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| α & β -Synuclein – Recombinant Proteins |
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AnaSpec is pleased to announce the release of two new recombinant proteins, α
-synuclein(SNCA) and β -Synuclein (SNCB). These proteins, along with
g-synuclein (SNCG), are members of the synuclein family of small proteins expressed
primarily in neural tissue and in some tumors.1 Synuclein proteins,
found only in vertebrates, possess a highly conserved N-terminal domain, with
a variable number of 11-residue repeats and a less conserved C-terminal, with
a preponderance of acidic residues.1
α-Synuclein
α-Synuclein is an abundant protein of 140 residues that is present in high
concentration at presynaptic terminals and is found in both soluble and membrane-associated
fractions of the brain. Several possible functions have been suggested, among
which are vesicle release and trafficking. In vitro incubation in the presence
of salt (i.e. 0.1M NaCl) with agitation causes α-Synuclein to form fibrils.2-6
α -Synuclein, labeled with AnaSpec’s proprietary green dye, HiLyte
Fluor™ 488 (Ex/Em=503/525 nm) is also available.
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| Figure. 1 SDS-PAGE of recombinant a-synuclein
showed a single band at ~17 kDa. |
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Figure 2. Western blot of recombinant
a-synuclein protein, cat# 55456 probed with anti-a-synuclein
(CT), cat # 53878. An immunoreactive band was detected at ~17 kDa (A);
the band was blocked by the immunizing peptide (B). HiLyte Fluor™ 750 conjugated
secondary antibody was used and signals were detected using a near infrared-fluorescence
scanner (Odyssey, Li-Cor). Right panel is the grayscale image of the western
blot. |
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| Figure 3. Mass spectrometry of recombinant human
asynuclein showed a single peak
with the mass of 14460 Da. |
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| Figure 4. Left: SDS-PAGE of HiLyte FluorTM
488-labeled human a-synuclein,
cat# 55457 showed a single band at ~17 kDa position. α-synuclein,
non-labeled (A), HiLyte FluorTM 488-labeled (B). Right: Fluorescence
spectrum of HiLyte FluorTM488-labeled human α-synuclein.
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The addition of a-synuclein protein further complements AnaSpec’s extensive
portfolio of Alzheimer’s research products.
β-Synuclein
N-terminal of β-synuclein is highly
homologous to α-, γ-synucleins and consists of degenerative “KTKEGV”
repeats.7-10 Similar to α-synuclein, beta-synuclein is found
primarily in the brain; however, it does not associate with Lewy bodies in
Parkinson disease like α-synuclein.7-10 Beta-synuclein was
found to inhibit production of phosphatidic acid by the phospholipase D2 transmembrane
protein in vitro.7 In addition, β-synuclein was detected
in many breast and ovarian tumors.7 Recent investigations demonstrated
that β-synuclein can induce mild experimental autoimmune encephalomyelitis
(EAE) in Lewis rats.8
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| Figure 5. Figure.
1 SDS-PAGE of recombinant human b-synuclein showed a single band at
~18 kDa (slightly different than the predicted mass), CL=crude lysate;
P=purified b-synuclein.
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Figure 6. Western
blot of recombinant b-synuclein protein, cat# 55458 probed with anti-b-synuclein
(CT), cat # 53879. HiLyte Fluor™ 750 conjugated secondary antibody
was used and signals were detected using a near infrared-fluorescence
scanner (Odyssey, Li-Cor).
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References
1. George, JM. Genome Biol. 3, reviews 3002.1 (2002).
2. Trojanowski, JQ. & VM. Lee, Ann. N. Y. Acad. Sci. 991,
107 (2003).
3. Masliah, E., et al. Science 287, 1265 (2000).
4. Van Der, P. H, et al. J. Neurosci. 20, 6021
(2000).
5. Feany, MB. & WW. Bender, Nature 404, 394(2000).
6. Weinreb, P. H., et al. Biochemistry 35, 13709 (1996).
7. Rivers, R.C. et al. Protein Sci 17, 887 (2008).
8. Sung, Y-H. et al. Protein Sci 15, 1162 (2006).
9. George, JM. Genome Biol 3, 3002.1 (2001).
10. Bruening, W. et al. Am Cancer Soc 88, 2154 (2000).
11. Kela-Madar, N. et al. J Neuroimmunol 208, 19 (2009).
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