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.