Recombinant Human alpha Synuclein protein (ab123758)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP37840
    • SpeciesHuman
    • SequenceMDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVH GVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
    • Molecular weight14 kDa
    • Amino acids1 to 140

Specifications

Our Abpromise guarantee covers the use of ab123758 in the following tested applications.

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

  • Applications

    SDS-PAGE

    HPLC

  • Purity> 95 % SDS-PAGE.
    Purity also by analysis by RP-HPLC. Purified by proprietary chromatographic techniques.
  • FormLiquid
  • Additional notesAlthough stable 4°C for 4 weeks, ab123758 should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Please see notes section.

    pH: 7.50
    Constituents: 0.01% Magnesium chloride, 0.32% Tris HCl, 0.58% Sodium chloride

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
    • PD 1
    • PD1
    • SNCA
    • 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
  • 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 diseaseGenetic 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 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.
    Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
  • Cellular localizationCytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
  • Information by UniProt

References for Recombinant Human alpha Synuclein protein (ab123758)

ab123758 has not yet been referenced specifically in any publications.

Product Wall

There are currently no Abreviews or Questions for ab123758.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"