Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat. HSP90 is a 90 kDa protein that is induced under stress conditions, but is also one of the most abundant cellular proteins found under non-stress conditions. HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90 has been found to be associated with a number of other intracellular proteins, including steroid receptors, actin, tubulin, aryl hydrocarbon (Ah) receptor, and some kinases.
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Protein Aliases: Heat shock 84 kDa; heat shock 90kD protein 1, beta; Heat shock protein; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; Heat shock protein HSP 90-beta; HSP; HSP 84; HSP 90; HSP90-beta; RP1-302G2.1
Gene Aliases: D6S182; HSP84; HSP90AB1; HSP90B; HSPC2; HSPCB
UniProt ID: (Human) P08238
Entrez Gene ID: (Human) 3326