Product Name

Amyloid Fibrils (OC)

Catalog #

SPC-507D

Alternative Names

OC, Fibrils

Immunogen

Fibrils prepared from human Aβ42 peptide.

Applications

IP, ICC, IHC, ELISA, WB, Dot Blot

Host Species

Rabbit

Species Reactivity

Human. Potentially mouse and rat based on species homology.

Recommended Dilutions

1:1000 (Dot Blot)

Form

Protein A Purified

Storage Buffer

PBS, 50% glycerol, 0.09% sodium azide

Concentration

N/A

Background Info

Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins.

Conjugate

N/A

Package Size

100uL

Storage Temp

-20°C

Shipping Temp

Blue Ice, 4ºC

Datasheet

SPC 507 Amyloid Fibrils (OC) Neuroscience

Research Area

Neuroscience

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.

Price

$275.00 USD Add to Cart Bulk Quote

Dot blot analysis of Aβ42 and polyQ36 prefibrillar oligomers and fibrils. Aβ42 and polyQ fibrils only stain with OC serum (Catalog # SPC-507), while Aβ42 and polyQ prefibrillar oligomers only react with A11 (Catalog # SPC-506).  Picture courtesy of Kayed et al., (2007) Biomed Central: Molecular Neurodegeneration, 2: 18.


Western blot analysis of Aβ42 fibrils and prefibrillar oligomers. Aβ42 fibrils (F) and prefibrillar oligomers (O) were run on SDS polyacrylamide gels, transferred to nitrocellulose and probed with OC and A11 antibodies.
Picture courtesy of Kayed et al., (2007) Biomed Central: Molecular Neurodegeneration, 2: 18.


Extensive OC labeling was observed in the hippocampus (A), subiculum (B) and frontal cortex (C) in Alzheimer disease.  A higher magnification photograph illustrates that OC positive deposits were dense and consisted of fine fibrillar material (D).
Picture courtesy of Kayed et al., (2007) Biomed Central: Molecular Neurodegeneration, 2: 18.

 

Research 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.