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Cat. Number
070289201225086
Chemical Name
Hsp90α Monoclonal Antibody (Clone D7α)
References
Synonyms
  • Heat Shock Protein 90α
Formula Weight 90.0
Formulation Mouse IgG at a concentration of 1 mg/ml in PBS buffer, containing 0.09% sodium azide and 50% glycerol
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Bovine Hsp90 +
Chicken Hsp90 +
Human Hsp90 +
Murine Hsp90 +
Porcine Hsp90 +
Rat Hsp90 +
Rabbit Hsp90 +
Human Hsp90α +
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Background Reading

Schuh, S., Yonemoto, W., Brugge, J., et al. A 90,000-dalton binding protein common to both steroid receptors and the rous sarcoma virus transforming protein, pp60v-src. J Biol Chem 260(26) 14292-14296 (1985).

Lipsich, L.A., Cutt, J.R., and Brugge, J.S. Association of the transforming proteins of rous, fujinami, and Y73 avian sarcoma viruses with the same two cellular proteins. Mol Cell Biol 2(7) 875-880 (1982).

Brugge, J., Yonemoto, W., and Darrow, D. Interaction between the rous sarcoma virus transforming protein and two cellular phosphoproteins: Analysis of the turnover and distribution of this complex. Mol Cell Biol 3(1) 9-19 (1983).

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).

Show all 10 Hide all but first 3
Size Global Purchasing
25 µg  
100 µg  

Description

Antigen: full length protein purified from chicken brain · Clone designation: D7α · Host: mouse · Application(s): IP and WB · 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% 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 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).

下一个：Hsp90 (salmonid) Polyclonal Antibody上一个：Hsp90α Monoclonal Antibody (Clone K41009)
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