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Rabbit Anti-Oligomer (A11) Polyclonal Antibody. 1 µg of soluble Abeta42 monomers, Abeta42 oligomers, Ab42 fibrils, IAPP oligomers and alpha-Synuclein oligomers was applied to a nitrocellulose membrane and probed with Rabbit Anti-oligomer (A11) polyclonal antibody (top row; Cat. no. AHB0052) or with 6E10 (bottom row, Cat. no. 44-352). Anti-oligomer antibody recognizes all types of oligomers, but not monomers or fibrils. 6E10 recognizes all species of Abeta without regard to conformation, but not IAPP or alpha-Synuclein.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rat, Mouse, Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic molecular mimic of soluble oligomers.|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Dot blot (DB)||0.1-1 µg/ml|
|ELISA (ELISA)||0.1-1 µg/ml|
|Immunohistochemistry (IHC)||1-5 µg/ml|
|Neutralization (Neu)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Immunocytochemistry (ICC)||See 1 publications below|
|Immunoprecipitation (IP)||See 1 publications below|
|Western Blot (WB)||See 4 publications below|
|Dot blot (DB)||See 6 publications below|
|Miscellaneous PubMed (MISC)||See 1 publications below|
|Immunohistochemistry (Paraffin, Frozen) (IHC (P, F))||See 2 publications below|
|Immunohistochemistry - Free Floating (IHC (Free))||See 1 publications below|
This antibody recognizes amino acid sequence-independent oligomers of proteins or peptides. A11 does not recognize monomers or mature fibers of proteins or peptides. A11 reacts with soluble AB40 oligomers and does not react with soluble low molecular weight AB40 or AB40 fibrils. A11 recognizes oligomeric species of several other amyloidogenic polypeptides including AB42, human insulin, prion, polyglutamine, lysozyme, alpha-synuclein and yeast prion Sup35.
Oligomeric AB42 is recommended as a positive control, monomeric and fibrillar AB42 as negative controls.
Many degenerative diseases are known to be related to the accumulation of misfolded proteins called, amyloid fibrils. Soluble amyloid oligomers are considered as the principal pathogenic species which play an important role in the formation of amyloid fibrils; therefore, oligomers are involved in the pathogenesis of the many neurodegenerative diseases. This anti-oligomer antibody provides a facile means of assessing the significance of oligomers in disease pathogenesis.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
DT-Diaphorase Prevents Aminochrome-Induced Alpha-Synuclein Oligomer Formation and Neurotoxicity.
AHB0052 was used in immunocytochemistry to test if DT-diaphorase has a protective role in alpha synuclein neurotoxicity
|Muñoz P,Cardenas S,Huenchuguala S,Briceño A,Couve E,Paris I,Segura-Aguilar J||Toxicological sciences : an official journal of the Society of Toxicology (145:37)||2015|
Loss of F-box only protein 2 (Fbxo2) disrupts levels and localization of select NMDA receptor subunits, and promotes aberrant synaptic connectivity.
AHB0052 was used in immunohistochemistry - frozen section and immunoprecipitation to investigate the role of Fbxo2 in regulating NMDAR subunits in the brain
|Atkin G,Moore S,Lu Y,Nelson RF,Tipper N,Rajpal G,Hunt J,Tennant W,Hell JW,Murphy GG,Paulson H||The Journal of neuroscience : the official journal of the Society for Neuroscience (35:6165)||2015|
Novel antioxidants protect mitochondria from the effects of oligomeric amyloid beta and contribute to the maintenance of epigenome function.
AHB0052 was used in western blot to investigate the link between metabolic and epigenetic deficits on reduced mitochondrial function
|Mastroeni D,Khdour OM,Arce PM,Hecht SM,Coleman PD||ACS chemical neuroscience (6:588)||2015|
Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide.
AHB0052 was used in western blot to examine the aggregation and toxicity of melittin and pancreatic polypeptide
|Singh PK,Ghosh D,Tewari D,Mohite GM,Carvalho E,Jha NN,Jacob RS,Sahay S,Banerjee R,Bera AK,Maji SK||PloS one (10:null)||2015|
Functional amyloids in the mouse sperm acrosome.
AHB0052 was used in immunocytochemistry and western blot to study the role of the amyloid core of the acrosomal matrix in sperm-zona pellucida interactions
|Guyonnet B,Egge N,Cornwall GA||Molecular and cellular biology (34:2624)||2014|
Experimental traumatic brain injury induces rapid aggregation and oligomerization of amyloid-beta in an Alzheimer's disease mouse model.
AHB0052 was used in western blot to study Abeta agggregation and oligomerization induced in a murine model of Alzheimer's disease by experimental traumatic brain injury
|Washington PM,Morffy N,Parsadanian M,Zapple DN,Burns MP||Journal of neurotrauma (31:125)||2014|
Neuroinflammatory signals in Alzheimer disease and APP/PS1 transgenic mice: correlations with plaques, tangles, and oligomeric species.
AHB0052 was used in dot blot to study neuroinflammation-related gene regulation during normal aging and in sporadic Alzheimer disease in mice
|López-González I,Schlüter A,Aso E,Garcia-Esparcia P,Ansoleaga B,LLorens F,Carmona M,Moreno J,Fuso A,Portero-Otin M,Pamplona R,Pujol A,Ferrer I||Journal of neuropathology and experimental neurology (74:319)||2015|
|Human||1:5000||A comparative analysis of the aggregation behavior of amyloid-β peptide variants.||Vandersteen A,Hubin E,Sarroukh R,De Baets G,Schymkowitz J,Rousseau F,Subramaniam V,Raussens V,Wenschuh H,Wildemann D,Broersen K||FEBS letters (586:4088)||2012|
|Mouse||Not Cited||Application of immunosignatures to the assessment of Alzheimer's disease.||Restrepo L,Stafford P,Magee DM,Johnston SA||Annals of neurology (70:286)||2011|
|Mouse||Not Cited||ATP-binding cassette transporter A1 mediates the beneficial effects of the liver X receptor agonist GW3965 on object recognition memory and amyloid burden in amyloid precursor protein/presenilin 1 mice.||Donkin JJ,Stukas S,Hirsch-Reinshagen V,Namjoshi D,Wilkinson A,May S,Chan J,Fan J,Collins J,Wellington CL||The Journal of biological chemistry (285:34144)||2010|
|Rat||Not Cited||Dieldrin induces ubiquitin-proteasome dysfunction in alpha-synuclein overexpressing dopaminergic neuronal cells and enhances susceptibility to apoptotic cell death.||Sun F,Anantharam V,Latchoumycandane C,Kanthasamy A,Kanthasamy AG||The Journal of pharmacology and experimental therapeutics (315:69)||2005|
|Human||Not Cited||Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function.||Cleary JP,Walsh DM,Hofmeister JJ,Shankar GM,Kuskowski MA,Selkoe DJ,Ashe KH||Nature neuroscience (8:79)||2005|
|Clustering and internalization of toxic amylin oligomers in pancreatic cells require plasma membrane cholesterol.||Trikha S,Jeremic AM||The Journal of biological chemistry (286:36086)||2011|
|Mouse||Not Cited||Early-onset and robust amyloid pathology in a new homozygous mouse model of Alzheimer's disease.||Willuweit A,Velden J,Godemann R,Manook A,Jetzek F,Tintrup H,Kauselmann G,Zevnik B,Henriksen G,Drzezga A,Pohlner J,Schoor M,Kemp JA,von der Kammer H||PloS one (4:null)||2009|
|Human||Not Cited||Mutations of presenilin genes in dilated cardiomyopathy and heart failure.||Li D,Parks SB,Kushner JD,Nauman D,Burgess D,Ludwigsen S,Partain J,Nixon RR,Allen CN,Irwin RP,Jakobs PM,Litt M,Hershberger RE||American journal of human genetics (79:1030)||2006|
Age-related accumulation of Reelin in amyloid-like deposits.
AHB0052 was used in immunohistochemistry - free floating to examine the Reelin accumulation of Reelin in amyloid-like deposits during ageing.
|Knuesel I,Nyffeler M,Mormède C,Muhia M,Meyer U,Pietropaolo S,Yee BK,Pryce CR,LaFerla FM,Marighetto A,Feldon J||Neurobiology of aging (30:697)||2009|
IDDM; IDDM1; IDDM2; ILPR; INS; IRDN; MODY10