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SPR-484B SPR-484C SPR-484E

Alpha Synuclein Oligomers (Kinetically Stable)

Stressmarq Biosciences

DESCRIPTION

Human Recombinant Alpha Synuclein Oligomers (Kinetically Stable)

DETAILS

  • Nature: Recombinant
  • Purity: >95%
  • Target: Alpha Synuclein Oligomers (Kinetically Stable)
  • Category: Protein
  • Conjugate: No Tag
  • References: 1. Chen, S.W., et. al. (2015). PNAS. E1994-E2003. 2. Lorenzen, N., et. al. (2014). JACS. 136: 3859-3868. 3. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013). 4. Zhang L., et al. (2008) Brain Res. 1244: 40-52. 5. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117. 6. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230. 7. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840. 8. Mezey E., et al. (1998) Nat Med. 4(7): 755-757.
  • Applications: WB | Native PAGE | In vivo assay | In vitro assay
  • Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
  • Protein Size: 650-1200 kDa
  • Purification: Ion-exchange Purified, monomer removed with 100K MWCO filter
  • Concentration: Lot/batch specific. See included datasheet.
  • Protein Length: Full Length
  • Research Areas: Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy
  • Storage Buffer: PB pH 7.4 (10 mM KH2PO4, 7.5 mM NaOH, pH 7.4)
  • Alternative Names: Alpha synuclein pre-formed fibrils, Alpha synuclein aggregates, Alpha synuclein protein aggregates, Alpha synuclein aggregates, 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, Parkison disease familial 1 Protein
  • Cite This Product: Human Recombinant Alpha Synuclein Oligomers (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-484B)
  • Expression System: E. coli
  • Species Full Name: Human
  • Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
  • Storage Temperature: -80ºC
  • Shipping Temperature: Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.
  • Cellular Localization: Cytoplasm | Cell Membrane | Nucleus | Presynaptic Termini
  • Scientific Background: Our kinetically stable oligomers of alpha-synuclein are generated without an inducer or inhibitor and remain stable for at least 2 weeks at 37oC. 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 (1,2). Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (3). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (4). Functionally, it has been shown to significantly interact with tubulin (5), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (6). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer’s disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (7, 8).
  • Certificate of Analysis: Certified >95% pure using Native-PAGE analysis.