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Cat. Number
070300562812897
Chemical Name
Hsp90 Monoclonal Antibody Complex (Clone 8D3)
References
Synonyms
  • Heat Shock Protein 90 Complex
Formula Weight 90.0
Formulation PEG purified IgG, at a concentration of 1 mg/ml in PBS, pH 7.2, containing 0.09% sodium azide and 50% glycerol
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Human Hsp90 +
Murine Hsp90 +
Rat Hsp90β +
Rabbit Hsp90 +
Show all 4 Hide all but first 3

Background Reading

Dalman, F.C., Bresnick, E.H., Patel, P.D., et al. Direct evidence that the glucocorticoid receptor binds to Hsp90 at or near the termination of receptor translation in vitro. J Biol Chem 264(33) 19815-19821 (1989).

Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).

Whitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91 8324-8328 (1994).

Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).

Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).

Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).

Perdew, G.H. Association of the Ah receptor with the 90 kDa heat shock protein. J Biol Chem 263(27) 13802-13805 (1988).

Uma, S., Hartson, S.D., Chen, J., et al. Hsp90 is obligatory for the heme-regulated eIF-2α kinase to acquire and maintain an activable conformation. J Biol Chem 272(17) 11648-11656 (1997).

Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).

Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).

Show all 10 Hide all but first 3
Size Global Purchasing
50 µg  
200 µg  

Description

Antigen: aryl hydrocarbon receptor Hsp90 complex · Clone designation: 8D3 · Host: mouse · Application(s): IP · 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.1,2,3,4 Despite its label of being a Hsp, Hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% 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.3 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 and kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit Hsp90 function.7

1 Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).

2 Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).

3 Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).

4 Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).

5 Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).

6 Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).

7 Whitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91 8324-8328 (1994).

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