Amyloid, OMAB), Biotinylated

  • Catalog number
    AS10 932B
  • Price
    Please ask
  • Size
    50 µg
  • Available ordering format
    Lyophilized
  • 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
  • Raised in
    Mouse
  • Clonality
    Monoclonal
  • Clone
    IgM
  • Purification
    Affinity purified
  • How to reconstitute
    For reconstitution add 100 µl of sterile water.
  • Storage condition
    store lyophilized/reconstituted at 4°C. 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.
  • Verified applications
    ELISA (ELISA), immunohistochemistry (IHC)
  • Connected products
    AS13 2716 | mAB-M | human Abeta protein (3-10) region, oligomer-specific, mouse monoclonal antibodyAS13 2715 | mAB-O | human Abeta protein (3-10) region, oligomer specific, mouse monoclonal antibodyAgrisera matching secondary antibody: Goat anti-mouse IgM (µ chain), HRP conjugated, min. cross-reactivity to human IgG/serum, AS10 969Secondary antibodies
  • Recommended dilutions for use
    coating antibody at 2 µg/ml (ELISA), 1: 500 (IHC)
  • Molecular weight expected аpparent
    4.5 kDa
  • Verified reactivity
    human Abeta oligomers only
  • Possible reactivity
    rat
  • No reactivity
    no confirmed exceptions from predicted reactivity known in the moment
  • Supplementary information
    OMAB antibody is a versatile tool within research of Alzheimer-™s disease. A sandwhich ELISA illustrates its potential regarding its high selectivity towards Aβ oligomers.
  • 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.
  • Scientific context
    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.
  • Notes
    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.
  • Protein number
    Refer to NCBI
  • TAIR number
    Refer to NCBI
  • Gene target
  • Short name
    Amyloid, OMAB), Biotinylated
  • Alternative name
    Amyloid, OMAB), Biotinylated
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