Storage Buffer | PBS pH 7.4 |
Storage Temperature | -80ºC |
Shipping Temperature | Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. |
Purification | Ion-exchange Purified |
Cite This Product | Human Recombinant A53T Alpha Synuclein Protein Monomer (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-325) |
Certificate of Analysis | Certified >95% pure using SDS-PAGE analysis. Low endotoxin <5 EU/mL @ 2mg/mL. |
Other Relevant Information | For corresponding PFFs, see catalog# SPR-325 |
Alternative Names | 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 |
Research Areas | Alzheimer's Disease, Neurodegeneration, Neuroscience, Parkinson's Disease, Synuclein, Tangles & Tau, Multiple System Atrophy |
Cellular Localization | Cytoplasm, Membrane, Nucleus |
Accession Number | NP_000336.1 |
Gene ID | 6622 |
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). 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 (7) and increased rates of alpha synuclein fibrillization (8). |
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), 2045–2047 8. Conway, K.E., et al. (1998). Nat Med. 4(11):1318-20 |
Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures such as those in alpha synuclein fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift and increased fluorescence intensity. Thioflavin T emission curves show a limited increase in fluorescence (correlated to alpha synuclein aggregation) over time in A53T alpha synuclein monomers (SPR-325). A much greater increase in fluorescence is seen when 100 µM monomer (SPR-325) is combined with 10 µM of fibrils (SPR-326) as the fibrils seed the formation of new fibrils from the pool of active monomers. Thioflavin T ex = 450 nm, em = 485 nm. Note: We use molecular weight of 14.46 kDa for both alpha synuclein monomer and fibril in calculations. We load 100µL/well for Thioflavin T assay so 100 µM is 144.6µg/well and 10 µM is 14.46 µg/well.
StressMarq Biosciences :
Based on validation through cited publications.