Anti-phospho Amyloid-beta, Ser8 [1E4E11] Antibody
![Anti-phospho Amyloid-beta, Ser8 [1E4E11] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1702_2001202001265817010.jpg "Anti-phospho Amyloid-beta, Ser8 [1E4E11] Antibody")
This mouse monoclonal antibody was raised against synthetic monomeric human Amyloid-beta 1-14 peptide: DAEFRHD(p)SGYEVHHC (pSer8-AΒ) conjugated with keyhole limpet hemocyanin and is specific for unaggregated and aggregated human Amyloid beta phosphorylated at Serine 8.
Highlights:
- Reacts with unaggregated and aggregated human Amyloid beta phosphorylated at Serine 8
- Not cross-reactive with other post-translationally modified variants of Amyloid beta, including N-terminally truncated (Aß3-42), nitrosylated (3NTyr10-Aß), pyroglutamated (pyroAß3-42) and Amyloid beta phosphorylated at Ser 26
- Suitable for Immunohistochemistry, Immunoprecipitation, Western Blot and ELISA applications
The progressive accumulation of extracellular amyloid plaques in the brain is a common hallmark of Alzheimer's disease. Forms of Amyloid beta phosphorylated at serine residue 8 have increased propensity to form toxic aggregates as compared to non-phosphorylated species.
From the laboratory of Jochen Walter, PhD, University of Bonn.
This mouse monoclonal antibody was raised against synthetic monomeric human Amyloid-beta 1-14 peptide: DAEFRHD(p)SGYEVHHC (pSer8-AΒ) conjugated with keyhole limpet hemocyanin and is specific for unaggregated and aggregated human Amyloid beta phosphorylated at Serine 8.
Highlights:
- Reacts with unaggregated and aggregated human Amyloid beta phosphorylated at Serine 8
- Not cross-reactive with other post-translationally modified variants of Amyloid beta, including N-terminally truncated (Aß3-42), nitrosylated (3NTyr10-Aß), pyroglutamated (pyroAß3-42) and Amyloid beta phosphorylated at Ser 26
- Suitable for Immunohistochemistry, Immunoprecipitation, Western Blot and ELISA applications
The progressive accumulation of extracellular amyloid plaques in the brain is a common hallmark of Alzheimer's disease. Forms of Amyloid beta phosphorylated at serine residue 8 have increased propensity to form toxic aggregates as compared to non-phosphorylated species.
From the laboratory of Jochen Walter, PhD, University of Bonn.
Specifications
| Product Type: | Antibody |
| Antigen: | Amyloid-beta |
| Accession ID: | P05067 |
| Clonality: | Monoclonal |
| Clone Name: | 1E4E11 |
| Reactivity: | Human |
| Immunogen: | Synthetic monomeric human Amyloid-beta 1-14 peptide: DAEFRHD(p)SGYEVHHC (pSer8-A&Beta, ) conjugated with keyhole limpet hemocyanin |
| Species Immunized: | Mouse |
| Buffer: | Cell Culture Supernatant |
| Tested Applications: | WB (1:500), IHC (1:200-1000), IP (1:100) ELISA (Use as an assay dependent dilution) |
| Storage: | -80C |
| Shipped: | Cold Packs |
Provider
From the laboratory of Jochen Walter, PhD, University of Bonn.
References
- Kumar S, Wirths O, Theil S, Gerth, J, Bayer TA, Walter J. Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's disease. Acta Neuropathol 2013; 125: 699709.
- Rijal Upadhaya A, Scheibe F, Kosterin l, Abramowski D, Gerth J, Kumar S, Liebau S, Yamaguchi H, Walter J, Staufenbiel M, Thal DR.The type of Aß-related neuronal degeneration differs between amyloid precursor protein (APP23) and amyloid ßpeptide (APP48) transgenic mice. Acta Neuropathol Commun. 2013; 1:77.
- Rijal Upadhaya A, Kosterin l, Kumar S, von Arnim CA, Yamaguchi H, Fändrich M, Walter J, Thal DR. Biochemical stages of amyloid-ß peptide aggregation and accumulation in the human brain and their association with symptomatic and pathologically preclinical Alzheimer's disease. Brain. 2014; 137(Pt 3):887-903.
- Balakrishnan K, Rijal Upadhaya A, Steinmetz J, Reichwald J, Abramowski D, Fändrich M, Kumar S, Yamaguchi H, Walter J, Staufenbiel M, Thal DR. Impact of amyloid ß aggregate maturation on antibody treatment in APP23 mice. Acta Neuropathol Commun. 2015; 3:41.
If you publish research with this product, please let us know so we can cite your paper.
