| Storage Buffer | PBS pH 7.4 |
| Storage Temperature | -80ºC |
| Shipping Temperature | Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. |
| Purification | Ion-exchange Purified |
| Cite This Product | Human Recombinant Alpha Synuclein Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-321) |
| Certificate of Analysis | Certified >95% pure using SDS-PAGE analysis. Low endotoxin <5 EU/mL @ 2mg/mL. |
| Other Relevant Information | For corresponding PFFs, see catalog# SPR-322 |
| Alternative Names | Alpha-synuclein, Alpha synuclein, Asyn, SNCA, NACP, PARK1, PARK4, PD1, Synuclein alpha, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein Alpha-140, SYN, Parkinson's disease familial 1 Protein Protein |
| Research Areas | Alzheimer's Disease, Neurodegeneration, Neuroscience, Parkinson's Disease, Synuclein, Tangles & Tau, Multiple System Atrophy |
| Cellular Localization | Cytoplasm, Membrane, Nucleus |
| Accession Number | NP_000336.1 |
| Gene ID | 6622 |
| Swiss Prot | P37840 |
| Scientific Background |
Alpha-synuclein (α-syn), a 140-amino acid neuronal protein encoded by the SNCA gene, plays a pivotal role in synaptic vesicle trafficking, neurotransmitter release, and SNARE-complex assembly. In its native monomeric form, α-syn enhances synaptic vesicle priming and fusion, contributing to efficient neuronal communication. However, dysregulation of α-syn monomers is increasingly recognized as a critical early event in the pathogenesis of neurodegenerative disorders, particularly synucleinopathies such as Parkinson’s disease (PD), Lewy body dementia (LBD), and multiple system atrophy (MSA). [www.uniprot.org] Recent studies reveal that monomeric α-syn can misfold and aggregate into toxic oligomers and fibrils, initiating a prion-like cascade of intracellular and intercellular propagation. This aggregation disrupts synaptic integrity, impairs dopamine neurotransmission, and triggers neuroinflammation, ultimately leading to neuronal death. Moreover, mutations in SNCA and environmental factors such as exposure to neurotoxins (e.g., rotenone) exacerbate α-syn pathology, accelerating disease progression. [www.mdpi.com], [link.springer.com] [www.frontiersin.org] Understanding the molecular dynamics of α-syn monomers, including their interactions with membrane receptors like P2RX7, offers promising avenues for therapeutic intervention. Targeting monomeric α-syn before pathological aggregation occurs may provide a strategic window for disease-modifying therapies. As research advances, α-syn monomers continue to emerge as a focal point in unraveling the mechanisms of neurodegeneration and developing precision treatments for synucleinopathies. |
| References |
1. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013). 2. Zhang L., et al. (2008) Brain Res. 1244: 40-52. 3. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117. 4. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230. 5. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840. 6. Mezey E., et al. (1998) Nat Med. 4(7): 755-757. |
Type 1 alpha synuclein pre-formed fibrils (SPR-322) seed the formation of new alpha synuclein fibrils from the pool of alpha synuclein monomers (SPR-321). Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha synuclein fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to alpha synuclein protein aggregation) over time when 10 nM of Type 1 alpha synuclein pre-formed fibrils (SPR-322) is combined with 100 µM of alpha synuclein monomer (SPR-321), as compared to when 10 nM of Type 1 alpha synuclein pre-formed fibrils (SPR-322) is combined with 100 µM of alpha Synuclein monomer (SPR-316). Thioflavin T ex = 450 nm, em = 485 nm.
StressMarq Biosciences :
Based on validation through cited publications.