HSP90 Protein (HSP90AA1 Protein)

Heat Shock Protein 90kDa alpha (cytosolic), class A member 1

HSP90 Products

HSP90 Protein, Recombinant

Molecule	Species	Description	Cat. No
HSP90/HSP90AA1	Human	HSP90/HSP90AA1 Protein, Recombinant	11445-HNCE

HSP90 cDNA Clone

Molecule	Species	Description	Cat. No
HSP90/HSP90AA1	Human	Homo sapiens HSP90/HSP90AA1 cDNA Clone	HG11445-M

HSP90 Related Areas

Cancer>>Apoptosis>>Heat-Shock Protein>>HSP90/HSP90AA1

HSP90 Alternative Names

Hsp90, HSP90AA1, Hsp89, HSP 86, FLJ31884, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, LAP2 [Homo sapiens]

Hsp90, Hsp90aa1, Hsp89, HSP86, HSP 86, RP23-60K23.1, 86kDa, 89kDa, AL024080, AL024147, Hsp86-1, Hspca, hsp4 [Mus musculus]

HSP90 Background

Heat shock protein 90 (90 kDa heat-shock protein, HSP90) 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. HSP90 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, HSP90 displays a multifaceted ability to influence signal transduction, chromatin remodelling and epigenetic regulation, development and morphological evolution. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis at the N-terminus. Disruption of HSP90 leads to client protein degradation and often cell death. Under stressful conditions, HSP90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Especially, several oncoproteins act as HSP90 client proteins and tumor cells require higher HSP90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer drug development.

HSP90 Related Studies

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