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Anti-Amyloid Oligomer Antibody, αβ, oligomeric

serum, Chemicon®


biological source


Quality Level

antibody form


antibody product type

primary antibodies



species reactivity

rat, eukaryotes, mouse

species reactivity (predicted by homology)





ELISA: suitable
immunofluorescence: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

Gene Information

human ... APP(351)

General description

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. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.


Recognizes amyloid oligomer. The antibody recognize all types of amyloid oligomers. The antibody 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. This antibody has been referred to as A11.


Epitope: Oligomeric


Anti-Amyloid Oligomer Antibody, αβ, oligomeric is an antibody against Amyloid Oligomer for use in ELISA, IF, IH, IH(P), IP & WB.
Research Category
Research Sub Category
Neurodegenerative Diseases
A 1:1,000-1:10,000 concentration was used on a previous lot.

A 1:1,000 concentration was used on a previous lot. Suggested cell lysis buffer is RIPA. Suggested capture agent is magnetic beads (Dynabeads). Known co-precipitatiing polypeptide: Amyloid beta, alpha synuclein oligomers.

ELISA (direct):
A previous lot of this antibody was used in ELISA.

Optimal working dilutions must be determined by the end user.


Evaluated by Western Blot on mouse brain lysates.

Western Blotting Analysis:
1:500 dilution of this antibody detected AMYLOID OLIGOMER on 10 μg of mouse brain lysates.

Physical form

Rabbit Serum. Contains no preservative.

Storage and Stability

Stable for 1 year at -20ºC from date of receipt.

Analysis Note


Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Quality

Enter Lot Number to search for Certificate of Quality (COQ).

Inhibition of Alzheimer's amyloid toxicity with a tricyclic pyrone molecule in vitro and in vivo.
Hyun-Seok Hong,Sandeep Rana,Lydia Barrigan,Aibin Shi,Yi Zhang,Feimeng Zhou,Lee-Way Jin,Duy H Hua
Journal of Neurochemistry null
Carolyn Hollands et al.
Molecular neurodegeneration, 12(1), 64-64 (2017-09-10)
The molecular mechanism underlying progressive memory loss in Alzheimer's disease is poorly understood. Neurogenesis in the adult hippocampus is a dynamic process that continuously changes the dentate gyrus and is important for hippocampal plasticity, learning and memory. However, whether impairments
S100A9 knockout decreases the memory impairment and neuropathology in crossbreed mice of Tg2576 and S100A9 knockout mice model.
Kim, HJ; Chang, KA; Ha, TY; Kim, J; Ha, S; Shin, KY; Moon, C; Nacken, W; Kim, HS; Suh, YH
Testing null
Sónia S Leal et al.
The Journal of biological chemistry, 288(35), 25219-25228 (2013-07-19)
Imbalance in metal ion homeostasis is a hallmark in neurodegenerative conditions involving protein deposition, and amyotrophic lateral sclerosis (ALS) is no exception. In particular, Ca(2+) dysregulation has been shown to correlate with superoxide dismutase-1 (SOD1) aggregation in a cellular model
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.
Shorter, James and Lindquist, Susan
Science (New York, N.Y.), 304, 1793-1797 (2004)

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