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Mouse Anti-Human HSP90 beta Monoclonal IgM Dylight 488

Mouse Anti-Human HSP90 beta Monoclonal IgM Dylight 488
353,04 €
Artikelnummer: STRSMC-136D-DY488

Verfügbarkeit: Regellieferzeit: Innerhalb 1 - 2 Wochen

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Mouse Anti-Human HSP90 beta Monoclonal IgM Dylight 488, Clone: Hyb-K3701

Details

HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively.HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 (9).

1 µg/ml was sufficient for detection of HSP90β in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

Zusatzinformation

Artikelnummer STRSMC-136D-DY488
Hersteller Stressmarq Biosciences
Herstellernummer SMC-136D-DY488
Verpackungseinheit 100 µg
Mengeneinheit FL
Reaktivität Human, Mouse (Murine)
Klonalität Monoclonal
Wirt / Host Mouse
Methode ELISA, Immunohistochemistry, Western Blotting
Isotype IgM
Gene ID NCBI (externer Link)
Datenblatt Download
MSDS Download