| References |
| Synonyms |
|
| Formulation |
Protein G affinity-purified IgG at a concentration of 1 mg/ml in PBS, pH 7.4, containing sodium azide in 50% glycerol |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human Hsp90 |
+ |
| Rabbit Hsp90 |
+ |
| Rat Hsp90β |
+ |
| Murine Hsp90 |
+ |
| Chicken Hsp90 |
+ |
| Achyla Hsp90 |
+ |
| Wheat germ Hsp90 |
+ |
| Sf9 cell line Hsp90 |
+ |
| Natieve form E. coli Hsp90 |
- |
| Natieve form yeast Hsp90 |
- |
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Background Reading
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).
Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).
Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).
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. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).
Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).
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| Size |
Global Purchasing |
| 50 µg |
|
| 200 µg |
|
Description
Antigen:
Hsp90 from the water mold Achlya ambisexualis
·
Clone designation:
AC-16
·
Host:
mouse
·
Isotype:
IgG2b
·
Application(s):
WB
·
Hsp90 is an 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 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 signalling.5,6 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.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 cytocolic heterocomplexs with it. In a number of cases, variations in Hsp90 expression or Hsp90 mutation has been shown to degrade signalling 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 radical, 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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