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alpha/beta Synuclein antibody - 128 011

Synucleins are involved in Parkinson's and Alzheimer's Disease
Mouse monoclonal purified IgG
Cat. No.: 128 011
Amount: 100 µg
Price: $415.00
Cat. No. 128 011 100 µg purified IgG, lyophilized. Azide was added before lyophilization. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: yes
ICC: 1 : 500 gallery  
IHC: 1 : 200 gallery  
IHC-P: 1 : 500 gallery  
ELISA: yes (see remarks)
Clone 94C1
Subtype IgG2b (κ light chain)
Immunogen Synthetic peptide corresponding to residues near the carboxy terminus of human α-Synuclein. (UniProt Id: P37840)
Reactivity Reacts with: human (P37840, Q16143), rat (P37377, Q63754), mouse (O55042, Q91ZZ3), mammals.
Other species not tested yet.
Peptide conserved in almost all mammals.
Specificity Recognizes α- and β-synuclein, no cross-reactivity to γ-synuclein.
Remarks

ELISA: This antibody is suitable as capture antibody for sandwich-ELISA with cat. no. 128 003 as detector antibody.

Data sheet 128_011.pdf

References for alpha/beta Synuclein - 128 011

Loss of the parkinsonism-associated protein FBXO7 in glutamatergic forebrain neurons in mice leads to abnormal motor behavior and synaptic defects.
Wang J, Joseph S, Vingill S, Dere E, Tatenhorst L, Ronnenberg A, Lingor P, Preisinger C, Ehrenreich H, Schulz JB, Stegmüller J, et al.
Journal of neurochemistry (2023) : . 128 011 IHC; tested species: mouse
Cat. No.: 128 011
Amount: 100 µg
Price: $415.00
Loss of the parkinsonism-associated protein FBXO7 in glutamatergic forebrain neurons in mice leads to abnormal motor behavior and synaptic defects.
Wang J, Joseph S, Vingill S, Dere E, Tatenhorst L, Ronnenberg A, Lingor P, Preisinger C, Ehrenreich H, Schulz JB, Stegmüller J, et al.
Journal of neurochemistry (2023) : . 128 011 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.