Target: Alpha Synuclein.
Nature: Recombinant.
Swiss-Prot: P37840 .
Biological Activity: 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.
Expression System: E. coli.
Protein Length: Full Length.
Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Purification: Ion-exchange Purified.
Purity: >95%.
Storage Buffer: PBS pH 7.4.
Protein Size: ~14.46 kDa.
Conjugate: No tag.
Cellular Localization: Cytoplasm, Membrane, Nucleus.
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). 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.
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. Polymeropoulos, M. H. (1998). Science. 276(5321), 2045–20478. Conway, K.E., et al. (1998). Nat Med. 4(11):1318-20.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
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