Hsp90 Beta (HSP90AB1) Human Active Protein

Human

Human

20mM Tris, pH 7.5, 175 mM NaCl, 0.1 mM EDTA, 10% glycerol, 1 mM DTT

Affinity Purified

2 mg/mL (lot specific)

-20 degree ; 1 year + Avoid freeze/thaw cycle

=90kD

140572

ModBase 3D Structure for P08238

Protein activity can be an ambiguous term. Please refer to the data sheet or inquire with Technical Support to determine the definition of activity for this product.

This product has been certified >90% pure using SDS-PAGE analysis.

No tag

Baculovirus/Sf9 cells

Heat shock

Cytoplasm; Melanosome

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 specifc 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 tracking 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 speci?c function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7).

Chaperones; Heat Shock; Trafficking