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alpha Synuclein antibody - 128 102

Synucleins are involved in Parkinson's and Alzheimer's Disease
Polyclonal rabbit antiserum
Cat. No.: 128 102
Amount: 200 µl
Price: $350.00
Cat. No. 128 102 200 µl antiserum, lyophilized. For reconstitution add 200 µl H2O, then aliquot and store at -20°C until use.
Applications WB: 1 : 1000 (AP staining) gallery  
IP: not recommended
ICC: 1 : 500 gallery  
IHC: 1 : 500 gallery  
IHC-P/FFPE: 1 : 500 gallery  
Immunogen Recombinant protein corresponding to AA 1 to 140 from human α-Synuclein (UniProt Id: P37840)
Reactivity Reacts with: rat (P37377), mouse (O55042).
No signal: zebrafish.
Other species not tested yet.
Specificity Specific for α synuclein with weak cross reactivity to β synuclein.
Data sheet 128_102.pdf

References for alpha Synuclein - 128 102

Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity.
Jüttner R, Moré MI, Das D, Babich A, Meier J, Henning M, Erdmann B, Mu Ller EC, Otto A, Grantyn R, Rathjen FG, et al.
Neuron (2005) 462: 233-45. 128 102 WB
Pulse-Chase Proteomics of the App Knockin Mouse Models of Alzheimer's Disease Reveals that Synaptic Dysfunction Originates in Presynaptic Terminals.
Hark TJ, Rao NR, Castillon C, Basta T, Smukowski S, Bao H, Upadhyay A, Bomba-Warczak E, Nomura T, O'Toole ET, Morgan GP, et al.
Cell systems (2020) : . 128 102 IHC; tested species: mouse
Cat. No.: 128 102
Quantity: 200 µl
Price: $350.00
Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity.
Jüttner R, Moré MI, Das D, Babich A, Meier J, Henning M, Erdmann B, Mu Ller EC, Otto A, Grantyn R, Rathjen FG, et al.
Neuron (2005) 462: 233-45. 128 102 WB
Pulse-Chase Proteomics of the App Knockin Mouse Models of Alzheimer's Disease Reveals that Synaptic Dysfunction Originates in Presynaptic Terminals.
Hark TJ, Rao NR, Castillon C, Basta T, Smukowski S, Bao H, Upadhyay A, Bomba-Warczak E, Nomura T, O'Toole ET, Morgan GP, et al.
Cell systems (2020) : . 128 102 IHC; tested species: mouse
Background
Synuclein proteins are produced by three genes. They share structural resemblance to apolipoproteins, but are abundant in the neuronal cytosol and present in enriched amounts at presynaptic terminals.
Synucleins have been specifically implicated in three diseases: Alzheimer's (AD), Parkinson's (PD) and breast cancer. In AD, a peptide derived from α-synuclein forms an intrinsic component of plaque amyloid. In PD, an α-synuclein allele is genetically linked to several independent familial cases, and the protein appears to accumulate in Lewy bodies. In breast cancer, increased expression of γ-synuclein correlates with disease progression.
In songbirds, α-synuclein expression is correlated with plasticity in the developing song control system. Although the normal function of synucleins is unknown, a role in synaptic plasticity seems likely.