AnaSpec, EGT Group is pleased to announce the release
of an ultrasensitive ELISA assay for quantitatingα-synuclein.
The SensoLyte® α-Synuclein
Quantitative ELISA Kit (Human/Mouse/Rat) provides a convenient and quantitative
assay for determining α-Synuclein amount in cell and tissue lysate as well
as in body fluids. Compared to other anti-α-Synuclein ELISA kits on the market,
this one-step, mix-and-read assay takes less time to run. HRP conjugated detection
antibody is added simultaneously with the samples and standards during the assay,
eliminating extra incubation and washing steps.
(Human) ELISA Kit
§ One Step Convenient Format
* Pre-coated and pre-blocked 96-well strip plate
* Ready-to-use substrate solution and other assay components
* One step assay (samples and detection antibody are added simultaneously)
* 1 hour assay time at room temperature (excluding incubation time)
§ Minimal Sample Size
* Requires only 10-20 μl of cell and tissue lysate or body fluids
§ High Sensitivity
* Detects 5 pg/ml of α-Synuclein (calculated as three standard deviations from the blank)
§ Broad Dynamic Range
* 8-500 pg α-Synuclein/ml in the assayed sample
Figure 1. An example of the α-Synuclein ELISA standard curve
α-Synuclein is a major
component of Lewy bodies found in affected neurons of patients with Parkinson's
disease.1-4 This protein has a mass of 14.5 kDa (140 amino acids
long) and consists of a conserved degenerative amino-terminal domain and an
acidic carboxyl-terminal that has a higher sequence divergence.1-4
α-Synuclein is predominantly expressed in brain, specifically in cerebellum,
thalamus, neocortex, hippocampus, and striatum regions.1-2 Other
tissues also express α-Synuclein but at very low levels.1-4
The physiological role of α-Synuclein is not well understood. However,
the presence of imperfect KTKEGV lipid interacting repeats suggests that it
may be involved in synaptic vesicle homeostasis.3
Table 1. A listing of Synuclein recombinant proteins
Table 1. A listing of Synuclein antibodies.
Anti-α-Synuclein (pSer 87)
Prusiner, B. S. (2015). Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism pnas 112 doi: 10.1073/pnas.1514475112.
Woerman, A. L. (2015). Propagation of prions causing synucleinopathies in cultured cells. PNAS 112 doi: 10.1073/pnas.1513426112.
Al-Nimer, MS. et al. (2014). Saliva α-synuclein and a high extinction coefficient protein: A novel approach in assessment biomarkers of Parkinson's disease. North Am J Med Sci 6, 633. doi: 10.4103/1947-2714.147980.
Maia, LF. et al. (2013). Changes in amyloid-β and tau in the cerebrospinal fluid of transgenic mice overexpressing amyloid precursor protein. Sci Transl Med 5, 194re2.
- Rivers, R. et al. Protein Science 17, 887 (2008).
- Bruening, W. et al. Cancer 88, 2154 (2000).
- George M. J. Genome Biology3, 1 (2001).
- Latawiec, D. et al. PloS ONE 5, 1 (2010).