Cat # changed from RSKT-107-480R to SKT-107-480
Type
Sandwich ELISA, Biotin-labelled antibody
Applications
Serum, Tissue extract, Cell lysate
Storage/Expiration
2–8°C
Calibration Curve
Calibration Range
28–0.44 ng/mL
Cat. No. | Size |
Price |
|
---|---|---|---|
SKT-107-480 | 5x 96 wells (1 kit) |
Cat # changed from RSKT-107-480R to SKT-107-480
Sandwich ELISA, Biotin-labelled antibody
Serum, Tissue extract, Cell lysate
2–8°C
28–0.44 ng/mL
Apoptosis, Oncology, Others
Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90- regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now known to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase(3). When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.
In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immune-oadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (7).