| EREG

Epiregulin consists of 46 amino acid residues. Its secondary structure contains approximately 30 percent of β-sheet in the strand.Some of the residues form loops and turns due to the hydrogen bonding.The percentage of β-sheet in epiregulin depends on the domain and the secondary structures that they occupy. Structural motifs in most proteins have typical connections in an all β motif. Meaning that the polypeptide chains do not make a crossover connection or in so far as this type of connection has not been observed. Epiregulin is one of the proteins that occupies a typical connection in all β motif. Furthermore, as the structure of epiregulin forms a chain in an all β motif, it also forms β hairpin structural motif.
 

| 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	2.6	1.51	0.78	0.46	0.32	0.24	0.2	0.09
Corrected OD	2.51	1.42	0.69	0.37	0.23	0.15	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 EREG 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)	85-101	96
Plasma(n=8)	92-105	103

 

| Linearity

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

 

		Serum(n=4)	Plasma(n=4)
1 : 2	Range (%)	84-95	88-96
	Average (%)	91	93
1 : 4	Range (%)	89-103	87-109
	Average (%)	95	98