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Hsp90 Alpha StressXpress® Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Hsp86, Hsp89A, Hsp90A, Hsp90AA1, HspC1, HspCA, HsoCAL3
  • Species:Human
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Cat. No. Size Price


RSKT-107R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Tissue extract, Cell lysate

Storage/Expiration

2–8°C

Calibration Curve

Calibration Range

28–0.44 ng/mL

Summary

Features

  • ELISA Kit is for the detection of human Hsp90α in cell lysates, tissue extracts, and serum samples
  • The total assay time is less than 4 hours

Research topic

Apoptosis, Oncology, Others

Summary

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 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 immune-oadsorption 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).

References to Product

References

  • Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577.
  • Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.
  • Pearl H., et al. (2001) Adv Protein Chem 59: 157-186.
  • Pratt W., Toft D. (2003) Exp Biol Med 228:111-133.
  • Pratt W., Toft D. (1997) Endocr Rev 18: 306–360.
  • Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434.
  • Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.
References to Summary

References to Heat Shock 90kDa Protein Alpha

  • Arlander SJ, Eapen AK, Vroman BT, McDonald RJ, Toft DO, Karnitz LM. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem. 2003 Dec 26;278 (52):52572-7
  • Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med. 2002;8 (4 Suppl):S55-61
  • Pearl LH, Prodromou C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem. 2001;59:157-86
  • Pratt WB. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med. 1998 Apr;217 (4):420-34
  • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood). 2003 Feb;228 (2):111-33
  • Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev. 1997 Jun;18 (3):306-60
  • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. 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 U S A. 1994 Aug 30;91 (18):8324-8
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