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Amyloid Oligomers (A11) Antibody

     
  • IHC - Amyloid Oligomers (A11) Antibody ASM10487
    Immunohistochemistry analysis using Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487). Tissue: Alzheimer's Disease brain. Species: Human. Fixation: Formalin fixed. Primary Antibody: Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487) at 1:1000. Secondary Antibody: Goat Anti-Rabbit ATTO 594 (red). Localization: Plaque. (A) Amyloid Fibril (OC) Antibody (SPC-507). (B) Amyloid Oligomer (A11) Antibody (ASM10487). (C) Composite. Courtesy of: Dr. Elizabeth Head, University of California, Irvine.
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  • WB - Amyloid Oligomers (A11) Antibody ASM10487
    Western blot analysis of Human Abeta42 fibrils and prefibrillar oligomers showing detection of Amyloid Oligomers (A11) protein using Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487). Primary Antibody: Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487) at 1:1000. Courtesy of: Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486–489. doi: 10.1126/science.1079469.
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  • DB - Amyloid Oligomers (A11) Antibody ASM10487
    Dot blot analysis using Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487). Tissue: Abeta42 fibrils and prefibrillar oligomers. Species: Human. Primary Antibody: Rabbit Anti-Amyloid Oligomers (A11) Polyclonal Antibody (ASM10487) at 1:1000. Courtesy of: Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486–489. doi: 10.1126/science.1079469.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
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
Research Areas
Citations (0)
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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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Cat# ASM10487
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