Alpha Synuclein S129A Mutant Monomers

• Background: Elevated levels of phosphoserine 129 (pS129) on alpha-synuclein has long been considered a hallmark of Parkinson’s disease and other synucleinopathies, where up to 90% of alpha-synuclein deposition in Lewy Bodies contains pS129, compared to ≤4% in normal brains (reviewed in [1]). Further, pS129 was recently shown to function as a physiological regulator of neuronal activity (2). Alpha-synuclein S129A monomers and fibrils cannot be phosphorylated at position 129, and therefore can be utilized to study phospho-S129-independent biology and pathology. Further, this material can be used to confirm induction of endogenous pS129 pathology in disease models.
• Description: Human Recombinant Alpha Synuclein S129A Mutant Monomers
• Product Name Alternative: Alpha synuclein protein, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkinson's disease familial 1 Protein, Alpha Synuclein S129A
• UNSPSC: 12352202
• Swiss Prot: P37840-1
• Host: E. coli
• Origin Species: Human
• Target: Alpha Synuclein S129A
• Conjugation: No Tag
• Sequence: MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPAEEGYQDYEPEA
• Applications: WB, In vivo Assay, In vitro Assay
• Purification Method: Ion-exchange Purified
• Concentration: 2 mg/ml
• Purity: >95%
• Weight: 0.02
• Length: Full length (1 - 140 aa)
• Buffer: 1X PBS pH7.4
• Molecular Weight: 14.44 kDa
• Precautions: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
• Additionnal Information: For corresponding PFFs, see catalog# SPR-506
• References & Citations: 1. Xu, Deng and Qing. 2015. The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease. Journal of Neurochemistry. https://doi.org/10.1111/jnc.13234 2. Ramalingam et al. 2023. Dynamic physiological α-synuclein S129 phosphorylation is driven by neuronal activity. NPJ Parkinsons Dis. doi: 10.1038/s41531-023-00444-w.