Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [MJF-R13 (8-8)] to Alpha-synuclein (phospho S129) - BSA and Azide free
- Suitable for: WB
- Reacts with: Human
Product nameAnti-Alpha-synuclein (phospho S129) antibody [MJF-R13 (8-8)] - BSA and Azide free
See all Alpha-synuclein primary antibodies
DescriptionRabbit monoclonal [MJF-R13 (8-8)] to Alpha-synuclein (phospho S129) - BSA and Azide free
Tested applicationsSuitable for: WBmore details
Unsuitable for: Flow Cyt,ICC/IF,IHC-P or IP
Species reactivityReacts with: Human
Synthetic phosphopeptide, corresponding to residues surrounding Serine 129 of Human alpha Synuclein (UniProt: P37840).
- Recombinant alpha-synuclein, expressed in BL21 bacterial cells in the presence of Human Polo-Like Kinase 2; HEK whole cell lysates, stably-transfected with Polo-Like Kinase 2 and alpha Synuclein.
ab209421 is the carrier-free version of ab168381 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.
Ab209421 is compatible with the Maxpar® Antibody Labeling Kit from Fluidigm.
Maxpar® is a trademark of Fluidigm Canada Inc.
Alpha-synuclein was the first gene to be linked to Parkinson’s disease (PD) and remains the most promising link to PD pathogenesis, where there is genetic evidence that it may play a causal role. In the brain, alpha-synuclein is concentrated in presynaptic nerve terminals. The deposition of the abundant presynaptic brain protein alpha-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of neurodegenerative disorders. These disorders include Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, collectively referred to as synucleinopathies. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin.
Recent studies also indicate that alpha-synuclein undergoes post-translational modification. Though the role of many of these modifications is still under investigation, phosphorylation at Serine 129 may affect alpha-synuclein aggregations and may also serve as marker of disease pathogenesis. With the advent of this phospho-specific Serine 129 antibody, The Michael J. Fox Foundation hopes to ensure that the putative role of this modification can be further examined by all researchers.
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. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferConstituent: PBS
Concentration information loading...
PurityImmunogen affinity purified
Clone numberMJF-R13 (8-8)
Our Abpromise guarantee covers the use of ab209421 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use at an assay dependent concentration. Predicted molecular weight: 14 kDa.|
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
ab209421 has not yet been referenced specifically in any publications.