A recombinant partial protein sequence (within amino acids 500-700) from the human protein was used as the immunogen for the HSP90AA1 antibody.
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 comiplex. HSP 90 also exists as a dimer with other proteins such as p60/sti1 and p23, forming an apo-receptor complex with estrogen and androgen receptors.
