Specifications
- Assay duration:Multiple steps
- Assay Type (ELISA with LOV):Competitive
- Conjugate ELISA:Biotin
- Format:Pre-coated
- Host:Rabbit
- Primary antibody reactivity:Human
- Target protein:Ab1-42
- Size:1 Kit
- Sample Type:Serum, Plasma and other biological fluids
- Cross Reactivity:No significant cross-reactivity or interference between Amyloid Beta Peptide 1-42 (Ab1-42) and analogues was observed
- Detection Method:Colorimetric
- Time to Results:2 h
- Shelf Life:12 Months
- Detection Range:3.70 - 300 pg/ml
- Storage Temperature:4 °C for one month (frequent use), −20 °C for one year
- Sample Volume:50 µl
- Sensitivity:1.44 pg/ml
- Regulatory Status:RUO
- Cat. No.:MSPP-CEA946HU
- No. of tests:96 wells
Specifications
About this item
This assay has high sensitivity and excellent specificity for detecting Human Ab1 to 42 (Amyloid Beta Peptide 1 to 42). The assay range is from 3.70 to 300 pg/ml (Competitive kit) with a sensitivity of 1.44 pg/ml. There is no detectable cross-reactivity with other relevant proteins. Activity loss rate and accelerated stability test ect have been conducted to guarantee the best performance of the products after long storage and delivery.
- High sensitivity and specificity
- Perfect reproducibility and consistency across batches
- Quality control with three-level inspections
- Wide range of targets/species available
- Intra-Assay: CV <10%, Inter-Assay: CV <12%
One of the hallmarks of Alzheimer's disease is the self-aggregation of the amyloid β peptide (Aβ) in extracellular amyloid fibrils. Aβ is a peptide composed of 40 to 42 (43) amino acids, and is said to be cleaved out of the precursor protein APP by the action of β- or γ-secretase.In addition, the presence of numerous variant A β molecules has been demonstrated in the culture fluid of mouse neuroblastoma cells transfected with cDNA coding human amyloid precursor protein (APP). Among the different forms of Aβ, the 42-residue fragment (Aβ1-42) readily self-associates and forms nucleation centers from where fibrils can quickly grow. The strong tendency of Aβ1-42 to aggregate is one of the reasons for the scarcity of data on its fibril formation process. Aβ1-40 is the most common form secreted from cultured cells and found in cerebro-spinal fluid (CSF). Aβ1-42 is the major component of senile plaques and considered as the most crucial factor in AD pathogenesis.