
Overview:
Product Name | Amyloid Fibrils (OC) Antibody | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | Rabbit Anti-Human Amyloid Fibrils (OC) Polyclonal | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Species Reactivity | Human | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Applications | WB, IHC, ICC/IF, IP, ELISA, DB | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Antibody Dilution | WB (1:1000), IHC (1:100); optimal dilutions for assays should be determined by the user. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Host Species | Rabbit | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Immunogen Species | Human | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Immunogen | Fibrils prepared from human amyloid beta 42 peptide | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Conjugates |
Alkaline Phosphatase, APC, ATTO 390, ATTO 488, ATTO 565, ATTO 594, ATTO 633, ATTO 655, ATTO 680, ATTO 700, Biotin, FITC, HRP, PE/ATTO 594, PerCP, RPE, Streptavidin, Unconjugated
StreptavidinProperties:
Streptavidin Datasheet BiotinProperties:
Biotin Datasheet HRP (Horseradish peroxidase)Properties:
HRP Datasheet AP (Alkaline Phosphatase)Properties:
AP Datasheet
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Properties
Storage Buffer | PBS, 50% glycerol, 0.09% sodium azide |
Storage Temperature | -20ºC |
Shipping Temperature | Blue Ice or 4ºC |
Purification | Protein A purified |
Clonality | Polyclonal |
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 h |
Cite This Product | StressMarq Biosciences Cat# SPC-507, RRID: AB_10960639 |
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. |
Biological Description
Alternative 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 |
Research Areas | Blood, Cardiovascular System, Cell Signaling, Neuroscience |
Cellular Localization | Membrane |
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-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. |
Product Images

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.

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, 486489. doi: 10.1126/science.1079469.

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, 486489. doi: 10.1126/science.1079469.

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, 486489. doi: 10.1126/science.1079469.

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, 486489. doi: 10.1126/science.1079469.

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.
Product Citations (3)
Immunohistochemistry
Acute amnestic encephalopathy in amyloid-ß oligomers injected mice is due to their widespread diffusion in vivo.
Epelbaum, S. et al. (2015) Neurobiol Aging. 36(6):2043-52.
PubMed ID: 25862419 Reactivity Human Applications: Immunohistochemistry
MEK Guards Proteome Stability and Inhibits Tumor-Suppressive Amyloidogenesis via HSF1.
Tang, Z. et al. (2015) Cell. 160(4):729-44.
PubMed ID: 25679764 Reactivity Human Applications: Immunohistochemistry
Other Citations
The polyphenol (−)-epigallocatechin-3-gallate prevents apoA-IIowa amyloidosis in vitro and protects human embryonic kidney 293 cells against amyloid cytotoxicity.
Nakajima, H. et al. (2015) Amyloid. 23(1):17-25.
PubMed ID: 26701221 Reactivity Human Applications: Dot Blot
PE/ATTO 594 | ||
PE/ATTO 594 is a tandem conjugate, where PE is excited at 535 nm and transfers energy to ATTO 594 via FRET (fluorescence resonance energy transfer), which emits at 627 nm. | ||
Overview:
PE/ATTO 594 Datasheet | ![]() | Optical Properties: λex = 535 nm λem = 627 nm Laser = 488 to 561 nm |