Alpha Synuclein S87N Mutant Monomers
Product Sizes
100 ug
SPR-499-100UG
2 x 100 ug
SPR-499-2X100UG
500 ug
SPR-499-500UG
About this Product
- SKU:
- SPR-499
- Additional Names:
- Alpha Synuclein S87N, Alpha-synuclein, Alpha synuclein, SNCA, synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, PARK1, SYN, Parkinson's disease familial 1 Protein, Asyn
- Application:
- Cell-based/Functional Assay, SDS-PAGE, Western Blot
- Buffer:
- 1X PBS pH 7.4
- CE/IVD:
- RUO
- Extra Details:
- Alpha-synuclein (A Alpha-synuclein), encoded by the SNCA gene, is a neuronal protein critically involved in synaptic vesicle trafficking, neurotransmitter release, and SNARE-complex assembly. The S87N mutation represents a single amino acid substitution within the non-amyloid-B Beta component (NAC) region, a domain essential for A Alpha-synuclein aggregation and membrane interactions. In its monomeric form, wild-type A Alpha-synuclein contributes to synaptic homeostasis by modulating vesicle fusion and exocytotic pore dynamics. However, the S87N mutant alters these physiological functions, potentially disrupting calcium-dependent exocytosis and impairing SNARE-complex formation. These changes may accelerate synaptic dysfunction and neuronal vulnerability, key features of Parkinson's disease and related synucleinopathies. Research utilizing S87N mutant monomers has revealed their distinct biophysical properties, including altered aggregation kinetics and membrane binding affinity. These characteristics make them valuable tools for modeling early-stage neurodegeneration, enabling precise investigation of pathogenic mechanisms such as protein misfolding, intracellular trafficking defects, and neuroinflammation. By mimicking disease-relevant molecular events, S87N mutant monomers serve as a robust platform for screening therapeutic candidates aimed at stabilizing A Alpha-synuclein structure, preventing toxic oligomer formation, and restoring synaptic function. Their use in cellular and animal models enhances translational research targeting the molecular underpinnings of Parkinson's disease and other A Alpha-synuclein-driven disorders. Human alpha synuclein S87N mutant (HuS87N) has Ser87 mutated to the equivalent mouse residue Asn87, effectively making it a human-mouse chimeric protein. Despite sequence differences at only seven residues, or 5% of the total 140 amino acids, the aggregation rate of wild-type mouse A Alpha-syn (MsWT) is faster than wild-type human A Alpha-syn (HuWT) in vitro. In wild-type mouse models, MsWT fibrils are more efficient than HuWT fibrils at inducing pathology of endogenous mouse A Alpha-syn (1). A53T or S87N substitutions in human A Alpha-syn substantially accelerate fibrilization rates in vitro (2,3). Chimeric HuS87N fibrils show enhanced pathogenicity to wild-type mouse neurons, greater than HuWT, HuA53T, and MsWT fibrils (4). HuS87N fibrils can be used as a more human-like alternative to MsWT fibrils to induce equivalent or greater endogenous A Alpha-syn seeding and pathology in wild-type mice.
- Immunogen:
- Alpha Synuclein S87N Monomers
- Molecular Weight:
- 14.46 kDa
- Purity:
- >95%
- Purification:
- Ion Exchange
- Sequence:
- MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
- Shipping Conditions:
- Dry Ice
- Storage Conditions:
- -70[o]C
- Supplier:
- StressMarq Biosciences
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
- Manufacturer's Data Sheet:https://www.stressmarq.com/products/protein/human-alpha-synuclein-s87n-monomers-spr-499/
