Amyloid Fibrils (OC) Antibody

Amyloid fibrils are highly ordered protein aggregates formed through the misfolding and oligomerization of normally soluble proteins. These fibrillar structures, often rich in β-sheet content, are hallmarks of numerous neurodegenerative diseases (1,2) . Even non-disease-related proteins can adopt amyloidogenic conformations under conditions of partial unfolding or denaturation, leading to the formation of toxic aggregates. In neurodegenerative research, amyloid fibrils—particularly those recognized by the OC antibody, which detects fibrillar oligomers—are critical biomarkers of disease progression and pathology. Their accumulation disrupts cellular homeostasis, impairs synaptic function, and triggers neuroinflammation. Prominent examples include amyloid-β (Aβ) plaques and tau neurofibrillary tangles in Alzheimer’s disease, α-synuclein aggregates in the Lewy bodies of Parkinson’s disease, and polyglutamine-rich inclusions in Huntington’s disease (2,3) . These fibrillar assemblies are not merely byproducts but active contributors to neuronal dysfunction and cell death. Understanding the structural and biochemical properties of amyloid fibrils is essential for developing targeted diagnostics and therapeutics. The OC antibody, which selectively binds to fibrillar but not prefibrillar or monomeric species, has become a valuable tool in distinguishing toxic conformers and mapping disease-specific aggregation pathways. As research advances, amyloid fibrils remain at the forefront of neurodegenerative disease studies, offering insights into protein misfolding disorders and potential avenues for intervention.

Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Expected to detect in Mouse and Rat based on species homology.

OC, Fibrils, Amyloid Oligomer aß, A11, Amyloid beta A4 protein, ABPP, APPI, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II, APP, A4, AD, Amyloid precursor protein, Amyloid-β

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.

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.

Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Expected to detect in Mouse and Rat based on species homology.