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Amyloid Oligomers (A11) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IP, ICC |
|---|---|
| Primary Accession | P05067 |
| Other Accession | NM_000484.2 |
| Host | Rabbit |
| Reactivity | Human, Eukaryote, Mouse, Rat |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human Amyloid Oligomers (A11) Polyclonal |
| Target/Specificity | Recognizes all types of amyloid oligomers. Appears to recognize a peptide backbone epitope that is common to amyloid oligomers, but is not found in native proteins, amyloidogenic monomer or mature amyloid fibrils. |
| Other Names | Amyloid Oligomer alpha beta Antibody, A11 Antibody, Amyloid Oligomer AlphaBeta Antibody, APP Antibody |
| Immunogen | Synthetic molecular mimic of soluble oligomers |
| Purification | Protein A Purified |
| Storage | -20ºC |
| Storage Buffer | PBS, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | A 1:1000 dilution of SPC-506 was sufficient for detection of amyloid oligomers in 10 µg of mouse brain lysates by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody. |
| Cellular Localization | Membrane |
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Provided below are standard protocols that you may find useful for product applications.
Background
Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. Many degenerative diseases are known to be related to the accumulation of misfolded proteins as amyloid fibres (1, 2). These include the amyloid-β peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer’s symptomology, the deposition of α-synuclein in the Lewy bodies of Parkinson’s disease, and accumulation of polyglutamine-containing aggregates in Huntington’s disease (2, 3).
References
1. Glabe C.G. (2004) Trends Biochem Sci. 29(10): 542-547.
2. Kayed R., et al. (2004) J Bio. Chem. 279: 46363-46366.
3. Kayed R., et al. (2003) Science. 300(5618): 486-489.
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