Rabbit Amyloid Fibrils (OC) Polyclonal Antibody
Amyloid Fibrils (OC) Antibody: ATTO 594
DB (Dot Blot)
(Dot blot analysis using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Tissue: Cell lysates. Species: Human. Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) at 1:500, 1:5000. Beta Amyloid HEPES-NaCl aggregation, showing 1:500 (L) and 1:5000 (R) time lapse dot blot.)
DB (Dot Blot)
(Dot blot analysis using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Tissue: Abeta42 fibrils and prefibrillar oligomers. Species: Human. Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) 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.)
IHC (Immunohistochemistry)
(Immunohistochemistry analysis using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Tissue: Alzheimer's Disease brain. Species: Human. Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) at 1:100. Showing no Amyloid Precursor Protein (APP) cross-reactivity (L), but when conducted with monoclonal 6E10 (R) shows considerable APP cross-reactivity. 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.)
WB (Western Blot)
(Western blot analysis of Human Abeta42 fibrils and prefibrillar oligomers showing detection of Amyloid Fibrils (OC) protein using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) 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.)
IHC (Immunohistochemistry)
(Immunohistochemistry analysis using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Tissue: Alzheimer's Disease brain. Species: Human. Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) at 1:100. Extensive OC labeling was observed in the hippocampus (A), subiculum (B) and frontal cortex (C) in Alzheimer disease. A higher magnification image illustrates that OC positive deposits were dense and consisted of fine fibrillar material (D). 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.)
IHC (Immunohistochemistry)
(Immunohistochemistry analysis using Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507). Tissue: Alzheimer's Disease brain. Species: Human. Fixation: Formalin fixed. Primary Antibody: Rabbit Anti-Amyloid Fibrils (OC) Polyclonal Antibody (SPC-507) at 1:5000. Secondary Antibody: Goat Anti-Rabbit ATTO 488 (green). Localization: Plaque. (A) Amyloid Fibril (OC) Antibody (SPC-507). (B) Amyloid Oligomer (A11) Antibody (SPC-506). (C) Composite. Courtesy of: Dr. Elizabeth Head, University of California, Irvine.)
Scientific 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-beta peptide plaques and tau neurofibrillary tangles in senile plaques of Alzheimer's symptomology, the deposition of alpha-synuclein in the Lewy bodies of Parkinson's disease, and accumulation of polyglutamine-containing aggregates in Huntington's disease (2, 3).