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General description
Amyloid beta A4 protein (UniProt P05067; also known as ABPP, Alzheimer disease amyloid protein, Amyloid precursor protein, APP, APPI, Cerebral vascular amyloid peptide, CVAP, PN-II, PreA4, Protease nexin-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID 351) in human. Amyloid precursor protein (APP) is initially produced with a signal peptide sequence (a.a. 1-17), the removal of which yields the mature protein with a large extracellular portion (a.a. 18-699), followed by a transmembrane segment (a.a. 700-723) and a cytoplasmic (a.a. 724-770) tail. APP can be further processed by the α-, β-, and γ-secretases in two alternative processing pathways. In the non-amyloidogenic pathway, APP is first cleaved by the plasma membrane-localized α-secretase to generate an N-terminal extracellular sAPPα fragment (a.a. 18-687) and a membrane-bound C-terminal fragment C83 (CTFα), which can be further cleaved by γ-secretase to produce a non-toxic small peptide p3 and a cytoplasmic APP intracellular domain (AICD). In the amyloidogenic pathway, APP undergoes β-cleavage in BACE-1 (β-site APP-cleaving enzyme)-enriched endosomes to generate an N-terminal extracellular sAPPβ fragment (a.a. 18-671) and a membrane-bound C-terminal fragment C99 (CTFβ). Subsequent cleavage of C99 by γ-secretase releases the amyloid β peptides, Aβ1-42 (672-713) & Aβ1-40 (672-711), and AICD. Aβ accumulation in the cortical and hippocampal regions of the brain is a major pathological feature of Alzheimer′s disease (AD). Aβ serine phosphorylation is shown to promote Aβ aggregation into oligomeric and fibrillar assemblies and to prevent Aβ proteolytic clearance by certain proteases.
~4/8 (monomer/dimer) and >188 (oligomer) kDa observed. 4.514/9.028 kDa (Abeta1-42 monomer/dimer), 4.330/8.660 kDa (Abeta1-40 monomer/dimer) calculated. Uncharacterized bands may be observed in some lysate(s).
Immunogen
KLH-conjugated linear peptide corresponding to human amyloid beta peptide target region sequence with phosphorylated Ser26.
Application
Anti-phospho-Amyloid beta (Ser26), clone 5H11C10, Cat. No. MABN879, is a highly specific mouse monoclonal antibody, that targets amyloid beta peptides Ser26 phosphorylation and has been tested in ELISA, Immunofluorescence, Western Blotting.
Western Blotting Analysis: 2 µg/mL from a representative lot detected monomeric and dimeric forms of synthetic A 1-40 peptide with phosphorylated Ser26, but not the non-phosphorylated A 1-40 peptide (Courtesy of Dr. Kumar Sathish, University of Bonn, Germany)
Western Blotting Analysis: 2 µg/mL from a representative lot detected Ser26-phosphorylated oligomeric amyloid beta (pA ) peptides in brain extracts from 8-month old APP/PS1KI transgenic mice, but not in extracts from age-matched non-transgenic mice (Courtesy of Dr. Kumar Sathish, University of Bonn, Germany).
Note: Formic acid (88%) treatment following heat retrieval is recommended for immunohistochemical detection of aggregated intraneuronal Abeta peptides in brain sections (Kumar, S., et al. (2013). Acta Neuropathol. 125(5):699-709; Christensen, D.Z., et al. (2009). Brain Res. 1301:116-125).
Biochem/physiol Actions
Clone 5H11C10 recognizes Aβ1-40 and Aβ1-42 peptides with phosphorylated Ser26, but not the non-phosphorylated peptides.
Physical form
Format: Purified
Analysis Note
Identity Confirmation by Isotyping Test.
Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG1κ.
Other Notes
Concentration: Please refer to lot specific datasheet.
| biological source | mouse |
| Quality Segment | 100 |
| antibody form | purified immunoglobulin |
| antibody product type | primary antibodies |
| clone | 5H11C10, monoclonal |
| species reactivity | human |
| technique(s) | ELISA: suitable,immunofluorescence: suitable,western blot: suitable |
| isotype | IgG1κ |
| NCBI accession no. | NP_000475 |
| UniProt accession no. | P05067 |
| shipped in | ambient |
| target post-translational modification | phosphorylation (pSer26) |
| Gene Information | human ... APP(351) |
| 长度(mm) | |
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