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HSP90 alpha ELISA Kit
Colorimetric detection of HSP90 alpha
Artikelnummer
STRSKT-107-96
Verpackungseinheit
96 well
Hersteller
Stressmarq Biosciences
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Target: HSP90
Product Type: ELISA Kits
Trademark: StressXpress®
Detection Method: Colorimetric Assay
Assay Type: Sandwich ELISA (Enzyme-linked Immunosorbent Assay)
Utility: ELISA kit used to quantitate HSP90 alpha concentration in samples.
Sample Type(s): Cell Lysates,Tissue,Serum,Whole Blood
Number of Samples: 40 samples in duplicate
Incubation Time: 30 minutes
Sensitivity: 0.117 ng/ml
Assay Range: 0.44 - 28 ng/ml
Scientific 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Product Type: ELISA Kits
Trademark: StressXpress®
Detection Method: Colorimetric Assay
Assay Type: Sandwich ELISA (Enzyme-linked Immunosorbent Assay)
Utility: ELISA kit used to quantitate HSP90 alpha concentration in samples.
Sample Type(s): Cell Lysates,Tissue,Serum,Whole Blood
Number of Samples: 40 samples in duplicate
Incubation Time: 30 minutes
Sensitivity: 0.117 ng/ml
Assay Range: 0.44 - 28 ng/ml
Scientific 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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