Alpha Synuclein A53T Mutant Monomers

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) . The A53T mutation is a missense point mutation where alanine is replaced by threonine at the 53rd amino acid. This mutation has been linked to early-onset Parkinson's Disease and increased rates of alpha synuclein fibrillization.

A53T mutant alpha synuclein, A53T mutated SNCA, A53T Alpha synuclein monomer, Ala53thr mutant alpha synuclein, 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, Alpha synuclein monomers, SYN protein, Parkinson disease familial 1 Protein

MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA

Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy

100 µM A53T alpha synuclein protein monomer (SPR-325) seeded with 10 uM A53T alpha synuclein protein PFF (SPR-326) in 25 µM Thioflavin T (PBS pH 7.4, 100 µl reaction volume) generated a fluorescence intensity of 28 000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 56 hours. Fluorescence was measured by excitation at 450 nm and emission at 485 nm on a Molecular Devices Gemini XPS microplate reader.

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. Polymeropoulos, M. H. (1998). Science. 276(5321), 2045–2047 8. Conway, K.E., et al. (1998). Nat Med. 4(11):1318-20

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. Polymeropoulos, M. H. (1998) . Science. 276 (5321), 2045–2047 8. Conway, K.E., et al. (1998) . Nat Med. 4 (11) :1318-20

MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA