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SPR-484

Alpha Synuclein Oligomers (Kinetically Stable)

Eine Lieferung in diese Region ist nicht möglich.

SKU:
SPR-484
Zusätzliche Namen:
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
Anwendung:
WB, FuncS
Konzentration:
2 mg/ml
Molekulargewicht:
650-1200 kDa
Reinheit:
>95%
Aufreinigung:
Ion Exchange
Lagerbedingungen:
-70[o]C
Hersteller:
StressMarq Biosciences
ABP:
No Import Docs
Buffer:
PB pH 7.4 (10 mM KH2PO4, 7.5 mM NaOH, pH 7.4)
Immunogen:
Alpha Synuclein Oligomers
Spezies:
Human
Sequenz:
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Uniprot:
P37840
Synonyme:
alpha-synuclein;I+/--synuclein;NACP;non A-beta component of AD amyloid;Non-A beta component of AD amyloid;Non-A4 component of amyloid precursor;PARK1;PARK4;PD1;synuclein alpha-140;synuclein, alpha (non A4 component of amyloid precursor);truncated alpha synuclein
Weitere Details:
Alpha-synuclein, encoded by the SNCA gene (UniProt ID: P37840), is a neuronal protein involved in synaptic vesicle trafficking and neurotransmitter release. While normally present as a soluble monomer, alpha-synuclein can misfold and aggregate under pathological conditions, forming oligomers and fibrils that contribute to neurodegenerative diseases such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Among these aggregated species, alpha-synuclein oligomers are increasingly recognized as the most neurotoxic intermediates. These soluble aggregates disrupt cellular homeostasis by impairing membrane integrity, mitochondrial function, and proteasomal activity. Their ability to propagate between neurons in a prion-like fashion facilitates the progressive spread of pathology throughout the brain. Alpha-synuclein oligomers are essential tools in experimental models for studying early-stage synucleinopathy. They enable researchers to investigate mechanisms of misfolding, oxidative stress, synaptic dysfunction, and neuroinflammation. Their structural relevance to human disease makes them ideal for evaluating therapeutic strategies aimed at stabilizing native alpha-synuclein, inhibiting oligomer formation, or enhancing aggregate clearance. By modeling the critical transition from functional protein to pathogenic species, alpha-synuclein oligomers provide a high-impact platform for advancing neurodegenerative disease research and accelerating the development of targeted interventions. StressMarq's kinetically stable oligomers of alpha synuclein are generated without an inducer or inhibitor and remain stable for at least 2 weeks at 37C. They present as globular structures under TEM, demonstrate toxicity in rat primary dopaminergic neurons and induce Parkinson's-associated alpha synuclein phosphoserine 129 pathology. These oligomers have been previously characterized as globular, cylindrical structures with a beta-sheet structure intermediate between monomers and fibrils, and were demonstrated to have a higher toxicity to neurons than alpha-synuclein fibrils.
Versandbedingungen:
Dry Ice