mAB-M | Mouse anti-human Abeta protein (3-10) region, oligomer-specific (clone 2D10.F6)

AS13 2716   | Clonality: monoclonal  |  Host: Mouse  |  Reactivity: Human

mAB-M | Mouse anti-human Abeta protein (3-10) region, oligomer-specific (clone 2D10.F6) in the group Antibodies for Human/Animal  / Human Proteins / Amyloid disorders / Alzheimer's disease at Agrisera AB (Antibodies for research) (AS13 2716)


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Product name, number (Agrisera, Sweden)

Data sheet Product citations Protocols Add review

Product Information


synthetic peptide chosen from human Abeta protein (3-10) pregion, oligomer specific

Host Mouse
Clonality Monoclonal
Subclass/isotype IgG1, kappa light chain, (clone number 2D10.F6)
Purity Affinity purified in PBS pH 7.4, no preservatives
Format Lyophilized
Quantity 50 µg
Reconstitution For reconstitution add 50 µl of sterile water.

For short time storage please add sodium azide and srote at +4°C.
For long time storage store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Tested applications Dot blot (Dot), ELISA (ELISA), Immunolocalization (IL)
Recommended dilution 10 ug/ml (IL), 1-2 ug/ml (Dot), 2-4 ug/ml (ELISA capture)
Expected | apparent MW

4.5 kDa


Confirmed reactivity Human
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Application examples application examples

dot blot

dot blot using anti-mAB-M antibodies
Dot blot reaction of the binding capacity of mAB-M to fibrils, monomers and oligomers. Equal amounts of each sample were spotted on a nitrocellulose membrane and then dried. The membrane was blocked with 5% non-fat milk before incubated for 1 h with anti-mAB-M (25nM) and then with secondary antibody, anti-mouse HRP-conjugated (1:1500). The membrane was washed with PBS containing 0.25% Tween-20 before detection using ECL prime (GE Healthcare).


IHC used to illustrate the lack of binding of mAB-M to plaques. Tissue sections from the human AD hippocampus were de-waxed and rehydrated in ethanol and then incubated with AS08 357 (A) and mAB-M(B) at RT for 1h. The immunoreactivity was detected with the anti-mouse Peroxidase Reagent Kit (ImmPRESS, Vector Laboratories, Inc.) and then developed using the ImmPACT AEC Peroxidase Substrate kit (Vector Laboratories, Inc.).

Additional information

Additional information

Immunolocalization: human tissue was paraffin-embedded and sectioned. De-waxed and rehydrated in an ethanol gradient. Antigens were retrieved in sodium citrate buffer (pH 6) at 95°C for 1 h. The tissue sections were separately incubated for 1 h at RT with primary antibody and antibody binding was visualized with IgG Preoxidase Reagent Kit.

This antibody is specific for human Amyloid-Beta oligomers.
Due to location of antigen used to elicit this antibody in 3-10 region, it should bind to full length APP.

Related products

Related products

AS10 932| Amyloid beta oligomer-specific monoclonal antibody (OMAB)
AS10 932B | Amyloid beta oligomer-specific monoclonal antibody (OMAB), Biotinylated
AS13 2715 | mAB-O oligomer-specific anti-abeta monoclonal antibody



Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the growing population of elderly people. A hallmark of AD is the accumulation of plaques in the brain of AD patients. The plaques predominantly consist of aggregates of amyloid-beta (Abeta), a peptide of 39-42 amino acids generated in vivo by specific, proteolytic cleavage of the amyloid precursor protein. Recent findings however suggest that smaller oligomeric forms of Abeta, formed in parallel to the amyloid plaques, excert the predominant tissue damaging effect.

Specific identification of the oligomeric forms is as a consequence of great interest. Based on a recently published technique a highly oligomer-specific antibody (mAB-M), targeting Abeta oligomers while omitting reactivity towards the monomeric and fibrillar counterpart, has been developed.

Product citations

Selected references Meilandt et al. (2019). Characterization of the selective in vitro and in vivo binding properties of crenezumab to oligomeric AÃ?Âē. Alzheimers Res Ther. 2019 Dec 1;11(1):97. doi: 10.1186/s13195-019-0553-5.
Brännström et al. (2014). A Generic Method for Design of Oligomer-Specific Antibodies. PLoS ONE. DOI: 10.1371/journal.pone.0090857.

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