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Alpha Synuclein Oligomers (Kinetically Stable)
Human Recombinant Alpha Synuclein Oligomers (Kinetically Stable)
Artikelnummer
STRSPR-484B
Verpackungseinheit
100 µg
Hersteller
Stressmarq Biosciences
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Target: Alpha Synuclein.
Nature: Recombinant.
Swiss-Prot: P37840.
Expression System: E. coli.
Protein Length: Full Length.
Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Purification: Ion-exchange Purified, monomer removed with 100K MWCO filter.
Purity: >95%.
Storage Buffer: PB pH 7.4 (10 mM KH2PO4, 7.5 mM NaOH, pH 7.4).
Protein Size: 650-1200 kDa.
Conjugate: No Tag.
Cellular Localization: Cytoplasm, Cell Membrane, Nucleus, Presynaptic Termini.
Scientific Background: Our kinetically stable oligomers of alpha-synuclein are generated without an inducer or inhibitor and remain stable for at least 2 weeks at 37oC. They present as globular structures under TEM, demonstrate toxicity in rat primary dopaminergic neurons and induce Parkinson’s-associated alpha synuclein phosphoserine 129 pathology. These oligomers have been previously characterized as globular, cylindrical structures with a beta-sheet structure intermediate between monomers and fibrils, and were demonstrated to have a higher toxicity to neurons than alpha-synuclein fibrils (1,2). Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (3). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (4). Functionally, it has been shown to significantly interact with tubulin (5), 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 (6). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer’s 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 (7, 8).
References: 1. Chen, S.W., et. al. (2015). PNAS. E1994-E2003.2. Lorenzen, N., et. al. (2014). JACS. 136: 3859-3868.3. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013).4. Zhang L., et al. (2008) Brain Res. 1244: 40-52.5. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117.6. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230.7. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840.8. Mezey E., et al. (1998) Nat Med. 4(7): 755-757.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Nature: Recombinant.
Swiss-Prot: P37840.
Expression System: E. coli.
Protein Length: Full Length.
Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
Purification: Ion-exchange Purified, monomer removed with 100K MWCO filter.
Purity: >95%.
Storage Buffer: PB pH 7.4 (10 mM KH2PO4, 7.5 mM NaOH, pH 7.4).
Protein Size: 650-1200 kDa.
Conjugate: No Tag.
Cellular Localization: Cytoplasm, Cell Membrane, Nucleus, Presynaptic Termini.
Scientific Background: Our kinetically stable oligomers of alpha-synuclein are generated without an inducer or inhibitor and remain stable for at least 2 weeks at 37oC. They present as globular structures under TEM, demonstrate toxicity in rat primary dopaminergic neurons and induce Parkinson’s-associated alpha synuclein phosphoserine 129 pathology. These oligomers have been previously characterized as globular, cylindrical structures with a beta-sheet structure intermediate between monomers and fibrils, and were demonstrated to have a higher toxicity to neurons than alpha-synuclein fibrils (1,2). Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (3). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (4). Functionally, it has been shown to significantly interact with tubulin (5), 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 (6). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer’s 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 (7, 8).
References: 1. Chen, S.W., et. al. (2015). PNAS. E1994-E2003.2. Lorenzen, N., et. al. (2014). JACS. 136: 3859-3868.3. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013).4. Zhang L., et al. (2008) Brain Res. 1244: 40-52.5. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117.6. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230.7. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840.8. Mezey E., et al. (1998) Nat Med. 4(7): 755-757.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
| Artikelnummer | STRSPR-484B |
|---|---|
| Hersteller | Stressmarq Biosciences |
| Hersteller Artikelnummer | SPR-484B |
| Green Labware | Nein |
| Verpackungseinheit | 100 µg |
| Mengeneinheit | STK |
| Reaktivität | Human |
| Methode | Western Blotting, In Vivo Assay, SDS-PAGE |
| Human Gene ID | 6622 |
| Produktinformation (PDF) |
|
| MSDS (PDF) | Download |
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
