Hsp90 alpha / HSP90AA1 (Protein | Antibody | cDNA Clone | ELISA Kit)

All Hsp90 alpha / HSP90AA1 reagents are produced in house and quality controlled, including 2 Hsp90 alpha / HSP90AA1 Antibody, 45 Hsp90 alpha / HSP90AA1 Gene, 1 Hsp90 alpha / HSP90AA1 IP Kit, 1 Hsp90 alpha / HSP90AA1 Protein, 2 Hsp90 alpha / HSP90AA1 qPCR. All Hsp90 alpha / HSP90AA1 reagents are ready to use.

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Hsp90 alpha / HSP90AA1 Related Research Area

Hsp90 alpha / HSP90AA1 Background

Heat shock protein 9 (9 kDa heat-shock protein, HSP9) is a molecular chaperone involved in the trafficking of proteins in the cell. It is a remarkably versatile protein involved in the stress response and in normal homoeostatic control mechanisms. HSP9 interacts with 'client proteins', including protein kinases, transcription factors and others, and either facilitates their stabilization and activation or directs them for proteasomal degradation. By this means, HSP9 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP9 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP9 leads to client protein degradation and often cell death. Under stressful conditions, HSP9 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP9 client proteins and tumor cells require higher HSP9 activity than normal cells to maintain their malignancy. For this reason, Hsp9 has emerged as a promising target for anti-cancer drug development.

Hsp90 alpha / HSP90AA1 References

  • Pearl LH, et al. (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 410(3): 439-53.
  • Hahn JS. (2009) The Hsp90 chaperone machinery: from structure to drug development. BMB Rep. 42(10): 623-30.
  • Holzbeierlein JM, et al. (2010) Hsp90: a drug target? Curr Oncol Rep. 12(2): 95-101.
  • Trepel J, et al. (2010) Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer. 10(8): 537-49.