Alpha Synuclein Monomers: Biotinylated
Product Sizes
100 ug
SPR-527-100UG
2 x 100 ug
SPR-527-2X100UG
5 x 100 ug
SPR-527-5X100UG
About this Product
- SKU:
- SPR-527
- Additional Names:
- Alpha-synuclein, A Alpha-synuclein, SNCA, Synelfin, NACP, Non-AB Beta component of Alzheimer's disease amyloid protein, Non-A beta component precursor, NACP140, PARK1 protein, PARK4 protein, Synuclein alpha, ASYN, Alpha-syn, Macaca fascicularis, UniProt: A0A2K5XN13
- Application:
- Cell-based/Functional Assay, SDS-PAGE, Western Blot
- Buffer:
- PBS
- CE/IVD:
- RUO
- Conjugate:
- Biotin
- Concentration:
- 2 mg/ml
- Extra Details:
- Alpha-synuclein is a 140-amino-acid neuronal protein encoded by the SNCA gene and is highly enriched at presynaptic terminals, where it regulates synaptic vesicle trafficking, neurotransmitter release, and membrane interactions. In neurodegenerative disorders such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, misfolded alpha-synuclein adopts aggregation-prone conformations that progress from soluble monomers to toxic oligomers and fibrils, ultimately forming Lewy body pathology and driving cellular dysfunction and neurodegeneration. Biotinylated alpha-synuclein monomers provide a powerful, targeted tool for dissecting the earliest molecular events underlying synuclein aggregation. Because monomeric alpha-synuclein participates directly in membrane binding, vesicle regulation, and aggregation initiation, biotinylated forms enable high-sensitivity tracking, pulldown assays, protein-protein interaction mapping, and real-time monitoring of conformational transitions essential to disease progression. These labeled monomers facilitate precise identification of proteins that associate with early aggregation intermediates, advancing mechanistic understanding of how monomeric alpha-synuclein transitions to pathogenic species. Biotinylated monomers also strengthen translational research by enabling controlled seeding assays, quantification of aggregation kinetics, and high-resolution characterization of structural changes during oligomer formation. Such approaches help model prion-like propagation, evaluate therapeutic candidates that target early misfolding, and refine biomarker discovery for synucleinopathies. Their versatility makes biotinylated alpha-synuclein monomers a critical component of modern neurodegenerative disease research, offering a direct window into the molecular determinants that initiate and accelerate pathological protein aggregation. A 15 amino acid tag on the C-terminal tail of alpha synuclein facilitates site-specific covalent biotinylation. Biotinylation of purified alpha synuclein allows for many biological applications, such as monitoring and detection using streptavidin-based conjugates. StressMarq's biotinylated monomers are also used to generate pre-formed fibrils in-vitro.
- Immunogen:
- Alpha Synuclein Monomers (Cynomolgus)
- Molecular Weight:
- 16.28 kDa
- Purity:
- >95%
- Purification:
- Ion Exchange
- Sequence:
- MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFIKKDQLGKNEGAPQEGILQDMPVDPDNEAYEMPSEEGYQDYEPEAGLNDIFEAQKIEWHE
- Shipping Conditions:
- Dry Ice
- Storage Conditions:
- -70[o]C
- Supplier:
- StressMarq Biosciences
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Conjugated Protein
- Manufacturer's Data Sheet:https://www.stressmarq.com/products/protein/alpha-synuclein-monomers:-biotinylated-spr-527/
