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Neuroscience Neurology process Neurodegenerative disease Parkinson's disease Synuclein

Recombinant Human Alpha-synuclein (mutated E46K) protein (ab51188)

Recombinant Human Alpha-synuclein (mutated E46K) protein (ab51188)
  • ChIP - Anti-Histone H3 antibody - Nuclear Loading Control and ChIP Grade (ab1791)

Key features and details

  • Expression system: Escherichia coli
  • Purity: > 95% SDS-PAGE
  • Suitable for: SDS-PAGE

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Description

  • Product name

    Recombinant Human Alpha-synuclein (mutated E46K) protein
    See all Alpha-synuclein proteins and peptides
  • Purity

    > 95 % SDS-PAGE.
    Alpha Synuclein E46K was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques.
  • Expression system

    Escherichia coli
  • Accession

    P37840
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MDVFMKGLSK/ AKEGVVAAAE/ KTKQGVAEAA/ GKTKEGVLYV/ GSKTK[K]GVVH/GVATVAEKTK/EQVTNVGGAV/VT GVTAVAQK/TVEGAGSIAA/ ATGFVKKDQL/GKNEEGAPQE/GILEDM PVDP/DNEAYEMPSE/EGYQDYEPEA
    • Predicted molecular weight

      14 kDa
    • Amino acids

      1 to 140
    • Modifications

      mutated E46K

Preparation and Storage

  • 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)
    • SYUA_HUMAN
    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
    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.
    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.
  • 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

Images

  • SDS-PAGE - Recombinant Human Alpha-synuclein (mutated E46K) protein (ab51188)
    SDS-PAGE - Recombinant Human Alpha-synuclein (mutated E46K) protein (ab51188)
    ab51188 in 15%SDS-PAGE

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

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