Amyloid beta oligomer-specific monoclonal antibody (OMAB), Biotinylated

Product no: AS10 932B

AS10 932B | Clonality: Monoclonal | Host: Mouse | Reactivity: amyloid beta

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  • Product Info
  • Immunogen: partly aggregated, recombinant peptide corresponding to the human Abeta (1-40), Amino acid sequence: D-A-E-F-R-H-D-S-G-Y-E-V-H-H-Q-K-L-V-F-F-A-E-D-V-G-S-N-K-G-A-I-I-G-L-M-V-G-G-V-V
    Sub class: IgM
    Host: Mouse
    Clonality: Monoclonal
    Purity: Affinity purified in PBS pH 7.4.
    Format: Lyophilized
    Quantity: 50 g
    Reconstitution: For reconstitution add 100 l of sterile water
    Storage: Store lyophilized/reconstituted at 4C. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
    Tested applications: ELISA (ELISA), Immunohistochemistry (IHC)
    Recommended dilution: Coating antibody at 2 µg/ml (ELISA), 1 : 500 (IHC)
    Expected | apparent MW: 4,5 kDa
  • Reactivity
  • Confirmed reactivity: Human Abeta oligomers only
    Predicted reactivity: Rat
    Not reactive in: No confirmed exceptions from predicted reactivity are currently known
  • Additional Information
  • Additional information:

    OMAB antibody has been purified by by ion-exchange chromatography and is supplied in PBS without any additives as carrier proteins or sodium azide.

    Binding of OMAB antibody and Abeta oligomers at RT takes about 15 min.

    Fibrils are inaccessible for OMAB antibodies therefore if a discrimination between fibrils and oligomers is to be achieved, dot blot can be used. Start with antigen concentration of 500 ng/dot followed by 2X dilution steps. Blocking: non-fat milk and washes with 0.3 % Tween 20 in TBS pH 7.4.

    Additional information (application): OMAB antibody is a versatile tool within research of Alzheimer’s disease, A sandwhich ELISA illustrates its potential regarding its high selectivity towards A? oligomers
  • Background
  • Background:

    Soluble oligomeric assemblies of the Amyloid-β peptide are today anticipated to be the direct cause regarding the Alzheimer pathology. As a consequence, oligomeric Aβ-assemblies constitute a very interesting therapeutic target. Identification of Aβ-oligomers is however, technically challenging due to there labile nature and low abundance. Abeta oligomer-specific OMAB antibody is based on the IgM isotype and represents a new concept of Aβ-oligomer binders using a combination of high avidity and very low monovalent affinity. This combination creates a selectivity of the antibody towards the oligomeric fraction and minimizes reactivity towards monomeric species.

  • Product Citations
  • Selected references: Richman et al. (2013). In Vitro and Mechanistic Studies of an Anti-Amyloidogenic Self-Assembled Cyclic D,L-#-Peptide Architecture. J. Americal Chemical Societ, Jan 19.
    Lindhagen-Persson et al. (2010). Amyloid-β Oligomer Specificity Mediated by the IgM Isotype – Implications for a Specific Protective Mechanism Exerted by Endogenous Auto-Antibodies. PLoS ONE.
  • Protocols
  • Antibody protocols
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