![Coomassie Brilliant Blue staining of SDS-PAGE gel of recombinant human synuclein proteins. Lane 1 shows protein standards of apparent molecular weight as indicated in kDa. Other lanes show ~2µg of [2] α-synuclein, [3] β-synuclein, and [4] γ-synuclein. Lanes [5] and [6] show 2.0 and 1.0μg of BSA respectively.](http://encorbio.com/cdn/shop/products/eba1901bc62e0da3b36595d29bb286db_20x_crop_center.jpg?v=1707404183)
EnCor Biotechnology
Recombinant Full Length Human β-Synuclein Protein, Cat# Prot-r-SNCB
Description
A codon optimized cDNA encoding full length human γ-synuclein was designed and inserted into the pET30a(+) expression vector. The vector adds an N-terminal His-tag, S-tag and proteolytic cleavage sites to the human sequence which increases the molecular weight by about 5kDa. The construct was expressed by standard methods in E. coli and purified using a Nickel column in 6M urea. The protein is supplied in 6M urea in phosphate buffer. The lane on the far left contains protein standards of the indicated molecular size. In the next lanes 2µg, 1µg and 0.5µg of the recombinant γ-synuclein were run as indicated and 1µg and 0.5µg of BSA were in the two right lanes.
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| Name: | Recombinant human β-synuclein, Prot-r-SNCB |
| Immunogen: | NA |
| HGNC Name: | SNCB |
| UniProt: | Q16143 |
| Molecular Weight: | ~21kDa |
| Host: | E. coli |
| RRID: | NA |
| Format: | 1mg/mL in 6M Urea |
| Applications: | Western blotting, ELISA, immunogen |
| Storage: | Store at -20°C |
β-synuclein is a member of the synuclein protein family, the other two members being α and γ-synuclein, each protein being coded for by a distinct but related gene. α-synuclein was originally isolated as a major synaptic vesicle associated protein from the electric organ of the fish Torpedo (1), and direct homologues of α-synuclein are found in all vertebrates. Later work connected α-synuclein expression with several human brain pathologies, so that it is a major component of the Lewy bodies of Parkinson’s disease (2-5). β-synuclein was isolated as a component of normal and diseased human brain as a protein clearly related to but distinct from α-synuclein (6). The human β-synuclein molecule is 134 amino acids in size compared to 140 amino acids for α-synuclein, and the N-terminal halves of the two molecules are virtually identical while the C-terminal regions is more variable. As a result we made our new β-synuclein antibodies to this region. Like α-synuclein, β-synuclein is heavily concentrated in the brain in presynaptic regions. A third synuclein, γ-synuclein was originally identified as breast cancer specific gene 1, (BCSG1), but is also heavily expressed in brain and also has a similar N-terminal sequence. The three synucleins appear to have overlapping functions so genetic deletion of all three in mice is required to obtain serious neurological deficits (7).
Human β-synuclein sequence was based on that was NP_003078.2 which was inserted into the eukaryotic expression vector pET30a(+) which adds an N-terminal His-tag underlined below. This sequence also includes a thrombin cleavage site (blue), an S-tag affinity peptide (red) and an enterokinase cleavage site (green).
MHHHHHHSSG LVPRGSGMKE TAAAKFERQH MDSPDLGTDD DDKAMADIGS EFMDVFMKGL 60
SMAKEGVVAA AEKTKQGVTE AAEKTKEGVL YVGSKTREGV VQGVASVAEK TKEQASHLGG 120
AVFSGAGNIA AATGLVKREE FPTDLKPEEV AQEAAEEPLI EPLMEPEGES YEDPPQEEYQ 180
EYEPEA 186
Number of amino acids: 186
Molecular weight: 19996.09
Theoretical pI: 4.68
Amino acid composition:
Ala (A) 23 12.4%
Arg (R) 4 2.2%
Asn (N) 1 0.5%
Asp (D) 10 5.4%
Cys (C) 0 0.0%
Gln (Q) 7 3.8%
Glu (E) 28 15.1%
Gly (G) 18 9.7%
His (H) 8 4.3%
Ile (I) 3 1.6%
Leu (L) 9 4.8%
Lys (K) 14 7.5%
Met (M) 8 4.3%
Phe (F) 5 2.7%
Pro (P) 10 5.4%
Ser (S) 11 5.9%
Thr (T) 9 4.8%
Trp (W) 0 0.0%
Tyr (Y) 4 2.2%
Val (V) 14 7.5%
This protein does not contain any Trp residues. Experience shows that
this could result in more than 10% error in the computed extinction coefficient.
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 5960
Abs 0.1% (=1 g/l) 0.298
1. Maroteaux L, Campanelli JT, Scheller RH. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8:2804-15 (1988).
2. Lavedan C. The Synuclein Family. Genome Research 8:871-80 (1998).
3. Polymeropoulos, MH et al. Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science 276:2045-7 (1997).
4. Kruger, R et al. Ala30-to-Pro mutation in the gene encoding alpha-synuclein in Parkinson’s disease. Nature Genet. 18:106-8 (1998).
5. Chartier-Harlin, M-C. et al. Alpha-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet 364:1167-9 (2004).
6. Ji H. et al. Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing. Cancer Res. 57:759-64 (1997).
7. Greten-Harrison, B. et al. αβγ-Synuclein triple knockout mice reveal age-dependent neuronal dysfunction. PNAS 107:19573-8 (2001).
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