English
HSP90 Antibody: FITC
Rabbit Anti-Human HSP90 Polyclonal
Artikelnummer
STRSPC-104D-FITC
Verpackungseinheit
100 µl
Hersteller
Stressmarq Biosciences
Verfügbarkeit:
wird geladen...
Preis wird geladen...
Target: HSP90
Conjugate: FITC
Product Type: Polyclonal
Immunogen: Full length Human Hsp90 protein
Swiss-Prot: P08238
Purification: Protein A Purified
Storage Buffer: PBS pH 7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects ~90kDa.
Cellular Localization: Cytoplasm,Melanosome
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 know 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.5. 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 immunoadsorption 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.
Conjugate: FITC
Product Type: Polyclonal
Immunogen: Full length Human Hsp90 protein
Swiss-Prot: P08238
Purification: Protein A Purified
Storage Buffer: PBS pH 7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects ~90kDa.
Cellular Localization: Cytoplasm,Melanosome
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 know 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.5. 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 immunoadsorption 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.
| Artikelnummer | STRSPC-104D-FITC |
|---|---|
| Hersteller | Stressmarq Biosciences |
| Hersteller Artikelnummer | SPC-104D-FITC |
| Green Labware | Nein |
| Verpackungseinheit | 100 µl |
| Mengeneinheit | STK |
| Reaktivität | Human, Mouse (Murine), Rat (Rattus) |
| Klonalität | Polyclonal |
| Methode | Immunofluorescence, Immunoprecipitation, Western Blotting, ELISA, Immunohistochemistry, Immunocytochemistry |
| Human Gene ID | 3326 |
| Wirt | Rabbit |
| Produktinformation (PDF) | Download |
| MSDS (PDF) | Download |
Verwandte Artikel
Markieren Sie die Artikel, um Sie dem Warenkorb hinzuzufügen oder
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
