anti-Hsp 90 antibody

Arigo Biolaboratories

anti-Hsp 90 antibody

23

ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin

Research Use Only

Polyclonal

Unconjugated

HSP90AB1

heat shock protein 90 alpha family class B member 1

D6S182; heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein HSP 90-beta; HSP84; HSP90B; HSP90-beta; HSPC2; HSPCB

Rabbit

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).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.

Human

-20°C

12352203