Formation and accumulation of misfolded α-Synuclein aggregates and fibrils is a hallmark of several neurodegenerative disorders known as Synucleinopathies including Parkinson’s disease (PD). Antibodies against this protein are used as the gold standard for immunostaining of Lewy bodies which are a common pathological feature of PD.
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To facilitate research in PD, BioLegend has licensed four mouse monoclonal antibodies (clones Syn-O2, Syn-O3, Syn-O4, and Syn-F1) that were generated in the laboratory of Professor Omar El-Agnaf at United Arab Emirates University (UAEU). These clones allow detection of diseased forms of α-Synuclein including those in the intermediate aggregation state. They provide unique specificity for:
- Aggregated and fibrillar forms of α-Synuclein
- Minimal cross-reactivity with its native form
- No cross-reactivity with Amyloid beta (Ab 1-42) or β- and γ-Synucleins
- Validated in FFPE PD brain tissue sections
- Suitable for IHC and dot blot
Highlighted relevant publications from Professor El-Agnaf Laboratory
The laboratory has explored the potential use of α-Synuclein as a biomarker for PD. They generated and characterized several novel conformation-specific antibodies for α-Synuclein including clone Syn-O2. They utilized various methods to validate the specificity of this clone in recognizing the oligomeric forms of α-Synuclein. For example, using immunohistochemical studies, they demonstrated staining of Lewy bodies and Lewy neurites with Syn-O2 in tissues derived from PD patients. They then developed a highly specific ELISA assay to quantify α-Synuclein species in biological samples from PD patients and aged-matched healthy controls using clone Syn-O2. Read more in the articles below:
Vaikath NN, et al. 2015. Neurobiol Dis. 79:81 (PubMed)
Majbour NK, et al. 2016. Mol Neurodegener. 11:7 (PubMed)
Learn more about Parkinson’s disease and associated proteins.
IHC staining of α-Synuclein deposits with anti-α-Synuclein, aggregated antibody (clone Syn-O3) on formalin-fixed paraffin-embedded Parkinson's disease brain tissue.
Dot-blot of anti-α-Synuclein antibodies (clones Syn-O3 and 4B12/Synuclein) demonstrating their binding to α-Synuclein conformers (monomeric and fibrillary forms). Note that these antibodies do not cross-react with amyloid beta peptide (Aβ1-42). Clone 4B12/Synuclein was included as a comparison for binding to monomeric and aggregated forms of α-Synuclein.
Purified anti-α-Synuclein Phospho (Tyr39)
Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson’s disease.
Purified anti-α-Synuclein, 117-122
α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-Synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.
Purified anti-α-Synuclein (C-Terminal Truncated x-122)
Alpha-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms include, α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. Phosphorylation of α-synuclein at Tyr39 may modulate clearance of the protein and contribute to Parkinson's disease.