| GST

Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function.[4] The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.

| Repeatability

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

| Recovery

The recovery of Mouse GST 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)	96-107	104

 

| Linearity

Samples were spiked with high concentrations of Mouse GST 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	89-96	90-110
	Average (%)	91	94	96
1 : 4	Range (%)	89-103	87-108	105-115
	Average (%)	94	98	108