Sigma-Aldrich Anti-#-Synuclein Amyloidfibrils Clsyn-F2

Full-length, GST-tagged, recombinant human -synuclein. (Ardah, et al., (2014), Front. Aging Neurosci. 6, Article 197).

Quality Control Testing

Evaluated by ELISA with -synuclein amyloid fibrils.

ELISA: A representative lot of this antibody detected -synuclein amyloid fibrils in ELISA application.

Tested Applications

Dot Blot: A representative lot detected -synuclein in Dot Blot application (Vaikath, N.N., et al. (2015). NeuroBiol Dis. 79:81-99).

ELISA Analysis: A representative lot detected -synuclein in ELISA application (Vaikath, N.N., et al. (2015). NeuroBiol. Dis. 79:81-99).

Immunohistochemistry Applications: A representative lot detected -synuclein in Immunohistochemistry applications (Vaikath, N.N., et al. (2015). NeuroBiol Dis. 79:81-99; El-Agnaf, O., et al. (2017). Neurobiol Dis. 104:85-96).

Dot Blot Analysis: A 1:1,000 dilution from a representative lot detected -synuclein amyloid fibrils.

Surface Plasmon Resonance: A representative lot detected -synuclein in Surface plasmon resonance applications (Vaikath, N.N., et al. (2015). NeuroBiol Dis. 79:81-99).

Immunofluorescence Analysis: A representative lot detected -synuclein in Immunofluorescence applications (Vaikath, N.N., et al. (2015). NeuroBiol. Dis. 79:81-99).

Inhibition: A representative lot of this antibody inhibited ELISA signal generated with -synuclein fibrils (Vaikath, N.N., et al. (2015). NeuroBiol Dis. 79:81-99).

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

Clone Syn-F2 is a mouse monoclonal antibody that detects -synuclein amyloid fibrils.

Purified mouse monoclonal antibody IgG1 in PBS without preservatives.

1.0 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.

Store at -10°C to -25°C. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Alpha-synuclein (UniProt: P37840; also known as Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor (NACP)) is encoded by the SNCA (also known as NACP, PARK1) gene (Gene ID: 6622) in human. -synuclein amyloid fibrils are highly ordered protein aggregates implicated in neurodegenerative diseases, particularly Parkinson s Disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). These fibrils are derived from the misfolding and aggregation of -synuclein, a presynaptic neuronal protein that plays critical roles in synaptic vesicle trafficking and membrane interactions. The fibrillation process disrupts cellular homeostasis, leading to neuronal toxicity and cell death. Cryo-electron microscopy (cryo-EM) has revealed protofilament arrangements in lipid-bound -synuclein fibrils, highlighting their polymorphic nature. These protofilaments are stabilized by cross-β structures within the central domain, referred to as the non-amyloid-β component (NAC). The N-terminal domain contributes to membrane binding, while the acidic C-terminal tail modulates fibril formation and aggregation dynamics. Specific residues, such as those in the N-terminal region (e.g. residues 2-7), have been shown to regulate fibril formation via lipid-dependent and lipid-independent pathways. Mutations associated with familial PD, such as A53T and E46K, further influence fibril conformation and aggregation propensity, exacerbating neuronal damage. The interaction of -synuclein fibrils with cellular membranes plays a central role in their pathogenicity. Fibrils disrupt lipid bilayers, leading to vesicle leakage and mitochondrial dysfunction. Structural analyses have demonstrated how -synuclein fibrils extract lipids from vesicles, forming stable fibril-lipid complexes that contribute to cellular toxicity. Additionally, environmental factors such as pH, ionic strength, and post-translational modifications (e.g., phosphorylation at serine 129) modulate fibril formation and structural polymorphism. The accumulation of -synuclein fibrils in Lewy bodies and neurites is a hallmark of PD and DLB. (Ref.: Miraglia F, et al, (2018). Neural Regen Res.13(7),1136-1144; Liu, K., et al., (2024). Proc Natl Acad Sci USA. 121(35), e232163312; Sant, V., et al., (2025). Nat Commun. 16, 760).

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.