Product nameAnti-Alpha-synuclein (phospho S129) antibody
See all Alpha-synuclein primary antibodies
DescriptionRabbit polyclonal to Alpha-synuclein (phospho S129)
SpecificityDetects endogenous levels of Synuclein only when phosphorylated at serine 129. Due to 69% sequence homology ab59264 might react with Beta synuclein
Tested applicationsSuitable for: ICC/IF, IHC-P, ELISA, IHC-FoFr, WB, IHC-Frmore details
Species reactivityReacts with: Mouse, Human
Synthetic peptide corresponding to Human Alpha-synuclein. Synthetic phosphopeptide derived from Human Synuclein around the phosphorylation site of serine 129 (M-P-SP-E-E).
- Human brain.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol, 0.87% Sodium chloride
Without Mg+2 and Ca+2
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab59264 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||Use at an assay dependent concentration. PubMed: 22513881|
|IHC-P||1/50 - 1/100.|
|IHC-FoFr||Use at an assay dependent concentration. PubMed: 20098733|
|WB||1/500 - 1/1000.|
|IHC-Fr||Use at an assay dependent concentration. PubMed: 23664753|
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
Locally administered rotenone induces alpha-synuclein phosphorylation, accumulation and aggregation with gliosis in ENS ganglia
Mouse ganglia tissue stained for Alpha-synuclein (phospho S129) using ab59264 at 1/50 dilution in immunohistochemical analysis.
Section from an untreated mouse is shown in Panel I. Section from a rotenone-treated mouse is shown in Panel J.
(After Figure 1 of Pan-Motojo et al)
All lanes : Anti-Alpha-synuclein (phospho S129) antibody (ab59264) at 1/500 dilution
Lane 1 : Mouse brain whole cell lysates
Lane 2 : Mouse brain whole cell lysates with immunogen phosphopeptide
Immunohistochemical analysis of paraffin-embedded human brain tissue using ab59264 at a dilution of 1/50-1/100. Left hand image - without immunising peptide; right hand image - with immunising peptide.
All lanes : Anti-Alpha-synuclein (phospho S129) antibody (ab59264) at 1/1000 dilution
Lanes 1-3 : Whole tissue lysate prepared from young transgenic mouse overexpressing human alpha-synuclein
Lanes 4-6 : Whole tissue lysate prepared from old transgenic mouse overexpressing human alpha-synuclein
Lane 7 : Whole tissue lysate prepared from KO mouse
Lysates/proteins at 50 µg per lane.
All lanes : Goat anti-rabbit Ig (H+L) HRP at 1/1000 dilution
Developed using the ECL technique.
Observed band size: 18,19 kDa why is the actual band size different from the predicted?
Additional bands at: 60 kDa, 80 kDa. We are unsure as to the identity of these extra bands.
Exposure time: 5 minutes
This product has been referenced in:
- Forrest SL et al. Coexisting Lewy body disease and clinical parkinsonism in frontotemporal lobar degeneration. Neurology 92:e2472-e2482 (2019). Read more (PubMed: 31019099) »
- Shahmoradian SH et al. Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes. Nat Neurosci 22:1099-1109 (2019). Read more (PubMed: 31235907) »