Anti α-Synuclein Antibodies

α-Synuclein (α-Syn) is a 140-amino acid protein. In humans, three synuclein isoforms have been identified: α-, β-, and γ-synuclein. Both α- and β-synuclein are abundantly expressed in the presynaptic terminals in the central nervous system¹⁾. In contrast, γ-synuclein is scarcely expressed in the nervous system and its association with breast and ovarian cancers has been reported^2-3). Although the precise physiological functions of synucleins have not yet been fully elucidated, α-synuclein is thought to be involved in the regulation of neurotransmitter release⁴⁾ and the formation and clustering of synaptic vesicles^5-6).

α-Synuclein readily undergoes fibrillization and is believed to accumulate in the brain in its aggregated form, where it exerts cytotoxic effects. Disorders characterized by the accumulation of α-synuclein are collectively referred to as synucleinopathies, including Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. In 1997, mutations in the α-synuclein gene were identified as the cause of familial Parkinson’s disease⁷⁾. Subsequently, α-synuclein was shown to be the principal component of Lewy bodies found in the brains of patients with sporadic Parkinson’s disease^8-9). These findings focused significant attention on the relationship between Parkinson’s disease and α-synuclein. Biochemical analyses have further revealed that α-synuclein present in Lewy bodies undergoes post-translational modifications such as phosphorylation and ubiquitination. Notably, nearly all accumulated α-synuclein is phosphorylated, and ongoing research is investigating how the phosphorylation of α-synuclein contributes to the onset and progression of Parkinson’s disease.

Previous studies suggest that fibrillized and abnormally accumulated α-synuclein may trigger neuronal cell death, which may be one of the underlying causes of Parkinson’s disease. However, it remains unclear whether the primary cytotoxic species is aggregated α-synuclein itself, intermediate species formed during aggregation, or earlier-stage α-synuclein fibrils. In recent years, α-synuclein fibrils have been reported to propagate between cells¹⁰⁾, with extracellular vesicles (EVs), such as exosomes, potentially playing a role in this transmission¹¹⁾. Such intercellular spread is thought to be a critical step in the onset and progression of Parkinson’s disease, and further elucidation of its underlying mechanisms is highly anticipated.

This product is a mouse monoclonal antibody that specifically reacts with Ser129-phosphorylated α-synuclein. α-Synuclein found in Lewy bodies of patients with Parkinson’s disease and dementia with Lewy bodies is known to be phosphorylated at Ser129^12-13). This product does not react with unphosphorylated α-synuclein and selectively recognizes only accumulated Ser129-phosphorylated α-synuclein. Accordingly, it is suitable for visualizing Lewy bodies by immunohistochemistry and for detecting Ser129-phosphorylated α-synuclein by Western blotting.

Antibody Information

Clonality	Monoclonal (Clone No. pSyn#64)
Antigen	Human α-synuclein (residues 124–134) phosphorylated at Ser129
Host	Mouse
Formulation	Cell culture supernatant containing serum, 0.05% sodium azide
Conjugate	Unconjugated
Cross-reactivity	Human, Mouse, Rat (α-synuclein phosphorylated at Ser129)
Application	Immunohistochemistry 1:1,000-10,000 Western blotting 1:1,000-10,000

Application Data

Immunohistochemistry

Detection of Ser129-phosphorylated α-synuclein in skin biopsy specimens from patients with synucleinopathies

Gibbons et al. (JAMA, 331(15), 1298 (2024))¹⁴⁾ investigated whether synucleinopathies—such as Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies—could be detected by analyzing α-synuclein in skin biopsy specimens using Fujifilm Wako’s Anti Phosphorylated α-Synuclein, Monoclonal Antibody (pSyn#64).

[Result]
The proportion of skin biopsy specimens positive for Ser129-phosphorylated α-synuclein was 92.7% in Parkinson’s disease, 98.2% in multiple system atrophy, 96.0% in dementia with Lewy bodies, and 100% in pure autonomic failure, whereas only 3.3% of individuals without a history of synucleinopathy (control group) tested positive (Table 1).

This product is a biotin-conjugated anti-Ser129-phosphorylated α-synuclein monoclonal antibody (pSyn#64). It enables sensitive detection of Ser129-phosphorylated α-synuclein with low background using techniques such as the avidin-biotin complex (ABC) method in combination with peroxidase-conjugated streptavidin.

Antibody Information

Clonality	Monoclonal (Clone No. pSyn#64)
Antigen	Human α-synuclein (residues 124–134) phosphorylated at Ser129
Host	Mouse
Formulation	D-PBS, 0.05% sodium azide
Conjugate	Biotin-conjugated
Cross-reactivity	Human, Mouse, Rat (α-synuclein phosphorylated at Ser129)
Application	Immunocytochemistry 1:200-5,000 Immunohistochemistry 1:200-5,000

Application Data

Immunohistochemistry

[Result]
By combining the biotin-labeled antibody with the ABC method, background staining was reduced compared with detection using a secondary antibody, resulting in clearer, more distinct staining.

Fujifilm Wako also offers bulk supply of this product (mg scale). Testing for antibody activity (titer) and protein concentration can also be performed upon request. For inquiries, please contact us at .

• Please note that, depending on your specific requirements, bulk supply may not be available, or delivery may take additional time.
• Certain products may not be available for commercial use. For commercial applications, please contact Fujifilm Wako prior to such use.

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    Skin Biopsy Detection of Phosphorylated α-Synuclein in Patients With Synucleinopathies