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Anti-Aβ-42, oligomeric (VIA), Cat. No. ABN1665, is a highly specific rabbit polyclonal antibody that targets Amyloid beta 42 oligomers and has been tested in Dot Blot, Neutralizing, and Western Blotting.
More>>Anti-Aβ-42, oligomeric (VIA), Cat. No. ABN1665, is a highly specific rabbit polyclonal antibody that targets Amyloid beta 42 oligomers and has been tested in Dot Blot, Neutralizing, and Western Blotting. Less<<
Anti-Aβ-42 Antibody, oligomeric (VIA): SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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). Growing evidences implicate soluble oligomers as the more toxic species and the extent of oligomer formation and assembly correlates better with disease progression and cognitive dysfunction. These Aβ oligomers are able to induce other aggregation-prone proteins, including α-synuclein (α-syn), prion protein (PrP), and TDP-43, to assume oligomeric conformations. These proteins can then seed tau aggregation, resulting in neurodegeneration.
References
Product Information
Format
Purified
Presentation
Purified rabbit polyclonal antibody in PBS without preservatives.
Anti-Aβ-42, oligomeric (VIA), Cat. No. ABN1665, is a highly specific rabbit polyclonal antibody that targets Amyloid beta 42 oligomers and has been tested in Dot Blot, Neutralizing, and Western Blotting.
Key Applications
Dot Blot
Neutralizing
Western Blotting
Application Notes
Dot Blot Analysis: A representative lot detected recombinant Aβ-42, but not Aβ-40, oligomers (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).
Neutralizing Analysis: A representative lot neutralized Aβ-42 toxicity to cultured SH-SY5Y cells (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).
Western Blotting Analysis: A representative lot detected oligomeric Aβ-42, but not monomeric Aβ-42, monomeric or oligomeric A -40 (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).
Note: Both purified antibody (Cat. No. ABN1665) and unpurified antiserum (Cat. No. ABN1650) are suitable for Dot blot, immunofluorescence, immunohistochemistry, and Western blotting applications. However, we recommend using only the purified antibody for neutralization studies.
Biological Information
Immunogen
Aggregated synthetic hexapeptide VIAVIA composed of two copies of Aβ-42 C-terminal end 3-amino acid sequence (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).
Concentration
Please refer to lot specific datasheet.
Host
Rabbit
Specificity
This polyclonal antiserum (VIA) recognizes a distinct epitope specific to Aβ-42 oligomers. VIA does not recognize classic amyloid plaques composed of fibrillar Aβ or Aβ-40 (Bodani, R.U., et al. (2015). ACS Chem. Neurosci. 6(12):1981-1989).
Variable depending on the sizes of the Aβ-42 oligmers.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Dot Bot analysis of A proteins.
Dot Blot Analysis: 6.67 µg/mL of this antibody detected recombinant Aβ-42, but not Aβ-40, oligomer.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.