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Proteins and Peptides

Alpha Synuclein Oligomers (Kinetically Stable)

Product Sizes
100 ug
SPR-484-100UG
2 x 100 ug
SPR-484-2X100UG
5 x 100 ug
SPR-484-5X100UG
About this Product
SKU:
SPR-484
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:
Cell-based/Functional Assay, Western Blot
Buffer:
PB pH 7.4 (10 mM KH2PO4, 7.5 mM NaOH, pH 7.4)
CE/IVD:
RUO
Concentration:
2 mg/ml
Extra 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.
Immunogen:
Alpha Synuclein Oligomers
Molecular Weight:
650-1200 kDa
Purity:
>95%
Purification:
Ion Exchange
Sequence:
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
TEM of kinetically stable alpha-synuclein oligomers (SPR-484). Negative stain transmission electron microscopy images of SPR-484 acquired at 80 Kv on carbon coated 400 mesh copper grids using phosphotungstic acid and uranyl acetate stain.
Kinetically stable alpha-synuclein oligomers (SPR-484) are stable after a freeze-thaw cycle and when incubated at 37 oC for 2 weeks. Tris-Gylcine Native PAGE migration of kinetically stable alpha-synuclein oligomers after a freeze-thaw cycle (A). Size-exclusion chromatography of SPR-484 after a freeze-thaw cycle (B) and 37oC incubation for 14 days (C). By peak area, approximately 90% of SPR-484 remains oligomeric after freeze-thaw and 37oC treatments. SEC was performed on Superdex 200 10/300 GL Increase column in phosphate buffer pH 7.4. Note: Monomeric alpha-synuclein is an intrinsically disordered 14 kDa protein. Due to its extended conformation in solution, migration of free monomeric alpha-synuclein is similar to that of a globular 60 kDa protein on Native PAGE and SEC.
Kinetically stable alpha-synuclein oligomers (SPR-484) are toxic to dopaminergic neurons and induce phosphorylation of alpha-synuclein Ser129, a pathology associated with Parkinson's disease. Survival of rat primary dopaminergic neurons 11 days after treatment quantified by anti-MAP2 antibody and expressed as a percentage of control (A). Levels of alpha-synuclein pSer129 present in rat primary dopaminergic neurons 11 days after treatment quantified by ratio of anti-alpha-synuclein pSer129 antibody to anti-MAP2 antibodyexpressed as a percentage of control (B). Mean +/- s.e.m; ** p<0.01 stats vs control, one-way Anova followed by Dunnett's test; p<0.05, stats vs control, Student's t-test. Data is representative of n=6 experimental repeats for each condition; # represents control, n.s. indicates not significant p>0.05.
Representative immunohistochemistry images of Parkinson's-associated pSer129 pathology induced in rat primary dopaminergic cells by kinetically stable alpha-synuclein oligomers (SPR-484). Primary rat dopaminergic neurons 11 days after treatment with control PBS buffer (A). Primary rat dopaminergic neurons 11 days after treatment with 10 ug/mL SPR-484 (B). Nuclei appear blue (Hoechst), dopaminergic neurons appear red (MAP2) and pathology appears green (A Alpha-syn pSer129). Both cultures treated with chicken polyclonal anti-MAP-2 antibody, mouse monoclonal anti-A Alphasyn pSer129-specific antibody, Alexa Fluor 488 goat anti-mouse IgG, Alexa Fluor 647 goat anti-chicken IgG, and fluorescent marker Hoechst in the same solution. White arrows emphasize several regions of strong pSer129 pathology. Scale bar represents 100 um. Note: SPR-484 is generated recombinantly in E.coli and is non-phosphorylated prior to addition on neurons.