ELISA Kits - Cellular Stress, Heat Shock Proteins (HSP), Oxidative Stress

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Product Name: Hsp90Alpha ELISA Kit
Catalog #: SKT-107-480
Alternative Names: Hsp86, Hsp89A, Hsp90A, Hsp90AA1, HspC1, HspCA, HsoCAL3
Size: 5 x 96-well
Type: ELISA
Description: ELISA kit used to quantitate the Hsp90Alpha concentration in samples
Sample Type: Cell lysates, tissue extracts, serum samples
Research Area: Chaperones, Heat Shock
Sensitivity: 0.5-32ng/mL
Storage Temp: 4°C
Shipping Temp: Blue Ice, 4°C
Price: $2,396.00 USD Add to Cart

Hsp90α ELISA Kit Catalog# SKT-107 (96 well kit)	Download .pdf
Hsp90α ELISA Kit Catalog# SKT-107 MSDS	Download .pdf

Research Background: 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).
References: 1. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577.
2. Pearl H., et al. (2001) Adv Protein Chem 59: 157-186.
3. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.
4. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133.
5. Pratt W., Toft D. (1997) Endocr Rev 18: 306-360.
6. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420-434.
7. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324- 8328.

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