a-Synuclein human recombinant, expressed in Escherichia coli N-terminal histidine tagged

Catalog Number: S7820 Storage Temperature: -20 °C

Synonym: NACP Reagent Supplied as a lyophilized powder Product Description a-Synuclein (also known as the non-amyloid Purity: ³ 90% (SDS-PAGE) component of plaques precursor or NACP) is a 140-amino acid protein (19-20 kDa, apparent molecular Precautions and Disclaimer weight) encoded by a simple gene consisting of six This product is for R&D use only, not for drug, exons on human .1 The physiological household, or other uses. Please consult the Material role of a-synuclein is not clear. In the search for its Safety Data Sheet for information regarding hazards function, it was found that a-synuclein induces and safe handling practices. polymerization of into microtubules.2 In addition, a-synuclein was found to function in the modulation of Storage/Stability dopamine transporter function, regulating the synaptic The lyophilized powder is to be stored at -20 °C, and is tone of dopamine.3 Disruption of this function can stable for 4 months at room temperature and over 2 ultimately lead to of nerve terminals. years at -20°C. a-Synuclein is highly abundant in presynaptic Reconstitute the product in water to ~1 mg/ml. Store terminals4 and is a major component of Lewy bodies the reconstituted solution in working aliquots at -20 °C. (LBs). LBs are neuronal cytoplasmic inclusions that are Reconstituted product (~1 mg/ml in water) is stable at found in diverse neurodegenerative disorders. The -20°C for 4 months. deposition of a-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of References: neurodegenerative disorders. These disorders include 1. Chen, X., et al., The human NACP/a-synuclein Parkinson’s disease (PD), dementia with Lewy bodies gene: chromosome assignment to 4q21.3-q22 and (filamentous inclusions), Lewy body variant of TaqI RFLP analysis, Genomics, 26, 425 (1995). Alzheimer’s disease, and multiple system atrophy.2 2. Alim, M.A., et al., Demonstration of a role for Pathogenic point mutations in the a-synuclein gene are a-synuclein as a functional microtubule-associated linked to familial Parkinson’s disease.5 However, most protein. J. Alzheimers Dis., 6, 435-442 (2004). neurodegenerative disorders with LBs are associated 3. Sidhu, A., Wersinger, C., and Vernier, P., with abnormal accumulation of wild-type a-synuclein. a-Synuclein regulation of the dopaminergic Deletion of the a-synuclein gene in mice results in transporter: a possible role in the pathogenesis of functional deficits of the nigrostriatal dopamine system.6 Parkinson's disease. FEBS Lett., 565, 1-5 (2004). Neuronal over-expression of wild-type human 4. Iwai, A., et al., The precursor protein of non-A b a-synuclein in mice resulted in progressive component of Alzheimer's disease amyloid is a accumulation of a-synuclein in neurons, associated presynaptic protein of the central nervous system. with loss of dopaminergic terminals in the basal ganglia Neuron, 14, 467-475 (1995). and with motor impairment, suggesting that a-synuclein 5. Polymeropoulos, M.H., et al., Mutation in the may play a role in Parkinson’s Disease and related a-synuclein gene identified in families with conditions.7 Parkinson's disease. Science, 276, 2045-2047 (1997). 6. Abeliovich, A., et al., Mice lacking a-synuclein 7. Masliah, E., et al., Dopaminergic loss and inclusion display functional deficits in the nigrostriatal body formation in a-synuclein mice: implications for dopamine system. Neuron, 25, 239-251(2000). neurodegenerative disorders. Science, 287, 1265- 1269 (2000).

EM,KAA,PHC 01/09-1

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