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HSP90 complex Antibody: Dylight 350, Monoclonal

HSP90 complex Antibody: Dylight 350, Monoclonal
552,58 €
Artikelnummer: STRSMC-109B-DY350

Verfügbarkeit: Regellieferzeit: Innerhalb 1 - 2 Wochen

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HSP90 complex Antibody: Dylight 350, Monoclonal, Clone: 8D3, Host: Mouse, Isotype: IgM

Details

Mouse Anti-Human HSP90 complex Monoclonal IgM
Target: HSP90
Purification: PEG Purified
Specificity: Detects 90kDa. Co-immunoprecipitates HSP90 complexes, including HSP70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase (HRI).
Conjugate: Dylight 350
Immunogen Species: Human
Cellular Location: Cytoplasm, Melanosome
Immunogen: Ah receptor (Aryl hydrocarbon receptor)
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).
Reference: 1. Arlander SJH, 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 WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.7. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.8. Perdew, G. H. (1988) JBC 263 (27): 13802-138059. Dalman, F. C. et al.(1989) JBC 264(33): 19815-1982110. Uma, S. et al. (1997) JBC 272(17): 11648-11656.

Zusatzinformation

Artikelnummer STRSMC-109B-DY350
Hersteller Stressmarq Biosciences
Herstellernummer SMC-109B-DY350
Verpackungseinheit 200 µg
Mengeneinheit FL
Reaktivität Human, Mouse (Murine), Rabbit, Rat (Rattus)
Klonalität Monoclonal
Wirt / Host Mouse
Methode Immunocytochemistry, Immunofluorescence, Immunoprecipitation
Isotype IgM
Gene ID NCBI (externer Link)
Datenblatt Download
MSDS Download