| HSP-90

Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.The Hsp90 protein contains three functional domains, the ATP-binding, protein-binding, and dimerizing domain, each of which playing a crucial role in the function of the protein.In unstressed cells, Hsp90 plays a number of important roles, which include assisting folding, intracellular transport, maintenance, and degradation of proteins as well as facilitating cell signaling.
 

| 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 (ng/mL)	10	5	2.5	1.25	0.625	0.312	0.156	0
OD	2.59	1.95	1.46	0.94	0.63	0.43	0.32	0.1
Corrected OD	2.49	1.85	1.36	0.84	0.53	0.33	0.22	-

 

| Repeatability

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

| Recovery

The recovery of Mouse HSP-90 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)	88-102	94
Plasma(n=8)	94-107	101
Cell Culture Supernates(n=8)	96-110	108

 

| Linearity

Samples were spiked with high concentrations of Mouse HSP-90 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 (%)	82-93	88-96	90-110
	Average (%)	91	95	99
1 : 4	Range (%)	89-103	87-110	105-115
	Average (%)	97	102	109