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HSP90/HSP90AA1  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: E. coli  
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HSP90/HSP90AA1 Related Area

HSP90/HSP90AA1 Related Pathways

HSP90/HSP90AA1 Summary & Protein Information

HSP90/HSP90AA1 Background

Gene Summary: The Hsp90 protein encoded by this HSP90AA1 gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this HSP90AA1 gene.
General information above from NCBI
Subunit structure: Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12604615, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:16307917, ECO:0000269|PubMed:16531226, ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:19875381, ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:9108479, ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9660753, ECO:0000269|PubMed:9817749}.
Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.
Subcellular location: Cytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Post-translational: ISGylated. {ECO:0000269|PubMed:16139798}.; S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.
Sequence similarity: Belongs to the heat shock protein 90 family. {ECO:0000305}.
General information above from UniProt

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/HSP90AA1 Alternative Name

LAP2,EL52,HSPN,HSP86,HSPC1,HSPCA,Hsp89,Hsp90,LAP-2,HSP89A,HSP90A,HSP90N,HSPCAL1,HSPCAL4, [homo-sapiens]
86kDa,89kDa,AL024080,AL024147,HSP 86,hsp4,HSP86,Hsp86-1,Hsp89,Hsp90,Hsp90aa1,Hspca,RP23-60K23.1, [mouse]
hsp4,86kDa,89kDa,Hsp89,Hsp90,Hspca,Hsp86-1,AL024080,AL024147, [mus-musculus]

HSP90/HSP90AA1 Related Studies

  • 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.