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Amyloid Fibrils (OC) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IP, DB, ICC |
|---|---|
| Host | Rabbit |
| Reactivity | Human |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human Amyloid Fibrils (OC) Polyclonal |
| Target/Specificity | Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins. Expected to detect in Mouse and Rat based on species homology. |
| Other Names | OC Antibody, Fibrils Antibody, Amyloid Oligomer aß Antibody, A11 Antibody, Amyloid beta A4 protein Antibody, ABPP Antibody, APPI Antibody, Alzheimer disease amyloid protein Antibody, Cerebral vascular amyloid peptide Antibody, PreA4 Antibody, Protease nexin-II Antibody, APP Antibody, A4 Antibody, AD Antibody |
| Immunogen | Fibrils prepared from human amyloid beta 42 peptide |
| 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-507 was sufficient for detection of amyloid fibrils on PVDF membranes using transferred fibrils by colorimetric dot blot 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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