Key features and details
- Rabbit polyclonal to Alpha-synuclein (phospho Y125)
- Suitable for: ELISA
- Reacts with: Recombinant fragment
- Isotype: IgG
Product nameAnti-Alpha-synuclein (phospho Y125) antibody
See all Alpha-synuclein primary antibodies
Species reactivityReacts with: Recombinant fragment
Predicted to work with: Mouse, Rat, Human
Synthetic peptide. This information is proprietary to Abcam and/or its suppliers.
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Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Batches of this product that have a concentration < 1mg/ml may have BSA added as a stabilising agent. If you would like information about the formulation of a specific lot, please contact our scientific support team who will be happy to help.
Concentration information loading...
PurityImmunogen affinity purified
Corresponding Unmodified Peptide
Use at an assay dependent concentration.
Use at an assay dependent concentration.
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.
modificationsPhosphorylated, 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
- Alpha synuclein antibody
- Alpha-synuclein antibody
- Alpha-synuclein, isoform NACP140 antibody
ab10789 has been referenced in 9 publications.
- Akiyama T et al. Synthetic mRNA-based differentiation method enables early detection of Parkinson's phenotypes in neurons derived from Gaucher disease-induced pluripotent stem cells. Stem Cells Transl Med 10:572-581 (2021). PubMed: 33342090
- Fayyad M et al. Investigating the presence of doubly phosphorylated a-synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases. Brain Pathol 30:831-843 (2020). PubMed: 32324926
- Krejciova Z et al. Replication of multiple system atrophy prions in primary astrocyte cultures from transgenic mice expressing human a-synuclein. Acta Neuropathol Commun 7:81 (2019). PubMed: 31109379
- Vicente Miranda H et al. Posttranslational modifications of blood-derived alpha-synuclein as biochemical markers for Parkinson's disease. Sci Rep 7:13713 (2017). PubMed: 29057912
- Kiely AP et al. a-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy? Acta Neuropathol 125:753-69 (2013). ICC/IF ; Human . PubMed: 23404372
- Schiess MC et al. CSF from Parkinson disease patients differentially affects cultured microglia and astrocytes. BMC Neurosci 11:151 (2010). ICC/IF ; Human . PubMed: 21114836
- Dinh K et al. Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Cytokine 45:179-83 (2009). ICC/IF ; Human . PubMed: 19157893
- Chen L et al. Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation. J Clin Invest : (2009). WB ; Drosophila melanogaster . PubMed: 19855133
- Bick RJ et al. Cytokines disrupt intracellular patterns of Parkinson's disease-associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Brain Res 1217:203-12 (2008). ICC/IF ; Human . PubMed: 18501880