ASyO5 | Mouse anti-human alpha-synuclein | oligomer-specific (clone number 2,4)
AS13 2718 | Clonality: monoclonal | Host: Mouse | Reactivity: Human
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Dot blot reaction of the binding capacity of ASyO5 to fibrils, monomers and oligomers. Equal amounts of each sample were spotted on a nitrocellulose membrane and then dried. The membrane was blocked with 5% non-fat milk before incubated for 1 h with anti-ASyO5 (25nM) and then with secondary antibody, anti-mouse HRP-conjugated (1:1500). The membrane was washed with PBS containing 0.25% Tween-20 before detection using ECL prime (GE Healthcare).
Preparation of α-synuclein oligomers and fibrils is described here.
Tissue sections from the human PD midbrain, substantia nigra, were de-waxed and rehydrated in ethanol and then incubated with ASyO5 at RT for 1h. The immunoreactivity was detected with the anti-mouse Peroxidase Reagent Kit (ImmPRESS, Vector Laboratories, Inc.) and then developed using the ImmPACT AEC Peroxidase Substrate kit (Vector Laboratories, Inc.).
This antibody is specific to oligomers in ELISA as a capture antibody. For specific details, please check: Brännström et al. (2014). A Generic Method for Design of Oligomer-Specific Antibodies. PLoS ONE. DOI: 10.1371/journal.pone.0090857.
Alpha-synuclein is normally an unstructured soluble protein that can aggregate to form insoluble fibrils in pathological conditions characterized by Lewy bodies, such as Parkinson's disease, dementia with Lewy-bodies, and multiple system atrophy. In analogy to many other amyloid associated disorders, alpha-synuclein may also form oligomeric assemblies. These small and soluble forms have been suggested to exert a stronger tissue damaging effect as compared to the monomeric and fibrillar counterpart. Using a recently developed technique a monoclonal oligomer-specific antibody has been designed.
Kilpeläinen et al. (2019). Behavioural and dopaminergic changes in double mutated human A30P*A53T alpha-synuclein transgenic mouse model of Parkinson´s disease.Sci Rep. 2019 Nov 22;9(1):17382. doi: 10.1038/s41598-019-54034-z.
Wu et al. (2017). The critical role of Nramp1 in degrading a-synuclein oligomers in microglia under iron overload condition. Neurobiol Dis. 2017 Aug;104:61-72. doi: 10.1016/j.nbd.2017.05.001. (human, mouse, immunolocalization)
Svarcbahs et al. (2016). Inhibition of Prolyl Oligopeptidase Restores Spontaneous Motor Behavior in the a-Synuclein Virus Vector-Based Parkinson's Disease Mouse Model by Decreasing a-Synuclein Oligomeric Species in Mouse Brain. J Neurosci. 2016 Dec 7;36(49):12485-12497.
Brännström et al. (2014). A Generic Method for Design of Oligomer-Specific Antibodies. PLoS ONE. DOI: 10.1371/journal.pone.0090857.