| Aβ1-42

The amyloid-β protein (Aβ) cascade theory is one of the mainstream theories on the pathogenesis of AD, and age spots formed by Aβ aggregation are one of the main pathological features of AD, which are mainly formed by the abnormal deposition of Aβ1-42. Aβ1-42 polypeptide can be aggregated to form oligomers, fibrils, and other different aggregated forms. The most common subtypes of Aβ in the human body are Aβ1-40 and Aβ1-42. In human cerebrospinal fluid and blood, the level of Aβ1-40 is 10 times and 1.5 times higher than that of Aβ1-42, respectively. Aβ1-42 has stronger toxicity and is more likely to aggregate, thus forming the core of Aβ precipitation and triggering neurotoxic effects.
 

| Typical data

As the OD values of the standard curve may vary according to the conditions of the actual assay performance (e.g. operator, pipetting technique, wash technique or temperature effects), the operator should establish a standard curve for each test. Typical standard curve and data are provided below for reference only.

 

Concentration (pg/mL)	1000	500	250	125	62.5	31.25	15.62	0
OD	2.65	1.5	0.96	0.58	0.39	0.26	0.18	0.07
Corrected OD	2.58	1.43	0.89	0.51	0.32	0.19	0.11	-

 

| Repeatability

Intra-assay Precision (Precision within an assay)：CV% < 10%; Inter-assay Precision (Precision between assays)：CV% < 10%
 

| Recovery

The recovery of Mouse Aβ1-42 spiked at three different levels in samples throughout the range of the assay was evaluated in various matrices.

 

Sample Type	Range(%)	Average Recovery(%)
Serum(n=8)	84-101	96
Plasma(n=8)	92-105	102
Cell Culture Supernates(n=8)	96-108	105

 

| Linearity

Samples were spiked with high concentrations of Mouse Aβ1-42 and diluted with Universal Diluent to produce samples with values within the range of the assay.

 

		Serum(n=4)	Plasma(n=4)	Cell Culture Supernates(n=4)
1 : 2	Range (%)	84-95	88-96	90-110
	Average (%)	91	93	96
1 : 4	Range (%)	89-103	87-107	105-115
	Average (%)	94	98	108