Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [EP1536Y] to Alpha-synuclein (phospho S129) - BSA and Azide free
- Suitable for: IHC-P, ELISA, WB, ICC/IF, Dot blot
- Reacts with: Mouse, Rat, Human
Product nameAnti-Alpha-synuclein (phospho S129) antibody [EP1536Y] - BSA and Azide free
See all Alpha-synuclein primary antibodies
DescriptionRabbit monoclonal [EP1536Y] to Alpha-synuclein (phospho S129) - BSA and Azide free
Tested applicationsSuitable for: IHC-P, ELISA, WB, ICC/IF, Dot blotmore details
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide within Human Alpha-synuclein. The exact sequence is proprietary.
(Peptide available as
- Fetal brain lysate.
ab209422 is the carrier-free version of ab51253 This format is designed for use in antibody labeling, including fluorochromes, metal isotopes, oligonucleotides, enzymes.
Our carrier-free formats are supplied in a buffer free of BSA, sodium azide and glycerol for higher conjugation efficiency.
Use our conjugation kits for antibody conjugates that are ready-to-use in as little as 20 minutes with <1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Ab209422 is compatible with the Maxpar® Antibody Labeling Kit from Fluidigm.
Maxpar® is a trademark of Fluidigm Canada Inc.
Rat: We have preliminary internal testing data to indicate this antibody may not react with these species. Please contact us for more information.
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
Storage instructionsShipped at 4°C. Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle.
Storage bufferpH: 7.20
Concentration information loading...
PurityProtein A purified
Immunizing Peptide (Blocking)
Our Abpromise guarantee covers the use of ab209422 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||Use at an assay dependent concentration. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.|
|ELISA||Use at an assay dependent concentration.|
|WB||Use at an assay dependent concentration. Detects a band of approximately 18 kDa (predicted molecular weight: 14 kDa).Can be blocked with Alpha-synuclein (phospho S129) peptide (ab188826).|
|ICC/IF||Use at an assay dependent concentration.|
|Dot blot||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
This IHC data was generated using the same anti-phospho alpha synuclein S129 antibody clone, EP1536Y, in a different buffer formulation (cat# ab51253).
IHC image of alpha Synuclein (phospho S129) staining in Human Parkinson Substantia Nigra formalin fixed paraffin embedded tissue section*, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with ab51253, 10µg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX. The inset negative control image is taken from an identical assay performed on Human normal Substantia Nigra.
For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.
*Tissue obtained from the Human Research Tissue Bank, supported by the NIHR Cambridge Biomedical Research Centre
Dot blot analysis of alpha Synuclein (pS129) peptide (Lane 1), alpha Synuclein (unmodified) peptide (Lane 2) labelling alpha Synuclein (pS129) with ab51253 at a dilution of 1/1000. Peroxidase conjugated goat anti-rabbit IgG (H+L) was used as the secondary antibody at a dilution of 1/2500.
Blocking and dilution buffer: 5% NFDM/TBST.
Exposure time: 3 minutes.
This data was developed using the same antibody clone in a different buffer formulation containing PBS, BSA, glycerol, and sodium azide (ab51253).
This ELISA data was generated using the same anti-phospho alpha synuclein S129 antibody clone, EP1536Y, in a different buffer formulation (cat# ab51253).
Direct ELISA antibody dose-response curve using ab51253. Antibody concentration of 0-5000 ng/mL. Antigen concentration of 1000 ng/mL. An alkaline phosphatase conjugated goat anti-rabbit IgG (1/1000) was used as the secondary antibody.
ab209422 has been referenced in 18 publications.
- 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 . PubMed: 29536165
- Sasaki A et al. Sensitive western blotting for detection of endogenous Ser129-phosphorylated a-synuclein in intracellular and extracellular spaces. Sci Rep 5:14211 (2015). WB ; Human . PubMed: 26381815
- Gispert S et al. Potentiation of neurotoxicity in double-mutant mice with Pink1 ablation and A53T-SNCA overexpression. Hum Mol Genet 24:1061-76 (2015). WB, IHC-P, IHC-FrFl ; Mouse . PubMed: 25296918
- Wang S et al. Phosphatidylethanolamine deficiency disrupts a-synuclein homeostasis in yeast and worm models of Parkinson disease. Proc Natl Acad Sci U S A 111:E3976-85 (2014). PubMed: 25201965
- Beekes M et al. Is there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles? Acta Neuropathol 128:463-76 (2014). IHC . PubMed: 25073522