| Storage Buffer | PBS pH 7.4 |
| Storage Temperature | -80ºC |
| Shipping Temperature | Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. |
| Purification | Ion-exchange Purified |
| Cite This Product | Human Recombinant Alpha Synuclein (1-114) Pre-formed Fibrils (C-term Truncated) (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-537) |
| Certificate of Analysis | Starting Monomers certified > 95% pure via SDS-PAGE and A260/A280 ratio. |
| Other Relevant Information | For corresponding monomers, see Catalog # SPR-536. |
| Alternative Names | α‑Synuclein (1–114), Alpha Synuclein 1‑114 Truncated, C‑Terminally Truncated Alpha‑Synuclein, Alpha‑Synuclein Fragment (1–114), SNCA (1–114) Fibrillar Protein, SNCA (1–114) Protein, Alpha‑Synuclein Fragment 1–114, Seeding‑Competent Alpha‑Synuclein (1–114) Fibrils, Alpha‑Synuclein (1–114) Aggregation Seeds |
| Research Areas | Neurodegeneration, Neuroscience, Parkinson's Disease, Synuclein |
| Swiss Prot | P37840 |
| Scientific Background | Human recombinant alpha-synuclein (1–114) is a C-terminally truncated form of α-synuclein lacking residues 115–140. C-terminal truncation is a pathological modification observed in synucleinopathies, including Parkinson’s disease and dementia with Lewy bodies, and has been associated with increased aggregation and fibril formation relative to the full-length protein. Cleavage at residue Glu114 has been identified as a major physiological processing event of α-synuclein aggregates, and the resulting 1–114 species has been detected in disease-associated inclusions. Studies suggest that truncation of the C-terminal region alters α-synuclein conformation and promotes the formation of aggregation-prone species that may contribute to the development and progression of α-synuclein pathology. StressMarq’s Alpha Synuclein (1-114) Pre-Formed Fibrils (PFFs) (C-Term Truncated) have been demonstrated to seed monomers in an in-vitro Thioflavin T seeding assay. |
| References |
1. Quintin, S., Lloyd, G. M., Paterno, G., Xia, Y., Sorrentino, Z., Bell, B. M., Gorion, K-M., Lee, E. B., Prokop, S., Giasson, B. I. (2023). Cellular processing of α-synuclein fibrils results in distinct physiological C-terminal truncations with a major cleavage site at residue Glu114. Journal of Biological Chemistry, 299(7), 104912. https://doi.org/10.1016/j.jbc.2023.104912 2. Sorrentino, Z. A., Vijayaraghavan, N., Gorion, K-M., Riffe, C. J., Strang, K. H., Caldwell, J., & Giasson, B. I. (2018). Physiological C-terminal truncation of α-synuclein potentiates the prion-like formation of pathological inclusions. Journal of Biological Chemistry, 293(49), 18914–18932. https://doi.org/10.1074/jbc.RA118.005603 3. Zhang, C., Pei, Y., Zhang, Z., Xu, L., Liu, X., Jiang, L., Peilak, G. J., Zhou, X., Liu, M., Li, C. (2022). C-terminal truncation modulates α-Synuclein’s cytotoxicity and aggregation by promoting the interactions with membrane and chaperone. Communications Biology, 5, 798. https://doi.org/10.1038/s42003-022-03768-0 |
Sedimentation assay on Alpha Synuclein (1-114) Pre-formed Fibrils (C-term Truncated). Samples were spun down at 15,000 x g, washed, and then spun down again. Fibril samples are prepared in denaturing conditions prior to running on the gel. SDS-PAGE analysis on a 12% Bis-Tris gel shows that the majority of the fibril is insoluble.
In vitro seeding activity of Alpha Synuclein (1-114) Pre-formed Fibrils (C-term Truncated) in ThT assay. Alpha Synuclein (1-114) Pre-formed Fibrils (C-term Truncated) (Cat # SPR-537) seed fibril formation of Alpha Synuclein (1-114) Monomers (C-term Truncated) (Cat # SPR-536) over 72 hours. Reactions (100uL) shaken at 600 rpm in Greiner-Bio 96 Well Non-Binding Cell Culture Microplates, Black (Greiner-Bio Catalog #655900) at 37oC in the presence of 25 uM ThT and read with an XPS Microplate Reader set at 450nmex/485nmem.
Dot Blot analysis using Stressmarq’s SMC-621 and SPC-800 comparing detection of C-terminal truncated Alpha Synuclein Monomers (Cat # SPR-536) and Pre-Formed Fibrils (Cat # SPR-537) with full-length Alpha Synuclein Monomers (Cat # SPR-321). Protein was blotted on nitrocellulose, incubated with 1:1000 primary antibodies and/or 1:4000 secondary antibodies. Secondary controls are goat-anti mouse:HRP or goat-anti rabbit:HRP. Exposed 1 second.
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