Overview

Description

  • Nature
    Synthetic
  • Amino Acid Sequence

    Associated products

    Specifications

    Our Abpromise guarantee covers the use of ab188826 in the following tested applications.

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

    • Applications

      Blocking - Blocking peptide for Anti-Alpha-synuclein (phospho S129) antibody [EP1536Y] (ab51253)

    • Form
      Liquid
    • Additional notes

      - First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
      - If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
      - Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
      - Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
      - Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.

    • Concentration information loading...

    Preparation and Storage

    • Stability and Storage

      Shipped at 4°C. Store at -20°C or -80°C.

      Information available upon request.

    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)
      • 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.
    • Information by UniProt

    References

    This product has been referenced in:
    • Martinez-Valbuena I  et al. Interaction of amyloidogenic proteins in pancreatic ß cells from subjects with synucleinopathies. Acta Neuropathol N/A:N/A (2018). IHC-P ; Human . Read more (PubMed: 29536165) »
    See 1 Publication for this product

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

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