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Alpha Synuclein Oligomers (Epigallocatechin gallate (EGCG) Stabilized)

SKU: BTL-SM-P-00165 | Brand: Stressmarq
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Product Description

Cat Number SPR-469E
Category Recombinant Protein
Pack Size 100 µg x5
Description Human Recombinant Alpha Synuclein Oligomers (Epigallocatechin gallate (EGCG) Stabilized)
Applications WB | SDS-PAGE | In vivo assay | In vitro assay
Target Alpha Synuclein Oligomers
Molecular Weight ~14.46kDa
Cellular Localization Cytoplasm | Membrane | Nucleus
Purity >95%
Research Area Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy
Swiss Prot P37840 
Scientific Background Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), 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 (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers 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 (5, 6). Epigallocatechin Gallate (EGCG) reduces alpha synuclein fibril formation in favour of spherical soluble oligomers (7).
Expression System E. coli
Accession Number NP_000336.1
Gene Id 6622
Protein Length Full length
Purification Ion-exchange Purified
Storage -80ºC
References 1. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013). 2. Zhang L., et al. (2008) Brain Res. 1244: 40-52. 3. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117. 4. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230. 5. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840. 6. Mezey E., et al. (1998) Nat Med. 4(7): 755-757. 7. Ehrnhoefer, D. E. et al. (2008). Nat Struct Mol Biol. 15(6):558-566.
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Note The product is for research use only
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