Recombinant Human Alpha-Synuclein
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| Amount : | 100 µg |
| Purification : | Greater than 95.0% as determined by SDS-PAGE. |
| Content : | The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. |
| AA sequence : | MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA. |
| Alternative Name : | Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PARK1, PARK4, MGC110988, a-Synuclein, SNCA. |
Source : Escherichia Coli. a-Synuclein Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (Real molecular weight on SDS-PAGE will be shift up). The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques. a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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