Full Name: Rat/Mouse Amyloid Beta (1-40) ELISA Kit (Aβ 1-40)
Reactivity: Rat, Mouse
Sample Type: Brain Extract, Plasma, Cell Culture Supernatant, Serum
Sensitivity: 0.28 pg/ml
Amyloid beta (which is commonly referred to as Aβ or Abeta) denotes peptides that are between 36-43 amino acids in length and are responsible in Alzheimer’s disease, since one of the main components has been identified in the brains of Alzheimer patients. Amyloid beta is produced in both neurons and glia, while only neurons produce Aγ. The first processing step occurs on APP mostly in the endoplasmic reticulum of cells, where a signal sequence is removed and two cytosines are added to form a uracil. Then, the enzyme ADAM10 removes the N-terminal lysine to produce an Aβ peptide. Some APP with this process produces a truncated Aβ peptide that lacks the amino-terminal sequence. The enzyme ADAM17 has been shown to catalyze a specific cleavage of APP at codon 691, which results in the production of βanglea and γcystatin C from residues 691–693 and 703–705, respectively.
Amyloid beta peptide is packaged in large transport vesicles by a process involving clathrin-mediated endocytosis and facilitated diffusion. Aβ undergoes proteolysis to remove the signal sequence, which occurs primarily within the endoplasmic reticulum of cells. The resulting amyloid beta molecule is secreted as a precursor protein that is 20–25 kDa in size. This processed form of Aβ can be further cleaved into its mature 22–24 kDa fragment at two locations: at positions 601 and 603.
Amyloid beta molecules can exist in many forms by aggregating to form flexible soluble oligomers. There have been several potential activities which have been identified for amyloid beta for example protection against oxidative stress, anti-microbial activity, activation of kinase enzymes, functioning as a transcription factor and regulation of cholesterol transport. Senile plaques have been discovered to contain both Aβ40 and Aβ42, whilst the vascular amyloid is identified to contain mainly the shorter Aβ40. peptide. There have been suggested mechanisms for how these differences may occur, including protein aggregation and proteolysis; however current evidence suggests that these mechanisms are only major contributors towards a minority of cases.
Rat/mouse amyloid beta (1-40) ELISA kit is designed for measuring quantitative levels of Aβ 1-40 (amyloid beta, Abeta, beta-amyloid) in rat or mouse serum, brain extract, cell culture supernatant and plasma samples. This assay has a minimum sensitivity detection limit of 0.28 pg/ml.
All reagents supplied need to be stored at 2 °C – 8 °C, unopened reagents will retain reactivity until expiration date. Do not use reagents beyond this date.
- Microtiter Plate: Coated with anti-amyloid beta (35-40).
- Enzyme Conjugate (30x).
- Assay Buffer.
- Conjugate Buffer.
- TMB Substrate Solution.
- Stop Solution.
- Wash Buffer (40x).
The minimum sensitivity detection limit of beta-amyloid (1-40)(Aβ, Abeta) using current rat/mouse amyloid beta (1-40) ELISA kit was approximately 0.28 pg/ml. The dynamic range for this assay is 1.56 – 100.0 pg/ml.
– Sensitivity: 0.28 pg/mL
– Specificity: Mouse/Rat Aβ (1-40)(100%) and Human Aβ (1-40)(0.8%)
– Intra Assay: 2.3 – 4.9%
– Inter Assay: 4.3 – 5.8%
- Co-injection of Aβ1-40 and ApoE4 impaired spatial memory and hippocampal long-term potentiation in rats. Neurosci Lett. (2017) 648: 47-52. Wu M., et al.
- Personalized medicine in Alzheimer’s disease and depression. Contemp Clin Trials. (2013) 36 (2): 616-23. Review. Souslova T., et al.
- Glial markers and emotional memory in rats following acute cerebral radiofrequency exposures. Environ Sci Pollut Res Int. (2016) 23 (24): 25343-25355. Barthélémy A., et al.
- Nanotechnological strategies for nerve growth factor delivery: Therapeutic implications in Alzheimer’s disease. Pharmacol Res. (2017) 120: 68-87. Review. Faustino C., et al.
- Analysis of hippocampal gene expression profile of Alzheimer’s disease model rats using genome chip bioinformatics. Neural Regen Res. (2012) 7 (5): 332-40. Li Y., et al.
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