µg BSA Control.

    Lane 3: 5 µg of ab218818.

    Lane 4: 2.5 µg of ab218818.



ab218818 has not yet been referenced specifically in any publications.

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