HSP 90 Background Information The heat shock response was first described for Drosophila salivary gland cells and morphologically consists of a change in their polytene chromosome puffing patterns that involves de novo synthesis of a few proteins. Similar heat shock proteins were later discovered in bacterial chicken and mammalian cells, and have been subsequently studied in other organisms. A series of proteins, including HSP 90, HSP 70, HSP 20-30 and ubiquitin, are induced by insults such as temperature shock, chemicals and other environmental stress. A major function of HSP 90 and other HSPs is to act as molecular chaperones. HSP 90 forms a complex with glucocorticoid receptor (GR), rendering the non ligand-bound receptor transcriptionally inactive. HSP 90 binds the GR as a heterocomplex composed of either HSP 56 or Cyclophilin D, forming an aporeceptor complex. HSP 90 also exists as a dimer with other proteins such as p60/STI1 and p23, forming an aporeceptor complex with estrogen and androgen receptors.
HSP 90 (4F10) Product Citations
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HSP 90 (4F10)
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HSP 90 (4F10): sc-69703. Western blot analysis of HSP 90 expression in non-transfected: sc-117752 (A) and human HSP 90 transfected: sc-114003 (B) 293T whole cell lysates.
HSP 90 (4F10): sc-69703. Western blot analysis of HSP 90α expression in non-transfected 293T: sc-117752 (A), mouse HSP 90α transfected 293T: sc-120913 (B) and HeLa (C) whole cell lysates.
HSP 90 (4F10): sc-69703. Western blot analysis of HSP 90 expression in non-transfected 293T: sc-117752 (A), human HSP 90 transfected 293T: sc-114003 (B) and HeLa (C) whole cell lysates.