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Overview

  • Product namealpha Synuclein proteinSee all alpha Synuclein proteins and peptides ...
  • Protein descriptionRecombinant full length protein (Human); A Parkinson's disease-related point mutant (A30P).
  • Expression hostE. coli

    • Properties

  • Purity> 95 % by SDS-PAGE
  • Purification notesThis recombinant protein was purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.
  • FormLiquid
  • Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
  • Concentration information loading...
  • Sequence notesMDVFMKGLSK/AKEGVVAAAE/KTKQGVAEA[P]/GKTKE GVLYV/GSKTKEGVVH/ GVATVAEKTK/EQVTNVGGAV /VTGVTAVAQK/TVEGAGSIAA/ATGFVKKDQL/ GKNEEGAPQE/GILEDMPVDP/DNEAYEMPSE/EGYQDYE PEA/
  • Research Areas

    • Applications

    Our Abpromise guarantee covers the use of ab51181 in the following tested applications.

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

    Application Notes
    SDS-PAGE SDS-PAGE: Use at an assay dependent dilution.

    Protein info

    • Alternative names
        Alpha synucleinAlpha-synucleinAlpha-synuclein, isoform NACP140
        alphaSYNMGC105443MGC110988MGC127560MGC64356NACPNon A beta component of AD amyloidNon A4 component of amyloidNon A4 component of amyloid precursorNon-A beta component of AD amyloidNon-A-beta component of alzheimers disease amyloid , precursor ofNon-A4 component of amyloid precursorOTTHUMP00000218549OTTHUMP00000218551OTTHUMP00000218552OTTHUMP00000218553OTTHUMP00000218554PARK 1PARK 4PARK1PARK4Parkinson disease (autosomal dominant, Lewy body) 4Parkinson disease familial 1PD 1PD1SNCASnca synuclein, alpha (non A4 component of amyloid precursor)Synuclein alphaSynuclein alpha 140Synuclein, alpha (non A4 component of amyloid precursor)SYUA_HUMAN
      see all
  • 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 diseaseNote=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.
    Defects in SNCA are the cause of Parkinson disease type 1 (PARK1) [MIM:168601]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.
    Defects in SNCA are the cause of Parkinson disease type 4 (PARK4) [MIM:605543]. A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia.
    Defects in SNCA are the cause of dementia Lewy body (DLB) [MIM:127750]. A neurodegenerative disorder clinically characterized by mental impairment leading to dementia, parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.
  • 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.
  • Post-translational
    modifications    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.
  • Cellular localizationCytoplasm. Membrane. Nucleus. Cell junction > synapse. Membrane-bound in dopaminergic neurons.

    • Target information above from: UniProt accession P37840 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    alpha Synuclein protein images

    • SDS-PAGE - alpha Synuclein protein (ab51181)
      SDS-PAGE - alpha Synuclein protein (ab51181)
      ab51181 in 14% SDS-PAGE

    References for alpha Synuclein protein (ab51181)

    ab51181 has not yet been referenced specifically in any publications.

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