SPR-481
Alpha Synuclein Monomers

Cannot supply to this region.
- SKU:
- SPR-481
- Additional 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
- Application:
- SDS-PAGE, WB, FuncS
- Concentration:
- 2 mg/ml
- Molecular Weight:
- 14.515 kDa
- Purity:
- >95%
- Purification:
- Ion Exchange
- Storage Conditions:
- -70[o]C
- Supplier:
- StressMarq Biosciences
- ABP:
- No Import Docs
- Buffer:
- PBS
- Immunogen:
- Alpha Synuclein Monomers
- Species:
- Rat
- Sequence:
- MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTK EQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDP SSEAYEMPSEEGYQDYEPEA
- Uniprot:
- P37377
- Synonyms:
- alpha-synuclein;synuclein, alpha (non A4 component of amyloid precursor);truncated alpha synuclein
- Extra Details:
- Alpha-synuclein is a neuronal protein that plays a central role in synaptic vesicle trafficking, neurotransmitter release, and dopamine regulation. In its native monomeric form, alpha-synuclein contributes to normal neuronal function by enhancing vesicle priming and fusion, and by acting as a molecular chaperone for SNARE complex assembly. In neurodegenerative diseases such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, alpha-synuclein undergoes pathological misfolding and aggregation. While oligomers and fibrils are widely studied for their neurotoxicity, monomeric alpha-synuclein is increasingly recognized as a critical starting point for understanding disease initiation. Subtle conformational changes in monomers-triggered by mutations, post-translational modifications, or environmental stress-can prime the protein for aggregation and disrupt its physiological roles. Alpha-synuclein monomers are essential tools in mechanistic studies aimed at identifying early biomarkers and therapeutic targets. Their use in biochemical and cellular models enables high-resolution analysis of folding dynamics, membrane interactions, and protein-protein associations. These insights inform strategies to stabilize native alpha-synuclein and prevent its pathological transformation.
- Shipping Conditions:
- Dry Ice

