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HSP90 Antibody: Dylight 405, Monoclonal

HSP90 Antibody: Dylight 405, Monoclonal
379,70 €
Artikelnummer: STRSMC-137D-DY405

Verfügbarkeit: Regellieferzeit: Innerhalb 1 - 2 Wochen

Kostenlose Lieferung innerhalb Österreichs!
HSP90 Antibody: Dylight 405, Monoclonal, Clone: D7A, Host: Mouse, Isotype: IgG1

Details

Mouse Anti-Chicken HSP90 Monoclonal IgG1
Target: HSP90
Purification: Protein G Purified
Specificity: Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37.
Conjugate: Dylight 405
Immunogen Species: Chicken
Cellular Location: Cytoplasm, Melanosome
Immunogen: Full length protein HSP90 purified from chicken brain
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 (4-7). 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 (8-9). 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(6). 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-adsorption 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 (10).
Reference: 1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296.2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880.3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19.4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133.8. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.

Zusatzinformation

Artikelnummer STRSMC-137D-DY405
Hersteller Stressmarq Biosciences
Herstellernummer SMC-137D-DY405
Verpackungseinheit 100 µg
Mengeneinheit FL
Reaktivität Chicken, Cow (Bovine), Human, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus)
Klonalität Monoclonal
Wirt / Host Mouse
Methode ELISA, Immunohistochemistry, Immunoprecipitation, Western Blotting
Isotype IgG1
Gene ID NCBI (externer Link)
Datenblatt Download
MSDS Download