Mouse anti-Human Amyloid-beta Monoclonal Antibody

Amyloid-beta (N-term), Human, mAb VU17

Cat. Num. AAA77809

• Reactivity: Human
• Applications: Immunoprecipitation, Immunohistochemistry
• Synonyms: Amyloid-beta, Antibody; Amyloid-beta (N-term), Human, mAb VU17; Abeta; beta-Amyloid; anti-Amyloid-beta antibody

• Host: Mouse
• Reactivity: Human
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: VU17
• Form/Format: 1 ml (100 ug/ml) 0.2 um filtered antibody solution in PBS, containing 0.1% bovine serum albumin and 0.02% sodium azide.; For unit size 0.5 mg or larger: PBS only (concentration< 0.5mg/ml)

• Applicable Applications for anti-Amyloid-beta antibody: IP (Immunoprecipitation), IA (Immunoassay), IHC (Immunohistochemistry)
• Preparation and Storage: Store at 4 degree C. Under recommended storage conditions, product is stable for at least one year.

IHC (Immunohiostchemistry)

IHC (Immunohistochemistry)

Related Product Information for anti-Amyloid-beta antibody

Antibody clone VU17, formerly known as alphaVU Abeta 17, recognizes the N-terminus of human amyloid beta (i.e. in: Abeta1-38; Abeta1-39; Abeta1-40; Abeta1-42). Amyloid beta peptides are of key importance in the development of Alzheimer's disease (AD) and are present in CSF. AD affects approximately 1% of the population over the age of 80. The disease is characterized by aggregation of Abeta into oligomers, fibrils and plaques deposition of insoluble and aggregated protein in the brain where its neurotoxic action leads to neuronal cell death. The deposits, also called amyloid plaques, are formed around the neuropil. The exact molecular mechanism is still unclear. Abeta is a proteolytic cleavage product, by APP-cleaving enzyme 1 (BACE1) and beta-secretase complex, of membrane bound amyloid precursor protein (APP). Amyloid is the term used for proteins that are misfolded into a cross beta-sheet structure. Abeta is produced by various cell types and is secreted in the interstitial fluid. There are multiple cleavage sites in Abeta domain leading to various fragments of 36-43 amino acids in length. The main peptide in the CSF terminate at residue 40. CSF contains many Abeta isoforms, of which Abeta40 is approximately 10 times more abundant than Abeta42. Abeta40 levels are unchanged in AD, but there is a change in Ab40:Abeta42 ratio in AD. This ratio has been thought of importance. Assessment of Abeta in brain tissue is essential for identification and is crucial for investigating the molecular mechanisms underlying AD. Antibody VU17 is raised against the N-terminus of Abeta. The antibody detects all forms of Abeta deposits without the need for formic acid pre-treatment on paraffin coupes and can be applied in a double staining strategy, making it suitable for investigating co-localization.

References

1. Verwey, N et al; Immunohistochemical characterization of novel monoclonal antibodies against the N-terminus of amyloid beta-peptide. Amyloid 2013, 20:3 2. Verwey, N et al; Quantification of amyloid beta 40 in cerebrospinal fluid. Journal of Immunology methods 2009, 348:1-2