Rabbit monoclonal [MJF-R13 (8-8)] to Alpha-synuclein (phospho S129)
ab168381 only detects alpha Synuclein phosphorylated on Ser129.
WBmore details Unsuitable for:
Flow Cyt,ICC/IF,IHC-P or IP
Synthetic peptide within Human Alpha-synuclein (phospho S129). The exact sequence is proprietary. Database link: 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.
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
We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.
This product is a recombinant rabbit monoclonal antibody.
Shipped 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.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Predicted molecular weight: 14 kDa.
Is unsuitable for Flow Cyt,ICC/IF,IHC-P or IP.
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.
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
Belongs to the synuclein family.
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.
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.
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Western blot - Anti-Alpha-synuclein (phospho S129) antibody [MJF-R13 (8-8)] (ab168381)This image is courtesy of Drs. Shyra Gardai and Jennifer Johnston (Elan Pharmaceuticals)
All lanes : Anti-Alpha-synuclein (phospho S129) antibody [MJF-R13 (8-8)] (ab168381) at 1/1000 dilution
Lane 1 : Recombinant alpha Synuclein expressed in BL21 bacterial cells Lane 2 : Recombinant alpha Synuclein expressed in BL21 bacterial cells, in the presence of Human Polo-Like Kinase 2 Lane 3 : HEK whole cell lysates, stably-transfected with Polo-Like Kinase 2 and alpha Synuclein
Tolö J et al. Pathophysiological Consequences of Neuronal a-Synuclein Overexpression: Impacts on Ion Homeostasis, Stress Signaling, Mitochondrial Integrity, and Electrical Activity. Front Mol Neurosci11:49 (2018).
Read more (PubMed: 29563864) »
Henderson MX et al. LRRK2 activity does not dramatically alter a-synuclein pathology in primary neurons. Acta Neuropathol Commun6:45 (2018).
Read more (PubMed: 29855356) »