Recombinant Human alpha-Synuclein Protein Summary
| Description |
An un-tagged recombinant protein corresponding to amino acids 1 to 140 of Human Synuclein-alpha
Source: E.coli Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA |
| Preparation Method |
E.coli
|
| Protein/Peptide Type |
Recombinant Protein
|
| Gene |
SNCA
|
| Purity |
>95% pure by SDS-PAGE
|
| Endotoxin Note |
< 1.0 EU per 1 microgram of protein (determined by LAL method)
|
Applications/Dilutions
| Theoretical MW |
14.4 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles.
|
| Buffer |
20 mM Tris-HCl buffer (pH 7.5) containing 0.1 M NaCl,1mM MgCl2
|
| Preservative |
No Preservative
|
| Concentration |
1.0 mg/ml
|
| Purity |
>95% pure by SDS-PAGE
|
Notes
The purity of this protein is > 95% by SDS-PAGE. Molecular weight is 14.4 kDa (140 aa), confirmed by MALDI-TOF. (Molecular weight on SDS-PAGE will appear higher)
Alternate Names for Recombinant Human alpha-Synuclein Protein
- alpha-Synuclein
- Lewy body) 4
- MGC110988
- NACP
- non A-beta component of AD amyloid
- Non-A beta component of AD amyloid
- Non-A4 component of amyloid precursor
- non-A4 component of amyloid
- PARK1
- PARK4
- PD1
- SNCA
- synuclein, alpha (non A4 component of amyloid precursor)
- Synuclein-alpha
Background
alpha-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. alpha-synuclein has been suggested to be implicated in the pathogenesis of Parkinsons 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 alpha-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
