Anti-Amyloid Beta Peptide, Pan-Specific [MOAB-2] Antibody
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MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to amyloid-beta peptide residues 1-4 as demonstrated by biochemical and immunohistochemical analyses, particularly compared to 6E10 (a commonly used commercial antibody to amyloid-beta peptide residues 3-8). The antibody specifically detects amyloid-beta peptide, but not amyloid precursor protein (APP).
Amyloid-beta is the main component of amyloid plaques (deposits found in the brains of patients with Alzheimer's disease). Similar plaques appear in some variants of Lewy body dementia and in inclusion body myositis, while amyloid-beta can also form the aggregates that coat cerebral blood vessels in cerebral amyloid angiopathy. The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers, a protein fold shared by other peptides such as the prions associated with protein misfolding diseases. Recent research suggests that soluble oligomeric forms of the peptide may be causative agents in the development of Alzheimer's disease. A number of genetic, cell biology, biochemical and animal studies support the concept that amyloid-beta plays a central role in the development of Alzheimer’s disease pathology.
From the laboratory of Mary Jo LaDu, PhD, University of Illinois at Chicago.
Part of The Investigator's Annexe program.
MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to amyloid-beta peptide residues 1-4 as demonstrated by biochemical and immunohistochemical analyses, particularly compared to 6E10 (a commonly used commercial antibody to amyloid-beta peptide residues 3-8). The antibody specifically detects amyloid-beta peptide, but not amyloid precursor protein (APP).
Amyloid-beta is the main component of amyloid plaques (deposits found in the brains of patients with Alzheimer's disease). Similar plaques appear in some variants of Lewy body dementia and in inclusion body myositis, while amyloid-beta can also form the aggregates that coat cerebral blood vessels in cerebral amyloid angiopathy. The plaques are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers, a protein fold shared by other peptides such as the prions associated with protein misfolding diseases. Recent research suggests that soluble oligomeric forms of the peptide may be causative agents in the development of Alzheimer's disease. A number of genetic, cell biology, biochemical and animal studies support the concept that amyloid-beta plays a central role in the development of Alzheimer’s disease pathology.
From the laboratory of Mary Jo LaDu, PhD, University of Illinois at Chicago.
Part of The Investigator's Annexe program.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Antibody |
| Antigen: | Amyloid-beta peptide |
| Accession ID: | P05067 |
| Isotype: | IgG2b |
| Clonality: | Monoclonal |
| Clone Name: | MOAB-2 (6C3) |
| Reactivity: | Human, Mouse, Rat |
| Immunogen: | Recombinant AB42 from R-peptide |
| Species Immunized: | Mouse |
| Epitope: | Amyloid-beta petide (amino acids 1-4) |
| Purification Method: | Protein G |
| Buffer: | Hepes buffered saline, pH 7.4, 50% glycerol |
| Tested Applications: | WB, ELISA, IF, IHC, IP |
| Concentration: | 1mg/mL |
| Storage: | Long-term storage -20C; Short-term storage 4C |
| Shipped: | Cold packs |
MOAB-2 detects multiple amyloid-beta conformations at low antibody concentrations.
(A) Dot blot of serial Abeta40 (unaggregated) and Abeta42 dilutions (unaggregated (U), oligomeric (O) or fibrillar (F)) probed with MOAB-2 or 6E10. (B) Antibody-binding saturation curve of 25 ng Abeta42 in the different aggregation states (U, O, and F) immobilized on microtiter plates, incubated with different MOAB-2 concentrations as indicated on figure. (C) Western-blot analysis of 1000 pmol U-Abeta40 or 200 pmol U-Abeta42 probed with MOAB-2 (lanes 1-2) or 200 pmol U-Abeta40 and U-Abeta42 probed with 6E10(lanes 3-4). (D) Western-blot analysis comparing antibody dilutions of MOAB-2 and 6E10 (0.5 mg/ml antibody stock concentrations) using U-, O- and F-Abeta42 (200 pmol). Quantification of Abeta immunoreactivity for each antibody dilution estimated using image J. (E) Immunoprecipitation of U- and O-Abeta42 (0.5 pmol) with 6E10 or MOAB-2 (Lane 1 = IP-6E10, 2 = IP-MOAB-2, 3 = 5% total input (0.025 pmol), 4 = 10% total input (0.05 pmol). The dilution of MOAB-2 for Figures 1A and C is 1:5000 from a stock of 0.5 mg/ml.
Adapted from: Tai, L.M., Youmans, K., Stine, W.B., Michon S.C., Kanekiyo, T., Manelli, A.M., Fu, Y., Eimer, W.A.,Bu, G., Binder, L., Yu, C., Hartley, D.M., and M.J. LaDu. Intraneuronal amyloid-beta detection in 5xFAD miceby a new amyloid-beta-specific antibody. Molecular Neurodegeneration, 7(8), doi:10.1186/1750-1326-7-8, 2012.
MOAB-2 detection of intraneuronal amyloid-beta but not intraneuronal APP in 5xFAD brain tissue.
Immunofluorescent detection of amyloid-beta and APP in the cortex of 1-month old 5xFAD mice with MOAB-2 and antibodies against the C-terminus (Cter) (CT695) or N-terminus (Nter) (2211) of APP with 6E10 or MOAB-2, plus antibodies CT695 and 22C11. (Coronal sections, representative confocal images at 100x). Antibody concentrations: MOAB-2 (1:1000), anti-Abeta40, (1:1700), anti-Abeta42 (1:200), 22C11 (1:40), CT695 (1:500), 6E10 (1:1000).
Adapted from: Tai, L.M., Youmans, K., Stine, W.B., Michon S.C., Kanekiyo, T., Manelli, A.M., Fu, Y., Eimer, W.A.,Bu, G., Binder, L., Yu, C., Hartley, D.M., and M.J. LaDu. Intraneuronal amyloid-beta detection in 5xFAD miceby a new amyloid-beta-specific antibody. Molecular Neurodegeneration, 7(8), doi:10.1186/1750-1326-7-8, 2012.
- Youmans KL, Tai LM, Nwabuisi-Heath E, Jungbauer L, Kanekiyo T, Gan M, Jungsu K, Eimer WA, Estus S, Rebeck GW, Weeber EJ, Bu G, Yu C, and LaDu MJ. APOE4-specific changes in amyloid-beta accumulationin a new transgenic mouse model of Alzheimer's disease. Journal of Biological Chemistry, 2012, doi: 10.1074/jbc.M112.407957.
- Tai, L.M., Youmans, K., Stine, W.B., Michon S.C., Kanekiyo, T., Manelli, A.M., Fu, Y., Eimer, W.A., Bu, G., Binder, L., Yu, C., Hartley, D.M., and M.J. LaDu. Intraneuronal amyloid-beta detection in 5xFAD mice by a new Aß-specific antibody. Molecular Neurodegeneration, 7(8), doi:10.1186/1750-1326-7-8, (2012).
- Wang J, Lu R, Yang J, Li H, He Z, Jing N, Wang X, Wang Y. TRPC6 specifically interacts with APP to inhibit its cleavage by γ-secretase and reduce Aβ production. Nat Commun. 2015 Nov 19;6:8876. View Article
- Ross JA, Reyes BAS, Thomas SA, Van Bockstaele EJ. Localization of endogenous amyloid-β to the coeruleo-cortical pathway: consequences of noradrenergic depletion. Brain Struct Funct. 2018 Jan;223(1):267-284. View Article
- Ross JA, Mathews PM, Van Bockstaele EJ. High resolution approaches for the identification of amyloid fragments in brain. J Neurosci Methods. 2019 May 1;319:7-15. View Article
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- Ross JA, Alexis R, Reyes BAS, Risbrough V, Van Bockstaele EJ. Localization of amyloid beta peptides to locus coeruleus and medial prefrontal cortex in corticotropin releasing factor overexpressing male and female mice. Brain Struct Funct. 2019 Jun 27. View Article
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